|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
7-361 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 581.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 7 QDTAAQIISALREFDIEAKVTGRTDGPSVTRYEIALGPGVRIQKVSQLQSQLAYALATESVRVVAPIPGKTAVGIELPRS 86
Cdd:COG1674 159 EENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 87 ERQTVRLQQIVP-----EDDHPLTVAVGKDVEGKDVSLNLAKMPHLLVAGATGSGKSSFINSMLVSMLYRANPDRVKLIM 161
Cdd:COG1674 239 KRETVYLREVLEsdefqNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLIL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 162 IDPKMVELTPYNGIPHLLQPVVTEPDEAVKTLRWLTVEMDDRYRQMQEAGVRH----------AEKLG--------LPYI 223
Cdd:COG1674 319 IDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNiagynekvreAKAKGeeeeglepLPYI 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 224 VVVVDELADLMMgGYKKEVEANIVRIAQKARAAGIHLVLATQRPSVDVVTGLIKSNVPSRLSFATASLTDSRVILDEGGA 303
Cdd:COG1674 399 VVIIDELADLMM-VAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGA 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971751354 304 EQLMGMGDGLFLPVGARGAIRIQGAFVSDGEIEAAVNNVR----------VTARVEEKVRELNPEPED 361
Cdd:COG1674 478 EKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKsqgepeyieeILEEEEEEDEGGDDDEDD 545
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
2-347 |
2.72e-124 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 391.76 E-value: 2.72e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 2 TTMLEQdtAAQIISA-LREFDIEAKVTGRTDGPSVTRYEIALGPGVRIQKVSQLQSQLAYALATESVRVVAPIPGKTAVG 80
Cdd:PRK10263 884 TFALEQ--MARLVEArLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVG 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 81 IELPRSERQTVRLQQIVP-----EDDHPLTVAVGKDVEGKDVSLNLAKMPHLLVAGATGSGKSSFINSMLVSMLYRANPD 155
Cdd:PRK10263 962 LELPNKKRQTVYLREVLDnakfrDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPE 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 156 RVKLIMIDPKMVELTPYNGIPHLLQPVVTEPDEAVKTLRWLTVEMDDRYRQMQEAGVRH----------AEKLG------ 219
Cdd:PRK10263 1042 DVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNlagynekiaeADRMMrpipdp 1121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 220 -----------------LPYIVVVVDELADLMMGGYKKeVEANIVRIAQKARAAGIHLVLATQRPSVDVVTGLIKSNVPS 282
Cdd:PRK10263 1122 ywkpgdsmdaqhpvlkkEPYIVVLVDEFADLMMTVGKK-VEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPT 1200
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971751354 283 RLSFATASLTDSRVILDEGGAEQLMGMGDGLFLPVGARGAIRIQGAFVSDGEIEAAVNNVRVTAR 347
Cdd:PRK10263 1201 RIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGR 1265
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
100-268 |
4.40e-58 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 190.28 E-value: 4.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 100 DDHPLTVAVGKDVEGKDVSLNLAKMP-HLLVAGATGSGKSSFINSMLVSMLYRANPDRVKLIMIDPKMVELTPYNGIPHL 178
Cdd:pfam01580 13 DYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 179 L-QPVVTEPDEAVKTLRWLTVEMDDRYRQMQEAGVR---------------------------------HAEKLGLPYIV 224
Cdd:pfam01580 93 LsVPVATDPKRALRALEWLVDEMERRYALFRALGVRsiagyngeiaedpldgfgdvflviygvhvmctaGRWLEILPYLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 971751354 225 VVVDELADLMMGGYKKE---VEANIVRIAQKARAAGIHLVLATQRPS 268
Cdd:pfam01580 173 VIVDERAELRLAAPKDSemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
104-298 |
3.19e-23 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 103.14 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 104 LTVAVGkdVEGKD--VSLNL---AKMPHLLVAGATGSGKSSFINSMLVSMLYRANPDRVKLIMIDPK---MVEltPYNGI 175
Cdd:TIGR03928 446 LAVPIG--LRGKDdiVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMAN--LFKNL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 176 PHLLQpVVTEPDEAvKTLRWLT---VEMDDRYRQMQEAGVRHAE------KLG-----LPYIVVVVDELADLmmggyKKE 241
Cdd:TIGR03928 522 PHLLG-TITNLDGA-QSMRALAsikAELKKRQRLFGENNVNHINqyqklyKQGkakepMPHLFLISDEFAEL-----KSE 594
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 242 VE---ANIVRIAQKARAAGIHLVLATQRPSvDVVTGLIKSNVPSRLSFATASLTDSRVIL 298
Cdd:TIGR03928 595 QPefmKELVSTARIGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
126-288 |
2.03e-09 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also 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.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 55.69 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 126 HLLVAGATGSGKSSFINSMLVSMLyranPDRVKLIMIDPKM---VELTPYNGIPHLLQPVVTEpdeavkTLRWLTVEMDD 202
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKGelfLVIPDRDDSFAALRALFFN------QLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 203 RYRQmqeagvrhaeKLGLPyIVVVVDELAdlMMGGYKkeveaNIVRIAQKARAAGIHLVLATQ------RPSVDVVTGLI 276
Cdd:cd01127 71 LSPG----------RLPRR-VWFILDEFA--NLGRIP-----NLPNLLATGRKRGISVVLILQslaqleAVYGKDGAQTI 132
|
170
....*....|..
gi 971751354 277 KSNVPSRLSFAT 288
Cdd:cd01127 133 LGNCNTKLYLGT 144
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
123-269 |
8.63e-03 |
|
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: 36.58 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 123 KMPHLLVAGATGSGKSSFINsmlvSMLYRANPDRVKLIMIDPKMVELTPYNGIPHLlqpvvtepdeavktlrwLTVEMDD 202
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLAR----ALARELGPPGGGVIYIDGEDILEEVLDQLLLI-----------------IVGGKKA 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 971751354 203 RYRQMQEAGVRHAEKLGLPYIVVVVDELADLMMGGYKKEVEANIVR--IAQKARAAGIHLVLATQRPSV 269
Cdd:smart00382 60 SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlLLLLKSEKNLTVILTTNDEKD 128
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
7-361 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 581.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 7 QDTAAQIISALREFDIEAKVTGRTDGPSVTRYEIALGPGVRIQKVSQLQSQLAYALATESVRVVAPIPGKTAVGIELPRS 86
Cdd:COG1674 159 EENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 87 ERQTVRLQQIVP-----EDDHPLTVAVGKDVEGKDVSLNLAKMPHLLVAGATGSGKSSFINSMLVSMLYRANPDRVKLIM 161
Cdd:COG1674 239 KRETVYLREVLEsdefqNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLIL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 162 IDPKMVELTPYNGIPHLLQPVVTEPDEAVKTLRWLTVEMDDRYRQMQEAGVRH----------AEKLG--------LPYI 223
Cdd:COG1674 319 IDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNiagynekvreAKAKGeeeeglepLPYI 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 224 VVVVDELADLMMgGYKKEVEANIVRIAQKARAAGIHLVLATQRPSVDVVTGLIKSNVPSRLSFATASLTDSRVILDEGGA 303
Cdd:COG1674 399 VVIIDELADLMM-VAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGA 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971751354 304 EQLMGMGDGLFLPVGARGAIRIQGAFVSDGEIEAAVNNVR----------VTARVEEKVRELNPEPED 361
Cdd:COG1674 478 EKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKsqgepeyieeILEEEEEEDEGGDDDEDD 545
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
2-347 |
2.72e-124 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 391.76 E-value: 2.72e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 2 TTMLEQdtAAQIISA-LREFDIEAKVTGRTDGPSVTRYEIALGPGVRIQKVSQLQSQLAYALATESVRVVAPIPGKTAVG 80
Cdd:PRK10263 884 TFALEQ--MARLVEArLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVG 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 81 IELPRSERQTVRLQQIVP-----EDDHPLTVAVGKDVEGKDVSLNLAKMPHLLVAGATGSGKSSFINSMLVSMLYRANPD 155
Cdd:PRK10263 962 LELPNKKRQTVYLREVLDnakfrDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPE 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 156 RVKLIMIDPKMVELTPYNGIPHLLQPVVTEPDEAVKTLRWLTVEMDDRYRQMQEAGVRH----------AEKLG------ 219
Cdd:PRK10263 1042 DVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNlagynekiaeADRMMrpipdp 1121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 220 -----------------LPYIVVVVDELADLMMGGYKKeVEANIVRIAQKARAAGIHLVLATQRPSVDVVTGLIKSNVPS 282
Cdd:PRK10263 1122 ywkpgdsmdaqhpvlkkEPYIVVLVDEFADLMMTVGKK-VEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPT 1200
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971751354 283 RLSFATASLTDSRVILDEGGAEQLMGMGDGLFLPVGARGAIRIQGAFVSDGEIEAAVNNVRVTAR 347
Cdd:PRK10263 1201 RIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGR 1265
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
100-268 |
4.40e-58 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 190.28 E-value: 4.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 100 DDHPLTVAVGKDVEGKDVSLNLAKMP-HLLVAGATGSGKSSFINSMLVSMLYRANPDRVKLIMIDPKMVELTPYNGIPHL 178
Cdd:pfam01580 13 DYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 179 L-QPVVTEPDEAVKTLRWLTVEMDDRYRQMQEAGVR---------------------------------HAEKLGLPYIV 224
Cdd:pfam01580 93 LsVPVATDPKRALRALEWLVDEMERRYALFRALGVRsiagyngeiaedpldgfgdvflviygvhvmctaGRWLEILPYLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 971751354 225 VVVDELADLMMGGYKKE---VEANIVRIAQKARAAGIHLVLATQRPS 268
Cdd:pfam01580 173 VIVDERAELRLAAPKDSemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
7-84 |
5.37e-27 |
|
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. FtsK can be split into three domains called alpha (this entry), beta and gamma. The alpha and beta domains contain the core ATPase machinery of the DNA translocase.
Pssm-ID: 436096 [Multi-domain] Cd Length: 101 Bit Score: 103.77 E-value: 5.37e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971751354 7 QDTAAQIISALREFDIEAKVTGRTDGPSVTRYEIALGPGVRIQKVSQLQSQLAYALATESVRVVAPIPGKTAVGIELP 84
Cdd:pfam17854 23 EETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSAPSIRIVAPIPGKSTIGIEVP 100
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
104-298 |
3.19e-23 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 103.14 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 104 LTVAVGkdVEGKD--VSLNL---AKMPHLLVAGATGSGKSSFINSMLVSMLYRANPDRVKLIMIDPK---MVEltPYNGI 175
Cdd:TIGR03928 446 LAVPIG--LRGKDdiVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMAN--LFKNL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 176 PHLLQpVVTEPDEAvKTLRWLT---VEMDDRYRQMQEAGVRHAE------KLG-----LPYIVVVVDELADLmmggyKKE 241
Cdd:TIGR03928 522 PHLLG-TITNLDGA-QSMRALAsikAELKKRQRLFGENNVNHINqyqklyKQGkakepMPHLFLISDEFAEL-----KSE 594
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 242 VE---ANIVRIAQKARAAGIHLVLATQRPSvDVVTGLIKSNVPSRLSFATASLTDSRVIL 298
Cdd:TIGR03928 595 QPefmKELVSTARIGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
104-331 |
4.39e-20 |
|
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274858 [Multi-domain] Cd Length: 658 Bit Score: 92.73 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 104 LTVAVGKDVEGKDVSLNLAK-----M-PHLLVAGATGSGKSSFINSMLVSMLYRANPDRVKLIMIDPKMvELT--PYNGI 175
Cdd:TIGR03924 409 LRVPIGVGDDGEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKG-GATflGLEGL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 176 PHLLQpVVTE-PDEAVKTLRW---LTVEMDDRYRQMQEAG----VRHAEKLG--------LPYIVVVVDELADLMmgGYK 239
Cdd:TIGR03924 488 PHVSA-VITNlADEAPLVDRMqdaLAGEMNRRQELLRAAGnfanVAEYEKARaagadlppLPALFVVVDEFSELL--SQH 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 240 KEVEANIVRIAQKARAAGIHLVLATQRPSVDVVTGLiKSNVPSRLSFATASLTDSRVILDEGGAEQL---MGMGdglFLP 316
Cdd:TIGR03924 565 PDFADLFVAIGRLGRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLpstPGAG---YLK 640
|
250
....*....|....*
gi 971751354 317 VGARGAIRIQGAFVS 331
Cdd:TIGR03924 641 VDTAEPVRFRAAYVS 655
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
116-269 |
2.01e-11 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 66.16 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 116 DVSLNLAKMPHLLVAGATGSGKSSFINSMLVSMLYRANPDRVKLIMIDPKMVELTPYNGIPHLLQPVVTEPDEAV-KTLR 194
Cdd:TIGR03928 802 PLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEEEKIeKLIR 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 195 WLTVEMDDRYRQMQEAGVRHA---EKLG---LPYIVVVVDELADLMMGGYKKEVEANIVRIAQKARAAGIHLVL-ATQRP 267
Cdd:TIGR03928 882 RIKKEIDRRKKLFSEYGVASIsmyNKASgekLPQIVIIIDNYDAVKEEPFYEDFEELLIQLAREGASLGIYLVMtAGRQN 961
|
..
gi 971751354 268 SV 269
Cdd:TIGR03928 962 AV 963
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
74-278 |
2.16e-10 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 63.08 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 74 PGKTAVGI-----ELPRSE-RQTVRLQQIVPEDDHPLTVAVgKDVEGkdVSLNLAKMPHLLVAGATGSGKSSFINSMLVS 147
Cdd:TIGR03928 1043 TGERPKPIpmvpeELSLEEfRERYEVRKILEEGSIPIGLDE-ETVEP--VYIDLTENPHLLIVGESDDGKTNVLKSLLKT 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 148 MLYRanpDRVKLIMIDPKMVELTPYNGIPHlLQPVVTEPDEAVKTLRWLTVEMDDRYRQMQEAGVRHAEKLGLPYIVVVV 227
Cdd:TIGR03928 1120 LAKQ---EKEKIGLIDSIDRGLLAYRDLKE-VATYIEEKEDLKEILAELKEEIELREAAYKEALQNETGEPAFKPILLII 1195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 971751354 228 DELADLMMggyKKEVEA--NIVRIAQKARAAGIHLVLATQRPSV----DVVTGLIKS 278
Cdd:TIGR03928 1196 DDLEDFIQ---RTDLEIqdILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ 1249
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
58-263 |
9.19e-10 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 60.78 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 58 LAYALATESVRVVAPIPGKTAVGIeLPRSerqtVRLQQIVPEDDHP-LTVAVGkdVEGKD---VSLNLAKMPHLLVAGAT 133
Cdd:TIGR03925 300 LGTRGLVAVIRDVWGGPPAPPVRL-LPAR----LPLSALPAGGGAPrLRVPLG--LGESDlapVYVDFAESPHLLIFGDS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 134 GSGKSSFINSMLVSMLYRANPDRVKLIMIDPK--MVELTPYNgipHLLQPVVTePDEAVKTLRWLTVEMDDRyrqMQEAG 211
Cdd:TIGR03925 373 ESGKTTLLRTIARGIVRRYSPDQARLVVVDYRrtLLGAVPED---YLAGYAAT-SAALTELIAALAALLERR---LPGPD 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 971751354 212 VRHAEKLGL-----PYIVVVVDELaDLMMGGYKKEVeANIVRIAQKARAAGIHLVLA 263
Cdd:TIGR03925 446 VTPQQLRARswwsgPEIYVVVDDY-DLVATGSGNPL-APLVELLPHARDIGLHVVVA 500
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
126-288 |
2.03e-09 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also 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.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 55.69 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 126 HLLVAGATGSGKSSFINSMLVSMLyranPDRVKLIMIDPKM---VELTPYNGIPHLLQPVVTEpdeavkTLRWLTVEMDD 202
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKGelfLVIPDRDDSFAALRALFFN------QLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 203 RYRQmqeagvrhaeKLGLPyIVVVVDELAdlMMGGYKkeveaNIVRIAQKARAAGIHLVLATQ------RPSVDVVTGLI 276
Cdd:cd01127 71 LSPG----------RLPRR-VWFILDEFA--NLGRIP-----NLPNLLATGRKRGISVVLILQslaqleAVYGKDGAQTI 132
|
170
....*....|..
gi 971751354 277 KSNVPSRLSFAT 288
Cdd:cd01127 133 LGNCNTKLYLGT 144
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
93-165 |
6.78e-07 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 51.15 E-value: 6.78e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971751354 93 LQQIVPEDDhplTVAVGKDV-EGKDVSLNLAKM--PHLLVAGATGSGKSSFInSMLVSMLYRANpdrVKLIMIDPK 165
Cdd:COG0433 16 LEELLGDGG---GILIGKLLsPGVPVYLDLDKLlnRHILILGATGSGKSNTL-QVLLEELSRAG---VPVLVFDPH 84
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
71-266 |
1.14e-05 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 47.68 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 71 APIPGKTAVGIELPRSERQTVRLQqivPEDDHPLTVAVG---------KDVEGKDVSLNLAkmpHLLVAGATGSGKSSFI 141
Cdd:TIGR03925 23 PPLPEPPALDDLLPRLDVDPWRVD---YGQRGRLTVPVGivdrpfeqrQDPLVVDLSGAAG---HVAIVGAPQSGKSTAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 142 NSMLVSMLYRANPDRVKLIMIDPKMVELTPYNGIPHL------------------LQPVVTEPDEAVKTLRWLTVEmddR 203
Cdd:TIGR03925 97 RTLILALALTHTPEEVQFYCLDFGGGGLASLADLPHVggvagrldpervrrtvaeVEGLLRRRERLFRTHGIDSMA---Q 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971751354 204 YRQMQEAGVRHAEKLGlpYIVVVVDELADLmmggyKKE---VEANIVRIAQKARAAGIHLVLATQR 266
Cdd:TIGR03925 174 YRARRAAGRLPEDPFG--DVFLVIDGWGTL-----RQDfedLEDKVTDLAARGLAYGVHVVLTASR 232
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
204-268 |
1.45e-04 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 43.83 E-value: 1.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971751354 204 YRQMQEAGvrHAEKLGLPyIVVVVDElADLMMGGYKKEVEANIVRIAQKARAAGIHLVLATQRPS 268
Cdd:COG0433 244 FEARPEVG--DADDRKLP-LVLVIDE-AHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS 304
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
125-164 |
6.73e-04 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 41.86 E-value: 6.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 971751354 125 PHLLVAGATGSGKSSFINSMLVSMLYRanpdRVKLIMIDP 164
Cdd:COG3451 205 GNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
116-164 |
2.36e-03 |
|
Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.
Pssm-ID: 376671 [Multi-domain] Cd Length: 220 Bit Score: 39.27 E-value: 2.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 971751354 116 DVSLNLAKM--PHLLVAGATGSGKSSFINSMLVSMLYRanpDRVKLIMIDP 164
Cdd:pfam01935 13 PVYLDVNKLvsRHFAILGSTGSGKSNTVAVLLEELLEK---KGATVLIFDP 60
|
|
| CDC_Septin |
cd01850 |
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ... |
127-164 |
2.75e-03 |
|
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.
Pssm-ID: 206649 Cd Length: 275 Bit Score: 39.45 E-value: 2.75e-03
10 20 30
....*....|....*....|....*....|....*...
gi 971751354 127 LLVAGATGSGKSSFINSMLVSMLYRANPDRVKLIMIDP 164
Cdd:cd01850 7 IMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITK 44
|
|
| Septin |
pfam00735 |
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ... |
127-153 |
3.47e-03 |
|
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.
Pssm-ID: 395596 Cd Length: 272 Bit Score: 39.20 E-value: 3.47e-03
10 20
....*....|....*....|....*..
gi 971751354 127 LLVAGATGSGKSSFINSMLVSMLYRAN 153
Cdd:pfam00735 6 LMVVGESGLGKTTFINTLFLTDLYRAR 32
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
123-269 |
8.63e-03 |
|
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: 36.58 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971751354 123 KMPHLLVAGATGSGKSSFINsmlvSMLYRANPDRVKLIMIDPKMVELTPYNGIPHLlqpvvtepdeavktlrwLTVEMDD 202
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLAR----ALARELGPPGGGVIYIDGEDILEEVLDQLLLI-----------------IVGGKKA 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 971751354 203 RYRQMQEAGVRHAEKLGLPYIVVVVDELADLMMGGYKKEVEANIVR--IAQKARAAGIHLVLATQRPSV 269
Cdd:smart00382 60 SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlLLLLKSEKNLTVILTTNDEKD 128
|
|
| |
