|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
157-398 |
7.78e-54 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 192.82 E-value: 7.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 157 TTHTNAIVAMAVNPWAPVVAIGGQ-KQVLLYNTDTLQPLGVLPFPEGFLDVLHFSRNGQVLMAGGGMGGksgkVALWDLK 235
Cdd:COG2319 159 TGHSGAVTSVAFSPDGKLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGT----VRLWDLA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 236 TGERIATIGNEFDQALAADLSPDQQFVALGGPLKLLKIYSTKDGKLVQSIKKHTDWVTAIAFSADGKYLASADRAGGIQI 315
Cdd:COG2319 235 TGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 316 WESGTWKEFNTLPGHKGMVTGLAFMP--GVLASCGEDGKVTLWDAKEGKEIKSWTAHAGGVEWVDFTPDGK-LISCGRDK 392
Cdd:COG2319 315 WDLATGKLLRTLTGHTGAVRSVAFSPdgKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRtLASGSADG 394
|
....*.
gi 494040510 393 IARVWD 398
Cdd:COG2319 395 TVRLWD 400
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
150-440 |
7.39e-53 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 190.12 E-value: 7.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 150 PLEPYVRTTHTNAIVAMAVNPWAPVVAIGGQ-KQVLLYNTDTLQPLGVLPFPEGFLDVLHFSRNGQVLMAGGGMGGksgk 228
Cdd:COG2319 110 GLLLRTLTGHTGAVRSVAFSPDGKTLASGSAdGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGT---- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 229 VALWDLKTGERIATIGNEFDQALAADLSPDQQFVALGGPLKLLKIYSTKDGKLVQSIKKHTDWVTAIAFSADGKYLASAD 308
Cdd:COG2319 186 VRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGS 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 309 RAGGIQIWESGTWKEFNTLPGHKGMVTGLAFMPG--VLASCGEDGKVTLWDAKEGKEIKSWTAHAGGVEWVDFTPDGK-L 385
Cdd:COG2319 266 ADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKtL 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 386 ISCGRDKIARVWD-QTGKKL----GETKPADDIALRAglENDRMIVGDWTGKIQVVKMDG 440
Cdd:COG2319 346 ASGSDDGTVRLWDlATGELLrtltGHTGAVTSVAFSP--DGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
131-407 |
4.34e-52 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 188.20 E-value: 4.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 131 VAAVSLTRPDGPPPMPGDLPLEPYVRTTHTNAIVAMAVNPWAPVVAIGGQKQVLLYNTDTLQPLGVLPFPEGFLDVLHFS 210
Cdd:COG2319 8 ALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 211 RNGQVLMAGGGMGGksgkVALWDLKTGERIATIGNEFDQALAADLSPDQQFVALGGPLKLLKIYSTKDGKLVQSIKKHTD 290
Cdd:COG2319 88 PDGRLLASASADGT----VRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 291 WVTAIAFSADGKYLASADRAGGIQIWESGTWKEFNTLPGHKGMVTGLAFMPG--VLASCGEDGKVTLWDAKEGKEIKSWT 368
Cdd:COG2319 164 AVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgkLLASGSADGTVRLWDLATGKLLRTLT 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 494040510 369 AHAGGVEWVDFTPDGK-LISCGRDKIARVWDQTGKKLGET 407
Cdd:COG2319 244 GHSGSVRSVAFSPDGRlLASGSADGTVRLWDLATGELLRT 283
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
159-406 |
1.64e-41 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 154.03 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 159 HTNAIVAMAVNPWAPVVAIGGQ-KQVLLYNTDTLQPLGVLPFPEGFLDVLHFSRNGQVLMAGGGMGGksgkVALWDLKTG 237
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKT----IRLWDLETG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 238 ERIATIGNEFDQALAADLSPDQQFVALGGPLKLLKIYSTKDGKLVQSIKKHTDWVTAIAFSADGKYLASADRAGGIQIWE 317
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 318 SGTWKEFNTLPGHKGMVTGLAFMP--GVLASCGEDGKVTLWDAKEGKEIKSWTAHAGGVEWVDFTPDGKLI-SCGRDKIA 394
Cdd:cd00200 164 LRTGKCVATLTGHTGEVNSVAFSPdgEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLaSGSEDGTI 243
|
250
....*....|...
gi 494040510 395 RVWD-QTGKKLGE 406
Cdd:cd00200 244 RVWDlRTGECVQT 256
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
157-398 |
3.42e-40 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 150.18 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 157 TTHTNAIVAMAVNPWAPVVAIGGQ-KQVLLYNTDTLQPLGVLpfpEGFLDV---LHFSRNGQVLMAGGGMGGksgkVALW 232
Cdd:cd00200 48 KGHTGPVRDVAASADGTYLASGSSdKTIRLWDLETGECVRTL---TGHTSYvssVAFSPDGRILSSSSRDKT----IKVW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 233 DLKTGERIATIGNEFDQALAADLSPDQQFVALGGPLKLLKIYSTKDGKLVQSIKKHTDWVTAIAFSADGKYLASADRAGG 312
Cdd:cd00200 121 DVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 313 IQIWESGTWKEFNTLPGHKGMVTGLAFMPG--VLASCGEDGKVTLWDAKEGKEIKSWTAHAGGVEWVDFTPDGK-LISCG 389
Cdd:cd00200 201 IKLWDLSTGKCLGTLRGHENGVNSVAFSPDgyLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKrLASGS 280
|
....*....
gi 494040510 390 RDKIARVWD 398
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
229-407 |
5.01e-36 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 138.24 E-value: 5.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 229 VALWDLKTGERIATIGNEFDQALAADLSPDQQFVALGGPLKLLKIYSTKDGKLVQSIKKHTDWVTAIAFSADGKYLASAD 308
Cdd:cd00200 33 IKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 309 RAGGIQIWESGTWKEFNTLPGHKGMVTGLAFMP--GVLASCGEDGKVTLWDAKEGKEIKSWTAHAGGVEWVDFTPDG-KL 385
Cdd:cd00200 113 RDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPdgTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGeKL 192
|
170 180
....*....|....*....|..
gi 494040510 386 ISCGRDKIARVWDQTGKKLGET 407
Cdd:cd00200 193 LSSSSDGTIKLWDLSTGKCLGT 214
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
218-435 |
7.31e-32 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 128.88 E-value: 7.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 218 AGGGMGGKSGKVALWDLKTGERIATIGNEFDQALAADLSPDQQFVALGGPLKLLKIYSTKDGKLVQSIKKHTDWVTAIAF 297
Cdd:COG2319 7 AALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 298 SADGKYLASADRAGGIQIWESGTWKEFNTLPGHKGMVTGLAFMP--GVLASCGEDGKVTLWDAKEGKEIKSWTAHAGGVE 375
Cdd:COG2319 87 SPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040510 376 WVDFTPDGK-LISCGRDKIARVWD-QTGKKL----GETKPADDIALRAglENDRMIVGDWTGKIQV 435
Cdd:COG2319 167 SVAFSPDGKlLASGSDDGTVRLWDlATGKLLrtltGHTGAVRSVAFSP--DGKLLASGSADGTVRL 230
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
281-404 |
1.92e-28 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 116.28 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 281 LVQSIKKHTDWVTAIAFSADGKYLASADRAGGIQIWESGTWKEFNTLPGHKGMVTGLAFMP--GVLASCGEDGKVTLWDA 358
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASAdgTYLASGSSDKTIRLWDL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 494040510 359 KEGKEIKSWTAHAGGVEWVDFTPDGKLI-SCGRDKIARVWD-QTGKKL 404
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSPDGRILsSSSRDKTIKVWDvETGKCL 128
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
254-435 |
4.56e-19 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 90.74 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 254 DLSPDQQFVALGGPLKLLKIYSTKDGKLVQSIKKHTDWVTAIAFSADGKYLASADRAGGIQIWESGTWKEFNTLPGHKGM 333
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 334 VTGLAFMP--GVLASCGEDGKVTLWDAKEGKEIKSWTAHAGGVEWVDFTPDGK-LISCGRDKIARVWD-QTGKKL----G 405
Cdd:COG2319 81 VLSVAFSPdgRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKtLASGSADGTVRLWDlATGKLLrtltG 160
|
170 180 190
....*....|....*....|....*....|.
gi 494040510 406 ETKPADDIALRAgleNDRMIV-GDWTGKIQV 435
Cdd:COG2319 161 HSGAVTSVAFSP---DGKLLAsGSDDGTVRL 188
|
|
| PSCyt1 |
pfam07635 |
Planctomycete cytochrome C; These proteins share a region of homology at their N-terminus that ... |
37-94 |
2.55e-14 |
|
Planctomycete cytochrome C; These proteins share a region of homology at their N-terminus that contains the C-{CPWHF}-{CPWR}-C-H-{CFYW} motif typical of cytochromes C, or CxxCH.
Pssm-ID: 429568 Cd Length: 59 Bit Score: 68.18 E-value: 2.55e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 494040510 37 CLNCHNPDKKKAGLDLSTYQAALQGSENGKVLESGNPASSLLVKCIKQTD-DPKMPPKG 94
Cdd:pfam07635 1 CFDCHGPDDQEGGLRLDSRDAALKGGDSGPAIVPGDPENSELWERIRSDDpDMEMPPPD 59
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
461-929 |
9.82e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 461 AKDLADAQIALPKLQDQLTAAEAKLQTEKTNADNAYKAALAAAQKHKDEAQKI--------VEAHKSAVPSAEKHLTELK 532
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAeaeaaadeAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 533 TQIAASQKTVADARTAVEAAQKTLADKQAAintpgaeidtarQEVTNKTTAQTEAEkQLTARKDEVTKAEaELTK----L 608
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKA------------DELKKAAAAKKKAD-EAKKKAEEKKKAD-EAKKkaeeA 1443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 609 RASTPAAIAAAEKVLQQANTQLATAQKPPAPVAAVTAAEQDVTKIKASIEDTKAQIIADKANADRWKVAQVLQSAHDAHD 688
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 689 ALLAKQAQYEQLMQTAKDAPQ---AIENARNDLANAQKTIADAPAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAKEKDK 765
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEkkkADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 766 NAQTVADNAptmgdvtnltKKMEGLNAEAAKLREERNSHSQgsPEYLAANTKYQAKKAEITNTQTGIDRREREEHGGPGS 845
Cdd:PTZ00121 1604 EKKMKAEEA----------KKAEEAKIKAEELKKAEEEKKK--VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 846 ESRaggiRQGPRCFRRSQAWLEAAHQGRGGSREGDRPGQEKRRGRDPARRAfAEGHAADHQGRGNAEDGGRKSRRDCRQG 925
Cdd:PTZ00121 1672 EDK----KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-EELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
....
gi 494040510 926 SGSR 929
Cdd:PTZ00121 1747 EEAK 1750
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
456-761 |
3.80e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 456 RATATAKDLADAQIALPKLQDQLTAAEAKLQTEKTNADNAYKAALAAAQKHKDEAQKIVEAHKSavpsaekhLTELKTQI 535
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE--------EYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 536 AASQKTVADARTAVEAAQKTLADKQAaintpgaEIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEAELTKLRASTPAA 615
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 616 IAAAEKVLQQANTQLATAQKPPAPVAAVTAAEQDVTKIKASIEDTKAQIIADKANADRwKVAQVLQSAHDAHDALLAKQA 695
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-ALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494040510 696 QYEQLMQTAKDAPQAIENARNDLANAQKTIADA---PAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAK 761
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELleeLAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
454-788 |
1.44e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 454 AERATATAKDLADAQIALpkLQDQLTAAEAKLQTektnadnaykaalaaAQKHKDEAQKIVEAHKSAVPSAEKHLTELKT 533
Cdd:TIGR02168 212 AERYKELKAELRELELAL--LVLRLEELREELEE---------------LQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 534 QIAASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEAELTKLR---A 610
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 611 STPAAIAAAEKVLQQANTQLATAQKP-PAPVAAVTAAEQDVTKIKASIEDTKAQIIADKANADRWKVAQVLQSAHDAHDA 689
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 690 LLAKQAQYEQLMQTAKDAPQAIENARNDLANAQKTIADAPAKAKEKEDAFAKAREAVEAAKKTVAAAEDL---AKEKDKN 766
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegVKALLKN 514
|
330 340
....*....|....*....|..
gi 494040510 767 AQTVADNAPTMGDVTNLTKKME 788
Cdd:TIGR02168 515 QSGLSGILGVLSELISVDEGYE 536
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
710-932 |
1.47e-08 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 58.76 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 710 AIENARNDLANAQKTIADAPAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAKEKDKNAQTVADNAPTMGDVTNLTKKMEG 789
Cdd:PRK12678 54 AIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRER 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 790 lnAEAAKLREERNSHSQGSPEYLAANTKYQAKKAEITNTQT--GIDRREREEHGGPGSESRAGGI-RQGPRCFRRSQAWL 866
Cdd:PRK12678 134 --GEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERrrRGDREDRQAEAERGERGRREERgRDGDDRDRRDRREQ 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494040510 867 EAAHQGRGGSREGDRPGQEKRRGRDPARRAFAEGHAADHQGRGNAEDGGRKSRRDC---RQGSGSRQGR 932
Cdd:PRK12678 212 GDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRdrdRRGRRGGDGG 280
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
454-814 |
1.95e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 454 AERATATAKD-LADAQIALPKLQDQLTAAEAKLQTEKTNADnAYKAALAAAQKHKDEAQKIVE-------AHKSAVPSAE 525
Cdd:PRK02224 270 TEREREELAEeVRDLRERLEELEEERDDLLAEAGLDDADAE-AVEARREELEDRDEELRDRLEecrvaaqAHNEEAESLR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 526 KHLTELKTQIAASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEAEL 605
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 606 TKLRAStpaaIAAAEKVLQQANTQLATAQ--------KPPAPVAAVTAAEQDVTKIKASIEDTKAQIIADKANADRwkvA 677
Cdd:PRK02224 429 AELEAT----LRTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER---A 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 678 QVLQSAHDAHDALLAKQAQYEQLMQTAKDapqAIENARNDLANAQKTIADAPAKAKEKEDAFAKAREAVEAAKKTVAAAE 757
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIAERRE---TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 494040510 758 DLAKEKDKNAQTVADNAPTMGDVTNLTKKMEGLNaEAAKLREERNSHSQgspEYLAA 814
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAAIADAEDEIERLR-EKREALAELNDERR---ERLAE 631
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
278-317 |
2.49e-08 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 50.39 E-value: 2.49e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 494040510 278 DGKLVQSIKKHTDWVTAIAFSADGKYLASADRAGGIQIWE 317
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
568-838 |
6.04e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 568 AEIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEAELTKLRastpaaiaaaeKVLQQANTQLATAQKP-PAPVAAVTAA 646
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR-----------KELEELSRQISALRKDlARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 647 EQDVTKIKASIEDTKAQIIAdkanadrwkVAQVLQSAHDAHDALLAKQAQYEQLMQTAKDAPQAIEnarndlanaqKTIA 726
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEE---------LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----------EALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 727 DAPAKAKEKEDAFAKAREAVEAAKKTVAA----AEDLAKEKDKNAQTVADNAPTMGDvtnLTKKMEGLNAEAAKLREERN 802
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAAterrLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERA 883
|
250 260 270
....*....|....*....|....*....|....*.
gi 494040510 803 SHSQGSPEylaANTKYQAKKAEITNTQTGIDRRERE 838
Cdd:TIGR02168 884 SLEEALAL---LRSELEELSEELRELESKRSELRRE 916
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
518-635 |
1.35e-07 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 54.73 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 518 KSAVPSAEKHLTELKTQIAASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTE-AEKQLTARKD 596
Cdd:TIGR04320 246 KTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQtAQNNLATAQA 325
|
90 100 110
....*....|....*....|....*....|....*....
gi 494040510 597 EVTKAEAELTKLrastpaaiaaaEKVLQQANTQLATAQK 635
Cdd:TIGR04320 326 ALANAEARLAKA-----------KEALANLNADLAKKQA 353
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
320-357 |
2.09e-07 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 48.08 E-value: 2.09e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 494040510 320 TWKEFNTLPGHKGMVTGLAFMP--GVLASCGEDGKVTLWD 357
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPdgKYLASGSDDGTIKLWD 40
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
454-800 |
2.94e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 454 AERATATAKDLADAQIALPKLQDQLTAAEAKLQTEKTNADNAYKAALAAAQKHKDEAQKIVEAHKSAvPSAEKHLTELKT 533
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA-DEAKKAEEAKKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 534 QIAASQKTVADARTAVEAAQKTLADK-QAAINTPGAE----IDTARQEVTNKTTAQTEAE---KQLTARKDEVTKAEAEL 605
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEekkkAEEAKKAEEDKNMALRKAEeakKAEEARIEEVMKLYEEE 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 606 TKLRASTPAAIAAAEKVLQQANTQLATAQKPPAPVAAVTAAEQDVTKIKASIEDT--KAQIIADKANADRWKVAQVLQSA 683
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENkiKAAEEAKKAEEDKKKAEEAKKAE 1684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 684 HDahdallaKQAQYEQLMQTAKDAPQAiENARNDLANAQKTiadAPAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAK-- 761
Cdd:PTZ00121 1685 ED-------EKKAAEALKKEAEEAKKA-EELKKKEAEEKKK---AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKde 1753
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 494040510 762 -EKDKNAQTVADNAPTMGDVTNLTKKM--EGLNAEAAKLREE 800
Cdd:PTZ00121 1754 eEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRME 1795
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
536-769 |
3.02e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.18 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 536 AASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEAELTKlrastpaa 615
Cdd:PRK05035 475 KAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPK-------- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 616 iaaaeKVLQQANTQLATAQKPPAPVAAVTAAEQDVTK---IKASIEDTKAQIIADKANADRWKVAQVLQSAHDAHDALLA 692
Cdd:PRK05035 547 -----KAAVAAAIARAKAKKAAQQAANAEAEEEVDPKkaaVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAI 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040510 693 KQAQYEQLMQTAKDAPQAIENARndLANAQKTIADAPAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAKEKdKNAQT 769
Cdd:PRK05035 622 ARAKAKKAEQQANAEPEEPVDPR--KAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAK-KAAQQ 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
510-750 |
6.63e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 510 AQKIVEAHKSAVPSAEKHLTELKTQIAASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTEAEK 589
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 590 QLTARKDEVTKAeaeltkLRASTPAAIAAAEKVLQQANTQLATAQKPPAPVAAVTAAEQDVTKIKASIEDTKAQiiADKA 669
Cdd:COG4942 98 ELEAQKEELAEL------LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL--RAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 670 NADRWKVAQVLQSAHDAHDALLAKQAQYEQLMQTAKDAPQAIENARNDLANAQKTIADAPAKAKEKEDAFAKAREAVEAA 749
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
.
gi 494040510 750 K 750
Cdd:COG4942 250 A 250
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
279-317 |
7.58e-07 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 46.18 E-value: 7.58e-07
10 20 30
....*....|....*....|....*....|....*....
gi 494040510 279 GKLVQSIKKHTDWVTAIAFSADGKYLASADRAGGIQIWE 317
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
533-776 |
2.35e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 533 TQIAASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEAELTKLRAS- 611
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 612 --TPAAIAAAEKVLQQANTQ--LATAQKPPAPVAAVTAAEQDVTKIKASIEDTKAQIIADKANADrwkvaQVLQSAHDAH 687
Cdd:COG3883 96 yrSGGSVSYLDVLLGSESFSdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE-----ALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 688 DALLAKQAQYEQLMQTAKDAPQAIENARNDLANAQKTIADAPAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAKEKDKNA 767
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
....*....
gi 494040510 768 QTVADNAPT 776
Cdd:COG3883 251 AAGAAGAAA 259
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
361-398 |
3.52e-06 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 44.61 E-value: 3.52e-06
10 20 30
....*....|....*....|....*....|....*....
gi 494040510 361 GKEIKSWTAHAGGVEWVDFTPDGK-LISCGRDKIARVWD 398
Cdd:smart00320 2 GELLKTLKGHTGPVTSVAFSPDGKyLASGSDDGTIKLWD 40
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
453-824 |
3.98e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 453 LAERA----TATAKDLADAQIALPKLQDQLTAAEAKLQTEKTNADNA---YKAALAAAQKHKDEAQKIVEAHKSA-VPSA 524
Cdd:PTZ00121 1099 KAEEAkkteTGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEArkaEDAKRVEIARKAEDARKAEEARKAEdAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 525 EKHLTELKTQIAASQKTVADARTAvEAAQKTLADKQAAiNTPGAEIDTARQEVTNKTTAQTEAEKQLTARK----DEVTK 600
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDARKA-EAARKAEEERKAE-EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEernnEEIRK 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 601 AEAELTKLRASTPAAIAAAEKVLQQANTQLATAQKPPAPVAAVTAAEQDVTKIKASiEDTKAQIIADKANADRWKVAQVL 680
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKKADAAK 1335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 681 QSAHDAHDALLAKQAQYEQLMQTAKDAPQAIENARNDLANAQKTIADAPAKAKEKEdafaKAREAVEAAKKTVAAAEDLA 760
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK----KADEAKKKAEEDKKKADELK 1411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040510 761 K--EKDKNAQTVADNAPTMGDVTNLTKKMEglnaEAAKLREERNSHSQGSPEYLAANTKYQAKKAE 824
Cdd:PTZ00121 1412 KaaAAKKKADEAKKKAEEKKKADEAKKKAE----EAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
361-398 |
9.43e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 43.10 E-value: 9.43e-06
10 20 30
....*....|....*....|....*....|....*....
gi 494040510 361 GKEIKSWTAHAGGVEWVDFTPDGK-LISCGRDKIARVWD 398
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKlLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
321-357 |
1.23e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 43.10 E-value: 1.23e-05
10 20 30
....*....|....*....|....*....|....*....
gi 494040510 321 WKEFNTLPGHKGMVTGLAFMPG--VLASCGEDGKVTLWD 357
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
467-610 |
1.28e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.51 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 467 AQIALPKLQDQLTAAEAKLQTEKTNADNAYKAALAAAQkhKDEAQKIVEAHKSAVPSAEKHLT---ELKTQIAASQKTVA 543
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEAE--IAAAEAQLAAAQAQLDLAQRELEryqALYKKGAVSQQELD 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494040510 544 DARTAVEAAQKTLADKQAAINTPGAEIDTARQevtnkttaQTEAEKQLTARKDEVTKAEAEL--TKLRA 610
Cdd:COG1566 152 EARAALDAAQAQLEAAQAQLAQAQAGLREEEE--------LAAAQAQVAQAEAALAQAELNLarTTIRA 212
|
|
| NBCH_WD40 |
pfam20426 |
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ... |
272-317 |
1.37e-05 |
|
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.
Pssm-ID: 466575 [Multi-domain] Cd Length: 350 Bit Score: 48.53 E-value: 1.37e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 494040510 272 KIYSTKDGKLVQSIKKHTDWVTAIAFSADGKYLASADRAGGIQIWE 317
Cdd:pfam20426 107 QVISLNDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVWE 152
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
535-911 |
1.91e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 535 IAASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEAELTKLRAstpa 614
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 615 aiaAAEKVLQQANTQLATAQKPPAPVAAVtaaeqDVTKIKASIED--TKAQIIADKANADRwkvaQVLQSAHDAHDALLA 692
Cdd:COG3883 80 ---EIEERREELGERARALYRSGGSVSYL-----DVLLGSESFSDflDRLSALSKIADADA----DLLEELKADKAELEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 693 KQAQYEQLMQTAKDAPQAIENARNDL----ANAQKTIADAPAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAKEKDKNAQ 768
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELeaqqAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 769 TVADNAPTMGDVTNLTKKMEGLNAEAAKLREERNSHSQGSPEYLAANTKYQAKKAEITNTQTGIDRREREEHGGPGSESR 848
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGS 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494040510 849 AGGIRQGPRCFRRSQAWLEAAHQGRGGSREGDRPGQEKRRGRDPARRAFAEGHAADHQGRGNA 911
Cdd:COG3883 308 GGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLS 370
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
504-606 |
2.98e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 47.41 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 504 QKHKDEAQKIVEAHKSAVPSAEKHLTELKTQIAASQKTVADARTAVEAAQKTLADKQA-AINTPGAEIDTARQEVTNKTT 582
Cdd:TIGR04320 253 PNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAqALQTAQNNLATAQAALANAEA 332
|
90 100
....*....|....*....|....
gi 494040510 583 AQTEAEKQLTARKDEVTKAEAELT 606
Cdd:TIGR04320 333 RLAKAKEALANLNADLAKKQAALD 356
|
|
| PRK12808 |
PRK12808 |
flagellin; Provisional |
534-782 |
3.41e-05 |
|
flagellin; Provisional
Pssm-ID: 237212 [Multi-domain] Cd Length: 476 Bit Score: 47.26 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 534 QIAASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEAELTKLRASTP 613
Cdd:PRK12808 178 NTDIEAVSTKIAALDKNTIAKATVEAKAAFDKAKDDTKAEDSNILDAAADGFKDGKADDAAKDVEAIKTALSAFTGAATL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 614 AAIAAAEKVLQQANTQLATAQkppapvaavtaaeqdvTKIKASIEDTKAQIIADKANADRWKVAQVLQSAHDAhdallAK 693
Cdd:PRK12808 258 EEAEAAKTAFEVAQKDLVDTY----------------TKKAALTKDAVADLDTAKTTSTRSKAAKDLVAAYDK-----AK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 694 Q-AQYEQLMQTAKDAPQAIENARNDLANAQKTIADAPA--KAKEKEDAFAKAREAVEAAKK----TVAAAEDLAKEKDKN 766
Cdd:PRK12808 317 SgAKPNDVAKAYLEAKMAYEKDNNAIDGKSKLEAADDAleKDAIKTDASKVLVPKLEAAKKattnSKADSLDAVKAIDEA 396
|
250
....*....|....*.
gi 494040510 767 AQTVADNAPTMGDVTN 782
Cdd:PRK12808 397 LKTVADNRATLGATLN 412
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
648-774 |
4.65e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 46.64 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 648 QDVTKIKASIEDTKAQIIADKANADRWKVAQVLQSAHDAHDALLAKQAQYEQLMQTAKDAPQAIENARNDLANAQKTIAD 727
Cdd:TIGR04320 221 SNDGGVTIHFVNFNDSYIADGNKFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALAT 300
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 494040510 728 APAK-AKEKEDAFAKAREAVEAAKKTVAAAED-LAKEKDKNAQTVADNA 774
Cdd:TIGR04320 301 AQKElANAQAQALQTAQNNLATAQAALANAEArLAKAKEALANLNADLA 349
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
471-696 |
4.77e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 471 LPKLQDQLTAAEAKLQTEKtnadnaykaalaaaqkhkdEAQKIVEAhKSAVPSAEKHLTELKTQIAASQKTVADARTAVE 550
Cdd:COG3206 184 LPELRKELEEAEAALEEFR-------------------QKNGLVDL-SEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 551 AAQKTLADKQAAINTPGA--EIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEAELTKLRAStpaAIAAAEKVLQQANT 628
Cdd:COG3206 244 ALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ---LQQEAQRILASLEA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494040510 629 QLATAQkppapvaavtaaeQDVTKIKASIEDTKAQIIADKANADRWKVAQ-VLQSAHDAHDALLAKQAQ 696
Cdd:COG3206 321 ELEALQ-------------AREASLQAQLAQLEARLAELPELEAELRRLErEVEVARELYESLLQRLEE 376
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
154-359 |
5.26e-05 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 45.84 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 154 YVRTTHTNAIVAMAVNPWAPVVAIGGQKQVLLYNTDTLQPLGVLPFPEGFLDVLHFSRNGQVLMAGGGMGGKsgkVALWD 233
Cdd:COG3391 20 ALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSGR---VSVID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 234 LKTGERIATIGNEFDQALAAdLSPDQQ--FVALGGPLKLLKIySTKDGKLVQSIKKHtDWVTAIAFSADGKYLASADRAG 311
Cdd:COG3391 97 LATGKVVATIPVGGGPRGLA-VDPDGGrlYVADSGNGRVSVI-DTATGKVVATIPVG-AGPHGIAVDPDGKRLYVANSGS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494040510 312 G-----IQIWESGTWKEFNTLPGHkGMVTGLAFMPG---VLASCGEDGKVTLWDAK 359
Cdd:COG3391 174 NtvsviVSVIDTATGKVVATIPVG-GGPVGVAVSPDgrrLYVANRGSNTSNGGSNT 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
536-762 |
1.12e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 536 AASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEAELTKLRASTPAA 615
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 616 IAAAEKVLQQANTQLATAQKPPapvaavtaaEQDVTKIKASIEDtkaqiiADKANADRWKVAQVLQSAHDAHDALLAKQA 695
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLG---------RQPPLALLLSPED------FLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040510 696 QYEQLMQTAKDAPQAIENARNDLANAQKTIAdapAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAKE 762
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
482-839 |
2.41e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 482 EAKLQTEKTNADNAYKAALAAAQKHKDEAQKI------VEAHKSAVPSAEKHLTELKTQIAASQKTVADARTaveaaqkT 555
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQGKNESLEKVssltaqLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA-------S 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 556 LADKQAAINTPGAEIDTARQEVTNKttaqTEAEKQLTARKDEVTKAEAELTKLRASTPAAIAAAEKVLQQAN--TQLAT- 632
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLK----LQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmTQLVGq 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 633 -AQKPPAPVAAVTAAEQDVTKIKASIEDTKaqIIADKANAdrwKVAQVLQSAHDAH-DALLAKQAQYEQLmQTAKDAPQ- 709
Cdd:pfam15921 581 hGRTAGAMQVEKAQLEKEINDRRLELQEFK--ILKDKKDA---KIRELEARVSDLElEKVKLVNAGSERL-RAVKDIKQe 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 710 ------AIENARNDLANAQKTIA----DAPAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAKE---KDKNAQTVADN--- 773
Cdd:pfam15921 655 rdqllnEVKTSRNELNSLSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegSDGHAMKVAMGmqk 734
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494040510 774 --APTMGDVTNLTKKMEGL-------NAEAAKLREERNSHSQgSPEYLAANTKYQAKKAEITNTQtgiDRREREE 839
Cdd:pfam15921 735 qiTAKRGQIDALQSKIQFLeeamtnaNKEKHFLKEEKNKLSQ-ELSTVATEKNKMAGELEVLRSQ---ERRLKEK 805
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
327-398 |
2.94e-04 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 44.50 E-value: 2.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494040510 327 LPGHKGMVTGLAFMP---GVLASCGEDGKVTLWDAKEGKE---IKSWTAHAGGVEWvdfTPDGKLI-SCGRDKIARVWD 398
Cdd:PTZ00421 121 LQGHTKKVGIVSFHPsamNVLASAGADMVVNVWDVERGKAvevIKCHSDQITSLEW---NLDGSLLcTTSKDKKLNIID 196
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
453-580 |
3.10e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 453 LAERATATAKDLADAQIALPKLQDQLTAAEAKLQTEKTNADNAYKA-ALAAAQKHKDEAQKIVEAHKSAVPSAEKHLTEL 531
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlGNVRNNKEYEALQKEIESLKRRISDLEDEILEL 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 494040510 532 KTQIAASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNK 580
Cdd:COG1579 116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
675-762 |
4.20e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 41.69 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 675 KVAQVLQSAHDAHDALLAKQAQYEQLMQTAK-DAPQAIENARndlANAQKTIADAPAKAK-EKEDAFAKAREAVEAAKKt 752
Cdd:PRK05759 39 KIADGLAAAERAKKELELAQAKYEAQLAEARaEAAEIIEQAK---KRAAQIIEEAKAEAEaEAARIKAQAQAEIEQERK- 114
|
90
....*....|
gi 494040510 753 vAAAEDLAKE 762
Cdd:PRK05759 115 -RAREELRKQ 123
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
454-564 |
4.74e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.56 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 454 AERATATAK-DLADAQIALPKLQDQLTAAEAKLQTEKTNADNAYkaalaaaqkhkdeaQKIVEAHKSAVPSAEKHLTELK 532
Cdd:TIGR04320 259 LQAKLATAQaDLAAAQTALNTAQAALTSAQTAYAAAQAALATAQ--------------KELANAQAQALQTAQNNLATAQ 324
|
90 100 110
....*....|....*....|....*....|..
gi 494040510 533 TQIAASQKTVADARTAVEAAQKTLADKQAAIN 564
Cdd:TIGR04320 325 AALANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
464-610 |
4.85e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 464 LADAQIALPKLQDQLTAAEAKLQTEKTNADNAYKAALAAAQKHKDEAQKIVEAHKSAVPSAEKHLTELKTQIAASQKTVA 543
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494040510 544 DARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNkttAQTEAEKQLTARKDEVTKAEAELTKLRA 610
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
453-721 |
4.89e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 453 LAERATATAKDLADAQIALPKLQDQLTAAEAKLQtektnadnaykaalaAAQKHKDEAQKIVEAHKSAVPSAEKHLTELK 532
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELA---------------ALKKEEKALLKQLAALERRIAALARRIRALE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 533 TQIAASQKTVADARTAVEAAQKTLADKQAAIntpgaeidtARQEVTNKTTAQTEAEKQLTARKDeVTKAEAELTKLRAST 612
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEEL---------AELLRALYRLGRQPPLALLLSPED-FLDAVRRLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 613 PAAIaaaekvlQQANTQLATAQKPPAPVAAVTAAEQDVTKIKASIEDTKAQIIADKANADRwKVAQVLQSAHDAHDALLA 692
Cdd:COG4942 146 PARR-------EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK-LLARLEKELAELAAELAE 217
|
250 260
....*....|....*....|....*....
gi 494040510 693 KQAQYEQLMQTAKDAPQAIENARNDLANA 721
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
688-830 |
6.35e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 43.32 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 688 DALLAKQAQYEQLMQTAKDAPQAIENARNDLANAQKTIADAPAKAKEKEDAFAKAREAVEAAKKTVAAAE-DLAKEKDKN 766
Cdd:PRK12472 183 EALAAAPARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRADKALAAAKtDEAKARAEE 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494040510 767 AQTVADNAptmgdVTNLTKKMEGLNAEAAKLREernshsqgspeyLAANTKYQAKKAEITNTQT 830
Cdd:PRK12472 263 RQQKAAQQ-----AAEAATQLDTAKADAEAKRA------------AAAATKEAAKAAAAKKAET 309
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
406-770 |
8.47e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 406 ETKPADDIALRAGLENDRMIVGDWTGKIQVVKMDGDvagTLSANPPTLAERATATAKDLADAQIALPKLQDQLTAAEAKL 485
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD---DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 486 QTEKTNADNAYKAalaaaqkhKDEAQKIVEAHKSAVPSAEKHLTELKTQIAASQKTVADARTAVEAAQ------------ 553
Cdd:PRK02224 394 EELRERFGDAPVD--------LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsp 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 554 --KTLADKQAAINTPGAEIDTARQEVT------NKTTAQTEAEKQLTARKDEVTKAEAELTKLRASTPAAIAAAEKVLQQ 625
Cdd:PRK02224 466 hvETIEEDRERVEELEAELEDLEEEVEeveerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 626 -------ANTQLATAQKPPAPVAAVTAA----EQDVTKIKASIE--DTKAQIIADKANAD------RWKVAQVLQSAHDA 686
Cdd:PRK02224 546 aaeleaeAEEKREAAAEAEEEAEEAREEvaelNSKLAELKERIEslERIRTLLAAIADAEdeierlREKREALAELNDER 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 687 HDALLAKQAQYEQLMQTAKDApqAIENARNDLANAQKTIADAPAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAKEKDKN 766
Cdd:PRK02224 626 RERLAEKRERKRELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREAL 703
|
....
gi 494040510 767 AQTV 770
Cdd:PRK02224 704 ENRV 707
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
231-312 |
8.68e-04 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 43.10 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 231 LW--DLKTGE-RIATIGNEFDQALAADLSPDQQFVA----LGGPLKLLKIYSTKDGKLVQsIKKHTDWVTAIAFSADGKY 303
Cdd:COG4946 412 LWvvDLASGKvRKVDTDGYGDGISDLAWSPDSKWLAyskpGPNQLSQIFLYDVETGKTVQ-LTDGRYDDGSPAFSPDGKY 490
|
90
....*....|
gi 494040510 304 LA-SADRAGG 312
Cdd:COG4946 491 LYfLSSRDFN 500
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
649-800 |
1.21e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.30 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 649 DVTKIKASIEDTKAQIIADKANADRWKVAQVLQSAHDAHDALLAKQAQYEQLMQTAKDAPqaiENARNDLANAQKTIADA 728
Cdd:pfam05262 202 DLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLP---KPADTSSPKEDKQVAEN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 729 PAKAKEKEDAFAKaREAVEAAKKTVAAAEDLAKE--------KDKNAQTVADNAPTMGDvtnLTKKMEGLNAEAAKLREE 800
Cdd:pfam05262 279 QKREIEKAQIEIK-KNDEEALKAKDHKAFDLKQEskasekeaEDKELEAQKKREPVAED---LQKTKPQVEAQPTSLNED 354
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
530-840 |
1.49e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 530 ELKTQIAASQKTVADARTAVEAAQKTLADKQAAIntpgAEIDTARQEVTNKTTAQTEAEKQLTARKDEV-----TKAEAE 604
Cdd:pfam12128 461 ELLLQLENFDERIERAREEQEAANAEVERLQSEL----RQARKRRDQASEALRQASRRLEERQSALDELelqlfPQAGTL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 605 LTKLRASTPAAIAAAEKVLQQAntQLATAQKPPAPVAAVTAAEQDVTKIKASIEDTKAQIIADKANADRWKVAQV---LQ 681
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPE--LLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAeeaLQ 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 682 SAHDAHDA----LLAKQAQYEQLMQTAKDAPQAIENARND---LANAQKTIADAPAKAKEKEDAFA-KAREAVEAAKKTV 753
Cdd:pfam12128 615 SAREKQAAaeeqLVQANGELEKASREETFARTALKNARLDlrrLFDEKQSEKDKKNKALAERKDSAnERLNSLEAQLKQL 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 754 AAAEDLAKE---KDKNAQTVADNAPTMGDVTNLTKKMEGLNAEAAKLREERNSHSQGSPEYLAANTKYQA--------KK 822
Cdd:pfam12128 695 DKKHQAWLEeqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGvdpdviakLK 774
|
330
....*....|....*...
gi 494040510 823 AEITNTQTGIDRREREEH 840
Cdd:pfam12128 775 REIRTLERKIERIAVRRQ 792
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
545-775 |
1.52e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.89 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 545 ARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTEAE-----------------KQLTARKDEVTKAEAELTK 607
Cdd:PRK07735 15 ARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEakrraaaaakakaaalaKQKREGTEEVTEEEKAKAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 608 LRASTPAAIAAAE--KVLQQANTQLATAQKPPAPVAAVTAAEQDVTKIKASIEDTKAQIIADKANADRWKVAQVLQSAHD 685
Cdd:PRK07735 95 AKAAAAAKAKAAAlaKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 686 AHDALLAKQAQYEQLMQTAKDAPQAIENARNDLANAQKTIADAPAKAK------EKEDAFAKAREAveAAKKTVAAAEDL 759
Cdd:PRK07735 175 AKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKasqgngDSGDEDAKAKAI--AAAKAKAAAAAR 252
|
250
....*....|....*.
gi 494040510 760 AKEKDKNAQTVADNAP 775
Cdd:PRK07735 253 AKTKGAEGKKEEEPKQ 268
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
693-838 |
1.62e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 693 KQAQYEQLMQTAKDAPQAIENARNDLANAQKTIADapakakeKEDAFAKAREAVEAAKKTVAAAEDLAKEKDKN------ 766
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED-------PSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptc 290
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040510 767 AQTVADNAPTMGDVT----NLTKKMEGLNAEAAKLREERNSHSQGSPEYLAANTKYQAKKAEITNTQTGIDRRERE 838
Cdd:PHA02562 291 TQQISEGPDRITKIKdklkELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAA 366
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
273-403 |
1.64e-03 |
|
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 40.04 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 273 IYSTKDGKLVQsIKKHTDWVTAIAFSADGKYLA-SADRAGGIQIW----ESGTWKefnTLPGHKGMVTGLAFMP-G--VL 344
Cdd:COG0823 15 VVDLDGGEPRR-LTNSPGIDTSPAWSPDGRRIAfTSDRGGGPQIYvvdaDGGEPR---RLTFGGGYNASPSWSPdGkrLA 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040510 345 ASCGEDGKVTLW--DAKEGKEikswTAHAGGVEWVDFTPDGKLI-----SCGRDKIARVwDQTGKK 403
Cdd:COG0823 91 FVSRSDGRFDIYvlDLDGGAP----RRLTDGPGSPSWSPDGRRIvfssdRGGRPDLYVV-DLDGRK 151
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
524-841 |
1.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 524 AEKHLTELKTQIAASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEVTNKTTAQTEAEKQLTARKDEVTKAEA 603
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 604 ELTKLRASTpAAIAAAEKVLQQANTQLATAQKPPAPVAAVTAA-----EQDVTKIKASIEDTKAQIIADKANADRWKVAQ 678
Cdd:COG4372 109 EAEELQEEL-EELQKERQDLEQQRKQLEAQIAELQSEIAEREEelkelEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 679 VLQSAHDAHDALLAKQAQYEQLMQTAKDAPQAIENARN-DLANAQKTIADAPAKAKEKEDAFAKAREAVEAAKKTVAAAE 757
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDsLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 758 DLAKEKDKNAQTVADNAPTMGDVTNLTKKMEGLNAEAAKLREERNSHSQGSPEYLAANTKYQAKKAEITNTQTGIDRRER 837
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
....
gi 494040510 838 EEHG 841
Cdd:COG4372 348 VGLL 351
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
675-765 |
2.51e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.96 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 675 KVAQVLQSAHDAHDALLAKQAQYEQLMQTAKDAPQAIenarndLANAQKTiadapaKAKEKEDAFAKAREavEAAKKTVA 754
Cdd:cd06503 34 KIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEI------IEEARKE------AEKIKEEILAEAKE--EAERILEQ 99
|
90
....*....|.
gi 494040510 755 AAEDLAKEKDK 765
Cdd:cd06503 100 AKAEIEQEKEK 110
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
451-610 |
2.94e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 451 PTLAERATATAK-DLADAQIALPKLQdqltaAEAKLQTEKTNADNAYKAALAAAQKHKDEAQKIVEAHKSAVPSAEKHLT 529
Cdd:pfam00529 53 PTDYQAALDSAEaQLAKAQAQVARLQ-----AELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 530 ELKT---QIAASQKTVADARTAVEAAQKTLADKQAAINTPGAEIDTARQEvtnkttAQTEAEKQLTARKDEVTKAEAELT 606
Cdd:pfam00529 128 RRRVlapIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAE------NQAEVRSELSGAQLQIAEAEAELK 201
|
....
gi 494040510 607 KLRA 610
Cdd:pfam00529 202 LAKL 205
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
647-825 |
3.00e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.47 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 647 EQDVTKIKASIEDTKAQiiadKANADRwKVAQVLQSAHDAHDALLAKQAQYEQLmQTAKDAPQAIENARNDLANAQKTIA 726
Cdd:PRK05035 482 AKDKDAVAAALARVKAK----KAAATQ-PIVIKAGARPDNSAVIAAREARKAQA-RARQAEKQAAAAADPKKAAVAAAIA 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 727 DAPAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAKEkdKNAQTVADNAPTMGDVTNLTKKMEGLNAEAAKLREERNSHSQ 806
Cdd:PRK05035 556 RAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKA--KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQA 633
|
170
....*....|....*....
gi 494040510 807 GSPEYLAANTKYQAKKAEI 825
Cdd:PRK05035 634 NAEPEEPVDPRKAAVAAAI 652
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
231-371 |
3.29e-03 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.
Pssm-ID: 467722 [Multi-domain] Cd Length: 381 Bit Score: 40.73 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 231 LWDLKTGERIATIGNEFDQALAAD----------LSPDQQFVALGGPLKLLkIYSTKDGKLVQSIKKHTDWVTAIAfSAD 300
Cdd:cd20778 214 LWKPERGVRRILLDYGKGEEKLPVykmphlegwaVAGDKAFVPAVGEHRVL-VYDTNDWKFIKSIPLAGQPVFAVA-RPD 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494040510 301 GKYLA---SADRAGGIQIWESGTWKEFNTL-PGhkGMVTGLAFMP---GVLASCGEDGKVTLWDAKEGKEIKSWTAHA 371
Cdd:cd20778 292 GRYVWvnfSGPDNDTVQVIDTKTLKVVKTLePG--KRVLHMEFTPrgeAVYISVNDDNKVVVYDTRTFREIKEVPAKK 367
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
648-756 |
3.58e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 648 QDVTKIKASIEDTKAQIiadkanadrwkvAQVLQSAHDAHDALLAKQAQYEQLMQTAKDAPQAIENARNDLAN-AQKTIA 726
Cdd:TIGR04320 254 NSLAALQAKLATAQADL------------AAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQtAQNNLA 321
|
90 100 110
....*....|....*....|....*....|
gi 494040510 727 DAPAKAKEKEDAFAKAREAVEAAKKTVAAA 756
Cdd:TIGR04320 322 TAQAALANAEARLAKAKEALANLNADLAKK 351
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
535-737 |
3.91e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 535 IAASQKTVADARTAVEAAQKTlADKQAAIntpgAEIdTARQEVTNKTTAQTEAEKqltARKDEVTKAEAELTKLRAStpa 614
Cdd:COG2268 198 IRDARIAEAEAERETEIAIAQ-ANREAEE----AEL-EQEREIETARIAEAEAEL---AKKKAEERREAETARAEAE--- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 615 aiaaaekvlQQANTQLATAQKPPAPVAAVTAAEQDVTKIKASIEDTKAQIIAD---KANADRWKVAQVLQSAHDAHDALL 691
Cdd:COG2268 266 ---------AAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADvrkPAEAEKQAAEAEAEAEAEAIRAKG 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494040510 692 AKQAQYEQLMQTA--KDAPQAIENArndLANAQKTIADAPAKAKEKED 737
Cdd:COG2268 337 LAEAEGKRALAEAwnKLGDAAILLM---LIEKLPEIAEAAAKPLEKID 381
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
788-933 |
4.49e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 40.66 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 788 EGLNAEAAKLREERNSHSQGSPEYLAANTKYQAKKAEITNTQTGIDRREREEHGGPGSESRAGGIRQGPRcfrrsqawle 867
Cdd:PRK12678 84 AAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPA---------- 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040510 868 AAHQGRGGSREGDRPGQEKRRGRDPARRafaeghaADHQGRGNAEDGGRKSRRDCRQGSGSRQGRS 933
Cdd:PRK12678 154 TEARADAAERTEEEERDERRRRGDREDR-------QAEAERGERGRREERGRDGDDRDRRDRREQG 212
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
327-374 |
4.74e-03 |
|
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,
Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 37.26 E-value: 4.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 494040510 327 LPGHKGMVTGLAFMPG--VLASCGEDGKVTLWDAKEGKEIKSWTAHAGGV 374
Cdd:pfam12894 34 PDKEDLEVTSLAWRPDgkLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLI 83
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
587-827 |
4.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 587 AEKQLTARKDEVTKAEAELTKLrastpaaiaaaEKVLQQANTQLATAQKPPAPVaavtaaeqdvtkikASIEDTKAQIIa 666
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEA-----------EERLEALEAELDALQERREAL--------------QRLAEYSWDEI- 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 667 dkanaDRWKVAQVLQSAHDAHDALLAKQAQYEQLMQTAKDAPQAIENARNDLANAQKTIADAPAKAKEKEDAFAKAREAV 746
Cdd:COG4913 662 -----DVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 747 EAAKKTVAAAEDLAKEKDKNAQTVADNAPTMGDvtNLTKKMEGLNAEAAKLREE-RNSHSQGSPEY----------LAAN 815
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRE--NLEERIDALRARLNRAEEElERAMRAFNREWpaetadldadLESL 814
|
250
....*....|..
gi 494040510 816 TKYQAKKAEITN 827
Cdd:COG4913 815 PEYLALLDRLEE 826
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
574-783 |
5.29e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 574 RQEVTNKTTAQTEAEKQLTARKDEVTKAEAELTKLRAstpaaiaaaEKVLQQANTQLATAQKPPAPVAAVTAAEQDVTKI 653
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAA---------QEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 654 KASIEDTKAQIIADKANADRWKVAQVLQSAHDAHDAllAKQAQYEQLMQTAKDApqaienarndlanAQKTIADAPAKAK 733
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA--KKKAEAEAAAKAAAEA-------------KKKAEAEAKKKAA 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494040510 734 EKEDAFAKAREAVEAAKKTVAAAEDLAKEKDKNAQTVADNAPTMGDVTNL 783
Cdd:PRK09510 213 AEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
475-768 |
5.34e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 475 QDQLTAAEAKLQTEKTNadnaykaalaaAQKHKDEAQKIVEAHksavpsAEKHLTELKtQIAASQKTVADARTAVEAAQK 554
Cdd:PRK11281 33 GDLPTEADVQAQLDALN-----------KQKLLEAEDKLVQQD------LEQTLALLD-KIDRQKEETEQLKQQLAQAPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 555 TLADKQAAINTPGAEIDTARQEvTNKTTAQTEAEKQLTARKDEVTKAEAELTklrastpaaiaaaekvlqQANTQLATAQ 634
Cdd:PRK11281 95 KLRQAQAELEALKDDNDEETRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLA------------------EYNSQLVSLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 635 ----KPPAPVAAVTAAEQDVTKIKASIEDTKAQIIADkanadrwkvaqvLQSAHDAHDALLAKQAQYEQLMQTAKDAPQA 710
Cdd:PRK11281 156 tqpeRAQAALYANSQRLQQIRNLLKGGKVGGKALRPS------------QRVLLQAEQALLNAQNDLQRKSLEGNTQLQD 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040510 711 IENARNDLANA-----QKTIADAPA--KAKEKEDAFAKAREAVEAAKKTVAAAEDL-AKEKDKNAQ 768
Cdd:PRK11281 224 LLQKQRDYLTAriqrlEHQLQLLQEaiNSKRLTLSEKTVQEAQSQDEAARIQANPLvAQELEINLQ 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
568-803 |
8.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 568 AEIDTARQEVTnKTTAQTEAEKQLTARKDEVTKAEAELTKLRAstpaaiaaaekvLQQANTQLATAQKPPAPVAAVTAAE 647
Cdd:COG4913 235 DDLERAHEALE-DAREQIELLEPIRELAERYAAARERLAELEY------------LRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494040510 648 QDVTKIKASIEDTKAQIiaDKANADRwkvaQVLQSAHDAHDAllakqAQYEQLMQTAKDAPQAIENARNDLANAQKTIAD 727
Cdd:COG4913 302 AELARLEAELERLEARL--DALREEL----DELEAQIRGNGG-----DRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494040510 728 APAKAKEKEDAFAKAREAVEAAKKTVAAAEDLAKEkdknaqtvadnaptmgDVTNLTKKMEGLNAEAAKLREERNS 803
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEE----------------ALAEAEAALRDLRRELRELEAEIAS 430
|
|
| |
