|
Archaea
| | | | | |
|
Aeropyrum pernix
| | | | | |
|
5106104_
|
2621953_Mth
|
2633525_Bs
|
Hydroxymethyl-
|
None
|
Pyrococci encode proteins with
|
|
APE2400
|
5e-27;
|
4e-54;
|
pyrimidine
| |
the same domain organization
|
|
Archaeal-bacterial
|
282-445;
|
16-272;
|
phosphate kinase
| |
andclosest similarity to A. pernix;
|
| |
uncharacterized domain
|
hydroxymethyl-
|
involved in thiamine
| |
M. jannaschii encodes a protein
|
| |
conserved among
|
pyrimidine phosphate
|
biosynthesis
| |
with the same domain
|
| |
archaea (homolog
|
kinase
|
(additional function?)
| |
organization but low similarity;
|
| |
of the amino-terminal
| | | |
Mt encodes a HMP-kinase with
|
| |
domain of sialic acid
| | | |
moderate similarity
|
| |
synthase)
| | | | |
|
Methanococcus jannaschii
| | | | | |
|
1591138_
|
2128140_Mj;
|
7270033_At;
|
Unknown;
|
None
|
The amino-terminal domain is
|
|
MJ0434
|
1e-19;
|
0.003;
|
possible role
| |
present in several stand-alone
|
|
Archaeal-
|
2-94;
|
120-222;
|
in stress response
| |
copies in M. jannaschii, but
|
|
bacterial-eukaryotic
|
uncharacterized
|
AIG2-like
| | |
otherwise, is seen mostly in
|
| |
domain
|
stress-related
| | |
bacteria; the possibility of
|
| | |
protein
| | |
acquisition of a bacterial gene
|
| | | | | |
by the Methanococcus lineage
|
| | | | | |
is conceivable
|
|
Methanobacterium thermoautotrophicum
| | | | | |
|
2621249_
|
5103547_Ap;
|
1651798_Ssp;
|
Membrane-associated
|
None
|
In Ssp, the amino-terminal
|
|
MTH204
|
1e-34;
|
0.002;
|
5-formyl-
| |
domain is fused to another
|
|
Archaeal-
|
137-326;
|
8-139;
|
tetrahydrofolate
| |
uncharacterized domain. An
|
|
eukaryotic/
|
5-formyl-
|
uncharacterized
|
cyclo-ligase(?);
| |
ortholog with conserved
|
|
bacterial
|
tetrahydrofolate
|
membrane-associated
|
exact function
| |
domain organization is seen
|
| |
cyclo-ligase
|
domain
|
unknown
| |
in Mycobacterium, but many
|
| | | | | |
other bacteria encode stand-
|
| | | | | |
alone versions of this domain,
|
| | | | | |
which could be the actual sources
|
| | | | | |
of horizontal gene transfer
|
|
2621673_
|
3256572_Ph;
|
2984130_Aa;
|
GTPase, possible
|
2621855
| |
|
MTH594
|
3e-10;
|
6e-19;
|
role in signal
| | |
|
Archaeal-bacterial
|
5-137;
|
233-390;
|
transduction
| | |
| |
inactivated RecA
|
GTPase
| | | |
| |
domain
| | | | |
|
2622642_
|
5105992_Ap;
|
2569943_Axy;
|
Glucose-1-phosphate
|
None
| |
|
MTH1523
|
3e-36;
|
2e-05;
|
thymidylyl transferase/
| | |
|
Archaeal-bacterial
|
5-226;
|
226-334;
|
glucose-6-phosphate
| | |
| |
glucose-1-phosphate
|
mannose-6-
|
isomerase
| | |
| |
thymidylyl transferase
|
phosphate isomerase
| | | |
|
Bacteria
| | | | | |
|
Aquifex aeolicus
| | | | | |
|
2983622_
|
2633696_Bs;
|
2650176_Af;
|
Signal
|
None
| |
|
aq_1151
|
5e-65;
|
0.005;
|
transduction
| | |
|
Bacterial-archaeal
|
325-795;
|
116-279;
|
c-di-GMP
| | |
| |
c-di-GMP phospho-
|
PAS/PAC
|
phospho-diesterase
| | |
| |
diesterase
|
domain
| | | |
|
2984285_
|
586875_Bs;
|
3915955_Mj;
|
Molybdenum
|
None
| |
|
aq_2060
|
4e-63
|
3e-09;
|
cofactor
| | |
|
Bacterial-archaeal
|
1-252;
|
270-441;
|
bisynthesis enzyme(?)
| | |
| |
PHP superfamily
|
pyruvate
| | | |
| |
hydrolase
|
formate-lyase
| | | |
| | |
activating enzyme
| | | |
| | |
(Fe-S cluster
| | | |
| | |
oxidoreductase)
| | | |
|
Bacillus subtilis
| | | | | |
|
2632283_yaaH,
|
4980914_Tm
|
399377_Rn
|
Chitinase
|
2635915
|
B. subtilis encodes two
|
|
1945087_ydhD
|
1e-06
|
2e-11
| | |
paralogous proteins with the
|
|
Bacterial-eukaryotic
|
2-92;
|
221-402;
| | |
same domain architecture
|
| |
LysM repeat domain
|
chitinase
| | | |
|
2633242_yhcR
|
645819_Dr;
|
2622704_Mth;
|
Nuclease-nucleotidase
|
None
| |
|
Bacterial-archaeal
|
1e-64;
|
0.008
|
(probable repair
| | |
| |
584-1068;
|
151-257;
|
enzyme)
| | |
| |
5'-nucleotidase;
|
nucleic acid-binding
| | | |
| |
1175987_
|
domain (OB-fold)
| | | |
| |
ECR100;
| | | | |
| |
2e-09;
| | | | |
| |
377-521;
| | | | |
| |
thermonuclease
| | | | |
|
2632325_yabN
|
4981449_Tm;
|
3873806_Ce;
|
Methyl-transferase/
|
None
|
Other than in chlamydiae,
|
|
Bacterial-eukaryotic
|
2e-62;
|
0.003;
|
pyro-phosphatase
| |
the SWI domain is seen
|
| |
223-483;
|
7-125;
|
(metabolic enzyme
| |
in eukaryotic chromatin-
|
| |
MazG (predicted pyro-
|
SAM-dependent
|
of an unknown
| |
associated proteins, leading
|
| |
phosphatase)
|
methyl-transferase
|
pathway?)
| |
to the suggestion that
|
| | | | | |
chlamydial topoisomerase
|
| | | | | |
is involved in chromosome
|
| | | | | |
condensation
|
|
Chlamydophyla pneumoniae
| | | | | |
|
4377077_
|
730965_Bs;
|
3581917_Sp;
|
DNA topoisomerase I,
|
7189103
|
SWI is a typical eukaryotic
|
|
CPn0769
|
e-148;
|
3e-10;
|
possibly involved in
| |
domain not found in
|
|
Bacterial-eukaryotic
|
1-727;
|
792-866;
|
chromatin
| |
prokaryotes other than
|
| |
DNA topoisomerase I
|
SWI domain
|
condensation
| |
chlamydia (the ortholog
|
| | | | | |
in Chlamydia trachomatis has the
|
| | | | | |
same domain architecture)
|
|
Deinococcus radiodurans
| | | | | |
|
6459294_
|
7248325_Sco;
|
6754878_Mm;
|
DNase
|
None
|
The G9a domain is not
|
|
DR1533
|
0.001;
|
9e-28;
| | |
detectable in other prokaryotes.
|
|
Bacterial-eukaryotic
|
171-265;
|
4-148;
| | |
In eukaryotes, this domain so
|
| |
McrA family
|
G9a domain (DNA-
| | |
far has been found only as part
|
| |
endonuclease
|
binding?)
| | |
of multidomain nuclear proteins,
|
| | | | | |
including transcription factors
|
|
Escherichia coli
| | | | | |
|
1787179_
|
94933_Ppu;
|
3747107_Rn;
|
Oxidoreductase
|
None
|
The eukaryotic domain is present
|
|
b0947
|
3e-10;
|
3e-32;
| | |
(as a partial sequence) also in the
|
|
Bacterial-eukaryotic
|
287-367;
|
4-261;
| | |
beta-proteobacterium Vogesella.
|
| |
ferredoxin
|
uncharacterized
| | |
This domain contains a conserved
|
| | |
domain (thiol
| | |
pair of cysteines, which together
|
| | |
oxidoreductase?)
| | |
with the ferredoxin fusion, may
|
| | | | | |
suggest a thiol oxidoreductase
|
| | | | | |
activity. Most of the eukaryotic
|
| | | | | |
proteins containing this domain
|
| | | | | |
appear to be mitochondrial,
|
| | | | | |
suggesting the possibility of an
|
| | | | | |
alternative evolutionary scenario
|
|
1787678_
|
487713_Sli;
|
5459012_Pab;
|
Methyl-transferase/
|
None
| |
|
b1410
|
3e-05;
|
1e-17;
|
Lipase (exact function
| | |
|
Bacterial-archaeal
|
408-522;
|
33-274;
|
unclear)
| | |
| |
SAM-dependent
|
lyso-phospholipase
| | | |
| |
methyl-transferase
| | | | |
|
1787679_ynbD
|
1591375_Mj;
|
7160233_Sp;
|
Membrane-associated
|
None
|
An unusual case of fusion
|
|
Archaeal-eukaryotic
|
4e-04;
|
1e-06;
|
bifunctional
| |
between an apparently archaeal
|
| |
50-218;
|
346-415;
|
phosphatase
| |
and a typical eukaryotic domain
|
| |
membrane-associated
|
tyrosine phosphatase
| | |
in a bacterium
|
| |
acid phosphatase
| | | | |
|
1788589_
|
5763950_Sco;
|
3860247_At;
|
Bifunctional enzyme;
|
None
| |
|
b2255
|
4e-35;
|
1e-55;
|
exact function unclear
| | |
|
Bacterial-eukaryotic
|
1-259;
|
318-652;
| | | |
| |
methionyl-tRNA
|
dTDP-glucose 4-6-
| | | |
| |
formyl-transferase
|
dehydratase
| | | |
|
1788938_yfiQ
|
929735_Nsp;
|
2649370_Af;
|
acetyl-CoA synthetase/
|
None
| |
|
bacterial-Archaeal/
|
8e-32;
|
4e-85;
|
acetyl-transferase; exact
| | |
|
eukaryotic
|
637-874;
|
6-689;
|
function unclear
| | |
| |
acetyl-transferase
|
acetyl-CoA synthetase
| | | |
|
Mycobacterium tuberculosis
| | | | | |
|
2909507_
|
6469244_Sco;
|
4151109_Tbr;
|
Adenylate cyclase/
|
7476546,
|
M. tuberculosis encodes three
|
|
Rv2488c,
|
5e-64;
|
6e-04;
|
ATPase; probable
|
7476738
|
paralogous proteins that consist
|
|
2791528_Rv1358,
|
19-603;
|
6-167;
|
transcription regulator
| |
of three domains, the eukaryotic-
|
|
1419061_
|
4726088_Rer;
|
adenylate cyclase
| | |
type adenylate cyclase, AP
|
|
Rv1358
|
2e-12;
| | | |
(apoptotic) ATPase and DNA-
|
|
Bacterial-eukaryotic
|
818-1073
| | | |
binding response regulator, and
|
| | | | | |
two stand-alone versions of
|
| | | | | |
adenylate cyclase, which show the
|
| | | | | |
closest similarity to the cyclase
|
| | | | | |
domain of the multidomain
|
| | | | | |
proteins
|
|
1314025_
|
120037_Tt;
|
178213_Hs;
|
Ferredoxin/
|
2076681
|
D. radiodurans also encodes the
|
|
Rv0886
|
1e-11;
|
4e-65;
|
ferredoxin reductase
| |
eukaryotic-type ferredoxin
|
|
Bacterial-eukaryotic
|
2-79;
|
93-543;
| | |
reductase, but the ferredoxin
|
| |
ferredoxin
|
ferredoxin reductase
| | |
fusion is unique to mycobacteria
|
|
3261732_
|
2661695_Sco;
|
279520_Dd;
|
cAMP-dependent
|
4455714
| |
|
Rv0998
|
3e-13;
|
7e-07;
|
acetyl-transferase(?)
|
(M. leprae)
| |
|
Bacterial-eukaryotic
|
148-328;
|
30-105;
| | | |
| |
acetyl-transferase
|
cAMP-binding domain
| | | |
|
2326726_
|
421331_Cvi;
|
2645721_Mm;
|
Bifunctional enzyme of
|
1929080
| |
|
Rv1683
|
1e-24;
|
6e-26;
|
poly (3-hydroxy-butyrate)
| | |
|
Bacterial-eukaryotic
|
23-359;
|
456-972;
|
synthesis
| | |
| |
poly (3-hydroxy-
|
very-long-chain
| | | |
| |
butyrate) synthase
|
acyl-CoA synthetase
| | | |
|
1403447_
|
6752338_Sco;
|
3892714_At;
|
Polyfunctional enzyme
|
2661651
|
In this protein, the domain of
|
|
Rv2006
|
2e-27;
|
8e-27;
|
of trehalose metabolism
| |
apparent eukaryotic origin
|
|
Bacterial-eukaryotic
|
23-240;
|
264-521;
| | |
is flanked by bacterial domains
|
| |
phosphatase;
|
trehalose-6-phosphate
| | |
from both sides
|
| |
6448751_Sco;
|
phosphatase
| | | |
| |
0.0;
| | | | |
| |
534-1320;
| | | | |
| |
trehalose hydrolase
| | | | |
|
2896788_
|
117648_Ec;
|
3073773_Mm;
|
Polyfunctional enzyme
|
2337823
|
The presence of the stand-alone
|
|
Rv2051c
|
1e-16;
|
4e-31;
|
of lipid metabolism
|
(M. leprae);
|
version of the eukaryotic
|
|
Bacterial-eukaryotic
|
94-514;
|
588-829;
| |
6468712
|
domain in Streptomyces suggests
|
| |
apolipoprotein
|
dolichol-phosphate-
| |
(Streptomyces
|
an ancient horizontal transfer
|
| |
N-acyltransferase
|
mannose synthase
| |
coelicolor)
| |
|
2791523_
|
6225563_Scy;
|
1098605_Cnu;
|
Multifunctional enzyme
|
None
| |
|
Rv2483c
|
7e-16;
|
5e-22;
|
of phospholipid
| | |
|
Bacterial-eukaryotic
|
36-253;
|
289-492;
|
metabolism
| | |
| |
phosphoserine
|
1-acyl-sn-
| | | |
| |
phosphatase
|
glycerol-3-phosphate
| | | |
| | |
acyltransferase
| | | |
|
2894233_
|
2633801_Bs;
|
4538974_At;
|
Molybdopterin synthase
|
2076687
|
The same domain organization
|
|
Rv3323c
|
3e-19;
|
7e-06;
| | |
is seen in D. radiodurans, but in
|
|
Bacterial-eukaryotic
|
89-208;
|
2-82;
| | |
this case, both components
|
| |
molybdopterin
|
molybdopterin
| | |
appear to be of bacterial origin
|
| |
synthase large subunit
|
synthase small subunit
| | | |
| |
(MoaE)
|
(MoaD)
| | | |
|
2960152_
|
4753872_Sco;
|
466119_Ce;
|
cAMP-regulated
|
2501688
|
M. tuberculosis encodes two
|
|
Rv3728,
|
1e-35;
|
7e-20;
|
efflux pump(?)
| |
strongly similar paralogs with
|
|
7477551_
|
56-428;
|
549-964;
| | |
the same domain architecture
|
|
Rv3239c
|
transmembrane
|
cAMP-binding domain-
| | | |
|
Bacterial-eukaryotic
|
efflux protein
|
phosphoesterase
| | | |
|
2960153_
|
4731342_Sl;
|
1591330_Mj;
|
Bifunctional enzyme
|
1806159
|
The amino-terminal domain
|
|
Rv3729
|
3e-14;
|
3e-58;
|
of molybdenum
| |
stand-alone paralog is more
|
|
Bacterial-archaeal
|
510-776;
|
molybdenum
|
cofactor biosynthesis
| |
similar to archaeal homologs
|
| |
C5-O-methyl-
|
cofactor biosynthesis
| | |
than to the stand-alone paralog,
|
| |
Transferase
|
protein MoaA
| | |
but nevertheless, the latter
|
| |
(mitomycin
|
(Fe-S oxidoreductase)
| | |
appears to be of archaeal origin
|
| |
biosynthesis)
| | | | |
|
3261806_
|
40487_Cg;
|
7304009_Dm;
|
Secreted protein
|
7649504
|
The stand-alone version of the
|
|
Rv3811
|
3e-12;
|
2e-12;
| |
(S. coelicolor)
|
eukaryotic domain is present
|
|
Bacterial-eukaryotic
|
404-494;
|
198-384;
| | |
only in Streptomyces
|
| |
major secreted
|
peptidoglycan
| | | |
| |
protein
|
recognition protein
| | | |
|
Treponema pallidum
| | | | | |
|
3322964_
|
7225946_Nm;
|
320868_Sc;
|
Uridine kinase
|
None
|
A co-linear ortholog is present
|
|
TP0667
|
9e-04;
|
2e-13;
| | |
in Thermotoga
|
|
Bacterial-eukaryotic
|
10-154;
|
290-488;
| | | |
| |
threonyl-tRNA
|
uridine kinase
| | | |
| |
synthetase (TGS and
| | | | |
| |
H3H domains)
| | | | |
|
Thermotoga maritima
| | | | | |
|
4981276_
|
68516_Bs;
|
3218401_Sp;
|
Uridine kinase
|
None
|
A co-linear ortholog is present
|
|
TM0751
|
3e-07;
|
2e-11;
| | |
in Treponema
|
|
Bacterial-eukaryotic
|
11-200;
|
288-475;
| | | |
| |
threonyl-tRNA
|
uridine kinase
| | | |
| |
synthetase (TGS and
| | | | |
| |
H3H domains)
| | | | |
|
Eukaryotes
| | | | | |
|
Saccharomyces cerevisiae
| | | | | |
|
536367_
|
586134_Bt;
|
7450047_Aa;
|
Bifunctional signal-
|
5249
|
SurE homologs are not
|
|
Ybr094w
|
9e-10;
|
8e-09;
|
transduction protein
|
(Yarrowia
|
detectable in eukaryotes other
|
|
Eukaryotic/
|
tubulin-tyrosine ligase
|
acid phosphatase
| |
lipolytica)
|
than yeasts
|
|
Bacterial-archaeal
| |
(SurE)
| | | |
|
1431219_
|
577625_Hs;
|
3328426_Ct
| | | |
|
YDL141w
|
1e-39
|
5e-27;
| | | |
|
Eukaryotic-
|
Biotin-[propionyl-
|
biotin protein ligase
|
Bifunctional biotin-
|
None
|
An ortholog with an identical
|
|
bacterial
|
CoA-carboxylase(ATP-
| |
protein ligase
| |
domain architecture is present
|
| |
hydrolysing)] ligase
| | | |
in S. pombe
|
|
458922_
|
477096_Gg;
|
1653075_Ssp;
|
heat shock
|
NONE
|
An ortholog with an identical
|
|
YHR206W
|
8e-18;
|
7e-17;
|
transcription
| |
domain architecture is present
|
|
Eukaryotic-bacterial
|
78-216
|
375-503;
|
factor
| |
in S. pombe (3327019)
|
| |
heat shock
|
CheY domain
| | | |
| |
transcription factor
| | | | |
| |
domain
|
2983676_Aa;
|
Siroheme synthase
|
2330809
|
S. pombe also encodes a co-linear
|
|
486539_
|
1146165_At;
|
1e-04;
| |
(S. pombe)
|
ortholog (3581882); apparent
|
|
YKR069w
|
3e-34;
|
22-188;
| | |
displacement of the bacterial
|
|
Eukaryotic-bacterial
|
249-556;
|
precorrin-2 oxidase
| | |
precorrin-2 oxidase by a distinct
|
| |
urophorphyrin III
| | | |
Rossmann fold domain
|
| |
methylase
| | | | |
|
1302305_
|
4938476_At;
|
3212189_Hi;
|
Multifunctional enzyme
|
None
|
Co-linear orthologs in S. pombe
|
|
YNL256w
|
5e-65;
|
5e-05;
|
of folate biosynthesis
| |
(7490442) and Pneumocystis
|
|
Eukaryotic-bacterial
|
324-861
|
62-148;
| | |
carinii (283062)
|
| |
7,8-dihydro-6-
|
187-297;
| | | |
| |
hydroxymethylpterin-
|
dihydro-neopterin
| | | |
| |
pyro-phosphokinase+
|
aldolase
| | | |
| |
Dihydro-pteroate
| | | | |
| |
synthase
| | | | |
|
1419887_
|
7297709_Dm;
|
5918510_Sco;
|
Bifunctional RNA
|
2213559
|
The known bacterial homologs
|
|
YOL066c
|
2e-72;
|
2e-10;
|
modification enzyme
|
(S. pombe)
|
have a two-domain organization;
|
|
Eukaryotic-bacterial
|
42-408;
|
436-574;
| | |
the evolutionary scenario could
|
| |
large ribosomal
|
pyrimidine deaminase
| | |
have included domain
|
| |
subunit pseudoU
| | | |
rearrangements
|
| |
synthase
| | | | |
|
1419865_
|
2462827_At;
|
1075360_Hi;
|
Transcriptional regulator None
| |
Yeast encodes three strongly
|
|
YOL055c,
|
1e-39;
|
6e-24;
|
of thiamine biosynthesis
| |
similar paralogs with identical
|
|
2132251_
|
22-390;
|
342-549;
|
genes(?)
| |
domain organization; co-linear
|
|
YPL258c,
|
phosphomethyl
|
transcriptional
| | |
orthologs are present in other
|
|
2132289_
|
pyrimidinekinase
|
activator
| | |
ascomycetes
|
|
YPR121w
|
(thiamine biosynthesis)
| | | | |
|
Eukaryotic-bacterial
| | | | | |
|
1370444_ YPL214c
|
2746079_Bn;
|
2648451_Af;
|
Bifunctional thiamine
|
None
|
Except for the one from
|
|
Eukaryotic-archaeal/
|
1e-27;
|
9e-27;
|
biosynthesis enzyme
| |
A. fulgidus, all highly conserved
|
|
Bacterial
|
9-233;
|
251-531;
| | |
homologs of the kinase domain
|
| |
thiamin-phosphate
|
hydroxyethyl-thiazole
| | |
of this protein are bacterial; it
|
| |
pyro-phosphorylase
|
kinase
| | |
appears likely that the A. fulgidus
|
| | | | | |
gene is the result of horizontal
|
| | | | | |
transfer
|
