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Conserved domains on  [gi|497293786|ref|WP_009608003|]
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MULTISPECIES: CpaF family protein [Eggerthella]

Protein Classification

CpaF family protein( domain architecture ID 10008984)

CpaF family protein is an ATPase associated with an integral membrane complex likely to act in pilus formation, secretion, or conjugal transfer; similar to Aggregatibacter actinomycetemcomitans TadA, a predicted secretion NTPase that is required for adherence

Gene Ontology:  GO:0005524|GO:0016887
PubMed:  11226268

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
14-428 9.92e-161

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


:

Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 458.48  E-value: 9.92e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  14 RDEAAVRLRgDAVGPDAVEALIRRLVEEIASESGISLPPYEFEGLASAMIDDFLRYGPLQRLLEDESVTEIMVNGGGIdl 93
Cdd:COG4962    2 SQELVERVR-RRLDREELREEVRAAVAEALRAEGLVLSDAEREALARAVLDELFGLGPLEPLLDDPDVTDIMVNGPDE-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  94 ddpalpfrapiVYVERAGRIEyRPDVEFDDAEHVRRIINKIAEQSGKRCDDAHAMGCAMLPGGrARATYVVPPIAPDGPA 173
Cdd:COG4962   79 -----------VFVERGGRLE-RTDVRFDSEEELRRLIERIAARVGRRLDESSPIVDARLPDG-SRVNAVIPPVARDGPS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 174 LNVRTFSSSMLGMEDLVRMGMLTDGMSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQT 253
Cdd:COG4962  146 LSIRKFRKRPLTLEDLVALGSLTPEMAEFLRAAVRARLNILVSGGTGSGKTTLLNALSGFIPPDERIVTIEDAAELQLQH 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 254 PHVERMQTREANTEGEGSVSMRELVALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTMV 333
Cdd:COG4962  226 PHVVRLETRPPNVEGAGEVTLRDLVRNALRMRPDRIIVGEVRGAEALDMLQAMNTGHDGSMSTLHANSARDALARLETLA 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 334 GYADGDLSRDVIVQQIAESLQggLVVHVERMQDGARRVTSIVAIDPLPEGSLVIprAELFVFDVEGVDAYGAVagewrac 413
Cdd:COG4962  306 LMAGENLPREAVRRQIASAID--LVVHLERLRDGRRRVTEIAEVTGMEGGRVVL--QPIFRFDPGGLDAAGGV------- 374
                        410
                 ....*....|....*
gi 497293786 414 gvqPQRIKERMRASG 428
Cdd:COG4962  375 ---RPRFLERLEAAG 386
 
Name Accession Description Interval E-value
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
14-428 9.92e-161

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 458.48  E-value: 9.92e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  14 RDEAAVRLRgDAVGPDAVEALIRRLVEEIASESGISLPPYEFEGLASAMIDDFLRYGPLQRLLEDESVTEIMVNGGGIdl 93
Cdd:COG4962    2 SQELVERVR-RRLDREELREEVRAAVAEALRAEGLVLSDAEREALARAVLDELFGLGPLEPLLDDPDVTDIMVNGPDE-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  94 ddpalpfrapiVYVERAGRIEyRPDVEFDDAEHVRRIINKIAEQSGKRCDDAHAMGCAMLPGGrARATYVVPPIAPDGPA 173
Cdd:COG4962   79 -----------VFVERGGRLE-RTDVRFDSEEELRRLIERIAARVGRRLDESSPIVDARLPDG-SRVNAVIPPVARDGPS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 174 LNVRTFSSSMLGMEDLVRMGMLTDGMSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQT 253
Cdd:COG4962  146 LSIRKFRKRPLTLEDLVALGSLTPEMAEFLRAAVRARLNILVSGGTGSGKTTLLNALSGFIPPDERIVTIEDAAELQLQH 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 254 PHVERMQTREANTEGEGSVSMRELVALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTMV 333
Cdd:COG4962  226 PHVVRLETRPPNVEGAGEVTLRDLVRNALRMRPDRIIVGEVRGAEALDMLQAMNTGHDGSMSTLHANSARDALARLETLA 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 334 GYADGDLSRDVIVQQIAESLQggLVVHVERMQDGARRVTSIVAIDPLPEGSLVIprAELFVFDVEGVDAYGAVagewrac 413
Cdd:COG4962  306 LMAGENLPREAVRRQIASAID--LVVHLERLRDGRRRVTEIAEVTGMEGGRVVL--QPIFRFDPGGLDAAGGV------- 374
                        410
                 ....*....|....*
gi 497293786 414 gvqPQRIKERMRASG 428
Cdd:COG4962  375 ---RPRFLERLEAAG 386
heli_sec_ATPase TIGR03819
helicase/secretion neighborhood ATPase; Members of this protein family comprise a distinct ...
17-374 2.13e-84

helicase/secretion neighborhood ATPase; Members of this protein family comprise a distinct clade of putative ATPase associated with an integral membrane complex likely to act in pilus formation, secretion, or conjugal transfer. The association of most members with a nearby gene for a DEAH-box helicase suggests a role in conjugal transfer.


Pssm-ID: 200328  Cd Length: 340  Bit Score: 262.27  E-value: 2.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   17 AAVRLR----GDAVGPDAVEALIRRlveeiasESGISLPPYEFEGLASAMIDDFLRYGPLQRLLEDESVTEIMVNGGGId 92
Cdd:TIGR03819   3 ERVRRRlaagSGPPTPAAVAAAVRA-------EAGRVLGDAEVLAAARALRRDLVGAGPLEPLLADPGVTDVLVNGPDE- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   93 lddpalpfrapiVYVERAGRIEyRPDVEFDDAEHVRRIINKIAEQSGKRCDDAHAMGCAMLPGGrARATYVVPPIAPDGP 172
Cdd:TIGR03819  75 ------------VWVDRGRGLE-RTDVRFPDEAAVRRLAQRLAAAAGRRLDDAQPWVDARLPDG-TRLHAVLPPVATDGT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  173 ALNVRTFSSSMLGMEDLVRMGMLTDGMSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQ 252
Cdd:TIGR03819 141 CLSLRVPRRRTFTLDELVAAGTIPPGVARLLRALVAARLAFLVSGGTGSGKTTLLSALLALVPPDERIVLVEDAAELRPD 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  253 TPHVERMQTREANTEGEGSVSMRELVALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTM 332
Cdd:TIGR03819 221 HPHVVRLEARPANVEGAGAVTLTDLVRQALRMRPDRIVVGEVRGAEVVDLLAALNTGHDGGAGTLHANSPADVPARLEAL 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 497293786  333 VgyADGDLSRDVIVQQIAESLQggLVVHVERMQDGARRVTSI 374
Cdd:TIGR03819 301 G--ALAGLDRAALHSQLAAALD--VVLHVRRTPRGRRRVAEI 338
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
199-377 1.29e-78

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.


Pssm-ID: 410874 [Multi-domain]  Cd Length: 177  Bit Score: 241.29  E-value: 1.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 199 MSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQTPHVERMQTREANtEGEGSVSMRELV 278
Cdd:cd01130    1 MAAFLRLAVRARKNILISGGTGSGKTTLLNALLSFIPPDERIVTIEDTRELQLPHPNVVHLLTRPGG-GEKGEVTMADLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 279 ALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTMVGYADGDLSRDVIVQQIAESLQggLV 358
Cdd:cd01130   80 KAALRMRPDRIIVGEVRGGEAYDMLQAMNTGHPGSITTIHANSAEDAIDRLATLVLEAGVNLDEEALRRLIASAID--VI 157
                        170
                 ....*....|....*....
gi 497293786 359 VHVERMQDGARRVTSIVAI 377
Cdd:cd01130  158 VHVKRLGDGVRRVTEIYEV 176
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
78-333 4.86e-45

Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.


Pssm-ID: 425681 [Multi-domain]  Cd Length: 269  Bit Score: 157.45  E-value: 4.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   78 DESVTEIMVNgggidlddpalPFRAPIVYVERAGRiEYRPdVEFDDAEHVRRIINKIAEQSGKRCDDAHAMGCAMLP--- 154
Cdd:pfam00437   9 DEGASDIHVE-----------PPERIVWIRFRVDG-VLRE-IPFPDADALARLISRIKVMARLDISERRPPQDGRLPlri 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  155 -GGRARATYVVPPIApDGPALNVRT--FSSSMLGMEDLVRMGMLTDGMSQFLRaavQARCPLVISGGTGSGKTTLLGALS 231
Cdd:pfam00437  76 gGKGVRVRVSTLPTA-GGEKLVIRLldPSNVALSLDELGMTGAQDEALLEFLR---QPRGNILVTGPTGSGKTTTLYAAL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  232 GFIP-PDERVITIEDTPELRLQTPHVERMQTReantegeGSVSMRELVALSLRRRPDRIIVGECRGAEAYDM-LQAMQTD 309
Cdd:pfam00437 152 GELNtRDENIVTVEDPVEIQLEGINQVQLNAR-------AGVTFADLLRAILRQDPDRIMVGEIRDLETAEIaLQAANTG 224
                         250       260
                  ....*....|....*....|....
gi 497293786  310 HPGsMTTVHANDPGNAISRLRTMV 333
Cdd:pfam00437 225 HLV-LSTLHTNSAAGALTRLQDMG 247
PRK13900 PRK13900
type IV secretion system ATPase VirB11; Provisional
61-374 3.14e-44

type IV secretion system ATPase VirB11; Provisional


Pssm-ID: 184381  Cd Length: 332  Bit Score: 157.23  E-value: 3.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  61 AMIDDFLRygPLQRLLEDESVTEIMVNgggidlddpalpfRAPIVYVERAGRIeYRPDVEFDDAEHVRRIINKIAEQSGK 140
Cdd:PRK13900   6 AALETYLE--PLKNIFAEDGVNEISIN-------------KPGEVWVEKKGDI-RCEQIPELDLSHLKALGRLVAQATEQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 141 RCDDAHAMGCAMLPGGrARATYVVPPIA-PDGPALNVRTFSSSMLGMEDLVRMGMLTDG--------------------- 198
Cdd:PRK13900  70 KISEEKPLLSATLPNG-YRIQIVFPPACeIGQIVYSIRKPSGMQLTLDDYEKMGAFDETateslvdeddvilnellaekk 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 199 MSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQTpHVERMQ-TREANTEGEGSVSMREL 277
Cdd:PRK13900 149 IKEFLEHAVISKKNIIISGGTSTGKTTFTNAALREIPAIERLITVEDAREIVLSN-HPNRVHlLASKGGQGRAKVTTQDL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 278 VALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTMVGYADGDLSRDVIVQQIAESLQggL 357
Cdd:PRK13900 228 IEACLRLRPDRIIVGELRGAEAFSFLRAINTGHPGSISTLHADSPAMAIEQLKLMVMQAGLGMPPDQIKKYILNVVD--I 305
                        330
                 ....*....|....*..
gi 497293786 358 VVHVERMQDGARRVTSI 374
Cdd:PRK13900 306 VVQLKRGSGGKRYVSEI 322
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
201-332 2.66e-14

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 72.48  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 201 QFLRAAVQARCPLVI-SGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLqtPHVERMQTREantegEGSVSMRELVA 279
Cdd:NF041000 118 QLLKQLLQRRSGLILfSGPTGSGKTTTMYSLARKLALNKQVITIEDPVEIKE--PNFLQLQVNE-----KAGMTYDTLLK 190
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497293786 280 LSLRRRPDRIIVGECRGAE-AYDMLQAMQTDHPgSMTTVHANDPGNAISRLRTM 332
Cdd:NF041000 191 AALRHRPDILIIGEIRDAEtAKAAIRAALTGHL-VLSTVHAKSAAGVIYRLLEL 243
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
212-291 2.82e-05

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: 43.90  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   212 PLVISGGTGSGKTTLLGALSGFIPPDERVItIEDTPELRLQTPHVERMQTREANTEGEGSVSMRELVALSLRRRPDRIIV 291
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGV-IYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVL 82
 
Name Accession Description Interval E-value
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
14-428 9.92e-161

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 458.48  E-value: 9.92e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  14 RDEAAVRLRgDAVGPDAVEALIRRLVEEIASESGISLPPYEFEGLASAMIDDFLRYGPLQRLLEDESVTEIMVNGGGIdl 93
Cdd:COG4962    2 SQELVERVR-RRLDREELREEVRAAVAEALRAEGLVLSDAEREALARAVLDELFGLGPLEPLLDDPDVTDIMVNGPDE-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  94 ddpalpfrapiVYVERAGRIEyRPDVEFDDAEHVRRIINKIAEQSGKRCDDAHAMGCAMLPGGrARATYVVPPIAPDGPA 173
Cdd:COG4962   79 -----------VFVERGGRLE-RTDVRFDSEEELRRLIERIAARVGRRLDESSPIVDARLPDG-SRVNAVIPPVARDGPS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 174 LNVRTFSSSMLGMEDLVRMGMLTDGMSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQT 253
Cdd:COG4962  146 LSIRKFRKRPLTLEDLVALGSLTPEMAEFLRAAVRARLNILVSGGTGSGKTTLLNALSGFIPPDERIVTIEDAAELQLQH 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 254 PHVERMQTREANTEGEGSVSMRELVALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTMV 333
Cdd:COG4962  226 PHVVRLETRPPNVEGAGEVTLRDLVRNALRMRPDRIIVGEVRGAEALDMLQAMNTGHDGSMSTLHANSARDALARLETLA 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 334 GYADGDLSRDVIVQQIAESLQggLVVHVERMQDGARRVTSIVAIDPLPEGSLVIprAELFVFDVEGVDAYGAVagewrac 413
Cdd:COG4962  306 LMAGENLPREAVRRQIASAID--LVVHLERLRDGRRRVTEIAEVTGMEGGRVVL--QPIFRFDPGGLDAAGGV------- 374
                        410
                 ....*....|....*
gi 497293786 414 gvqPQRIKERMRASG 428
Cdd:COG4962  375 ---RPRFLERLEAAG 386
heli_sec_ATPase TIGR03819
helicase/secretion neighborhood ATPase; Members of this protein family comprise a distinct ...
17-374 2.13e-84

helicase/secretion neighborhood ATPase; Members of this protein family comprise a distinct clade of putative ATPase associated with an integral membrane complex likely to act in pilus formation, secretion, or conjugal transfer. The association of most members with a nearby gene for a DEAH-box helicase suggests a role in conjugal transfer.


Pssm-ID: 200328  Cd Length: 340  Bit Score: 262.27  E-value: 2.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   17 AAVRLR----GDAVGPDAVEALIRRlveeiasESGISLPPYEFEGLASAMIDDFLRYGPLQRLLEDESVTEIMVNGGGId 92
Cdd:TIGR03819   3 ERVRRRlaagSGPPTPAAVAAAVRA-------EAGRVLGDAEVLAAARALRRDLVGAGPLEPLLADPGVTDVLVNGPDE- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   93 lddpalpfrapiVYVERAGRIEyRPDVEFDDAEHVRRIINKIAEQSGKRCDDAHAMGCAMLPGGrARATYVVPPIAPDGP 172
Cdd:TIGR03819  75 ------------VWVDRGRGLE-RTDVRFPDEAAVRRLAQRLAAAAGRRLDDAQPWVDARLPDG-TRLHAVLPPVATDGT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  173 ALNVRTFSSSMLGMEDLVRMGMLTDGMSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQ 252
Cdd:TIGR03819 141 CLSLRVPRRRTFTLDELVAAGTIPPGVARLLRALVAARLAFLVSGGTGSGKTTLLSALLALVPPDERIVLVEDAAELRPD 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  253 TPHVERMQTREANTEGEGSVSMRELVALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTM 332
Cdd:TIGR03819 221 HPHVVRLEARPANVEGAGAVTLTDLVRQALRMRPDRIVVGEVRGAEVVDLLAALNTGHDGGAGTLHANSPADVPARLEAL 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 497293786  333 VgyADGDLSRDVIVQQIAESLQggLVVHVERMQDGARRVTSI 374
Cdd:TIGR03819 301 G--ALAGLDRAALHSQLAAALD--VVLHVRRTPRGRRRVAEI 338
VirB11 COG0630
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ...
6-387 2.23e-81

Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440395 [Multi-domain]  Cd Length: 462  Bit Score: 258.47  E-value: 2.23e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   6 ERALKRAVRDEAAVRLRGDAVGPDAVEALIRRLVEEIASESGISLPPYEFEGLASAMIDDFLRYGPLQRLLEDESVTEIM 85
Cdd:COG0630   98 EELLEEEERLLEELLLLEEEDALEDLEVLLLRELDSLLKDYKIKVSEERLEKLLYYLLRDFVGYGKLDPLMRDPNIEDIS 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  86 VNGGGIDlddpalpfrapiVYVE--RAGRIEyrPDVEFDDAEHVRRIINKIAEQSGKRCDDAHAMGCAMLPGG-RARATY 162
Cdd:COG0630  178 CNGVGIP------------VYVYhrDYERIP--TNIVFESEEELDNFVVKLAQRSGKHISVARPIVDATLPDGsRIALTL 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 163 VvPPIAPDGPALNVRTFSSSMLGMEDLVRMGMLTDGMSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVIT 242
Cdd:COG0630  244 G-PEVSRRGSSFTIRKFREVPLTPIDLIEWGTLSPELAAYLWLLLENGKSVLVAGGTASGKTTLLNALLSFIPPDAKIVT 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 243 IEDTPELRLQTPHVERMQTREANTEGEGSVSMRELVALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHPGsMTTVHANDP 322
Cdd:COG0630  323 IEDTRELNLPHENWISLVTRESFGGEEGDVTMFDLLKAALRQRPDYIVVGEVRGEEAYTLFQAMATGHGV-LSTFHADSV 401
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497293786 323 GNAISRLRTmvgyADGDLSRDVIvqqiaESLqgGLVVHVERMQDG---ARRVTSIVAIDPLPEGSLVI 387
Cdd:COG0630  402 ESAINRLTS----PPINVPRTLL-----QAL--DLVVFQKRVRVGgkrVRRVTSIVEIVGYDPETGEI 458
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
199-377 1.29e-78

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.


Pssm-ID: 410874 [Multi-domain]  Cd Length: 177  Bit Score: 241.29  E-value: 1.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 199 MSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQTPHVERMQTREANtEGEGSVSMRELV 278
Cdd:cd01130    1 MAAFLRLAVRARKNILISGGTGSGKTTLLNALLSFIPPDERIVTIEDTRELQLPHPNVVHLLTRPGG-GEKGEVTMADLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 279 ALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTMVGYADGDLSRDVIVQQIAESLQggLV 358
Cdd:cd01130   80 KAALRMRPDRIIVGEVRGGEAYDMLQAMNTGHPGSITTIHANSAEDAIDRLATLVLEAGVNLDEEALRRLIASAID--VI 157
                        170
                 ....*....|....*....
gi 497293786 359 VHVERMQDGARRVTSIVAI 377
Cdd:cd01130  158 VHVKRLGDGVRRVTEIYEV 176
VirB11 TIGR02788
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of ...
76-374 2.29e-62

P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for DNA transfer. VirB11 is believed to be an ATPase. VirB11 is a homolog of the P-like conjugation system TrbB protein and the Flp pilus sytem protein TadA.


Pssm-ID: 274301  Cd Length: 308  Bit Score: 204.12  E-value: 2.29e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   76 LEDESVTEIMVNGGGIdlddpalpfrapiVYVERAGRIEyRPDVEFDDAEHVRRIINKIAEQSGKRCDDAHAMGCAMLPG 155
Cdd:TIGR02788   2 LDDEDVTEICINRPGE-------------VWVEGPGGWQ-RFDVPDLTFSHLMRLARAIASFSKQSISEENPILSATLPG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  156 GrARATYVVPPIAP-DGPALNVRTFSSSMLGMEDLVRMGML----------------------TDGMSQFLRAAVQARCP 212
Cdd:TIGR02788  68 G-ERVQIVIPPACEnDTVSITIRKPSLVDFSLDDYEEKGFFdtvraqsgtlsdndeqllelldAGDIKEFLRLAIASRKN 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQTP-HVERMQTREAntEGEGSVSMRELVALSLRRRPDRIIV 291
Cdd:TIGR02788 147 IIISGGTGSGKTTFLKSLVDEIPKDERIITIEDTREIFLPHPnYVHLFYSKGG--QGLAKVTPKDLLQSCLRMRPDRIIL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  292 GECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTMV--GYADGDLSRDVIVQQIAESLQggLVVHVERMQDGaR 369
Cdd:TIGR02788 225 GELRGDEAFDFIRAVNTGHPGSITTLHAGSPEEAFEQLALMVksSQAGLGLDFAYIVKLVREVID--IVVQINRRGGG-R 301

                  ....*
gi 497293786  370 RVTSI 374
Cdd:TIGR02788 302 KITEV 306
TrbB_P TIGR02782
P-type conjugative transfer ATPase TrbB; The TrbB protein is found in the trb locus of ...
74-383 3.46e-50

P-type conjugative transfer ATPase TrbB; The TrbB protein is found in the trb locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for plasmid conjugative transfer. TrbB is a homolog of the vir system VirB11 ATPase, and the Flp pilus sytem ATPase TadA. [Cellular processes, Conjugation]


Pssm-ID: 274297  Cd Length: 299  Bit Score: 172.23  E-value: 3.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   74 RLLEDESVTEIMVNGGGIdlddpalpfrapiVYVERAGRIEYrpDVEFDDAEHVRRIINKIAEQSGKRCDDAHAMGCAML 153
Cdd:TIGR02782  12 AALDDPGVVEIMLNPDGR-------------LWVERLGSGMS--PLGEMSPADAQRIIGLVADYLGTEVDRDKPIVEGEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  154 PGGRARATYVVPPIAPdGPALNVRTFSSSMLGMEDLVRMGMLTDGMSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGF 233
Cdd:TIGR02782  77 PLDGSRFEGLIPPVVA-APSFAIRKKAVAVFTLDDYVEAGIMTAAQRDVLREAVLARKNILVVGGTGSGKTTLANALLAE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  234 I---PPDERVITIEDTPELRLQTPHVERMQTREantegeGSVSMRELVALSLRRRPDRIIVGECRGAEAYDMLQAMQTDH 310
Cdd:TIGR02782 156 IaknDPTDRVVIIEDTRELQCAAPNVVQLRTSD------DAISMTRLLKATLRLRPDRIIVGEVRGGEALDLLKAWNTGH 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497293786  311 PGSMTTVHANDPGNAISRLRTMVGYAdgdlSRDVIVQQIAESLQggLVVHVERMQDGaRRVTSIVAIDPLPEG 383
Cdd:TIGR02782 230 PGGIATIHANNAKAALDRLEQLIQEV----SVTPMQTLIAEAVD--LVIFIARTPAG-RRVQEIAKVKGFDDG 295
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
78-333 4.86e-45

Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.


Pssm-ID: 425681 [Multi-domain]  Cd Length: 269  Bit Score: 157.45  E-value: 4.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   78 DESVTEIMVNgggidlddpalPFRAPIVYVERAGRiEYRPdVEFDDAEHVRRIINKIAEQSGKRCDDAHAMGCAMLP--- 154
Cdd:pfam00437   9 DEGASDIHVE-----------PPERIVWIRFRVDG-VLRE-IPFPDADALARLISRIKVMARLDISERRPPQDGRLPlri 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  155 -GGRARATYVVPPIApDGPALNVRT--FSSSMLGMEDLVRMGMLTDGMSQFLRaavQARCPLVISGGTGSGKTTLLGALS 231
Cdd:pfam00437  76 gGKGVRVRVSTLPTA-GGEKLVIRLldPSNVALSLDELGMTGAQDEALLEFLR---QPRGNILVTGPTGSGKTTTLYAAL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  232 GFIP-PDERVITIEDTPELRLQTPHVERMQTReantegeGSVSMRELVALSLRRRPDRIIVGECRGAEAYDM-LQAMQTD 309
Cdd:pfam00437 152 GELNtRDENIVTVEDPVEIQLEGINQVQLNAR-------AGVTFADLLRAILRQDPDRIMVGEIRDLETAEIaLQAANTG 224
                         250       260
                  ....*....|....*....|....
gi 497293786  310 HPGsMTTVHANDPGNAISRLRTMV 333
Cdd:pfam00437 225 HLV-LSTLHTNSAAGALTRLQDMG 247
PRK13900 PRK13900
type IV secretion system ATPase VirB11; Provisional
61-374 3.14e-44

type IV secretion system ATPase VirB11; Provisional


Pssm-ID: 184381  Cd Length: 332  Bit Score: 157.23  E-value: 3.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  61 AMIDDFLRygPLQRLLEDESVTEIMVNgggidlddpalpfRAPIVYVERAGRIeYRPDVEFDDAEHVRRIINKIAEQSGK 140
Cdd:PRK13900   6 AALETYLE--PLKNIFAEDGVNEISIN-------------KPGEVWVEKKGDI-RCEQIPELDLSHLKALGRLVAQATEQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 141 RCDDAHAMGCAMLPGGrARATYVVPPIA-PDGPALNVRTFSSSMLGMEDLVRMGMLTDG--------------------- 198
Cdd:PRK13900  70 KISEEKPLLSATLPNG-YRIQIVFPPACeIGQIVYSIRKPSGMQLTLDDYEKMGAFDETateslvdeddvilnellaekk 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 199 MSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQTpHVERMQ-TREANTEGEGSVSMREL 277
Cdd:PRK13900 149 IKEFLEHAVISKKNIIISGGTSTGKTTFTNAALREIPAIERLITVEDAREIVLSN-HPNRVHlLASKGGQGRAKVTTQDL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 278 VALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTMVGYADGDLSRDVIVQQIAESLQggL 357
Cdd:PRK13900 228 IEACLRLRPDRIIVGELRGAEAFSFLRAINTGHPGSISTLHADSPAMAIEQLKLMVMQAGLGMPPDQIKKYILNVVD--I 305
                        330
                 ....*....|....*..
gi 497293786 358 VVHVERMQDGARRVTSI 374
Cdd:PRK13900 306 VVQLKRGSGGKRYVSEI 322
PRK13894 PRK13894
conjugal transfer ATPase TrbB; Provisional
70-377 9.44e-39

conjugal transfer ATPase TrbB; Provisional


Pssm-ID: 184377  Cd Length: 319  Bit Score: 142.19  E-value: 9.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  70 GP-LQRLLEDESVTEIMVNGGGIdlddpalpfrapiVYVERAG-RIEYRPDVEFDDAEhvrRIINKIAEQSGKRCDDAHA 147
Cdd:PRK13894  23 GPeLLAALNDPKTVEIMLNADGK-------------LWQERLGePMRCIGTLRVAQAQ---AIIETIAGYHGKEVTRSKP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 148 MGCAMLPGGRARATYVVPPIAPdGPALNVRTFSSSMLGMEDLVRMGMLTDGMSQFLRAAVQA-RCPLVIsGGTGSGKTTL 226
Cdd:PRK13894  87 ILEGELPLDGSRFAGQLPPVVP-APTFAIRKKAVAIFTLDQYVERGIMTAAQREAIIAAVRAhRNILVI-GGTGSGKTTL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 227 LGALSG---FIPPDERVITIEDTPELRLQTPHVERMQTREantegegSVSMRELVALSLRRRPDRIIVGECRGAEAYDML 303
Cdd:PRK13894 165 VNAIINemvIQDPTERVFIIEDTGEIQCAAENYVQYHTSI-------DVNMTALLKTTLRMRPDRILVGEVRGPEALDLL 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497293786 304 QAMQTDHPGSMTTVHANDPGNAISRLRTMVGYADGdlSRDVIVQQIAESLQggLVVHVERmQDGARRVTSIVAI 377
Cdd:PRK13894 238 MAWNTGHEGGAATLHANNAKAGLDRLKSLISMHPD--APKPIEPLIGEAVH--VVVHIAR-TPGGRRIQEILEV 306
PRK13833 PRK13833
conjugal transfer protein TrbB; Provisional
76-378 2.31e-36

conjugal transfer protein TrbB; Provisional


Pssm-ID: 172360 [Multi-domain]  Cd Length: 323  Bit Score: 136.08  E-value: 2.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  76 LEDESVTEIMVNGGGIdlddpalpfrapiVYVERAGR-IEYRPDVEFDDAEHVrriINKIAEQSGKRCDDAHAMGCAMLP 154
Cdd:PRK13833  26 LDDATVVEIMLNPDGK-------------LFIERLGHgVAPAGEMSAAAAEVV---IGSVAHALQSEADDERPIISGELP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 155 GGRARATYVVPPIAPdGPALNVRTFSSSMLGMEDLVRMGMLTDGMSQFLRAAVQARCPLVISGGTGSGKTTLLGALSGFI 234
Cdd:PRK13833  90 IGGHRFEGLLPPVVS-GPAFTIRRRASRLIPLDDYVTSKIMTEAQASVIRSAIDSRLNIVISGGTGSGKTTLANAVIAEI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 235 ---PPDERVITIEDTPELRLQTPHVERMQTREantegegSVSMRELVALSLRRRPDRIIVGECRGAEAYDMLQAMQTDHP 311
Cdd:PRK13833 169 vasAPEDRLVILEDTAEIQCAAENAVALHTSD-------TVDMARLLKSTMRLRPDRIIVGEVRDGAALTLLKAWNTGHP 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497293786 312 GSMTTVHANDPGNAISRLRTMVGYADGDLSRDVIVQQIaeslqgGLVVHVERMQDGaRRVTSIVAID 378
Cdd:PRK13833 242 GGVTTIHSNTAMSALRRLEQLTAEASQQPMQEVIGEAV------DLIVSIERTGKG-RRVREVIHVE 301
PRK13851 PRK13851
type IV secretion system protein VirB11; Provisional
71-333 1.85e-27

type IV secretion system protein VirB11; Provisional


Pssm-ID: 172375  Cd Length: 344  Bit Score: 111.91  E-value: 1.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786  71 PLQRLLEDESVTEIMVNGGGIdlddpalpfrapiVYVERAGRIEYRP-DVEFDDAEHVRRIINKIAEQS-GKRcddaHAM 148
Cdd:PRK13851  13 PVLEWLDDPRTEEVAINRPGE-------------AFVRQAGVFTKFPlPLSYDDLEDIAILAGALRKQDvGPR----NPL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 149 GCAMLPGGRaRATYVVPPIAPDGP-ALNVRTFSSSMLGM---------------------EDLVRMGMLTD----GMSQF 202
Cdd:PRK13851  76 CATELPGGE-RLQICLPPTVPSGTvSLTIRRPSSRVSELkevssrydasrwnqwqerrkrRDQLDEAILRHydngDLEAF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 203 LRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQTP-HVERMQTReaNTEGEGSVSMRELVALS 281
Cdd:PRK13851 155 LHACVVGRLTMLLCGPTGSGKTTMSKTLISAIPPQERLITIEDTLELVIPHEnHVRLLYSK--NGAGLGAVTAEHLLQAS 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497293786 282 LRRRPDRIIVGECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLRTMV 333
Cdd:PRK13851 233 LRMRPDRILLGEMRDDAAWAYLSEVVSGHPGSISTIHGANPVQGFKKLFSLV 284
type_II_IV_secretion_ATPases cd19477
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ...
213-361 4.16e-22

type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family 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. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410885 [Multi-domain]  Cd Length: 168  Bit Score: 92.46  E-value: 4.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELrlqtphVERMQTREANTEGEGSVSMRELVALSLRRRPDRIIVG 292
Cdd:cd19477   13 VIVCGGTGSGKTTYIKSILEFIPKEERIISIEDTEEI------VFKHHKNYTQLFFGGNITSADCLKSCLRQRPDRIILG 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497293786 293 ECRGAEAYDMLQAMQTDHPGSMTTVHANDPGNAISRLR--TMVGYADGDLSRDVIVQQIAESLQGglVVHV 361
Cdd:cd19477   87 ELRSSEAYDFYNVLCSGHKGTLTTLHAGSSEEAFIRLAn*SSSNSAARNIKFESLIEGFKDLIDG--IVHI 155
DotB_TraJ cd19516
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ...
207-358 2.01e-21

dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.


Pssm-ID: 410924 [Multi-domain]  Cd Length: 179  Bit Score: 90.90  E-value: 2.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 207 VQARCPL----VISGGTGSGKTTLLGALSGFI----PPDERVITIEDTPELRL---QTPHVERMQT---REANTEGEGsv 272
Cdd:cd19516    4 VEALFPReglvYVAGATGSGKSTLLAAIYRYIlendPPDRKIITYEDPIEFVYdgiKSKHSIIVQSqipRHFKSFAKA-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 273 sMRElvalSLRRRPDRIIVGECRGAEAYD-MLQAMQTDHPgSMTTVHANDPGNAISRLRTMV--------GYADGDLSRD 343
Cdd:cd19516   82 -VRE----ALRRKPSLIGVGELRDQETISaAVEASLTGHP-VYSTVHTKSVAETIRRLISLFppeerdaaAYDLLSTLRF 155
                        170
                 ....*....|....*
gi 497293786 344 VIVQQIAESLQGGLV 358
Cdd:cd19516  156 IIVQRLVRTTDGKRV 170
PulE-GspE-like cd01129
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ...
213-332 9.26e-18

PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.


Pssm-ID: 410873 [Multi-domain]  Cd Length: 159  Bit Score: 80.22  E-value: 9.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 213 LVISGGTGSGKTTLLGA-LSGFIPPDERVITIEDTPELRLqtPHVERMQTREantegEGSVSMRELVALSLRRRPDRIIV 291
Cdd:cd01129   14 ILVTGPTGSGKTTTLYAmLRELNGPERNIITIEDPVEYQI--PGINQSQVNE-----KIGLTFADALRAILRQDPDIIMV 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 497293786 292 GECRGAEAYDM-LQAMQTDHPgSMTTVHANDPGNAISRLRTM 332
Cdd:cd01129   87 GEIRDAETAEIaIRAALTGHL-VLSTLHTNDALGAITRLLDM 127
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
201-332 2.66e-14

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 72.48  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 201 QFLRAAVQARCPLVI-SGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLqtPHVERMQTREantegEGSVSMRELVA 279
Cdd:NF041000 118 QLLKQLLQRRSGLILfSGPTGSGKTTTMYSLARKLALNKQVITIEDPVEIKE--PNFLQLQVNE-----KAGMTYDTLLK 190
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497293786 280 LSLRRRPDRIIVGECRGAE-AYDMLQAMQTDHPgSMTTVHANDPGNAISRLRTM 332
Cdd:NF041000 191 AALRHRPDILIIGEIRDAEtAKAAIRAALTGHL-VLSTVHAKSAAGVIYRLLEL 243
PilT COG2805
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ...
171-371 6.14e-13

Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];


Pssm-ID: 442056  Cd Length: 342  Bit Score: 69.35  E-value: 6.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 171 GPALNVRTFSSSMLGMEDLvrmgmltdGMSQFLRAAVQARCPLV-ISGGTGSGKTTLLGALSGFI--PPDERVITIEDTP 247
Cdd:COG2805   93 GVAAVLRLIPSEIPTLEEL--------GLPPVLKELAELPRGLVlVTGPTGSGKSTTLAAMIDYIneTRAKHIITIEDPI 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 248 ELRlqtpHVERMqtreantegeGSVSMREL--------VAL--SLRRRPDRIIVGECRGAEAYDM-LQAMQTDHPgSMTT 316
Cdd:COG2805  165 EFV----HKHKK----------SLINQREVgrdtpsfaNALraALREDPDVILVGEMRDLETIEAaLTAAETGHL-VFAT 229
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497293786 317 VHANDPGNAISRlrtMVGYADGDlSRDVIVQQIAESLQG----GLVvhveRMQDGARRV 371
Cdd:COG2805  230 LHTNSAAQTIDR---IIDVFPPE-EQAQIRSQLAESLRGvisqRLL----PRADGGGRV 280
PilT cd01131
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ...
215-371 4.00e-09

Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.


Pssm-ID: 410875 [Multi-domain]  Cd Length: 223  Bit Score: 56.78  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 215 ISGGTGSGKTTLLGALSGFIPPDER--VITIEDTPELRlqtpHVERMQT---REAnteGEGSVSMRELVALSLRRRPDRI 289
Cdd:cd01131   26 VTGPTGSGKSTTLAAMIDYINETRSkhIITIEDPIEFV----HKHKKSLinqREV---GRDTESFAAALRAALREDPDVI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 290 IVGECRGAEAYDM-LQAMQTDHPgSMTTVHANDPGNAISRLRTMV-GYAdgdlsRDVIVQQIAESLQGGLVVHVERMQDG 367
Cdd:cd01131   99 LVGEMRDLETIELaLTAAETGHL-VFSTLHTNSAAQTIDRIIDVFpPEQ-----QEQVRIQLASSLRGVISQRLLPKKDG 172

                 ....
gi 497293786 368 ARRV 371
Cdd:cd01131  173 GGRV 176
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
180-332 1.27e-08

Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442055 [Multi-domain]  Cd Length: 561  Bit Score: 57.13  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 180 SSSMLGMEDLvrmGMLTDGMSQFLRAAVQarcP---LVISGGTGSGKTTLL-GALSGFIPPDERVITIEDTPELRLqtPH 255
Cdd:COG2804  286 SAALLDLEQL---GFSPDQLERLRRLIRR---PhgiILVTGPTGSGKTTTLyAALNELNTPERNIITVEDPVEYQL--PG 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 256 VERMQTRE------ANTegegsvsMRELvalsLRRRPDRIIVGECRGAEAYDM-LQAMQTDHpGSMTTVHAND-PGnAIS 327
Cdd:COG2804  358 INQVQVNPkigltfASA-------LRSI----LRQDPDVIMVGEIRDLETAEIaVQAALTGH-LVLSTLHTNDaPS-AIT 424

                 ....*
gi 497293786 328 RLRTM 332
Cdd:COG2804  425 RLLDM 429
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
212-291 2.82e-05

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: 43.90  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786   212 PLVISGGTGSGKTTLLGALSGFIPPDERVItIEDTPELRLQTPHVERMQTREANTEGEGSVSMRELVALSLRRRPDRIIV 291
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGV-IYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVL 82
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
213-258 4.60e-05

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 43.41  E-value: 4.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 497293786  213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQTPHVER 258
Cdd:pfam00005  14 LALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK 59
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
213-258 1.38e-04

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 42.23  E-value: 1.38e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQTPHVER 258
Cdd:cd00267   28 VALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR 73
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
213-247 2.55e-04

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 42.08  E-value: 2.55e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTP 247
Cdd:COG4133   31 LALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP 65
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
213-247 2.90e-04

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 41.21  E-value: 2.90e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTP 247
Cdd:cd03228   31 VAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD 65
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
213-263 1.06e-03

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 40.63  E-value: 1.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTpELRLQTPHVERMQTRE 263
Cdd:cd03256   30 VALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT-DINKLKGKALRQLRRQ 79
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
203-247 1.48e-03

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 40.73  E-value: 1.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 497293786  203 LRAAVQARCPLVISGGTGSGKTTLLGALSGFIPPDERVITIEDTP 247
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP 385
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
213-258 1.82e-03

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 40.07  E-value: 1.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPelrLQTPHVER 258
Cdd:PRK11248  30 LVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP---VEGPGAER 72
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
213-247 1.94e-03

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 39.37  E-value: 1.94e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTP 247
Cdd:cd03225   30 VLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKD 64
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
220-286 2.59e-03

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 39.26  E-value: 2.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497293786 220 GSGKTTLLGALSGFIPPDERVITIEDTPelrlqtphVERMQTREA---------NTEGEGSVSMRELVALSlrRRP 286
Cdd:COG1120   37 GSGKSTLLRALAGLLKPSSGEVLLDGRD--------LASLSRRELarriayvpqEPPAPFGLTVRELVALG--RYP 102
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
213-247 2.73e-03

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 39.04  E-value: 2.73e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTP 247
Cdd:cd03259   29 LALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD 63
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
213-247 3.14e-03

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 38.98  E-value: 3.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTP 247
Cdd:PRK13548  31 VAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP 65
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
213-252 3.36e-03

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 38.49  E-value: 3.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 497293786  213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPELRLQ 252
Cdd:TIGR01189  29 LQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR 68
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
220-263 4.29e-03

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 38.19  E-value: 4.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 497293786 220 GSGKTTLLGALSGFIPPDERVITIEDTPelrlqtphVERMQTRE 263
Cdd:cd03214   35 GAGKSTLLKTLAGLLKPSSGEILLDGKD--------LASLSPKE 70
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
213-258 4.47e-03

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 38.22  E-value: 4.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTPelrLQTPHVER 258
Cdd:cd03293   33 VALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP---VTGPGPDR 75
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
213-247 5.42e-03

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 38.08  E-value: 5.42e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 497293786 213 LVISGGTGSGKTTLLGALSGFIPPDERVITIEDTP 247
Cdd:COG1122   30 VAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD 64
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
217-290 6.00e-03

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 37.41  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497293786 217 GGTGSGKTTLLGALSGFIPPDERVITIEDTPelrlqtphVERMQTREANTEGEG-----SVSMRELVAL--SLRRRPDRI 289
Cdd:cd03216   33 GENGAGKSTLMKILSGLYKPDSGEILVDGKE--------VSFASPRDARRAGIAmvyqlSVGERQMVEIarALARNARLL 104

                 .
gi 497293786 290 I 290
Cdd:cd03216  105 I 105
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
220-247 7.77e-03

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 37.91  E-value: 7.77e-03
                         10        20
                 ....*....|....*....|....*...
gi 497293786 220 GSGKTTLLGALSGFIPPDERVITIEDTP 247
Cdd:COG4555   37 GAGKTTLLRMLAGLLKPDSGSILIDGED 64
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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