|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09183 |
PRK09183 |
transposase/IS protein; Provisional |
1-259 |
0e+00 |
|
transposase/IS protein; Provisional
Pssm-ID: 181681 Cd Length: 259 Bit Score: 501.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 1 MMELQHQRLMALAGQLQLESLISAAPALSQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFT 80
Cdd:PRK09183 1 MMELQHQRLMALCGQLQLESLISAAPALAQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 81 FATGAPQKQLQSLRSLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQR 160
Cdd:PRK09183 81 FATGAPQKQLQSLRSLSFIERNENIVLLGPSGVGKTHLAIALGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 161 GVMAPRLLIIDEIGYLPFSQEEAKLFFQVIAKRYEKSAMILTSNLPFGQWDQTFAGDAALTSAMLDRILHHSHVVQIKGE 240
Cdd:PRK09183 161 GVMAPRLLIIDEIGYLPFSQEEANLFFQVIAKRYEKGSMILTSNLPFGQWDQTFAGDAALTSAMLDRLLHHSHVVQIKGE 240
|
250
....*....|....*....
gi 807069027 241 SYRLRQKRKAGVIAEANPE 259
Cdd:PRK09183 241 SYRLKQKRKAGVIAEANPE 259
|
|
| IstB_IS21 |
pfam01695 |
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ... |
11-250 |
8.31e-132 |
|
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.
Pssm-ID: 426385 [Multi-domain] Cd Length: 238 Bit Score: 372.16 E-value: 8.31e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 11 ALAGQLQLESLISAAPALSQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFTFATGAPQKQL 90
Cdd:pfam01695 1 TQLKQLKLPGMAEAWEELSQQAASTSLSYEEFLEHLLEEELAWRDTRRLERLLRMAKLPPHKTLEDFDFTFAPGLDQRIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 91 QSLRSLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRgVMAPRLLII 170
Cdd:pfam01695 81 AELASLSFIDRAQNVVLLGPPGVGKTHLAIALGVEACRAGYSVRFTSAADLVNQLKRAHGDGKLTRKLQQ-LLKPDVLIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 171 DEIGYLPFSQEEAKLFFQVIAKRYEKSAMILTSNLPFGQWDQTFaGDAALTSAMLDRILHHSHVVQIKGESYRLRQKRKA 250
Cdd:pfam01695 160 DEWGYLPLDQAEANLLFQVISKRYEHRSIILTSNLPFGEWGQVF-GDAVLATAILDRLLHHCHIVPIKGESYRLKTKSEA 238
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
15-246 |
3.04e-122 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 347.54 E-value: 3.04e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 15 QLQLESLISAAPALSQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFTFATGAPQKQLQSLR 94
Cdd:NF038214 3 QLKLPGMARALEELAEQAAREELSFEEFLALLLEAELAERENRRIERRLKRARFPAAKTLEDFDFTAAPGLDKAQIRELA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 95 SLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRgVMAPRLLIIDEIG 174
Cdd:NF038214 83 TLDFIERAENVLLLGPPGTGKTHLAIALGYAACRQGYRVRFTTAADLVEQLAQARADGRLGRLLRR-LARYDLLIIDELG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807069027 175 YLPFSQEEAKLFFQVIAKRYEKSAMILTSNLPFGQWDQTFaGDAALTSAMLDRILHHSHVVQIKGESYRLRQ 246
Cdd:NF038214 162 YLPFSREGANLLFELIADRYERGSTIITSNLPFSEWGEVF-GDPTLAAAILDRLVHHAHILELKGESYRLKE 232
|
|
| DnaC |
COG1484 |
DNA replication protein DnaC [Replication, recombination and repair]; |
5-247 |
1.18e-108 |
|
DNA replication protein DnaC [Replication, recombination and repair];
Pssm-ID: 441093 [Multi-domain] Cd Length: 242 Bit Score: 313.64 E-value: 1.18e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 5 QHQRLMALAGQLQLESLISAAPALSQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFTFATG 84
Cdd:COG1484 2 LMEELKELLKALKLPGMAEALDELLAQAACDELSYEEFLALLLEAEVAEREQRRIERRLKAARFPAAKTLEDFDFDAQPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 85 APQKQLQSLRSLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRgVMA 164
Cdd:COG1484 82 LDRRQILELATLDFIERGENLILLGPPGTGKTHLAIALGHEACRAGYRVRFTTAPDLVNELKEARADGRLERLLKR-LAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 165 PRLLIIDEIGYLPFSQEEAKLFFQVIAKRYEKSAMILTSNLPFGQWDQTFaGDAALTSAMLDRILHHSHVVQIKGESYRL 244
Cdd:COG1484 161 VDLLILDELGYLPLDAEGAELLFELISDRYERRSTIITSNLPFSEWGEVF-GDPTLATAILDRLVHHAHIIELKGESYRL 239
|
...
gi 807069027 245 RQK 247
Cdd:COG1484 240 KEA 242
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
87-187 |
5.36e-12 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 62.16 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 87 QKQLQSLRSLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRGVMA-- 164
Cdd:cd00009 4 EEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEka 83
|
90 100
....*....|....*....|....
gi 807069027 165 -PRLLIIDEIGYLPFSQEEAKLFF 187
Cdd:cd00009 84 kPGVLFIDEIDSLSRGAQNALLRV 107
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
101-231 |
1.04e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 101 RNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTL--------QRGVMA------PR 166
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKasgsgelrLRLALAlarklkPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807069027 167 LLIIDEIGYLPFSQEEAKLFFQV------IAKRYEKSAMILTSNLPfgqwdqtFAGDAALTSAMLDRILHH 231
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEelrlllLLKSEKNLTVILTTNDE-------KDLGPALLRRRFDRRIVL 144
|
|
| DnaA |
TIGR00362 |
chromosomal replication initiator protein DnaA; DnaA is involved in DNA biosynthesis; ... |
109-203 |
3.23e-03 |
|
chromosomal replication initiator protein DnaA; DnaA is involved in DNA biosynthesis; initiation of chromosome replication and can also be transcription regulator. The C-terminal of the family hits the pfam bacterial DnaA (bac_dnaA) domain family. For a review, see Kaguni (2006). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273037 [Multi-domain] Cd Length: 437 Bit Score: 38.28 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 109 GPSGVGKTHLAIAMGYEAVR--AGIKVRFTTAADLLLQLSTAQRQGR---YKTTLqRGVmapRLLIIDEIGYL---PFSQ 180
Cdd:TIGR00362 144 GGVGLGKTHLLHAIGNEILEnnPNAKVLYVSSEKFTNDFVNALRNNKmeeFKEKY-RSV---DLLLIDDIQFLagkERTQ 219
|
90 100
....*....|....*....|....
gi 807069027 181 EEaklFFQVIAKRYEKS-AMILTS 203
Cdd:TIGR00362 220 EE---FFHTFNALHENNkQIVLTS 240
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09183 |
PRK09183 |
transposase/IS protein; Provisional |
1-259 |
0e+00 |
|
transposase/IS protein; Provisional
Pssm-ID: 181681 Cd Length: 259 Bit Score: 501.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 1 MMELQHQRLMALAGQLQLESLISAAPALSQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFT 80
Cdd:PRK09183 1 MMELQHQRLMALCGQLQLESLISAAPALAQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 81 FATGAPQKQLQSLRSLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQR 160
Cdd:PRK09183 81 FATGAPQKQLQSLRSLSFIERNENIVLLGPSGVGKTHLAIALGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 161 GVMAPRLLIIDEIGYLPFSQEEAKLFFQVIAKRYEKSAMILTSNLPFGQWDQTFAGDAALTSAMLDRILHHSHVVQIKGE 240
Cdd:PRK09183 161 GVMAPRLLIIDEIGYLPFSQEEANLFFQVIAKRYEKGSMILTSNLPFGQWDQTFAGDAALTSAMLDRLLHHSHVVQIKGE 240
|
250
....*....|....*....
gi 807069027 241 SYRLRQKRKAGVIAEANPE 259
Cdd:PRK09183 241 SYRLKQKRKAGVIAEANPE 259
|
|
| IstB_IS21 |
pfam01695 |
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ... |
11-250 |
8.31e-132 |
|
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.
Pssm-ID: 426385 [Multi-domain] Cd Length: 238 Bit Score: 372.16 E-value: 8.31e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 11 ALAGQLQLESLISAAPALSQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFTFATGAPQKQL 90
Cdd:pfam01695 1 TQLKQLKLPGMAEAWEELSQQAASTSLSYEEFLEHLLEEELAWRDTRRLERLLRMAKLPPHKTLEDFDFTFAPGLDQRIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 91 QSLRSLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRgVMAPRLLII 170
Cdd:pfam01695 81 AELASLSFIDRAQNVVLLGPPGVGKTHLAIALGVEACRAGYSVRFTSAADLVNQLKRAHGDGKLTRKLQQ-LLKPDVLIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 171 DEIGYLPFSQEEAKLFFQVIAKRYEKSAMILTSNLPFGQWDQTFaGDAALTSAMLDRILHHSHVVQIKGESYRLRQKRKA 250
Cdd:pfam01695 160 DEWGYLPLDQAEANLLFQVISKRYEHRSIILTSNLPFGEWGQVF-GDAVLATAILDRLLHHCHIVPIKGESYRLKTKSEA 238
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
15-246 |
3.04e-122 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 347.54 E-value: 3.04e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 15 QLQLESLISAAPALSQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFTFATGAPQKQLQSLR 94
Cdd:NF038214 3 QLKLPGMARALEELAEQAAREELSFEEFLALLLEAELAERENRRIERRLKRARFPAAKTLEDFDFTAAPGLDKAQIRELA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 95 SLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRgVMAPRLLIIDEIG 174
Cdd:NF038214 83 TLDFIERAENVLLLGPPGTGKTHLAIALGYAACRQGYRVRFTTAADLVEQLAQARADGRLGRLLRR-LARYDLLIIDELG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807069027 175 YLPFSQEEAKLFFQVIAKRYEKSAMILTSNLPFGQWDQTFaGDAALTSAMLDRILHHSHVVQIKGESYRLRQ 246
Cdd:NF038214 162 YLPFSREGANLLFELIADRYERGSTIITSNLPFSEWGEVF-GDPTLAAAILDRLVHHAHILELKGESYRLKE 232
|
|
| DnaC |
COG1484 |
DNA replication protein DnaC [Replication, recombination and repair]; |
5-247 |
1.18e-108 |
|
DNA replication protein DnaC [Replication, recombination and repair];
Pssm-ID: 441093 [Multi-domain] Cd Length: 242 Bit Score: 313.64 E-value: 1.18e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 5 QHQRLMALAGQLQLESLISAAPALSQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFTFATG 84
Cdd:COG1484 2 LMEELKELLKALKLPGMAEALDELLAQAACDELSYEEFLALLLEAEVAEREQRRIERRLKAARFPAAKTLEDFDFDAQPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 85 APQKQLQSLRSLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRgVMA 164
Cdd:COG1484 82 LDRRQILELATLDFIERGENLILLGPPGTGKTHLAIALGHEACRAGYRVRFTTAPDLVNELKEARADGRLERLLKR-LAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 165 PRLLIIDEIGYLPFSQEEAKLFFQVIAKRYEKSAMILTSNLPFGQWDQTFaGDAALTSAMLDRILHHSHVVQIKGESYRL 244
Cdd:COG1484 161 VDLLILDELGYLPLDAEGAELLFELISDRYERRSTIITSNLPFSEWGEVF-GDPTLATAILDRLVHHAHIIELKGESYRL 239
|
...
gi 807069027 245 RQK 247
Cdd:COG1484 240 KEA 242
|
|
| PRK06526 |
PRK06526 |
transposase; Provisional |
8-247 |
1.08e-71 |
|
transposase; Provisional
Pssm-ID: 180607 Cd Length: 254 Bit Score: 220.12 E-value: 1.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 8 RLMALAGQLQLESLISAAPALSQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFTFATGAPQ 87
Cdd:PRK06526 4 ELAYLTRALKAPTLAGAVERLAERARAESWSHEEFLAACLQREVAARESHGGEGRIRAARFPARKSLEEFDFDHQRSLKR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 88 KQLQSLRSLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRGVMAPrL 167
Cdd:PRK06526 84 DTIAHLGTLDFVTGKENVVFLGPPGTGKTHLAIGLGIRACQAGHRVLFATAAQWVARLAAAHHAGRLQAELVKLGRYP-L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 168 LIIDEIGYLPFSQEEAKLFFQVIAKRYEKSAMILTSNLPFGQWDQTFaGDAALTSAMLDRILHHSHVVQIKGESYRLRQK 247
Cdd:PRK06526 163 LIVDEVGYIPFEPEAANLFFQLVSSRYERASLIVTSNKPFGRWGEVF-GDDVVAAAMIDRLVHHAEVISLKGDSYRLKDR 241
|
|
| PRK08181 |
PRK08181 |
transposase; Validated |
8-251 |
8.15e-42 |
|
transposase; Validated
Pssm-ID: 136670 [Multi-domain] Cd Length: 269 Bit Score: 143.92 E-value: 8.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 8 RLMALAGQLQLESLISAAPALSQQAVDQEWSYMDFLEHLLHEEKLARHQRKQAMYTRMAAFPAVKTFEEYDFTFATGAPQ 87
Cdd:PRK08181 11 RLGLLLNELRLPTIKTLWPQFAEQADKEGWPAARFLAAIAEHELAERARRRIERHLAEAHLPPGKTLDSFDFEAVPMVSK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 88 KQLQSLRS-LSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRgVMAPR 166
Cdd:PRK08181 91 AQVMAIAAgDSWLAKGANLLLFGPPGGGKSHLAAAIGLALIENGWRVLFTRTTDLVQKLQVARRELQLESAIAK-LDKFD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 167 LLIIDEIGYLPFSQEEAKLFFQVIAKRYEKSAMILTSNLPFGQWDQTFAgDAALTSAMLDRILHHSHVVQIKGESYRLR- 245
Cdd:PRK08181 170 LLILDDLAYVTKDQAETSVLFELISARYERRSILITANQPFGEWNRVFP-DPAMTLAAVDRLVHHATIFEMNVESYRRRt 248
|
....*....
gi 807069027 246 ---QKRKAG 251
Cdd:PRK08181 249 aleRKRGPG 257
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
87-187 |
5.36e-12 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 62.16 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 87 QKQLQSLRSLSFIERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRGVMA-- 164
Cdd:cd00009 4 EEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEka 83
|
90 100
....*....|....*....|....
gi 807069027 165 -PRLLIIDEIGYLPFSQEEAKLFF 187
Cdd:cd00009 84 kPGVLFIDEIDSLSRGAQNALLRV 107
|
|
| PRK08116 |
PRK08116 |
hypothetical protein; Validated |
73-243 |
4.07e-10 |
|
hypothetical protein; Validated
Pssm-ID: 236153 [Multi-domain] Cd Length: 268 Bit Score: 58.49 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 73 TFEEYDFTfatGAPQKQLQSLRS--LSFIE-RNENIVLL--GPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLst 147
Cdd:PRK08116 83 TFENFLFD---KGSEKAYKIARKyvKKFEEmKKENVGLLlwGSVGTGKTYLAACIANELIEKGVPVIFVNFPQLLNRI-- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 148 aqrQGRYKTTLQ-------RGVMAPRLLIIDEIGY---LPFSQEEaklFFQVIAKRY-EKSAMILTSNLPFGQWDQTfag 216
Cdd:PRK08116 158 ---KSTYKSSGKedeneiiRSLVNADLLILDDLGAerdTEWAREK---VYNIIDSRYrKGLPTIVTTNLSLEELKNQ--- 228
|
170 180
....*....|....*....|....*..
gi 807069027 217 daaLTSAMLDRILHHSHVVQIKGESYR 243
Cdd:PRK08116 229 ---YGKRIYDRILEMCTPVENEGKSYR 252
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
101-231 |
1.04e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 101 RNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTL--------QRGVMA------PR 166
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKasgsgelrLRLALAlarklkPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807069027 167 LLIIDEIGYLPFSQEEAKLFFQV------IAKRYEKSAMILTSNLPfgqwdqtFAGDAALTSAMLDRILHH 231
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEelrlllLLKSEKNLTVILTTNDE-------KDLGPALLRRRFDRRIVL 144
|
|
| PRK06835 |
PRK06835 |
DNA replication protein DnaC; Validated |
94-251 |
4.90e-09 |
|
DNA replication protein DnaC; Validated
Pssm-ID: 235871 [Multi-domain] Cd Length: 329 Bit Score: 55.68 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 94 RSLSFIE----RNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTA----QRQGRYKTTLQRGVmap 165
Cdd:PRK06835 171 KCKNFIEnfdkNNENLLFYGNTGTGKTFLSNCIAKELLDRGKSVIYRTADELIEILREIrfnnDKELEEVYDLLINC--- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 166 RLLIIDEIGYLP---FSQEEaklFFQVIAKRYEKS-AMILTSNLPFGQWDQTFagdaalTSAMLDRILHHSHVVQIKGES 241
Cdd:PRK06835 248 DLLIIDDLGTEKiteFSKSE---LFNLINKRLLRQkKMIISTNLSLEELLKTY------SERISSRLLGNFTLLKFYGED 318
|
170
....*....|
gi 807069027 242 YRLRQKRKAG 251
Cdd:PRK06835 319 IRIKKNLQKK 328
|
|
| PRK12377 |
PRK12377 |
putative replication protein; Provisional |
104-193 |
7.28e-08 |
|
putative replication protein; Provisional
Pssm-ID: 183482 [Multi-domain] Cd Length: 248 Bit Score: 51.76 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 104 NIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRGVMAPRLLIIDEIGYLPFSQEEA 183
Cdd:PRK12377 103 NFVFSGKPGTGKNHLAAAIGNRLLAKGRSVIVVTVPDVMSRLHESYDNGQSGEKFLQELCKVDLLVLDEIGIQRETKNEQ 182
|
90
....*....|
gi 807069027 184 KLFFQVIAKR 193
Cdd:PRK12377 183 VVLNQIIDRR 192
|
|
| DnaA |
COG0593 |
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair]; |
105-211 |
1.85e-06 |
|
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
Pssm-ID: 440358 [Multi-domain] Cd Length: 303 Bit Score: 47.88 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 105 IVLLGPSGVGKTHLAIAMGYEAVRA--GIKVRFTTAADLLLQLSTAQRQGRyKTTLQRGVMAPRLLIIDEIGYL---PFS 179
Cdd:COG0593 37 LFLYGGVGLGKTHLLHAIGNEALENnpGARVVYLTAEEFTNDFINAIRNNT-IEEFKEKYRSVDVLLIDDIQFLagkEAT 115
|
90 100 110
....*....|....*....|....*....|...
gi 807069027 180 QEEaklFFQVI-AKRYEKSAMILTSNLPFGQWD 211
Cdd:COG0593 116 QEE---FFHTFnALREAGKQIVLTSDRPPKELP 145
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
93-201 |
2.94e-06 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 46.08 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 93 LRSLSF-IERNENIVLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAAD-------------LLLQLSTAQRQgryKTTL 158
Cdd:cd00267 15 LDNVSLtLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaklpleelrrrigYVPQLSGGQRQ---RVAL 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 807069027 159 QRGVM-APRLLIIDEigylPFS---QEEAKLFFQVIAKRYEKSAMIL 201
Cdd:cd00267 92 ARALLlNPDLLLLDE----PTSgldPASRERLLELLRELAEEGRTVI 134
|
|
| PRK07952 |
PRK07952 |
DNA replication protein DnaC; Validated |
100-250 |
2.58e-05 |
|
DNA replication protein DnaC; Validated
Pssm-ID: 181180 [Multi-domain] Cd Length: 244 Bit Score: 44.37 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 100 ERNENI---VLLGPSGVGKTHLAIAMGYEAVRAGIKVRFTTAADLLLQL-STAQRQGRYKTTLQRGVMAPRLLIIDEIGY 175
Cdd:PRK07952 94 EFDGNIasfIFSGKPGTGKNHLAAAICNELLLRGKSVLIITVADIMSAMkDTFSNSETSEEQLLNDLSNVDLLVIDEIGV 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807069027 176 LPFSQEEAKLFFQVIAKR--YEKSAMILTsnlpfgqwDQTFAG-DAALTSAMLDRI-LHHSHVVQIKGESYRLRQKRKA 250
Cdd:PRK07952 174 QTESRYEKVIINQIVDRRssSKRPTGMLT--------NSNMEEmTKLLGERVMDRMrLGNSLWVIFNWDSYRSRVTGKE 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
93-192 |
2.39e-04 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 40.49 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 93 LRSLSF-IERNENIVLLGPSGVGKTHLA-IAMGYEAVRAG------IKVRFTTAAD-------LLLQLSTAQRQgryKTT 157
Cdd:cd03216 16 LDGVSLsVRRGEVHALLGENGAGKSTLMkILSGLYKPDSGeilvdgKEVSFASPRDarragiaMVYQLSVGERQ---MVE 92
|
90 100 110
....*....|....*....|....*....|....*....
gi 807069027 158 LQRGVM-APRLLIIDEigylP---FSQEEAKLFFQVIAK 192
Cdd:cd03216 93 IARALArNARLLILDE----PtaaLTPAEVERLFKVIRR 127
|
|
| PhoH |
pfam02562 |
PhoH-like protein; PhoH is a cytoplasmic protein and predicted ATPase that is induced by ... |
99-134 |
5.79e-04 |
|
PhoH-like protein; PhoH is a cytoplasmic protein and predicted ATPase that is induced by phosphate starvation.
Pssm-ID: 460592 [Multi-domain] Cd Length: 204 Bit Score: 39.77 E-value: 5.79e-04
10 20 30
....*....|....*....|....*....|....*.
gi 807069027 99 IERNENIVLLGPSGVGKTHLAIAMGYEAVRAGiKVR 134
Cdd:pfam02562 15 IKKNDIVFGIGPAGTGKTYLAVAMAVDALKNG-KVK 49
|
|
| COG4930 |
COG4930 |
Predicted ATP-dependent Lon-type protease [Posttranslational modification, protein turnover, ... |
87-118 |
1.00e-03 |
|
Predicted ATP-dependent Lon-type protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443958 [Multi-domain] Cd Length: 672 Bit Score: 40.25 E-value: 1.00e-03
10 20 30
....*....|....*....|....*....|..
gi 807069027 87 QKQLQSLRSLSFIERNENIVLLGPSGVGKTHL 118
Cdd:COG4930 201 QKLLLLLRLIPFVERNYNLVELGPRGTGKSHV 232
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
105-187 |
1.08e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 105 IVLLGPSGVGKTHLA--IAMGYEAVRAG-IKVR---FTTAADLL--------LQLSTAQRQGRYKTTLQRGV---MAPRL 167
Cdd:pfam13401 8 LVLTGESGTGKTTLLrrLLEQLPEVRDSvVFVDlpsGTSPKDLLrallralgLPLSGRLSKEELLAALQQLLlalAVAVV 87
|
90 100
....*....|....*....|.
gi 807069027 168 LIIDEIGYLPFSQ-EEAKLFF 187
Cdd:pfam13401 88 LIIDEAQHLSLEAlEELRDLL 108
|
|
| DnaA |
TIGR00362 |
chromosomal replication initiator protein DnaA; DnaA is involved in DNA biosynthesis; ... |
109-203 |
3.23e-03 |
|
chromosomal replication initiator protein DnaA; DnaA is involved in DNA biosynthesis; initiation of chromosome replication and can also be transcription regulator. The C-terminal of the family hits the pfam bacterial DnaA (bac_dnaA) domain family. For a review, see Kaguni (2006). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273037 [Multi-domain] Cd Length: 437 Bit Score: 38.28 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 109 GPSGVGKTHLAIAMGYEAVR--AGIKVRFTTAADLLLQLSTAQRQGR---YKTTLqRGVmapRLLIIDEIGYL---PFSQ 180
Cdd:TIGR00362 144 GGVGLGKTHLLHAIGNEILEnnPNAKVLYVSSEKFTNDFVNALRNNKmeeFKEKY-RSV---DLLLIDDIQFLagkERTQ 219
|
90 100
....*....|....*....|....
gi 807069027 181 EEaklFFQVIAKRYEKS-AMILTS 203
Cdd:TIGR00362 220 EE---FFHTFNALHENNkQIVLTS 240
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
104-173 |
3.97e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 38.21 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 104 NIVLLGPSGVGKTHLAIA-----MGYEAVRagikVRFTTA------ADLLLQLSTAQRQGRYKttLQRGVMA-------- 164
Cdd:COG1401 223 NVILAGPPGTGKTYLARRlaealGGEDNGR----IEFVQFhpswsyEDFLLGYRPSLDEGKYE--PTPGIFLrfclkaek 296
|
90
....*....|...
gi 807069027 165 ----PRLLIIDEI 173
Cdd:COG1401 297 npdkPYVLIIDEI 309
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
80-153 |
3.99e-03 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 37.49 E-value: 3.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807069027 80 TFATGapQKQLQSLRSLSF-IERNENIVLLGPSGVGKTHLA-IAMGYEAVRAGiKVRFttAADLLLQLSTAQRQGR 153
Cdd:cd03257 10 SFPTG--GGSVKALDDVSFsIKKGETLGLVGESGSGKSTLArAILGLLKPTSG-SIIF--DGKDLLKLSRRLRKIR 80
|
|
| dnaA |
PRK00149 |
chromosomal replication initiator protein DnaA; |
107-206 |
4.12e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 234667 [Multi-domain] Cd Length: 401 Bit Score: 38.19 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 107 LLGPSGVGKTHLAIAMGYEAVRA--GIKVRFTTAADLLLQLSTAQRQG-------RYkttlqRGVmapRLLIIDEIGYL- 176
Cdd:PRK00149 104 IYGGVGLGKTHLLHAIGNYILEKnpNAKVVYVTSEKFTNDFVNALRNNtmeefkeKY-----RSV---DVLLIDDIQFLa 175
|
90 100 110
....*....|....*....|....*....|...
gi 807069027 177 --PFSQEEaklFFQVIAKRYEKSA-MILTSNLP 206
Cdd:PRK00149 176 gkERTQEE---FFHTFNALHEAGKqIVLTSDRP 205
|
|
| Bac_DnaA |
pfam00308 |
Bacterial dnaA protein; |
109-187 |
5.69e-03 |
|
Bacterial dnaA protein;
Pssm-ID: 278724 [Multi-domain] Cd Length: 219 Bit Score: 36.92 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 109 GPSGVGKTHLAIAMGYEAVR--AGIKVRFTTAADLLLQLSTAQRQGRyKTTLQRGVMAPRLLIIDEIGYLPF---SQEEa 183
Cdd:pfam00308 41 GGVGLGKTHLLHAIGNYALQnaPNLRVVYLTAEEFLNDFVDAIRDNK-TNQFKEKYRNVDVLLIDDIQFLAGkegTQEE- 118
|
....
gi 807069027 184 klFF 187
Cdd:pfam00308 119 --FF 120
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
104-181 |
6.36e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 37.19 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807069027 104 NIVLLGPSGVGKTHLAIAMGYEA---VRAGIKVRFTTAADlllqlSTAQRQgRYKTTLQRGVmAP------RLLIIDEIG 174
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATgaiDRLGRVEDGNTVSD-----YDPEEK-KRKMSIETSV-APlewnghKINLIDTPG 73
|
....*..
gi 807069027 175 YLPFSQE 181
Cdd:cd04170 74 YADFVGE 80
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
109-133 |
6.60e-03 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 36.76 E-value: 6.60e-03
10 20
....*....|....*....|....*
gi 807069027 109 GPSGVGKTHLAIAMGYEAVRAGIKV 133
Cdd:PRK09361 30 GPPGSGKTNICLQLAVEAAKNGKKV 54
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
93-130 |
9.45e-03 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 37.00 E-value: 9.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 807069027 93 LRSLSF-IERNENIVLLGPSGVGKTHL--AIAmGYEAVRAG 130
Cdd:COG3842 21 LDDVSLsIEPGEFVALLGPSGCGKTTLlrMIA-GFETPDSG 60
|
|
| |
