|
Name |
Accession |
Description |
Interval |
E-value |
| SpoIIIAA |
COG3854 |
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ... |
6-284 |
9.93e-112 |
|
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443063 Cd Length: 309 Bit Score: 331.34 E-value: 9.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 6 DFEKLIENLPFFLQQTLKKHRYH--DQMIEIVLDLGRRPEARFTYGPEYLSQ-KIISWQDIDFVTKHLSKFS-----NE- 76
Cdd:COG3854 1 DLEEILAILPPTIREALEKLPDPvlDKLEEIRLRLGRPLELRFPGGEYFLSEaYPVTREDLERTLNRISNYSlyaleEEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 77 ----------NRAGIERTLHRISCIRNRQFLINGLTCRIGRSIFGTVSVIRDLLESEKSM---LILGKPGVGKTTIIREI 143
Cdd:COG3854 81 rqgyitipggHRVGIAGTVVRESGIVKRIKDISGLNIRIAREVKGTADPILPYIISGGRIyntLIISPPGCGKTTLLRDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 144 GRVLANEME----KRVVIIDTSNEIGGDS-DITHSGIGRarRMQVPKTELQHQVMIEAVENHMPQVIIIDEIGTELEVLA 218
Cdd:COG3854 161 ARVLSDGLLgfpgKRVGVVDERSEIAGCYgGIPQPDIGI--RTDVLDGCPKAEGMIMAIRSMSPEVIVVDEIGREEDAEA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127877510 219 ARTIAEKGVQLIGTTHGNCLENLIKNPPLSDLIGGI---QYVTLSDDEAkrRGTQKSILERKAYPAFEI 284
Cdd:COG3854 239 LREAANAGVQLIATAHGNSLEDLLKRPTLSDLIGGGvfeRYVTLSRREG--PGTVETILDRKADVLVEM 305
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
120-244 |
1.59e-10 |
|
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: 59.08 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 120 LESEKSMLILGKPGVGKTTIIREIGRvLANEMEKRVVIIDTSNEIGGDSDITHSGIGRARRMQvpktelqhqvmiEAVEN 199
Cdd:cd00009 16 LPPPKNLLLYGPPGTGKTTLARAIAN-ELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF------------ELAEK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2127877510 200 HMPQVIIIDEIGT-----------ELEVLAARTIAEKGVQLIGTTHGNCLENLIKN 244
Cdd:cd00009 83 AKPGVLFIDEIDSlsrgaqnallrVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
|
|
| Spore_III_AA |
pfam19568 |
Sporulation stage III, protein AA; |
91-251 |
9.69e-10 |
|
Sporulation stage III, protein AA;
Pssm-ID: 437400 Cd Length: 306 Bit Score: 59.42 E-value: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 91 IRNRQFlINGLTCRIGRSIFGTV-SVIRDLLESE--KSMLILGKPGVGKTTIIREIGRVLANEMEKR----VVIIDTSNE 163
Cdd:pfam19568 110 IKNIQY-ISSLNIRLAHEVRGCAdGVMPYIWCNEevRHTLIISPPRCGKTTLLRDMIRQISDGNQYVpgvtVGVVDERSE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 164 IGGdsdiTHSGIGR---ARRMQV----PKTElqhqVMIEAVENHMPQVIIIDEIGTELEVLAARTIAEKGVQLIGTTHGN 236
Cdd:pfam19568 189 LGA----CYLGVPQndlGRRTDIldccPKAE----GMIMLIRSMSPTVVAVDEIGGQEDIEALEYAMNCGCTIIATVHGA 260
|
170
....*....|....*
gi 2127877510 237 CLENLIKNPPLSDLI 251
Cdd:pfam19568 261 CMEDISNRPVLRRLI 275
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
124-234 |
1.33e-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: 56.61 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 124 KSMLILGKPGVGKTTIIREIGRvLANEMEKRVVIIDTSNEIGGDSDItHSGIGRARRMQVPKTELQHQVMIEAVENHMPQ 203
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALAR-ELGPPGGGVIYIDGEDILEEVLDQ-LLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2127877510 204 VIIIDEIGT-------------ELEVLAARTIAEKGVQLIGTTH 234
Cdd:smart00382 81 VLILDEITSlldaeqealllllEELRLLLLLKSEKNLTVILTTN 124
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
109-210 |
2.70e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 43.15 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 109 IFGTVSVIRDLLESEK--SMLILGKPGVGKTTIIreigRVLANEMEKRVVIIDTSNeiggdsdithSGIgrarrmqvpkT 186
Cdd:PRK13342 20 LLGPGKPLRRMIEAGRlsSMILWGPPGTGKTTLA----RIIAGATDAPFEALSAVT----------SGV----------K 75
|
90 100
....*....|....*....|....*..
gi 2127877510 187 ELQhQVMIEAVENHMPQ---VIIIDEI 210
Cdd:PRK13342 76 DLR-EVIEEARQRRSAGrrtILFIDEI 101
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SpoIIIAA |
COG3854 |
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ... |
6-284 |
9.93e-112 |
|
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443063 Cd Length: 309 Bit Score: 331.34 E-value: 9.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 6 DFEKLIENLPFFLQQTLKKHRYH--DQMIEIVLDLGRRPEARFTYGPEYLSQ-KIISWQDIDFVTKHLSKFS-----NE- 76
Cdd:COG3854 1 DLEEILAILPPTIREALEKLPDPvlDKLEEIRLRLGRPLELRFPGGEYFLSEaYPVTREDLERTLNRISNYSlyaleEEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 77 ----------NRAGIERTLHRISCIRNRQFLINGLTCRIGRSIFGTVSVIRDLLESEKSM---LILGKPGVGKTTIIREI 143
Cdd:COG3854 81 rqgyitipggHRVGIAGTVVRESGIVKRIKDISGLNIRIAREVKGTADPILPYIISGGRIyntLIISPPGCGKTTLLRDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 144 GRVLANEME----KRVVIIDTSNEIGGDS-DITHSGIGRarRMQVPKTELQHQVMIEAVENHMPQVIIIDEIGTELEVLA 218
Cdd:COG3854 161 ARVLSDGLLgfpgKRVGVVDERSEIAGCYgGIPQPDIGI--RTDVLDGCPKAEGMIMAIRSMSPEVIVVDEIGREEDAEA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127877510 219 ARTIAEKGVQLIGTTHGNCLENLIKNPPLSDLIGGI---QYVTLSDDEAkrRGTQKSILERKAYPAFEI 284
Cdd:COG3854 239 LREAANAGVQLIATAHGNSLEDLLKRPTLSDLIGGGvfeRYVTLSRREG--PGTVETILDRKADVLVEM 305
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
120-244 |
1.59e-10 |
|
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: 59.08 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 120 LESEKSMLILGKPGVGKTTIIREIGRvLANEMEKRVVIIDTSNEIGGDSDITHSGIGRARRMQvpktelqhqvmiEAVEN 199
Cdd:cd00009 16 LPPPKNLLLYGPPGTGKTTLARAIAN-ELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF------------ELAEK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2127877510 200 HMPQVIIIDEIGT-----------ELEVLAARTIAEKGVQLIGTTHGNCLENLIKN 244
Cdd:cd00009 83 AKPGVLFIDEIDSlsrgaqnallrVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
|
|
| Spore_III_AA |
pfam19568 |
Sporulation stage III, protein AA; |
91-251 |
9.69e-10 |
|
Sporulation stage III, protein AA;
Pssm-ID: 437400 Cd Length: 306 Bit Score: 59.42 E-value: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 91 IRNRQFlINGLTCRIGRSIFGTV-SVIRDLLESE--KSMLILGKPGVGKTTIIREIGRVLANEMEKR----VVIIDTSNE 163
Cdd:pfam19568 110 IKNIQY-ISSLNIRLAHEVRGCAdGVMPYIWCNEevRHTLIISPPRCGKTTLLRDMIRQISDGNQYVpgvtVGVVDERSE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 164 IGGdsdiTHSGIGR---ARRMQV----PKTElqhqVMIEAVENHMPQVIIIDEIGTELEVLAARTIAEKGVQLIGTTHGN 236
Cdd:pfam19568 189 LGA----CYLGVPQndlGRRTDIldccPKAE----GMIMLIRSMSPTVVAVDEIGGQEDIEALEYAMNCGCTIIATVHGA 260
|
170
....*....|....*
gi 2127877510 237 CLENLIKNPPLSDLI 251
Cdd:pfam19568 261 CMEDISNRPVLRRLI 275
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
124-234 |
1.33e-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: 56.61 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 124 KSMLILGKPGVGKTTIIREIGRvLANEMEKRVVIIDTSNEIGGDSDItHSGIGRARRMQVPKTELQHQVMIEAVENHMPQ 203
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALAR-ELGPPGGGVIYIDGEDILEEVLDQ-LLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2127877510 204 VIIIDEIGT-------------ELEVLAARTIAEKGVQLIGTTH 234
Cdd:smart00382 81 VLILDEITSlldaeqealllllEELRLLLLLKSEKNLTVILTTN 124
|
|
| NTPase_1 |
pfam03266 |
NTPase; This domain is found across all species from bacteria to human, and the function was ... |
127-234 |
8.68e-06 |
|
NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.
Pssm-ID: 460869 Cd Length: 168 Bit Score: 45.70 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 127 LILGKPGVGKTTIIREIGRVLAN--------------EMEKRV--VIIDTSNEIGGdsdiTHSGIGRARRMQVPK----T 186
Cdd:pfam03266 3 FITGPPGVGKTTLVLKVAELLKSsgvkvggfytpevrEGGRRIgfKIVDLASGEEG----WLARVGAVSGPRVGKyvvnV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2127877510 187 ELQHQVMIEAVENHM--PQVIIIDEIGT-ELEVL----AARTIAEKGVQLIGTTH 234
Cdd:pfam03266 79 ESFEEIAVPALRRALeeADLIIIDEIGPmELKSKkfreAVREVLDSGKPVLAVIH 133
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
121-234 |
2.81e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 43.48 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 121 ESEKSMLILGKPGVGKTTIIREIGRvLANEMEKRVVIIDTSNEIGGDSDITH--SGIGRARRMQVPKTELQHQVMIEAVE 198
Cdd:pfam13401 3 FGAGILVLTGESGTGKTTLLRRLLE-QLPEVRDSVVFVDLPSGTSPKDLLRAllRALGLPLSGRLSKEELLAALQQLLLA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2127877510 199 NHMPQVIIIDEI----GTELEVLAART-IAEKGVQ--LIGTTH 234
Cdd:pfam13401 82 LAVAVVLIIDEAqhlsLEALEELRDLLnLSSKLLQliLVGTPE 124
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
113-210 |
5.56e-05 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 45.22 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 113 VSVIRDLLESEKS--MLILGKPGVGKTTIIREIGRVLANEMEKRVV----------IIDTS--------NEIGGDSDITH 172
Cdd:COG1474 39 ASALRPALRGERPsnVLIYGPTGTGKTAVAKYVLEELEEEAEERGVdvrvvyvncrQASTRyrvlsrilEELGSGEDIPS 118
|
90 100 110
....*....|....*....|....*....|....*...
gi 2127877510 173 SGIGRArrmqvpktELQHQVMIEAVENHMPQVIIIDEI 210
Cdd:COG1474 119 TGLSTD--------ELFDRLYEALDERDGVLVVVLDEI 148
|
|
| DEXSc_Pif1_like |
cd18037 |
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ... |
118-230 |
6.28e-05 |
|
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350795 [Multi-domain] Cd Length: 183 Bit Score: 43.78 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 118 DLLESEKSMLILGKPGVGKTTIIREIGRVLaNEMEKRVVIIDT----SNEIGGdsdIT-HS--GIGrarRMQVPKTELQH 190
Cdd:cd18037 7 DLVLDGKNVFFTGSAGTGKSYLLRRIIRAL-PSRPKRVAVTAStgiaACNIGG---TTlHSfaGIG---LGSEPAEDLLE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2127877510 191 QVMIE-AVENH--MPQVIIIDEIG-------TELEvLAARTIAEK-----GVQLI 230
Cdd:cd18037 80 RVKRSpYLVQRwrKCDVLIIDEISmldadlfDKLD-RVAREVRGSdkpfgGIQLI 133
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
126-210 |
8.07e-05 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 42.20 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 126 MLILGKPGVGKTTIIREIgrvlANEMEKRVVIIDtsneiGGDSDITHSGIGRARrmqvpkteLQHqvMIEAVENHMPQVI 205
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAV----AKELGAPFIEIS-----GSELVSKYVGESEKR--------LRE--LFEAAKKLAPCVI 61
|
....*
gi 2127877510 206 IIDEI 210
Cdd:pfam00004 62 FIDEI 66
|
|
| RecA-like_Thep1 |
cd19482 |
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ... |
127-251 |
8.64e-05 |
|
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the THEP1 family ATPase domain. It includes nucleoside-triphosphatase THEP 1 from Aquifex aeolicus (aaTHEP1) a nucleoside-phosphatase, with activity towards ATP, GTP, CTP, TTP and UTP; and which may hydrolyze nucleoside diphosphates with lower efficiency. The catalytic function of aaTHEP1 remains unclear, it may be a DNA/RNA modifying enzyme. Human THEP1 (hsTHEP1) may have a general function in many human tissues, as it is widely expressed in most examined tissues (such as in brain, heart, lymph node, skin, pancreas); it is especially highly expressed in embryonic and various tumor tissues. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410890 [Multi-domain] Cd Length: 164 Bit Score: 42.97 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 127 LILGKPGVGKTTIIREIGRVLAN--------------EMEKRV--VIIDTSNeigGDSDI-THSGIGRARRMQVPK-TEL 188
Cdd:cd19482 2 FITGPPGVGKTTLVLKVAELLKEsglkvggfytpevrEGGKRIgfKIVDLAS---GERGWlARVGAGSPKVGKYGVdVDE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 189 QHQVMIEAVENHM--PQVIIIDEIG-TEL---EVLAA-RTIAEKGVQLIGTTHGNCLENLIKNPPLSDLI 251
Cdd:cd19482 79 LEEIAVPALRRALeeADVIIIDEIGpMELkspKFREAvEEVLKSDKPLLATVHRRSYPRLAEIRGLGEVF 148
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
116-230 |
1.12e-04 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 44.58 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 116 IRDLLESEKSMLILGKPGVGKTTIIREIgRVLANEMEKRVVI--------IDTSNEIGGDSDITHSGIGRARRMQVPKTE 187
Cdd:COG0507 133 VALALTTRRVSVLTGGAGTGKTTTLRAL-LAALEALGLRVALaaptgkaaKRLSESTGIEARTIHRLLGLRPDSGRFRHN 211
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2127877510 188 LQHQVmieavenHMPQVIIIDE---IGTEL--EVLAArtIAEKGVQLI 230
Cdd:COG0507 212 RDNPL-------TPADLLVVDEasmVDTRLmaALLEA--LPRAGARLI 250
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
127-215 |
2.08e-04 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 40.87 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 127 LILGKPGVGKTTIIREigrvLANEMEKRVVIIDTSNEIGGDSDITHsGIGRARRMQVPKTELQHQVMIEAVENHMPQVII 206
Cdd:pfam13238 2 LITGTPGVGKTTLAKE----LSKRLGFGDNVRDLALENGLVLGDDP-ETRESKRLDEDKLDRLLDLLEENAALEEGGNLI 76
|
....*....
gi 2127877510 207 IDEIGTELE 215
Cdd:pfam13238 77 IDGHLAELE 85
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
109-210 |
2.70e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 43.15 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 109 IFGTVSVIRDLLESEK--SMLILGKPGVGKTTIIreigRVLANEMEKRVVIIDTSNeiggdsdithSGIgrarrmqvpkT 186
Cdd:PRK13342 20 LLGPGKPLRRMIEAGRlsSMILWGPPGTGKTTLA----RIIAGATDAPFEALSAVT----------SGV----------K 75
|
90 100
....*....|....*....|....*..
gi 2127877510 187 ELQhQVMIEAVENHMPQ---VIIIDEI 210
Cdd:PRK13342 76 DLR-EVIEEARQRRSAGrrtILFIDEI 101
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
125-210 |
3.79e-04 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 40.35 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 125 SMLILGKPGVGKTTIIREIGRVLANemekrvviiDTSNEIGGDSDITHSGIGRARRMQVPKTELQHQVMIEAVENhmPQV 204
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSN---------RPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAARE--GEI 69
|
....*.
gi 2127877510 205 IIIDEI 210
Cdd:pfam07728 70 AVLDEI 75
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
124-310 |
7.80e-04 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 41.44 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 124 KSMLILGKPGVGKTTIIreigRVLANEMEKRVVIIDTsneiggdSDITHSGIGrarrmqvpKTELQHQVMIEAVENHMPQ 203
Cdd:COG0464 192 RGLLLYGPPGTGKTLLA----RALAGELGLPLIEVDL-------SDLVSKYVG--------ETEKNLREVFDKARGLAPC 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 204 VIIIDEI-------GTELEVLAARTIAE---------KGVQLIGTThgncleNLIKNpplsdliggiqyvtlSDDEAKRR 267
Cdd:COG0464 253 VLFIDEAdalagkrGEVGDGVGRRVVNTlltemeelrSDVVVIAAT------NRPDL---------------LDPALLRR 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2127877510 268 gtqksilerkaypaFEIIIEINHPN------IWTIH-ENVAISADLFLRK 310
Cdd:COG0464 312 --------------FDEIIFFPLPDaeerleIFRIHlRKRPLDEDVDLEE 347
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
127-212 |
1.26e-03 |
|
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.
Pssm-ID: 410866 [Multi-domain] Cd Length: 268 Bit Score: 40.59 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 127 LILGKPGVGKTTIIREIGRVLANEmEKRVVII---DTSNEIGgdsdithsgiGRARRMQVPK--------TELQHqvMIE 195
Cdd:cd01121 86 LIGGDPGIGKSTLLLQVAARLAQR-GGKVLYVsgeESLSQIK----------LRAERLGLGSdnlyllaeTNLEA--ILA 152
|
90
....*....|....*..
gi 2127877510 196 AVENHMPQVIIIDEIGT 212
Cdd:cd01121 153 EIEELKPSLVVIDSIQT 169
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
122-211 |
1.72e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 39.62 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 122 SEKSMLILGKPGVGKTTIIREIGRVLanemekrvvIIDTSneiGGDSDIthsgigRARRMQVPKTELQHQVMIEAV---- 197
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTLPKPL---------FLDTE---KGSKAL------DGDRFPDIVIRDSWQDFLDAIdelt 62
|
90
....*....|....*.
gi 2127877510 198 --ENHMPQVIIIDEIG 211
Cdd:pfam13479 63 aaELADYKTIVIDTVD 78
|
|
| COG2842 |
COG2842 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
114-304 |
2.41e-03 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 39.55 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 114 SVIRDLLESEKSMLILGKPGVGKTTIIREigrvLANEMeKRVVII-----DTSNEIggdsditHSGIGRARRMQVPKT-- 186
Cdd:COG2842 41 EALDEARALPGIGVVYGESGVGKTTAARE----YANRN-PNVIYVtaspsWTSKEL-------LEELAEELGIPAPPGti 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127877510 187 -ELQHQVmIEAVENHmPQVIIIDE-----IGTeLEVLaaRTIAEK---GVQLIGTthGNCLENLIKNPPLSDLIG-GIQY 256
Cdd:COG2842 109 aDLRDRI-LERLAGT-GRLLIIDEadhlkPKA-LEEL--RDIHDEtgvGVVLIGM--ERLPAKLKRYEQLYSRIGfWVEF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2127877510 257 VTLSDDEAKRRGTQKSILERKAypAFEIIIEINHPNIWTIHENVAISA 304
Cdd:COG2842 182 KPLSLEDVRALAEAWGELTDPD--LLELLHRITRGNLRRLDRTLRLAA 227
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
97-159 |
4.44e-03 |
|
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440255 [Multi-domain] Cd Length: 289 Bit Score: 39.01 E-value: 4.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127877510 97 LINGLTCRIGRSIFGTVSVIRDLLESEKSMLIL---GKPGVGKTTIIREIGRVLAnEMEKRVVIID 159
Cdd:COG0489 64 LLLLGLLLLLLLALALLLLLLLLLLRLLLEVIAvtsGKGGEGKSTVAANLALALA-QSGKRVLLID 128
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
123-158 |
6.32e-03 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 36.81 E-value: 6.32e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2127877510 123 EKSMLILGKPGVGKTTIIREIGRVLA--NEMEKRVVII 158
Cdd:pfam13245 11 SKVVLLTGGPGTGKTTTIRHIVALLValGGVSFPILLA 48
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
110-150 |
6.34e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.02 E-value: 6.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2127877510 110 FGTVSVIRDLLESEKSMLILGKPGVGKTTIIREIGRVLANE 150
Cdd:COG5635 167 IESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAER 207
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
130-188 |
9.04e-03 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 35.87 E-value: 9.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127877510 130 GKPGVGKTTIIREIGRVLAnEMEKRVVIIDTSN----EIGGDSDITHSGIGRARRMQVPKTEL 188
Cdd:cd01983 8 GKGGVGKTTLAAALAVALA-AKGYKVLLIDLDDyvliDGGGGLETGLLLGTIVALLALKKADE 69
|
|
| |
