|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-479 |
4.74e-177 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 514.41 E-value: 4.74e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 9 VPAHISLLHVEQEVAGDDTPALQSVLESDSVREDLLRRERELTAQ-------IAAGRAEGSE---------AAELAEIYA 72
Cdd:PLN03073 231 IPKNCQILHVEQEVVGDDTTALQCVLNTDIERTQLLEEEAQLVAQqrelefeTETGKGKGANkdgvdkdavSQRLEEIYK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 73 KLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTW 152
Cdd:PLN03073 311 RLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 153 PSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQ 232
Cdd:PLN03073 391 PKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 233 VQSKLKMLEKLPELKPVDKESEVVMKFPDGFEKFSPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKST 312
Cdd:PLN03073 471 VQSRIKALDRLGHVDAVVNDPDYKFEFPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKST 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 313 MLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPLASLSG 392
Cdd:PLN03073 551 ILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSG 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 393 GQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGFD 472
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFH 710
|
....*..
gi 1189438346 473 QYRALLQ 479
Cdd:PLN03073 711 DYKKTLQ 717
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-476 |
2.05e-175 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 502.67 E-value: 2.05e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 6 SLRVPAHISLLHVEQEV-AGDDTPALQSVLESDSVREDLLRRERELTAQIAAGRAEGseaAELAEIYAKLEEIEADKAPA 84
Cdd:COG0488 54 EVSIPKGLRIGYLPQEPpLDDDLTVLDTVLDGDAELRALEAELEELEAKLAEPDEDL---ERLAELQEEFEALGGWEAEA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 85 RASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRN 164
Cdd:COG0488 131 RAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 165 FLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLP 244
Cdd:COG0488 211 FLDRVATRILELDRGKLTLYPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 245 ELKPVDKESEVVMKFPDGfEKFSPPILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPV 324
Cdd:COG0488 291 REEPPRRDKTVEIRFPPP-ERLGKKVLELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 325 RGIRHAHRNLKIGYFSQHHvEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMT 404
Cdd:COG0488 369 SGTVKLGETVKIGYFDQHQ-EELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLL 447
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 405 MPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGFDQYRA 476
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-486 |
4.75e-115 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 352.55 E-value: 4.75e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 6 SLRVPAHISLLHVEQEVAGDDTPALQSVLESDsvredllRRERELTAQIAAGRAEGSEAAeLAEIYAKLEEIEADKAPAR 85
Cdd:PRK10636 57 SYTFPGNWQLAWVNQETPALPQPALEYVIDGD-------REYRQLEAQLHDANERNDGHA-IATIHGKLDAIDAWTIRSR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 86 ASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNF 165
Cdd:PRK10636 129 AASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 166 LNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPE 245
Cdd:PRK10636 209 LDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 246 LKP--VDKESEVVMKFPdgfEKFSPPILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP 323
Cdd:PRK10636 289 IAPahVDNPFHFSFRAP---ESLPNPLLKMEKVSAGYGDR-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 324 VRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQM 403
Cdd:PRK10636 365 VSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALI 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 404 TMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGFDQYRALLQEQFR 483
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQK 524
|
...
gi 1189438346 484 REG 486
Cdd:PRK10636 525 QEN 527
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
59-474 |
3.00e-84 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 269.45 E-value: 3.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 59 AEGSEAAELAEIYAkleEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:PRK15064 111 EDGMKVADLEVKFA---EMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 139 VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSK---QERLLNQQREYEAQQqyrQH 215
Cdd:PRK15064 188 INTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAAtqaRERLLADNAKKKAQI---AE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 216 IQVFIDRFRYNANRASQVQSKLKMLEK--LPELKPVDKESEVVmKFPDGfEKFSPPILQLDEVDFYYDPKhVIFSRLSVS 293
Cdd:PRK15064 265 LQSFVSRFSANASKAKQATSRAKQIDKikLEEVKPSSRQNPFI-RFEQD-KKLHRNALEVENLTKGFDNG-PLFKNLNLL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 294 ADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLAR-KFPGRPEEEYRHQ 372
Cdd:PRK15064 342 LEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLTLFDWMSQwRQEGDDEQAVRGT 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 373 LGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLV 452
Cdd:PRK15064 422 LGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSL 501
|
410 420
....*....|....*....|..
gi 1189438346 453 CRELWVCEGGGVTRVEGGFDQY 474
Cdd:PRK15064 502 ATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
66-471 |
1.08e-63 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 217.90 E-value: 1.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 66 ELAEIYAKLEEIEADKAPARASVILAGLGFTPKMqqqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWL 145
Cdd:PRK11147 119 ELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 146 ENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERL---LNQQREYE---AQQQY--RQHIQ 217
Cdd:PRK11147 196 EGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALrveELQNAEFDrklAQEEVwiRQGIK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 218 VFIDRF--RYNANRA-----SQ---VQSKLKMleklpELKPVDKESEVVmkfpdgFEkfsppilqLDEVDFYYDPKHVI- 286
Cdd:PRK11147 276 ARRTRNegRVRALKAlrrerSErreVMGTAKM-----QVEEASRSGKIV------FE--------MENVNYQIDGKQLVk 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 287 -FSRLSVSADlesRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHvEQLDLNVSAVELLAR-----K 360
Cdd:PRK11147 337 dFSAQVQRGD---KIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHR-AELDPEKTVMDNLAEgkqevM 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 361 FPGRPeeeyRHQLG---RYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG 437
Cdd:PRK11147 413 VNGRP----RHVLGylqDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG 488
|
410 420 430
....*....|....*....|....*....|....*
gi 1189438346 438 GVILVSHDERFIRLVCRELWVCEG-GGVTRVEGGF 471
Cdd:PRK11147 489 TVLLVSHDRQFVDNTVTECWIFEGnGKIGRYVGGY 523
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-476 |
9.15e-55 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 192.07 E-value: 9.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 19 EQEVAGDDTPALQSVLEsDSVRE--DLLRRERELTAQIAAgraEGSEAAELAEIYAKLEE-IEADKA---PARASVILAG 92
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVE-EGVAEikDALDRFNEISAKYAE---PDADFDKLAAEQAELQEiIDAADAwdlDSQLEIAMDA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 93 LGFTPKmqQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATD 172
Cdd:TIGR03719 150 LRCPPW--DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGW 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 173 IIHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIdrfRYNAnRASQVQSK--LKMLEKLpelkpvd 250
Cdd:TIGR03719 228 ILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWV---RQSP-KGRQAKSKarLARYEEL------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 251 kESEVVMKFPDGFEKFSPP-------ILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP 323
Cdd:TIGR03719 297 -LSQEFQKRNETAEIYIPPgprlgdkVIEAENLTKAFGDK-LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 324 VRGIRHAHRNLKIGYFSQHHvEQLDLNVSAVELLA----------RKFPGRpeeEYrhqLGRYGISGELAMRPLASLSGG 393
Cdd:TIGR03719 375 DSGTIEIGETVKLAYVDQSR-DALDPNKTVWEEISggldiiklgkREIPSR---AY---VGRFNFKGSDQQKKVGQLSGG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 394 QKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGG-VTRVEGGFD 472
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDShVEWFEGNFS 527
|
....
gi 1189438346 473 QYRA 476
Cdd:TIGR03719 528 EYEE 531
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
271-463 |
6.92e-50 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 167.24 E-value: 6.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQhhveqldln 350
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 351 vsavellarkfpgrpeeeyrhqlgrygisgelamrplasLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGR 430
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 1189438346 431 ALNNFRGGVILVSHDERFIRLVCRELWVCEGGG 463
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-476 |
1.57e-46 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 169.91 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 19 EQEVAGDDTpalQSVLES--DSVRE--DLLRRERELTAQIAAGRAEGSE-AAELAEIYAKLEEIEADKAPARASVILAGL 93
Cdd:PRK11819 76 PQEPQLDPE---KTVRENveEGVAEvkAALDRFNEIYAAYAEPDADFDAlAAEQGELQEIIDAADAWDLDSQLEIAMDAL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 94 GFTPKmqQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDI 173
Cdd:PRK11819 153 RCPPW--DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 174 IHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIdrfRYNAnRASQVQSK--LKMLEKLpelkpVDK 251
Cdd:PRK11819 231 LELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWV---RQSP-KARQAKSKarLARYEEL-----LSE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 252 ESEvvmKFPDGFEKFSPP-------ILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPV 324
Cdd:PRK11819 302 EYQ---KRNETNEIFIPPgprlgdkVIEAENLSKSFGDR-LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPD 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 325 RGIRHAHRNLKIGYFSQHHvEQLDLN------VSA----VELLARKFPGRpeeEYrhqLGRYGISGELAMRPLASLSGGQ 394
Cdd:PRK11819 378 SGTIKIGETVKLAYVDQSR-DALDPNktvweeISGgldiIKVGNREIPSR---AY---VGRFNFKGGDQQKKVGVLSGGE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 395 KSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGG-VTRVEGGFDQ 473
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSqVEWFEGNFQE 530
|
...
gi 1189438346 474 YRA 476
Cdd:PRK11819 531 YEE 533
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
282-485 |
1.58e-41 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 155.22 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 282 PKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNV---------S 352
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVldtvldgdaE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 353 AVELLARKF-----PGRPEEEYRHQ----------------------LGRYGISGELAMRPLASLSGGQKSRVAFAQMTM 405
Cdd:COG0488 89 LRALEAELEeleakLAEPDEDLERLaelqeefealggweaearaeeiLSGLGFPEEDLDRPVSELSGGWRRRVALARALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 406 PCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGFDQYRALLQEQFRRE 485
Cdd:COG0488 169 SEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRAERLEQE 248
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
107-180 |
1.25e-38 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 137.19 E-value: 1.25e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQR 180
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
267-461 |
2.16e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL-----KIGYFS 340
Cdd:COG1121 3 MMPAIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtVRLFGKPPrrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 341 QHHVEQLDLNVSAVELLA------RKFPGRPEEEYR----HQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNF 410
Cdd:COG1121 82 QRAEVDWDFPITVRDVVLmgrygrRGLFRRPSRADReavdEALERVGLE-DLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 411 YILDEPTNHLDMETIEALGRALNNFRG---GVILVSHD-----ERFIRLVC--RELwVCEG 461
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDlgavrEYFDRVLLlnRGL-VAHG 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
272-445 |
3.43e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.56 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 272 QLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLKIGYFSQHHVE 345
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtsgsirVFGKPLEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 346 QLDLNVSAVELLA------RKFPGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDE 415
Cdd:cd03235 80 DRDFPISVRDVVLmglyghKGLFRRLSKADKAKvdeaLERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190
....*....|....*....|....*....|...
gi 1189438346 416 PTNHLDMETIEALGRALNNFRG---GVILVSHD 445
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRRegmTILVVTHD 191
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
270-464 |
1.13e-28 |
|
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: 113.60 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGY 338
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGeVLLDGRDLaslsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQHHVEQLDLNVSAVELLAR----KFPGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNF 410
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRyphlGLFGRPSAEDREAveeaLERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 411 YILDEPTNHLDM----ETIEALgRALNNFRG-GVILVSHDerfIRLVCR---ELWVCEGGGV 464
Cdd:COG1120 159 LLLDEPTSHLDLahqlEVLELL-RRLARERGrTVVMVLHD---LNLAARyadRLVLLKDGRI 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
64-458 |
4.99e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 116.93 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 64 AAELAEIyAKLEEIEADKAPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---R 140
Cdd:COG1123 102 GDQIAEA-LENLGLSRAEARARVLELLEAVGLERRLDRYPH-QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVttqA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 141 AILWLENYLQTWP-STILVVSHDRNFLNAIATDIIHLHSQRLdgyrgdfetfikskQErllnqqreyeaqqqyrqhiqvf 219
Cdd:COG1123 180 EILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRI--------------VE---------------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 220 idrfrynANRASQVQSKLKMLEKLPELKPVDKESEVVmkfpdgfEKFSPPILQLDEVDFYYDPKHVIFSRL--SVSADLE 297
Cdd:COG1123 224 -------DGPPEEILAAPQALAAVPRLGAARGRAAPA-------AAAAEPLLEVRNLSKRYPVRGKGGVRAvdDVSLTLR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 298 S--RICVVGENGAGKSTMLKLLLG--------------DLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLA--- 358
Cdd:COG1123 290 RgeTLGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAepl 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 359 RKFPGRPEEEYRHQ----LGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEA 427
Cdd:COG1123 370 RLHGLLSRAERRERvaelLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqaqiLNLLRD 449
|
410 420 430
....*....|....*....|....*....|.
gi 1189438346 428 LGRALNnfrGGVILVSHDERFIRLVCRELWV 458
Cdd:COG1123 450 LQRELG---LTYLFISHDLAVVRYIADRVAV 477
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
174-256 |
6.34e-28 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 106.12 E-value: 6.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 174 IHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKPVDKES 253
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
...
gi 1189438346 254 EVV 256
Cdd:pfam12848 81 PKL 83
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
272-462 |
2.15e-24 |
|
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: 98.86 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 272 QLDEVDFYYdPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIrhahrnlkigyfsqhhveqldlnv 351
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE------------------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 352 saVELLARKFPGRPEEEYRHQLGRygisgelamrpLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRA 431
Cdd:cd00267 56 --ILIDGKDIAKLPLEELRRRIGY-----------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....
gi 1189438346 432 LNNFRGG---VILVSHDERFIRLVCRELWVCEGG 462
Cdd:cd00267 123 LRELAEEgrtVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
272-465 |
8.10e-23 |
|
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: 95.19 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 272 QLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIGYFS 340
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGeilldgkdlasLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 341 QhhveqldlnvsAVELLarkfpgrpeeeyrhqlgryGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHL 420
Cdd:cd03214 80 Q-----------ALELL-------------------GLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 421 D-------METIEALGRALNNfrgGVILVSHDERFIRLVCRELWVCEGGGVT 465
Cdd:cd03214 129 DiahqielLELLRRLARERGK---TVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
271-464 |
1.05e-22 |
|
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: 96.25 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlKIgyfsqhHVEQLDLN 350
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG--------EV------LVDGKDIT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 351 VSAVELLARK------FP--------------------GRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAF 400
Cdd:COG1122 67 KKNLRELRRKvglvfqNPddqlfaptveedvafgpenlGLPREEIRERveeaLELVGLE-HLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 401 AQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG---GVILVSHDERFIRLVCRELWVCEGGGV 464
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
267-481 |
7.98e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 98.68 E-value: 7.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLK 335
Cdd:COG4988 333 GPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGsilingvdlsdLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 336 IGYFSQH-HVEQLDL--NVsaveLLARkfPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSRVAFAQ 402
Cdd:COG4988 413 IAWVPQNpYLFAGTIreNL----RLGR--PDASDEELEAALEAAGLDEFVAALPDgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 403 MTM-PCPnFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLvCRELWVCEGGGVtrVEGGfdQYRALLQ 479
Cdd:COG4988 487 ALLrDAP-LLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQ-ADRILVLDDGRI--VEQG--THEELLA 560
|
..
gi 1189438346 480 EQ 481
Cdd:COG4988 561 KN 562
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
269-458 |
1.36e-21 |
|
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: 92.54 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 269 PILQLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKI---GYFSQ--- 341
Cdd:COG4133 1 MMLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGeVLWNGEPIRDareDYRRRlay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 342 --HHVEqLDLNVSAVELLA--RKFPGR--PEEEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDE 415
Cdd:COG4133 80 lgHADG-LKPELTVRENLRfwAALYGLraDREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189438346 416 PTNHLDMETIEALGRALNNFR---GGVILVSHDERFIRlVCRELWV 458
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELA-AARVLDL 202
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
300-461 |
2.10e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 92.55 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRGI---------------RHAHRNLKIGY-FSQHH------VEQldlNVSAVELL 357
Cdd:cd03255 33 VAIVGPSGSGKSTLLNILGGLDRPTSGEvrvdgtdisklsekeLAAFRRRHIGFvFQSFNllpdltALE---NVELPLLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 358 ARKFPGRPEEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGRALNN 434
Cdd:cd03255 110 AGVPKKERRERAEELLERVGLGDRLNHYP-SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkeVMELLRELNK 188
|
170 180
....*....|....*....|....*...
gi 1189438346 435 FRG-GVILVSHDERFIRLVCRELWVCEG 461
Cdd:cd03255 189 EAGtTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
299-418 |
3.04e-21 |
|
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: 90.01 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 299 RICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIGYFSQHHV--------EQLDLNVSAVELLAR 359
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPTEGtilldgqdltdDERKSLRKEIGYVFQDPQlfprltvrENLRLGLLLKGLSKR 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 360 KFPGRPEEeYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTN 418
Cdd:pfam00005 93 EKDARAEE-ALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
279-462 |
2.00e-20 |
|
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: 89.45 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 279 YYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGY--------F 339
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGeVLVDGKDLtklslkelrrKVGLvfqnpddqF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 340 SQHHVEQlDLNVSAVELlarkfpGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDE 415
Cdd:cd03225 89 FGPTVEE-EVAFGLENL------GLPEEEIEERveeaLELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1189438346 416 PTNHLDMETIEALGRALNNFRG---GVILVSHDERFIRLVCRELWVCEGG 462
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
299-450 |
2.14e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 94.25 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 299 RICVVGENGAGKSTMLKLLLGDLA--------------------PVR------------GIRHAHRNLKIGYFSQHHVEQ 346
Cdd:PRK11147 31 RVCLVGRNGAGKSTLMKILNGEVLlddgriiyeqdlivarlqqdPPRnvegtvydfvaeGIEEQAEYLKRYHDISHLVET 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 347 lDLNVSAVELLARKfpgrpEEEYRHQ------------LGRYGISGElamRPLASLSGGQKSRVAFAQMTMPCPNFYILD 414
Cdd:PRK11147 111 -DPSEKNLNELAKL-----QEQLDHHnlwqlenrinevLAQLGLDPD---AALSSLSGGWLRKAALGRALVSNPDVLLLD 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 1189438346 415 EPTNHLDMETIEALGRALNNFRGGVILVSHDERFIR 450
Cdd:PRK11147 182 EPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIR 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
270-460 |
2.67e-20 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 93.85 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHhvEQLDL 349
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQE--PQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 350 ------NV-----SAVELLAR------KFpGRPEEEYRHQLGRYG-----ISG----------ELAM---------RPLA 388
Cdd:TIGR03719 82 tktvreNVeegvaEIKDALDRfneisaKY-AEPDADFDKLAAEQAelqeiIDAadawdldsqlEIAMdalrcppwdADVT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 389 SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRelWVCE 460
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILE 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
271-453 |
2.94e-20 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter 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: 213197 [Multi-domain] Cd Length: 173 Bit Score: 87.84 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSrlsVSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG---------IRHAHRNLK-IGY 338
Cdd:cd03230 1 IEVRNLSKRYGKKTALDD---ISLTVEkgEIYGLLGPNGAGKTTLIKIILGLLKPDSGeikvlgkdiKKEPEEVKRrIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQHhvEQLDLNVSAVELLarkfpgrpeeeyrhqlgrygisgelamrplaSLSGGQKSRVAFAQMTMPCPNFYILDEPTN 418
Cdd:cd03230 78 LPEE--PSLYENLTVRENL-------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 1189438346 419 HLDMETIEALGRALNNFR---GGVILVSHDERFIRLVC 453
Cdd:cd03230 125 GLDPESRREFWELLRELKkegKTILLSSHILEEAERLC 162
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
300-464 |
5.88e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II 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. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most 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: 213193 [Multi-domain] Cd Length: 205 Bit Score: 88.08 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLKIGYFSQHHVEQLDLNVSAVELLAR-KFPGRPEEEYR 370
Cdd:cd03226 29 IALTGKNGAGKTTLAKILAGLIKESSGsillngkpIKAKERRKSIGYVMQDVDYQLFTDSVREELLLGlKELDAGNEQAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 371 HQLGRYGISGELAMRPLaSLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD---METIEALGRALNNFRGGVILVSHDER 447
Cdd:cd03226 109 TVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYE 187
|
170
....*....|....*...
gi 1189438346 448 FIRLVC-RELWVCEGGGV 464
Cdd:cd03226 188 FLAKVCdRVLLLANGAIV 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
271-462 |
1.78e-19 |
|
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: 85.51 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPK-HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlKIgYFSQHHVEQLDL 349
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG--------EI-LIDGVDLRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 350 nvsavellarkfpgrpeEEYRHQLG-------------RYGIsgelamrplasLSGGQKSRVAFAQMTMPCPNFYILDEP 416
Cdd:cd03228 72 -----------------ESLRKNIAyvpqdpflfsgtiRENI-----------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438346 417 TNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLvCRELWVCEGG 462
Cdd:cd03228 124 TSALDPETEALILEALRALAKGktVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
240-481 |
1.79e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 91.82 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 240 LEKLPELkpVDKESEVvmkfPDGFEKFSPPILQ----LDEVDFYYDPKHV-IFSRLSVSADLESRICVVGENGAGKSTML 314
Cdd:COG2274 445 LERLDDI--LDLPPER----EEGRSKLSLPRLKgdieLENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 315 KLLLGDLAPVRG--------IRHAHRNL---KIGYFSQHhvEQLdLNVSAVE--LLARkfPGRPEEEYRHQLGRYGISGE 381
Cdd:COG2274 519 KLLLGLYEPTSGrilidgidLRQIDPASlrrQIGVVLQD--VFL-FSGTIREniTLGD--PDATDEEIIEAARLAGLHDF 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 382 LAMRPL----------ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFI 449
Cdd:COG2274 594 IEALPMgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTI 673
|
250 260 270
....*....|....*....|....*....|....*....
gi 1189438346 450 RLvCRELWVCEGGGVTRvEGGFDQ-------YRALLQEQ 481
Cdd:COG2274 674 RL-ADRIIVLDKGRIVE-DGTHEEllarkglYAELVQQQ 710
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
268-444 |
4.60e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 86.29 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 268 PPILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------------IRHa 330
Cdd:COG1119 1 DPLLELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvweLRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 331 hrnlKIGYFSQHHVEQLDLNVSAVELLARKF------PGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAF 400
Cdd:COG1119 79 ----RIGLVSPALQLRFPRDETVLDVVLSGFfdsiglYREPTDEQRERarelLELLGLA-HLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438346 401 AQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG----VILVSH 444
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVTH 201
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
303-445 |
9.74e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 85.12 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 303 VGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLK--IGYFSQHHVeqLDLNVSAVELL-----ARKFPGRPEE 367
Cdd:COG1131 32 LGPNGAGKTTTIRMLLGLLRPTSGevrvlgedVARDPAEVRrrIGYVPQEPA--LYPDLTVRENLrffarLYGLPRKEAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 368 EYRHQ-LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VILVS 443
Cdd:COG1131 110 ERIDElLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgktVLLST 188
|
..
gi 1189438346 444 HD 445
Cdd:COG1131 189 HY 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
271-445 |
9.82e-19 |
|
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: 85.29 E-value: 9.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDpKHVIFSRLSVSADlESRI-CVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL---------KIGYF 339
Cdd:COG4555 2 IEVENLSKKYG-KVPALKDVSFTAK-DGEItGLLGPNGAGKTTLLRMLAGLLKPDSGsILIDGEDVrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 340 SQHHVeqLDLNVSA---VELLARKFPGRPE------EEYRHQLGRygisGELAMRPLASLSGGQKSRVAFAQMTMPCPNF 410
Cdd:COG4555 80 PDERG--LYDRLTVrenIRYFAELYGLFDEelkkriEELIELLGL----EEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1189438346 411 YILDEPTNHLDMETIEALGRALNNFRG---GVILVSHD 445
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHI 191
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
271-464 |
1.02e-18 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 84.48 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKhVIFSrlSVSADLES--RICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIG 337
Cdd:COG4619 1 LELEGLSFRVGGK-PILS--PVSLTLEAgeCVAITGPSGSGKSTLLRALADLDPPTSGeIYLDGKPLsampppewrrQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 338 YFSQH------HVEQldlNVSAVELLARKFPGRpeEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFY 411
Cdd:COG4619 78 YVPQEpalwggTVRD---NLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 412 ILDEPTNHLDMETIEALGRALNNFR----GGVILVSHDERFIRLVCRELWVCEGGGV 464
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
302-464 |
1.20e-18 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 85.64 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAP-----------VRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLAR-----KFPGRP 365
Cdd:TIGR03873 32 LLGPNGSGKSTLLRLLAGALRPdagtvdlagvdLHGLSRRARARRVALVEQDSDTAVPLTVRDVVALGRiphrsLWAGDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 366 EEEY---RHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD----METIEALgRALNNFRGG 438
Cdd:TIGR03873 112 PHDAavvDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDvraqLETLALV-RELAATGVT 189
|
170 180
....*....|....*....|....*.
gi 1189438346 439 VILVSHDERFIRLVCRELWVCEGGGV 464
Cdd:TIGR03873 190 VVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
270-468 |
1.31e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.33 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL-------------K 335
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGqVLVNGQDLsrlkrreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 336 IGYFSQHHveQL--DLNVSavELLArkFP----GRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTM 405
Cdd:COG2884 81 IGVVFQDF--RLlpDRTVY--ENVA--LPlrvtGKSRKEIRRRvrevLDLVGLSDKAKALP-HELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 406 PCPNFYILDEPTNHLDMETIEALGRALNNF-RGG--VILVSHDERFIRLVCRELWVCEGGGVTRVE 468
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEInRRGttVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
83-181 |
2.49e-18 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 83.33 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 83 PARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS----TILV 158
Cdd:COG4619 107 RERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAeegrAVLW 186
|
90 100
....*....|....*....|...
gi 1189438346 159 VSHDRNFLNAIATDIIHLHSQRL 181
Cdd:COG4619 187 VSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
64-162 |
5.42e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 83.19 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 64 AAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAIL 143
Cdd:COG1131 90 VRENLRFFARLYGLPRKEARERIDELLELFGLTDAADR-KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR 168
|
90 100
....*....|....*....|..
gi 1189438346 144 WLENYLQTWPS---TILVVSHD 162
Cdd:COG1131 169 ELWELLRELAAegkTVLLSTHY 190
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
271-464 |
5.62e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 82.64 E-value: 5.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDP-KHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIGY 338
Cdd:cd03245 3 IEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsvlldgtdirqLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQHHV-------EQL---DLNVSAVELL-ARKFPGRPEEEYRH------QLGRYGisgelamrplASLSGGQKSRVAFA 401
Cdd:cd03245 83 VPQDVTlfygtlrDNItlgAPLADDERILrAAELAGVTDFVNKHpngldlQIGERG----------RGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 402 QMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLVCReLWVCEGGGV 464
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLVDR-IIVMDSGRI 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
106-180 |
8.19e-18 |
|
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: 80.37 E-value: 8.19e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWP---STILVVSHDRNFLNAIATDIIHLHSQR 180
Cdd:cd00267 80 QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAeegRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
280-460 |
2.12e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.79 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 280 YDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQhhvE-QLDL------NV- 351
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ---EpQLDPektvreNVe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 352 ----SAVELLAR------KFpGRPEEEYR----------------------HQLgrygisgELAM---R------PLASL 390
Cdd:PRK11819 93 egvaEVKAALDRfneiyaAY-AEPDADFDalaaeqgelqeiidaadawdldSQL-------EIAMdalRcppwdaKVTKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 391 SGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRelWVCE 460
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILE 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
66-181 |
3.30e-17 |
|
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: 81.06 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 66 ELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQpTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWL 145
Cdd:COG4555 93 ENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRR-VGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
90 100 110
....*....|....*....|....*....|....*....
gi 1189438346 146 ENYLQTW---PSTILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:COG4555 172 REILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
77-180 |
4.74e-17 |
|
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: 79.82 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 77 IEADKAPARASVILAGLGFTPkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS-- 154
Cdd:cd03225 106 LPEEEIEERVEEALELVGLEG-LRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeg 184
|
90 100
....*....|....*....|....*..
gi 1189438346 155 -TILVVSHDRNFLNAIATDIIHLHSQR 180
Cdd:cd03225 185 kTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
106-181 |
4.92e-17 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter 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: 213197 [Multi-domain] Cd Length: 173 Bit Score: 78.59 E-value: 4.92e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:cd03230 95 KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKegkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
83-199 |
6.16e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 83.24 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 83 PARASVilAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAilwLENYLQTWPSTILVV 159
Cdd:PRK11819 424 PSRAYV--GRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVetlRA---LEEALLEFPGCAVVI 498
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1189438346 160 SHDRNFLNAIATDIIhlhSQRLDG----YRGDFETFIKSKQERL 199
Cdd:PRK11819 499 SHDRWFLDRIATHIL---AFEGDSqvewFEGNFQEYEEDKKRRL 539
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
267-461 |
1.87e-16 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 82.12 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDP-KHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLK--------- 335
Cdd:COG4987 330 GGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGsITLGGVDLRdldeddlrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 336 -IGYFSQH-HV------EQLdlnvsaveLLARkfPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSR 397
Cdd:COG4987 410 rIAVVPQRpHLfdttlrENL--------RLAR--PDATDEELWAALERVGLGDWLAALPDgldtwlgeggRRLSGGERRR 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 398 VAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLVCRELWVCEG 461
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLERMDRILVLEDG 545
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
77-181 |
2.52e-16 |
|
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: 78.14 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 77 IEADKAPARASVILAGLGFTpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS-- 154
Cdd:COG1122 106 LPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeg 184
|
90 100
....*....|....*....|....*...
gi 1189438346 155 -TILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:COG1122 185 kTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
229-454 |
2.97e-16 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 81.45 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 229 RASQVQSKLKMLEKLPELkPVDkesevvmkFPDGFEKFSPPILQ----LDEVDFYY--DPKHVIfsrLSVSADLE--SRI 300
Cdd:TIGR03375 427 RYQQAKTALQSLDELMQL-PVE--------RPEGTRFLHRPRLQgeieFRNVSFAYpgQETPAL---DNVSLTIRpgEKV 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 301 CVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAH-----RNlkIGYFSQHHV-------EQLDLNVSAV---ELL 357
Cdd:TIGR03375 495 AIIGRIGSGKSTLLKLLLGLYQPTEGsvlldgvdIRQIDpadlrRN--IGYVPQDPRlfygtlrDNIALGAPYAddeEIL 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 358 --ARK-----FPGRPEEEYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGR 430
Cdd:TIGR03375 573 raAELagvteFVRRHPDGLDMQIGERG----------RSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKD 642
|
250 260
....*....|....*....|....*.
gi 1189438346 431 ALNNFRGG--VILVSHDERFIRLVCR 454
Cdd:TIGR03375 643 RLKRWLAGktLVLVTHRTSLLDLVDR 668
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
301-445 |
4.15e-16 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 77.16 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 301 CVVGENGAGKSTMLKLLLGDLAPVRG------------IRHAHRNlkIGYFSQHHVeqLDLNVSAVELL---ARkFPGRP 365
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPTSGtayingysirtdRKAARQS--LGYCPQFDA--LFDELTVREHLrfyAR-LKGLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 366 EEEYRHQLGRYGISGEL---AMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VI 440
Cdd:cd03263 107 KSEIKEEVELLLRVLGLtdkANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGrsII 186
|
....*
gi 1189438346 441 LVSHD 445
Cdd:cd03263 187 LTTHS 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
102-461 |
4.36e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 80.98 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 102 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR-----AILWLEnyLQTWPSTILVVSHDRNFLNAIAtDIIHL 176
Cdd:COG1245 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrlnvARLIRE--LAEEGKYVLVVEHDLAILDYLA-DYVHI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 177 hsqrLDGYRGDFETFIKSKQerllnqqreyeaqqqYRQHIQVFID--------RFRynanrasqvQSKLKMLEKLPelkP 248
Cdd:COG1245 285 ----LYGEPGVYGVVSKPKS---------------VRVGINQYLDgylpeenvRIR---------DEPIEFEVHAP---R 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 249 VDKESEVVMKFPDgFEKfsppilQLDEvdfyydpkhviFSrLSVSADlESR----ICVVGENGAGKSTMLKLLLGDLAPV 324
Cdd:COG1245 334 REKEEETLVEYPD-LTK------SYGG-----------FS-LEVEGG-EIRegevLGIVGPNGIGKTTFAKILAGVLKPD 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 325 RGIrhAHRNLKIGYFSQHHVEQLDLNVSAV--ELLARKFPGRPeeeYRHQLGR-YGISgELAMRPLASLSGGQKSRVAFA 401
Cdd:COG1245 394 EGE--VDEDLKISYKPQYISPDYDGTVEEFlrSANTDDFGSSY---YKTEIIKpLGLE-KLLDKNVKDLSGGELQRVAIA 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 402 QmtmpC----PNFYILDEPTNHLDMETIEALGRALNNF---RG-GVILVSHDERFIRLVCRELWVCEG 461
Cdd:COG1245 468 A----ClsrdADLYLLDEPSAHLDVEQRLAVAKAIRRFaenRGkTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
267-451 |
6.32e-16 |
|
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: 80.02 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLK 335
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGsiavngvpladADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 336 IGYFSQHHVeQLDLNVSAVELLARkfPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSRVAFAQMTM 405
Cdd:TIGR02857 398 IAWVPQHPF-LFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALPQgldtpigeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438346 406 PCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRL 451
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALAAL 522
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
269-446 |
8.67e-16 |
|
thiol reductant ABC exporter, CydC 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.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 79.71 E-value: 8.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 269 PILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIG 337
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevtldgvpvssLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 338 YFSQH-HVeqLDLNVSAVELLARkfPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSRVAFAQMTMP 406
Cdd:TIGR02868 413 VCAQDaHL--FDTTVRENLRLAR--PDATDEELWAALERVGLADWLRALPDgldtvlgeggARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1189438346 407 CPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDE 446
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHHL 530
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
283-462 |
1.05e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213264 [Multi-domain] Cd Length: 214 Bit Score: 75.79 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 283 KHVIFSRLSVSADL-ESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------------KIGYFSQHHveQ 346
Cdd:cd03297 8 KRLPDFTLKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtIVLNGTVLfdsrkkinlppqqrKIGLVFQQY--A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 347 LDLNVSAVELLA----RKFPGRPEEEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM 422
Cdd:cd03297 86 LFPHLNVRENLAfglkRKRNREDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438346 423 ET----IEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGG 462
Cdd:cd03297 165 ALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
102-461 |
1.16e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 102 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV-------RAILWL-ENylqtwpSTILVVSHDRNFLNAIAtDI 173
Cdd:PRK13409 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrqrlnvaRLIRELaEG------KYVLVVEHDLAVLDYLA-DN 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 174 IHLhsqrLDGYRGDFETFIKSKQERllnqqreyEAQQQYrqhIQVFID----RFRynanrasqvQSKLKMLEKLPElkpV 249
Cdd:PRK13409 281 VHI----AYGEPGAYGVVSKPKGVR--------VGINEY---LKGYLPeenmRIR---------PEPIEFEERPPR---D 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 250 DKESEVVMKFPDgFEKfsppilQLDevDFyydpkhvifsRLSVSADlESR----ICVVGENGAGKSTMLKLLLGDLAPVR 325
Cdd:PRK13409 334 ESERETLVEYPD-LTK------KLG--DF----------SLEVEGG-EIYegevIGIVGPNGIGKTTFAKLLAGVLKPDE 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 326 GirHAHRNLKIGYFSQHHVEQLDLNVSavELLARKFPGRPEEEYRHQLGR-YGISgELAMRPLASLSGGQKSRVAFAQMT 404
Cdd:PRK13409 394 G--EVDPELKISYKPQYIKPDYDGTVE--DLLRSITDDLGSSYYKSEIIKpLQLE-RLLDKNVKDLSGGELQRVAIAACL 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 405 MPCPNFYILDEPTNHLDME----TIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEG 461
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
64-176 |
1.41e-15 |
|
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: 75.21 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 64 AAELAEIYAKLEEIEADKAPARASVILAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAIL 143
Cdd:COG4133 92 VRENLRFWAALYGLRADREAIDEALEAVGLA---GLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
90 100 110
....*....|....*....|....*....|....*.
gi 1189438346 144 WLENYLQTWPS---TILVVSHDRnfLNAIATDIIHL 176
Cdd:COG4133 169 LLAELIAAHLArggAVLLTTHQP--LELAAARVLDL 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
285-443 |
2.26e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 285 VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIG-YFSQ-H---HVEQLDLNVSAVELLA 358
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDIDDPdVAEAcHylgHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 359 --RKFPGRPEEEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRA----L 432
Cdd:PRK13539 96 fwAAFLGGEELDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELirahL 174
|
170
....*....|.
gi 1189438346 433 NnfRGGVILVS 443
Cdd:PRK13539 175 A--QGGIVIAA 183
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
268-447 |
2.55e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.08 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 268 PPILQLDEVDFYYDPKHVIFSRLS-VSADLES--RICVVGENGAGKSTMLKLLLGDLAP------VRGI---------RH 329
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRgVSLSIEAgeFVAIVGPSGSGKSTLLNILGGLDRPtsgevlIDGQdisslsereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 330 AHRNLKIGY-FSQHH------VEQldlNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQ 402
Cdd:COG1136 82 RLRRRHIGFvFQFFNllpeltALE---NVALPLLLAGVSRKERRERARELLERVGLGDRLDHRP-SQLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1189438346 403 MTMPCPNFYILDEPTNHLDMET----IEALgRALNNFRG-GVILVSHDER 447
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTgeevLELL-RELNRELGtTIVMVTHDPE 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
108-195 |
2.55e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 78.39 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGD 187
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGT 519
|
....*...
gi 1189438346 188 FETFIKSK 195
Cdd:PRK15064 520 YEEYLRSQ 527
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
92-181 |
7.42e-15 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 73.41 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 92 GLGFTPKmqqQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNA 168
Cdd:cd03268 115 GLKDSAK---KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQK 191
|
90
....*....|...
gi 1189438346 169 IATDIIHLHSQRL 181
Cdd:cd03268 192 VADRIGIINKGKL 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
74-453 |
1.41e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.99 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 74 LEEI--EADKAPARASVILAGLGFTPKMQQQpTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDvrailwlenylqt 151
Cdd:TIGR03269 135 LEEIgyEGKEAVGRAVDLIEMVQLSHRITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD------------- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 152 wPSTilvvshdrnflnaiaTDIIHlhsqrldgyrgdfetfikskqERLLNQQREYEAQQQYRQHIQVFIdrfrynanraS 231
Cdd:TIGR03269 201 -PQT---------------AKLVH---------------------NALEEAVKASGISMVLTSHWPEVI----------E 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 232 QVQSKLKMLEKlPELKPVDKESEVVMKFPDGFEKFSP--------PILQLDEVDFYYDP--KHVIFSRLSVSADLESR-- 299
Cdd:TIGR03269 234 DLSDKAIWLEN-GEIKEEGTPDEVVAVFMEGVSEVEKecevevgePIIKVRNVSKRYISvdRGVVKAVDNVSLEVKEGei 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPV-----------------RGIRHAHRNLK-IGYFSQH-----HVEQLDLNVSAVEL 356
Cdd:TIGR03269 313 FGIVGTSGAGKTTLSKIIAGVLEPTsgevnvrvgdewvdmtkPGPDGRGRAKRyIGILHQEydlypHRTVLDNLTEAIGL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 357 -----LAR-------KFPGRPEEEYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET 424
Cdd:TIGR03269 393 elpdeLARmkavitlKMVGFDEEKAEEILDKYP----------DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPIT 462
|
410 420 430
....*....|....*....|....*....|...
gi 1189438346 425 IEALGRALNNFRGGV----ILVSHDERFIRLVC 453
Cdd:TIGR03269 463 KVDVTHSILKAREEMeqtfIIVSHDMDFVLDVC 495
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
303-453 |
1.63e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 75.70 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 303 VGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAV------ELLARK--------FPGRPEEE 368
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTvimghtELWEVKqerdriyaLPEMSEED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 369 YRH------QLGRY----------------GISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIE 426
Cdd:PRK15064 113 GMKvadlevKFAEMdgytaearagelllgvGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIR 192
|
170 180
....*....|....*....|....*..
gi 1189438346 427 ALGRALNNFRGGVILVSHDERFIRLVC 453
Cdd:PRK15064 193 WLEDVLNERNSTMIIISHDRHFLNSVC 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
275-449 |
1.81e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 72.44 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 275 EVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL------KIGYFS 340
Cdd:cd03292 5 NVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtirvngqdVSDLRGRAipylrrKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 341 QHHVEQLDLNVSAVELLARKFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEP 416
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPPREIRKRvpaaLELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1189438346 417 TNHLDMETIEALGRALN--NFRGGVILVS-HDERFI 449
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKkiNKAGTTVVVAtHAKELV 199
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
302-445 |
2.05e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 73.23 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGYFSQHHVEQLDLNVSAVELLAR----KFPGRPE 366
Cdd:COG4559 32 IIGPNGAGKSTLLKLLTGELTPSSGeVRLNGRPLaawspwelarRRAVLPQHSSLAFPFTVEEVVALGRaphgSSAAQDR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 367 EEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFA-------QMTMPCPNFYILDEPTNHLD-------MEtieaLGRAL 432
Cdd:COG4559 112 QIVREALALVGLAH-LAGRSYQTLSGGEQQRVQLArvlaqlwEPVDGGPRWLFLDEPTSALDlahqhavLR----LARQL 186
|
170
....*....|...
gi 1189438346 433 NNFRGGVILVSHD 445
Cdd:COG4559 187 ARRGGGVVAVLHD 199
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
299-462 |
3.16e-14 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 72.14 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 299 RICVVGENGAGKSTMLKLLLG-----------DLAPVRGIRHAHRNLKIGYFSQHHVEQLD--LNVSAV--ELLARKFPG 363
Cdd:COG1124 33 SFGLVGESGSGKSTLLRALAGlerpwsgevtfDGRPVTRRRRKAFRRRVQMVFQDPYASLHprHTVDRIlaEPLRIHGLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 364 RPEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGRALNNFRG-GV 439
Cdd:COG1124 113 DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeILNLLKDLREERGlTY 192
|
170 180
....*....|....*....|...
gi 1189438346 440 ILVSHDERFIRLVCRELWVCEGG 462
Cdd:COG1124 193 LFVSHDLAVVAHLCDRVAVMQNG 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
302-445 |
6.89e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQ--HHVEQLDLNVSAVELLArkfPGRPEEEYRHQLGRYGiS 379
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDTTLPLTVNRFLRLR---PGTKKEDILPALKRVQ-A 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 380 GELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG----GVILVSHD 445
Cdd:PRK09544 111 GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRReldcAVLMVSHD 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
302-445 |
9.39e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.96 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLK----------IGYFSQHHVEQLDLNVSAVELLAR----KFPGRPE 366
Cdd:PRK13548 33 ILGPNGAGKSTLLRALSGELSPDSGeVRLNGRPLAdwspaelarrRAVLPQHSSLSFPFTVEEVVAMGRaphgLSRAEDD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 367 EEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFA----QMTMPC--PNFYILDEPTNHLDM---ETIEALGRALNNFRG 437
Cdd:PRK13548 113 ALVAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLArvlaQLWEPDgpPRWLLLDEPTSALDLahqHHVLRLARQLAHERG 191
|
....*....
gi 1189438346 438 -GVILVSHD 445
Cdd:PRK13548 192 lAVIVVLHD 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
271-464 |
1.15e-13 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 68.78 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYY-DPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLK---IGY 338
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGrvrldgadISQWDPNELgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQHhveqldlnvsaVELLarkfpgrpeeeyrhqlgrygiSGELAMrplASLSGGQKSRVAFAQMTMPCPNFYILDEPTN 418
Cdd:cd03246 81 LPQD-----------DELF---------------------SGSIAE---NILSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1189438346 419 HLDMETIEALGRALNNFRGG---VILVSHDERFIRLVCRELwVCEGGGV 464
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAgatRIVIAHRPETLASADRIL-VLEDGRV 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
271-453 |
1.16e-13 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; 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: 213228 [Multi-domain] Cd Length: 235 Bit Score: 70.22 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVifsrLS-VSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG------------IRHAHRNL- 334
Cdd:cd03261 1 IELRGLTKSFGGRTV----LKgVDLDVRrgEILAIIGPSGSGKSTLLRLIVGLLRPDSGevlidgedisglSEAELYRLr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 335 -KIGYFSQHHVEQLDLNVSA-VELLARKFPGRPEEEYR----HQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCP 408
Cdd:cd03261 77 rRMGMLFQSGALFDSLTVFEnVAFPLREHTRLSEEEIReivlEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1189438346 409 NFYILDEPTNHLD---METIEALGRALNNFRG-GVILVSHDERFIRLVC 453
Cdd:cd03261 156 ELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIA 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
269-470 |
2.58e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 71.86 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 269 PILQLDEVDFYYdPKHVIFSRLSVSADLE--SRICVVGENGAGKSTMLKLLLGDLAP--------------VRGIRHAHR 332
Cdd:COG1123 3 PLLEVRDLSVRY-PGGDVPAVDGVSLTIApgETVALVGESGSGKSTLALALMGLLPHggrisgevlldgrdLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 333 NLKIGYFSQHHVEQLD-LNVSAVELLARKFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPC 407
Cdd:COG1123 82 GRRIGMVFQDPMTQLNpVTVGDQIAEALENLGLSRAEARARvlelLEAVGLERRLDRYP-HQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 408 PNFYILDEPTNHLDMET---IEALGRALNNFRG-GVILVSHDERFIRLVCRELWVCEGGGVtrVEGG 470
Cdd:COG1123 161 PDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI--VEDG 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
271-445 |
3.09e-13 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 69.13 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSrlsVSADLESRIC--VVGENGAGKSTMLKLL-----LGDLAPVRG-IRHAHRNLkigYFSQH 342
Cdd:cd03260 1 IELRDLNVYYGDKHALKD---ISLDIPKGEItaLIGPSGCGKSTLLRLLnrlndLIPGAPDEGeVLLDGKDI---YDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 343 HVEQLDLNVSAVELLARKFPG-------------------RPEEEYRHQLGRYGISGELAMRPLA-SLSGGQKSRVAFAQ 402
Cdd:cd03260 75 DVLELRRRVGMVFQKPNPFPGsiydnvayglrlhgiklkeELDERVEEALRKAALWDEVKDRLHAlGLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189438346 403 MTMPCPNFYILDEPTNHLD---METIEALGRALNNfRGGVILVSHD 445
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDpisTAKIEELIAELKK-EYTIVIVTHN 199
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
271-445 |
3.52e-13 |
|
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: 68.65 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSRLS-VSADLESR--ICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRnlKIGYF 339
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEdISLSVEEGefVALVGPSGCGKSTLLRIIAGLERPTSGevlvdgepVTGPGP--DRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 340 SQHH-------VEQldlNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYI 412
Cdd:cd03293 79 FQQDallpwltVLD---NVALGLELQGVPKAEARERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1189438346 413 LDEPTNHLDMETIEALGRAL----NNFRGGVILVSHD 445
Cdd:cd03293 155 LDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
298-445 |
4.07e-13 |
|
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: 68.75 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 298 SRICVVGENGAGKSTMLKLLLGDLAPVRG------------IRHAHRNL--KIGYFSQHH--VEQLDL--NV-------- 351
Cdd:cd03256 28 EFVALIGPSGAGKSTLLRCLNGLVEPTSGsvlidgtdinklKGKALRQLrrQIGMIFQQFnlIERLSVleNVlsgrlgrr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 352 SAVELLARKFPGRPEEEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALG-- 429
Cdd:cd03256 108 STWRSLFGLFPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMdl 186
|
170
....*....|....*...
gi 1189438346 430 -RALNNFRGGVILVS-HD 445
Cdd:cd03256 187 lKRINREEGITVIVSlHQ 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
300-485 |
4.47e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 68.97 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNlKIGYFSQHhvEQLDLNVSAVELLARKFPGRpeeeYRHQLGRYGIS 379
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQY--IKADYEGTVRDLLSSITKDF----YTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 380 GELAM-----RPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF----RGGVILVSHDERFIR 450
Cdd:cd03237 101 KPLQIeqildREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMID 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1189438346 451 LVCRELWVCEG-GGVTRV-------EGGFDQYRALLQEQFRRE 485
Cdd:cd03237 181 YLADRLIVFEGePSVNGVanppqslRSGMNRFLKNLDITFRRD 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
61-135 |
5.09e-13 |
|
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: 66.52 E-value: 5.09e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 61 GSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKM---QQQPTREFSGGWRMRLALARALFARPDLLLLDEPTN 135
Cdd:pfam00005 73 RLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
285-444 |
8.15e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 67.13 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 285 VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIGYFSQH-------HVEQLDLNVSAVEL 356
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrVLLNGGPLDFQRDSIArgllylgHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 357 LARKFPGRPEEEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF- 435
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHc 172
|
170
....*....|.
gi 1189438346 436 -RGG-VILVSH 444
Cdd:cd03231 173 aRGGmVVLTTH 183
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
101-176 |
1.01e-12 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 67.17 E-value: 1.01e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 101 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHL 176
Cdd:cd03235 127 DRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKtqeDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
271-444 |
1.04e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.19 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLK----------IGYF 339
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrILIDGVDIRdltleslrrqIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 340 SQHHV-------EQL---DLNVSAVELLA-----------RKFPgrpeEEYRHQLGRYGisgelamrplASLSGGQKSRV 398
Cdd:COG1132 420 PQDTFlfsgtirENIrygRPDATDEEVEEaakaaqahefiEALP----DGYDTVVGERG----------VNLSGGQRQRI 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438346 399 AFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSH 444
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH 533
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
105-181 |
1.06e-12 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 67.91 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILW--LENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQR 180
Cdd:COG1124 137 HQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsVQAEILnlLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
.
gi 1189438346 181 L 181
Cdd:COG1124 217 I 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
285-447 |
1.11e-12 |
|
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: 66.61 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 285 VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIGYFSQH-------HVEQLDLNVSAVEL 356
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGeVRWNGTPLAEQRDEPHenilylgHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 357 LA--RKFPGRPEEEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNN 434
Cdd:TIGR01189 94 LHfwAAIHGGAQRTIEDALAAVGLTG-FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
170
....*....|....*.
gi 1189438346 435 F--RGG-VILVSHDER 447
Cdd:TIGR01189 173 HlaRGGiVLLTTHQDL 188
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
271-444 |
1.35e-12 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. 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: 213220 [Multi-domain] Cd Length: 236 Bit Score: 67.26 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLL-------G----DLAPVRGIRHAHRNLKIGYF 339
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFrfydvssGsiliDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 340 SQ----------HHVEQLDLNVSAVELLA-----------RKFPgrpeEEYRHQLGRYGISgelamrplasLSGGQKSRV 398
Cdd:cd03253 81 PQdtvlfndtigYNIRYGRPDATDEEVIEaakaaqihdkiMRFP----DGYDTIVGERGLK----------LSGGEKQRV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438346 399 AFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSH 444
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAH 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
273-481 |
2.22e-12 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 66.79 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 273 LDEVDFYYD--PKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IR----HAHRNlKIGY 338
Cdd:cd03249 3 FKNVSFRYPsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGeilldgvdIRdlnlRWLRS-QIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQhhvEQLDLNVSAVELLARKFPGRPEEE--------------------YRHQLGRYGisgelamrplASLSGGQKSRV 398
Cdd:cd03249 82 VSQ---EPVLFDGTIAENIRYGKPDATDEEveeaakkanihdfimslpdgYDTLVGERG----------SQLSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 399 AFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIR---LVCrelwVCEGGGVtrVE-GGFD 472
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAHRLSTIRnadLIA----VLQNGQV--VEqGTHD 222
|
250
....*....|....*.
gi 1189438346 473 Q-------YRALLQEQ 481
Cdd:cd03249 223 ElmaqkgvYAKLVKAQ 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
291-453 |
3.50e-12 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 65.99 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 291 SVSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL-------------KIGYFSQHHVEQLD--LNVS 352
Cdd:cd03257 23 DVSFSIKkgETLGLVGESGSGKSTLARAILGLLKPTSGsIIFDGKDLlklsrrlrkirrkEIQMVFQDPMSSLNprMTIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 353 A--VELLARKFPGRPEEEYRHQLGRYGISGELA-----MRPlASLSGGQKSRVAFAqMTMPC-PNFYILDEPTNHLDMET 424
Cdd:cd03257 103 EqiAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeevlnRYP-HELSGGQRQRVAIA-RALALnPKLLIADEPTSALDVSV 180
|
170 180 190
....*....|....*....|....*....|...
gi 1189438346 425 ---IEALGRALNNFRG-GVILVSHDERFIRLVC 453
Cdd:cd03257 181 qaqILDLLKKLQEELGlTLLFITHDLGVVAKIA 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
301-444 |
3.70e-12 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 65.32 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 301 CVVGENGAGKSTMLKLLLGDLAPVRGI---------RHAHRNLKIGYFSQHHVeqLDLNVSAVE--LLARKFPGRPEEEY 369
Cdd:cd03268 30 GFLGPNGAGKTTTMKIILGLIKPDSGEitfdgksyqKNIEALRRIGALIEAPG--FYPNLTAREnlRLLARLLGIRKKRI 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 370 RHQLGRYGISGElAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI---EALGRALNNFRGGVILVSH 444
Cdd:cd03268 108 DEVLDVVGLKDS-AKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIkelRELILSLRDQGITVLISSH 184
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
267-445 |
3.83e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 66.27 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDPK---HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLKIG 337
Cdd:COG1116 4 AAPALELRGVSKRFPTGgggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtsgevlVDGKPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 338 Y-FSQHH------VEQldlNVsaveLLARKFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMP 406
Cdd:COG1116 84 VvFQEPAllpwltVLD---NV----ALGLELRGVPKAERRERarelLELVGLAGFEDAYP-HQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1189438346 407 CPNFYILDEPTNHLDMETIEALG----RALNNFRGGVILVSHD 445
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQdellRLWQETGKTVLFVTHD 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
65-174 |
5.45e-12 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 65.22 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 65 AELAEIYAKLEEIEADKApaRASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RA 141
Cdd:cd03257 106 AEPLRIHGKLSKKEARKE--AVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVsvqAQ 183
|
90 100 110
....*....|....*....|....*....|....
gi 1189438346 142 ILWLENYLQT-WPSTILVVSHDRNFLNAIATDII 174
Cdd:cd03257 184 ILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVA 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
108-178 |
5.86e-12 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. 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: 213196 [Multi-domain] Cd Length: 178 Bit Score: 64.13 E-value: 5.86e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQT----WPSTILVVSHDRNFLNAIATDIIHLHS 178
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
102-176 |
5.88e-12 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 65.50 E-value: 5.88e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 102 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHL 176
Cdd:COG1121 135 RPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLL 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
270-470 |
6.87e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.02 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYY-DPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL-----K 335
Cdd:PRK13636 5 ILKVEELNYNYsDGTHAL-KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGrilfdgkpIDYSRKGLmklreS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 336 IGYFSQHHVEQL-------DLNVSAVELlarkfpGRPEEEYR----HQLGRYGISgELAMRPLASLSGGQKSRVAFAQMT 404
Cdd:PRK13636 84 VGMVFQDPDNQLfsasvyqDVSFGAVNL------KLPEDEVRkrvdNALKRTGIE-HLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 405 MPCPNFYILDEPTNHLD----METIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTrVEGG 470
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGN 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
302-461 |
7.67e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.22 E-value: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRG---------------IRHAHRNLKIGYFSQHHVEQLDL----NVSAVELLARKFP 362
Cdd:PRK11629 40 IVGSSGSGKSTLLHLLGGLDTPTSGdvifngqpmsklssaAKAELRNQKLGFIYQFHHLLPDFtaleNVAMPLLIGKKKP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 363 GRPEEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETIEALGRALNNFRGGV 439
Cdd:PRK11629 120 AEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTA 198
|
170 180
....*....|....*....|...
gi 1189438346 440 IL-VSHDERFIRLVCRELWVCEG 461
Cdd:PRK11629 199 FLvVTHDLQLAKRMSRQLEMRDG 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
269-445 |
7.80e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.81 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 269 PILQLDEVDFYY-DPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KI 336
Cdd:PRK13635 4 EIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGtITVGGMVLseetvwdvrrQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 337 GYFSQHHVEQLdlnVSA-VE------LLARKFPgRPE--EEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPC 407
Cdd:PRK13635 84 GMVFQNPDNQF---VGAtVQddvafgLENIGVP-REEmvERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189438346 408 PNFYILDEPTNHLD-------METIealgRALNNFRG-GVILVSHD 445
Cdd:PRK13635 159 PDIIILDEATSMLDprgrrevLETV----RQLKEQKGiTVLSITHD 200
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
271-423 |
8.19e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. 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: 213231 [Multi-domain] Cd Length: 211 Bit Score: 64.52 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIfsrLSVSADLESRICV-VGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL--KIGYF 339
Cdd:cd03264 1 LQLENLTKRYGKKRAL---DGVSLTLGPGMYGlLGPNGAGKTTLMRILATLTPPSSGtiridgqdVLKQPQKLrrRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 340 SQHHveQLDLNVSAVELLA------RKFPGRPEEEYRHQLGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYIL 413
Cdd:cd03264 78 PQEF--GVYPNFTVREFLDyiawlkGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170
....*....|
gi 1189438346 414 DEPTNHLDME 423
Cdd:cd03264 155 DEPTAGLDPE 164
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
106-199 |
8.34e-12 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 65.00 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQ-TWPSTILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:COG1127 141 ELSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
90
....*....|....*...
gi 1189438346 182 DGYrGDFETFIKSKQERL 199
Cdd:COG1127 221 IAE-GTPEELLASDDPWV 237
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
66-181 |
1.31e-11 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 64.05 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 66 ELAEIYAKLEEIEAdkaPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD------- 138
Cdd:cd03255 104 ELPLLLAGVPKKER---RERAEELLERVGLGDRLNHYPS-ELSGGQQQRVAIARALANDPKIILADEPTGNLDsetgkev 179
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1189438346 139 VRAILWLENYLQTwpsTILVVSHDRNfLNAIATDIIHLHSQRL 181
Cdd:cd03255 180 MELLRELNKEAGT---TIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
301-453 |
1.32e-11 |
|
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: 62.83 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 301 CVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLKigyfsqhhvEQLDLNVSAVellarkfpgrpeeeyrHQLg 374
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPdsgeilVDGKEVSFASPR---------DARRAGIAMV----------------YQL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 375 rygisgelamrplaslSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG---GVILVSHDERFIRL 451
Cdd:cd03216 84 ----------------SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVFE 147
|
..
gi 1189438346 452 VC 453
Cdd:cd03216 148 IA 149
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
292-481 |
1.36e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.33 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 292 VSADLES--RICVVGENGAGKSTMLKLLLGDLAPVRGirHAHRNLKIGYFsqhhveqLDLNV------SAVE---LLARk 360
Cdd:COG1134 45 VSFEVERgeSVGIIGRNGAGKSTLLKLIAGILEPTSG--RVEVNGRVSAL-------LELGAgfhpelTGREniyLNGR- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 361 FPGRPEEEYRH---------QLGRYgisgelAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDeptnhldmetiEALG-- 429
Cdd:COG1134 115 LLGLSRKEIDEkfdeivefaELGDF------IDQPVKTYSSGMRARLAFAVATAVDPDILLVD-----------EVLAvg 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 430 ---------RALNNFR---GGVILVSHDERFIRLVC-RELWVcEGGGVT---RVEGGFDQYRALLQEQ 481
Cdd:COG1134 178 daafqkkclARIRELResgRTVIFVSHSMGAVRRLCdRAIWL-EKGRLVmdgDPEEVIAAYEALLAGR 244
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
271-465 |
1.38e-11 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 64.08 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSrLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IR-----------HAHRNLKIGY 338
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRG-VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGsIRldgeditklppHERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 -------FSQHHVEQlDLNVSAvELLARKFPGRPEEEYrhqlGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFY 411
Cdd:TIGR03410 80 vpqgreiFPRLTVEE-NLLTGL-AALPRRSRKIPDEIY----ELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 412 ILDEPTNHLDMETIEALGRALNNFRG----GVILVSHDERFIRLVCRELWVCEGGGVT 465
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAeggmAILLVEQYLDFARELADRYYVMERGRVV 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
101-181 |
1.45e-11 |
|
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: 63.22 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 101 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AIL-WLENYLQTWPSTILVVSHDRNFLNAIATDIIHL 176
Cdd:cd03214 92 DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAhqiELLeLLRRLARERGKTVVMVLHDLNLAARYADRVILL 171
|
....*
gi 1189438346 177 HSQRL 181
Cdd:cd03214 172 KDGRI 176
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
271-453 |
1.48e-11 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. 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: 213196 [Multi-domain] Cd Length: 178 Bit Score: 62.97 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYdPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLG--------------DLAPVRGIRHAHRNlKI 336
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleepdsgsilidgeDLTDLEDELPPLRR-RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 337 GYFSQHHveQLDLNVSAVELLArkfpgrpeeeyrhqlgrYGisgelamrplasLSGGQKSRVAFAQMTMPCPNFYILDEP 416
Cdd:cd03229 79 GMVFQDF--ALFPHLTVLENIA-----------------LG------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1189438346 417 TNHLDMET---IEALGRALN-NFRGGVILVSHDERFIRLVC 453
Cdd:cd03229 128 TSALDPITrreVRALLKSLQaQLGITVVLVTHDLDEAARLA 168
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
271-445 |
1.48e-11 |
|
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: 63.69 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------KIGYFSQ 341
Cdd:cd03259 1 LELKGLSKTYGSVRAL-DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGeILIDGRDVtgvpperrNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 342 HH-------VEQldlNVsAVELLARKFPgRPEEEYRHQ--LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYI 412
Cdd:cd03259 80 DYalfphltVAE---NI-AFGLKLRGVP-KAEIRARVRelLELVGLEGLLNRYP-HELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1189438346 413 LDEPTNHLD----METIEALGRALNNFRGGVILVSHD 445
Cdd:cd03259 154 LDEPLSALDaklrEELREELKELQRELGITTIYVTHD 190
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
64-186 |
1.65e-11 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 63.93 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 64 AAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---R 140
Cdd:cd03266 95 ARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDR-RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVmatR 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1189438346 141 AILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLdGYRG 186
Cdd:cd03266 174 ALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV-VYEG 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
302-462 |
1.77e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 63.31 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLG--DLAPVRG-IRHAHRNLkigyfsqhhveqLDLNvsavellarkfpgrPEEeyRHQLGRY-- 376
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMGhpKYEVTEGeILFKGEDI------------TDLP--------------PEE--RARLGIFla 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 377 --------GISGELAMRPL-ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG---GVILVSH 444
Cdd:cd03217 83 fqyppeipGVKNADFLRYVnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITH 162
|
170 180
....*....|....*....|....*.
gi 1189438346 445 DER--------FIRLVCRELWVCEGG 462
Cdd:cd03217 163 YQRlldyikpdRVHVLYDGRIVKSGD 188
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
80-177 |
1.92e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 63.32 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 80 DKAPARASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTI 156
Cdd:cd03262 110 AEAEERALELLEKVGLADKADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTM 188
|
90 100
....*....|....*....|.
gi 1189438346 157 LVVSHDRNFLNAIATDIIHLH 177
Cdd:cd03262 189 VVVTHEMGFAREVADRVIFMD 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
78-176 |
1.97e-11 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II 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. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most 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: 213193 [Multi-domain] Cd Length: 205 Bit Score: 63.43 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 78 EADKAPARASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPS 154
Cdd:cd03226 99 ELDAGNEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGK 177
|
90 100
....*....|....*....|..
gi 1189438346 155 TILVVSHDRNFLNAIATDIIHL 176
Cdd:cd03226 178 AVIVITHDYEFLAKVCDRVLLL 199
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
267-447 |
1.98e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 63.61 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYY-DPKH--VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI---------------R 328
Cdd:COG4181 5 SAPIIELRGLTKTVgTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTvrlagqdlfaldedaR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 329 HAHRNLKIGYFSQHhvEQLDLNVSAVE--LLARKFPGRPE--EEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMT 404
Cdd:COG4181 85 ARLRARHVGFVFQS--FQLLPTLTALEnvMLPLELAGRRDarARARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1189438346 405 MPCPNFYILDEPTNHLDMET---IEALGRALNNFRGG-VILVSHDER 447
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATgeqIIDLLFELNRERGTtLVLVTHDPA 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
292-458 |
2.00e-11 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 64.00 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 292 VSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRH--AHR-----------------------NLKI 336
Cdd:cd03219 19 VSFSVRpgEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlfdgedITGlpPHEiarlgigrtfqiprlfpeltvleNVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 337 GYFSQHHVEQLDLNVSAVELLARkfpgrpeEEYRHQLGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEP 416
Cdd:cd03219 99 AAQARTGSGLLLARARREEREAR-------ERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1189438346 417 T---NHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWV 458
Cdd:cd03219 171 AaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTV 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
73-181 |
2.57e-11 |
|
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: 62.92 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 73 KLEEIEADKAPARASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQT- 151
Cdd:cd03259 98 KLRGVPKAEIRARVRELLELVGLEGLLNRYP-HELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKEl 176
|
90 100 110
....*....|....*....|....*....|...
gi 1189438346 152 ---WPSTILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:cd03259 177 qreLGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
302-451 |
2.74e-11 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 62.62 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLL----GDLAPvRGIRHAHRNLKIGyfSQHHVEQLDLNVSAVE----LLARKFPGRPEEEYRHQl 373
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPP-NSKGGAHDPKLIR--EGEVRAQVKLAFENANgkkyTITRSLAILENVIFCHQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 374 gryGISGELAMRPLASLSGGQKS------RVAFAQ-MTMPCPnFYILDEPTNHLDMETIE-ALGRALNNFRGG----VIL 441
Cdd:cd03240 103 ---GESNWPLLDMRGRCSGGEKVlasliiRLALAEtFGSNCG-ILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIV 178
|
170
....*....|
gi 1189438346 442 VSHDERFIRL 451
Cdd:cd03240 179 ITHDEELVDA 188
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
276-444 |
3.64e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. 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: 213221 [Multi-domain] Cd Length: 229 Bit Score: 63.01 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 276 VDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLG-----------DLAPVRGI-RHAHRNlKIGY----- 338
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydpqkgqiliDGIDIRDIsRKSLRS-MIGVvlqdt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 --FSQHHVEQLDLN----------VSAVELLARKFPGRPEEEYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTMP 406
Cdd:cd03254 87 flFSGTIMENIRLGrpnatdeeviEAAKEAGAHDFIMKLPNGYDTVLGENG----------GNLSQGERQLLAIARAMLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438346 407 CPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSH 444
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAH 196
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
105-162 |
3.64e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 63.57 E-value: 3.64e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDV--RAIL--WLENYLQTWPSTILVVSHD 162
Cdd:COG1116 137 HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltRERLqdELLRLWQETGKTVLFVTHD 198
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
81-199 |
3.84e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 81 KAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTIL 157
Cdd:PRK10619 127 EARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMV 206
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1189438346 158 VVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERL 199
Cdd:PRK10619 207 VVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
303-458 |
4.05e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 63.12 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 303 VGENGAGKSTMLKLLLGDLAPVRG-------------IRHAHRnlkIGY-FSQHhvEQLDLNVSAVE---LLARKFpGRP 365
Cdd:cd03267 53 IGPNGAGKTTTLKILSGLLQPTSGevrvaglvpwkrrKKFLRR---IGVvFGQK--TQLWWDLPVIDsfyLLAAIY-DLP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 366 EEEYRHQLGRygIS-----GELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETIEALGRALNNFRG 437
Cdd:cd03267 127 PARFKKRLDE--LSelldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqENIRNFLKEYNRERG 204
|
170 180
....*....|....*....|..
gi 1189438346 438 G-VILVSHDERFIRLVCRELWV 458
Cdd:cd03267 205 TtVLLTSHYMKDIEALARRVLV 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
106-470 |
4.08e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYL-QTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 182 dgyrgdFETfikSKQERLLNQqreyeAQQQYRQhiqvfidrfrynanrasqvqsklKMLEKLPELKPVDKESEvvmkfpd 261
Cdd:PRK15134 236 ------VEQ---NRAATLFSA-----PTHPYTQ-----------------------KLLNSEPSGDPVPLPEP------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 262 gfekfSPPILQLDEVDFYYDPKHVIFSRL--------SVSADL---ESrICVVGENGAGKSTMlKLLLGDLAPVRG---- 326
Cdd:PRK15134 272 -----ASPLLDVEQLQVAFPIRKGILKRTvdhnvvvkNISFTLrpgET-LGLVGESGSGKSTT-GLALLRLINSQGeiwf 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 327 ----IRHAHRNLKIGYFSQHHVEQLD--------LNVSAV--ELLARKFP----GRPEEEYRHQLGRYGISGELAMRPLA 388
Cdd:PRK15134 345 dgqpLHNLNRRQLLPVRHRIQVVFQDpnsslnprLNVLQIieEGLRVHQPtlsaAQREQQVIAVMEEVGLDPETRHRYPA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 389 SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD---METIEALGRALNN-FRGGVILVSHDERFIRLVCRELWVCEGGGV 464
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLQQkHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
....*.
gi 1189438346 465 trVEGG 470
Cdd:PRK15134 505 --VEQG 508
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
107-181 |
4.27e-11 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 61.46 E-value: 4.27e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSHDRNFLnAIATDIIHLHSQRL 181
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVegeRALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
271-464 |
4.39e-11 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). 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.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 62.45 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSrLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHA--HR--NLKIGY 338
Cdd:cd03224 1 LEVENLNAGYGKSQILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsirfdgrdITGLppHEraRAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 -------FSQHHVEQlDLNVSAVELLARKFPGRPEE---------EYRHQLGrygisgelamrplASLSGGQKSRVAFAQ 402
Cdd:cd03224 80 vpegrriFPELTVEE-NLLLGAYARRRAKRKARLERvyelfprlkERRKQLA-------------GTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 403 MTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VILVSHDERFIRLVCRELWVCEGGGV 464
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgvtILLVEQNARFALEIADRAYVLERGRV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
267-453 |
5.07e-11 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 62.69 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDPKHVifsrLS-VSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL-------- 334
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVV----LDgVSLDVPrgEILAIIGGSGSGKSVLLKLIIGLLRPDSGeILVDGQDItglsekel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 335 -----KIGY-------FSqhhveqlDLNVSA-VELLARKFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSR 397
Cdd:COG1127 78 yelrrRIGMlfqggalFD-------SLTVFEnVAFPLREHTDLSEAEIRELvlekLELVGLPGAADKMP-SELSGGMRKR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 398 VAFAQMTMPCPNFYILDEPTNHLD---METIEALGRALNNFRGG-VILVSHDERFIRLVC 453
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDpitSAVIDELIRELRDELGLtSVVVTHDLDSAFAIA 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
300-445 |
5.34e-11 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 63.22 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRG-----------------IRHahrnlKIGYFSQHHVEQLdlnVSAV-------- 354
Cdd:TIGR04520 31 VAIIGHNGSGKSTLAKLLNGLLLPTSGkvtvdgldtldeenlweIRK-----KVGMVFQNPDNQF---VGATveddvafg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 355 -ELLarkfpGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQ-MTMPcPNFYILDEPTNHLD------- 421
Cdd:TIGR04520 103 lENL-----GVPREEMRKRvdeaLKLVGME-DFRDREPHLLSGGQKQRVAIAGvLAMR-PDIIILDEATSMLDpkgrkev 175
|
170 180
....*....|....*....|....*
gi 1189438346 422 METIealgRALNNFRG-GVILVSHD 445
Cdd:TIGR04520 176 LETI----RKLNKEEGiTVISITHD 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
270-465 |
5.71e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.72 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGY 338
Cdd:PRK11231 2 TLRTENLTVGYGTKRIL-NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGtVFLGDKPIsmlssrqlarRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQHHVEQLDLNVSavELLAR------KFPGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRvAFAQMTMPC- 407
Cdd:PRK11231 81 LPQHHLTPEGITVR--ELVAYgrspwlSLWGRLSAEDNARvnqaMEQTRIN-HLADRRLTDLSGGQRQR-AFLAMVLAQd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 408 PNFYILDEPTNHLDM-ETIEALG--RALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVT 465
Cdd:PRK11231 157 TPVVLLDEPTTYLDInHQVELMRlmRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
300-424 |
5.75e-11 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 62.70 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLK--------------LLLGDLAPVRG--IRHAHRnlKIGYFSQHH--VEQLDL--NV-------- 351
Cdd:TIGR02315 31 VAIIGPSGAGKSTLLRcinrlvepssgsilLEGTDITKLRGkkLRKLRR--RIGMIFQHYnlIERLTVleNVlhgrlgyk 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 352 SAVELLARKFPGRPEEEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET 424
Cdd:TIGR02315 109 PTWRSLLGRFSEEDKERALSALERVGLA-DKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKT 180
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
303-444 |
5.91e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. 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: 213236 [Multi-domain] Cd Length: 210 Bit Score: 61.91 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 303 VGENGAGKSTMLKLLLGDLAPVRGIRH--------AHRNlKIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQ-- 372
Cdd:cd03269 32 LGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldiAARN-RIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRid 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 373 --LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VILVSH 444
Cdd:cd03269 111 ewLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTH 186
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
107-180 |
5.96e-11 |
|
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: 60.86 E-value: 5.96e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR-AILWLENyLQTWP--STILVVSHDRNfLNAIATDIIHLHSQR 180
Cdd:cd03228 97 LSGGQRQRIAIARALLRDPPILILDEATSALDPEtEALILEA-LRALAkgKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
267-444 |
6.22e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLKIGY 338
Cdd:PRK13543 8 APPLLAAHALAFSRNEE-PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGqiqidgktATRGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSqhHVEQLDLNVSAVELL----------ARKFPGrpeeeyrHQLGRYGISGElAMRPLASLSGGQKSRVAFAQMTMPCP 408
Cdd:PRK13543 87 LG--HLPGLKADLSTLENLhflcglhgrrAKQMPG-------SALAIVGLAGY-EDTLVRQLSAGQKKRLALARLWLSPA 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1189438346 409 NFYILDEPTNHLDMETIEALGRALN---NFRGGVILVSH 444
Cdd:PRK13543 157 PLWLLDEPYANLDLEGITLVNRMISahlRGGGAALVTTH 195
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
105-162 |
9.69e-11 |
|
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: 61.33 E-value: 9.69e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDV--RAIL--WLENYLQTWPSTILVVSHD 162
Cdd:cd03293 130 HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltREQLqeELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
85-181 |
1.00e-10 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; 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: 213228 [Multi-domain] Cd Length: 235 Bit Score: 61.75 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 85 RASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAILWLENYLQTwpsTIL 157
Cdd:cd03261 116 IVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELGL---TSI 191
|
90 100
....*....|....*....|....
gi 1189438346 158 VVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:cd03261 192 MVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
67-181 |
1.18e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 61.58 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 67 LAEIYakleEIEADKAPARASVILAGLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLE 146
Cdd:cd03267 119 LAAIY----DLPPARFKKRLDELSELLDLEELLDT-PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
90 100 110
....*....|....*....|....*....|....*....
gi 1189438346 147 NYLQTW----PSTILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:cd03267 194 NFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
283-449 |
1.21e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 283 KHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGdlapvrgirhAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFP 362
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG----------ALKGTPVAGCVDVPDNQFGREASLIDAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 363 GRPEEEYrhqLGRYGISGELAM-RPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRAL----NNFRG 437
Cdd:COG2401 112 FKDAVEL---LNAVGLSDAVLWlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLqklaRRAGI 188
|
170
....*....|..
gi 1189438346 438 GVILVSHDERFI 449
Cdd:COG2401 189 TLVVATHHYDVI 200
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
74-186 |
1.25e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 61.22 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 74 LEEIEADKAPARASV--ILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWL--E 146
Cdd:COG2884 104 LRVTGKSRKEIRRRVreVLDLVGLSDKAKALP-HELSGGEQQRVAIARALVNRPELLLADEPTGNLDpetSWEIMELleE 182
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1189438346 147 -NYLQTwpsTILVVSHDRNFLNAIATDIIHLHSQRL--DGYRG 186
Cdd:COG2884 183 iNRRGT---TVLIATHDLELVDRMPKRVLELEDGRLvrDEARG 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
302-470 |
1.29e-10 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. 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: 213225 [Multi-domain] Cd Length: 233 Bit Score: 61.44 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLL-----------------LGDLAPvRGIRHAHRnlKIGYFSQHhveqldlnvsaVELLARK---- 360
Cdd:cd03258 36 IIGRSGAGKSTLIRCInglerptsgsvlvdgtdLTLLSG-KELRKARR--RIGMIFQH-----------FNLLSSRtvfe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 361 ---FP----GRP----EEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IE 426
Cdd:cd03258 102 nvaLPleiaGVPkaeiEERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1189438346 427 ALGRALNNFRG-GVILVSHDERFIRLVCRELWVCEGGGVtrVEGG 470
Cdd:cd03258 181 ALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEV--VEEG 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
292-457 |
1.42e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 61.01 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 292 VSADLES--RICVVGENGAGKSTMLKLLLGDLAPVRGirHAHRNLKIGYFsqhhveqLDLNVSavelLARKFPGRpeeEY 369
Cdd:cd03220 41 VSFEVPRgeRIGLIGRNGAGKSTLLRLLAGIYPPDSG--TVTVRGRVSSL-------LGLGGG----FNPELTGR---EN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 370 RHQLGR-YGIS-----------------GELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRA 431
Cdd:cd03220 105 IYLNGRlLGLSrkeidekideiiefselGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRR 184
|
170 180 190
....*....|....*....|....*....|
gi 1189438346 432 LNNFR---GGVILVSHDERFIRLVC-RELW 457
Cdd:cd03220 185 LRELLkqgKTVILVSHDPSSIKRLCdRALV 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
89-162 |
1.72e-10 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213264 [Multi-domain] Cd Length: 214 Bit Score: 60.77 E-value: 1.72e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 89 ILAGLGFTPkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS----TILVVSHD 162
Cdd:cd03297 115 LLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKnlniPVIFVTHD 191
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
285-451 |
2.12e-10 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 59.30 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 285 VIFSRLSVSADLESRICVVGENGAGKSTMLKlllgDLAPVRGIRHAHRNlkigyfsQHHVEQLDLNVSAVELLARKFpgr 364
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILD----AIGLALGGAQSATR-------RRSGVKAGCIVAAVSAELIFT--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 365 peeeyRHQlgrygisgelamrplasLSGGQKSRVAFA-----QMTMPCPnFYILDEPTNHLDMETIEALGRALNNFRGG- 438
Cdd:cd03227 75 -----RLQ-----------------LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKg 131
|
170
....*....|....*
gi 1189438346 439 --VILVSHDERFIRL 451
Cdd:cd03227 132 aqVIVITHLPELAEL 146
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-162 |
2.14e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. 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: 213232 [Multi-domain] Cd Length: 220 Bit Score: 60.46 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 22 VAGDDTpalqsVLESDSVREDL------LRRERELTAQiaagraegseaaELAEIYAKLEEIEADKAPARASVILAGLGF 95
Cdd:cd03265 59 VAGHDV-----VREPREVRRRIgivfqdLSVDDELTGW------------ENLYIHARLYGVPGAERRERIDELLDFVGL 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 96 TPKmQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV--RAILW--LENYLQTWPSTILVVSHD 162
Cdd:cd03265 122 LEA-ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPqtRAHVWeyIEKLKEEFGMTILLTTHY 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
286-477 |
2.46e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.17 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 286 IFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNlkIGYFSQHHVEQLDLNVSAVELLARKFPGR 364
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGtVLVAGDD--VEALSARAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 365 PEEEY-RH-QLGRYGISGE-----------------LAMRPLASLSGGQKSRV----AFAQMTmpcPNFyILDEPTNHLD 421
Cdd:PRK09536 96 QVVEMgRTpHRSRFDTWTEtdraaveramertgvaqFADRPVTSLSGGERQRVllarALAQAT---PVL-LLDEPTASLD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 422 M----ETIEALGRALNNFRGGVILVsHDERFIRLVCRELWVCEGGGVT------------RVEGGFDQYRAL 477
Cdd:PRK09536 172 InhqvRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRaagppadvltadTLRAAFDARTAV 242
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
271-445 |
2.50e-10 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 61.31 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPK----HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-------------------I 327
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGtvtidgrditakkkkklkdL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 328 RHahrnlKIGY---FSQHhveQL--------------DLNVSAVELLARKFpgrpeeEYRHQLGrygISGELAMRPLASL 390
Cdd:TIGR04521 81 RK-----KVGLvfqFPEH---QLfeetvykdiafgpkNLGLSEEEAEERVK------EALELVG---LDEEYLERSPFEL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 391 SGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEALGRALNNfrgGVILVSHD 445
Cdd:TIGR04521 144 SGGQMRRVAIAGVLAMEPEVLILDEPTAGLDpkgrkeiLDLFKRLHKEKGL---TVILVTHS 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
271-461 |
2.92e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 60.15 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSrLSVSADleSRICVVGENGAGKSTMLKLLLGDLAPVRG-IR-----HAHR------------ 332
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD-LTIAAG--ERVAILGPSGAGKSTLLNLIAGFLPPDSGrILwngqdLTALppaerpvsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 333 --NLkigyFSQHHVEQldlNVSavelLARKfPG-RPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTM 405
Cdd:COG3840 79 enNL----FPHLTVAQ---NIG----LGLR-PGlKLTAEQRAQveqaLERVGLAGLLDRLP-GQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 406 ---PCpnfYILDEPTNHLD-------METIEALGRALNNfrgGVILVSHD-ERFIRLVCRELWVCEG 461
Cdd:COG3840 146 rkrPI---LLLDEPFSALDpalrqemLDLVDELCRERGL---TVLMVTHDpEDAARIADRVLLVADG 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
301-453 |
3.08e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 60.14 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 301 CVV--GENGAGKSTMLKLLLGDLAPVRG---IRHAHRNL----------------KIGYFSQHhveqldLN----VSAVE 355
Cdd:COG4778 39 CVAltGPSGAGKSTLLKCIYGNYLPDSGsilVRHDGGWVdlaqaspreilalrrrTIGYVSQF------LRviprVSALD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 356 -----LLARkfpGRPEEEYRHQ----LGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET-- 424
Cdd:COG4778 113 vvaepLLER---GVDREEARARarelLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANra 189
|
170 180 190
....*....|....*....|....*....|..
gi 1189438346 425 --IEALGRALNnfRG-GVILVSHDERFIRLVC 453
Cdd:COG4778 190 vvVELIEEAKA--RGtAIIGIFHDEEVREAVA 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
272-445 |
4.32e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 60.10 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 272 QLDEVDFYYDPKHVIFSrlsVSADLESR--ICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlKIgyfsqhHVEQLDL 349
Cdd:COG4604 3 EIKNVSKRYGGKVVLDD---VSLTIPKGgiTALIGPNGAGKSTLLSMISRLLPPDSG--------EV------LVDGLDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 350 NVSAVELLARK------------------------FP---GRPEEEYRHQLGRYgIS----GELAMRPLASLSGGQKSR- 397
Cdd:COG4604 66 ATTPSRELAKRlailrqenhinsrltvrelvafgrFPyskGRLTAEDREIIDEA-IAyldlEDLADRYLDELSGGQRQRa 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 398 -VA--FAQMTMpcpnfYI-LDEPTNHLDM----ETIEALGRALNNFRGGVILVSHD 445
Cdd:COG4604 145 fIAmvLAQDTD-----YVlLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
105-162 |
4.94e-10 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 59.50 E-value: 4.94e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL----QTWpsTILVVSHD 162
Cdd:cd03260 140 LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIaelkKEY--TIVIVTHN 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
271-450 |
4.97e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 59.02 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPK----HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirHAHRNLKIGYFSQ----- 341
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG--SVSVPGSIAYVSQepwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 342 -------------HHVEQLDLNVSAVELLA--RKFPGRPEEEyrhqLGRYGIsgelamrplaSLSGGQKSRVAFAQMTMP 406
Cdd:cd03250 79 ngtirenilfgkpFDEERYEKVIKACALEPdlEILPDGDLTE----IGEKGI----------NLSGGQKQRISLARAVYS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1189438346 407 CPNFYILDEPTNHLDMET---I--EALGRALNNFRgGVILVSHDERFIR 450
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgrhIfeNCILGLLLNNK-TRILVTHQLQLLP 192
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
76-139 |
5.65e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 61.62 E-value: 5.65e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 76 EIEADKAPARASVI--LAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 139
Cdd:COG4172 393 GPGLSAAERRARVAeaLEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
66-181 |
5.68e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 59.29 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 66 ELAEIYAKleeIEADKAPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD------V 139
Cdd:COG1136 108 ALPLLLAG---VSRKERRERARELLERVGLGDRLDHRPS-QLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeeV 183
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1189438346 140 RAIlwLENYLQTWPSTILVVSHDRNFLnAIATDIIHLHSQRL 181
Cdd:COG1136 184 LEL--LRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
105-181 |
5.81e-10 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 61.32 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIlwLENYLQTWP-STILVVSHDRNFLnAIATDIIHLHSQR 180
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAateQAL--LADLLEALAgRTVLLITHRLAGL-ERMDRILVLEDGR 546
|
.
gi 1189438346 181 L 181
Cdd:COG4987 547 I 547
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
271-444 |
5.95e-10 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 58.48 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKH-VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlKIgYFSQHHVEQLDL 349
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQG--------EI-TLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 350 NVS-AVELLARKfPGRPEEEYRHQLGRygisgelamrplaSLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEAL 428
Cdd:cd03247 72 ALSsLISVLNQR-PYLFDTTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170
....*....|....*...
gi 1189438346 429 GRALNNFRGG--VILVSH 444
Cdd:cd03247 138 LSLIFEVLKDktLIWITH 155
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
77-176 |
6.90e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 58.98 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 77 IEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILwleNYLQ 150
Cdd:COG4778 123 VDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravVVELI---EEAK 199
|
90 100
....*....|....*....|....*.
gi 1189438346 151 TWPSTILVVSHDRNFLNAIATDIIHL 176
Cdd:COG4778 200 ARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
282-452 |
7.20e-10 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 61.21 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 282 PKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL---KIGYFSQ--------- 341
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGsvrldgadLKQWDRETfgkHIGYLPQdvelfpgtv 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 342 -HHVEQLDLNVSAVELL-ARKFPG------RPEEEYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTMPCPNFYIL 413
Cdd:TIGR01842 409 aENIARFGENADPEKIIeAAKLAGvhelilRLPDGYDTVIGPGG----------ATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1189438346 414 DEPTNHLDMETIEALGRALNNF--RGG-VILVSHDERFIRLV 452
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALkaRGItVVVITHRPSLLGCV 520
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
108-163 |
7.20e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 60.55 E-value: 7.20e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAIL--WLENYLQTWPSTILVVSHDR 163
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDakVRKELrrWLRRLHDELGGTTVFVTHDQ 194
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
80-198 |
8.04e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 8.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 80 DKAPARASVILAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILwleNYLQTWP 153
Cdd:COG4161 116 EQAREKAMKLLARLRLTDKADRFPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqVVEII---RELSQTG 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1189438346 154 STILVVSHDRNFLNAIATDIIHLHSQRLDGYrGDFETFIKSKQER 198
Cdd:COG4161 192 ITQVIVTHEVEFARKVASQVVYMEKGRIIEQ-GDASHFTQPQTEA 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
270-445 |
8.32e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.81 E-value: 8.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYY-DPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP---------VRGIRHAHRNL----- 334
Cdd:PRK13640 5 IVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskitVDGITLTAKTVwdire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 335 KIGYFSQHHVEQ-LDLNVS---AVELLARKFPgRPEEE--YRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCP 408
Cdd:PRK13640 85 KVGIVFQNPDNQfVGATVGddvAFGLENRAVP-RPEMIkiVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1189438346 409 NFYILDEPTNHLD---METIEALGRALNNFRG-GVILVSHD 445
Cdd:PRK13640 163 KIIILDESTSMLDpagKEQILKLIRKLKKKNNlTVISITHD 203
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
271-462 |
9.08e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 58.70 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIfsrLSVSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL-----K 335
Cdd:cd03262 1 IEIKNLHKSFGDFHVL---KGIDLTVKkgEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglkLTDDKKNInelrqK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 336 IGYFSQH-----HVEQLDlNVSaveLLARKFPGRPEEEY----RHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMP 406
Cdd:cd03262 78 VGMVFQQfnlfpHLTVLE-NIT---LAPIKVKGMSKAEAeeraLELLEKVGLADKADAYP-AQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 407 CPNFYILDEPTNHLDMETI-EALGRALNNFRGG--VILVSHDERFIRLVCRELWVCEGG 462
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVgEVLDVMKDLAEEGmtMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
79-183 |
9.37e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.95 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 79 ADKAPAR--ASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VR-AILWLENYLQTWP 153
Cdd:PRK09493 108 ASKEEAEkqARELLAKVGLAERAHHYPS-ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpeLRhEVLKVMQDLAEEG 186
|
90 100 110
....*....|....*....|....*....|..
gi 1189438346 154 STILVVSHDRNFLNAIATDIIHLHSQRL--DG 183
Cdd:PRK09493 187 MTMVIVTHEIGFAEKVASRLIFIDKGRIaeDG 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
80-162 |
9.88e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.67 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 80 DKAPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPST- 155
Cdd:PRK11629 120 AEINSRALEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVLADEPTGNLDARnadSIFQLLGELNRLQGTa 198
|
....*..
gi 1189438346 156 ILVVSHD 162
Cdd:PRK11629 199 FLVVTHD 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
105-183 |
1.13e-09 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 58.37 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHdRNFLNAIATDIIHLHSQRL- 181
Cdd:cd03245 139 RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRIv 217
|
...
gi 1189438346 182 -DG 183
Cdd:cd03245 218 aDG 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
266-472 |
1.20e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.25 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 266 FSPPILqLDEVDFYYDPKHVIFSRLSVSADLESR----ICVVGENGAGKSTMLKL------------LLGDL---APVRG 326
Cdd:PRK13645 3 FSKDII-LDNVSYTYAKKTPFEFKALNNTSLTFKknkvTCVIGTTGSGKSTMIQLtngliisetgqtIVGDYaipANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 327 IRHAHRNLK-IGYFSQHHVEQL-------DLNVSAVELLARKfpgrpEEEYR---HQLGRYGISGELAMRPLASLSGGQK 395
Cdd:PRK13645 82 IKEVKRLRKeIGLVFQFPEYQLfqetiekDIAFGPVNLGENK-----QEAYKkvpELLKLVQLPEDYVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 396 SRVAFAQMTMPCPNFYILDEPTNHLD----METIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGF 471
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
.
gi 1189438346 472 D 472
Cdd:PRK13645 237 E 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
265-421 |
1.45e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.85 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 265 KFSPPILQLDEVDFYYDPKH-VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirhahrNLKI-GY-FSQ 341
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSG------EIKIdGItISK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 342 HHVEQLDLNV-------------SAVE------LLARKFPgrPEE------EYRHQLgryGISGELAMRPLaSLSGGQKS 396
Cdd:PRK13632 76 ENLKEIRKKIgiifqnpdnqfigATVEddiafgLENKKVP--PKKmkdiidDLAKKV---GMEDYLDKEPQ-NLSGGQKQ 149
|
170 180
....*....|....*....|....*
gi 1189438346 397 RVAFAQMTMPCPNFYILDEPTNHLD 421
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLD 174
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
66-173 |
1.47e-09 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 57.90 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 66 ELAEIYAKLEEIEADKAPARASVILAGLGFTPKmQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA--IL 143
Cdd:cd03263 94 EHLRFYARLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASrrAI 172
|
90 100 110
....*....|....*....|....*....|..
gi 1189438346 144 WleNYLQTWP--STILVVSHDRNFLNAIATDI 173
Cdd:cd03263 173 W--DLILEVRkgRSIILTTHSMDEAEALCDRI 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
80-174 |
1.88e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.22 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 80 DKAPARASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTI 156
Cdd:PRK11264 119 EEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQEKRTM 197
|
90
....*....|....*...
gi 1189438346 157 LVVSHDRNFLNAIATDII 174
Cdd:PRK11264 198 VIVTHEMSFARDVADRAI 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
107-195 |
2.08e-09 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 59.77 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR--AILW--LENYLQTwpSTILVVSHDRNFLnAIATDIIHLHSQRLD 182
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLAKG--RTVILITHRLALL-AQADRILVLDDGRIV 550
|
90
....*....|...
gi 1189438346 183 GyRGDFETFIKSK 195
Cdd:COG4988 551 E-QGTHEELLAKN 562
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
287-445 |
2.15e-09 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213266 [Multi-domain] Cd Length: 235 Bit Score: 57.73 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 287 FSRLSVSADLE-SRICVV-GENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------KIGYFSQHHVEQLDLNVS--- 352
Cdd:cd03299 13 FKLKNVSLEVErGDYFVIlGPTGSGKSVLLETIAGFIKPDSGkILLNGKDItnlppekrDISYVPQNYALFPHMTVYkni 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 353 AVELLARKFPgRPEEEYR-HQLGRY-GISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET----IE 426
Cdd:cd03299 93 AYGLKKRKVD-KKEIERKvLEIAEMlGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklRE 170
|
170
....*....|....*....
gi 1189438346 427 ALGRALNNFRGGVILVSHD 445
Cdd:cd03299 171 ELKKIRKEFGVTVLHVTHD 189
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
107-162 |
2.27e-09 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 59.85 E-value: 2.27e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILwleNYLQTW--PSTILVVSHD 162
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAeteAIIL---ENLRRLlkGRTVIIIAHR 669
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
302-445 |
2.54e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 57.76 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIGYFSQHHVEQLDLNVSA--VELLARKFPGRPEE- 367
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeiLDEFRGSELQNYFTKLLEGDVKVIVKPqyVDLIPKAVKGKVGEl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 368 ----EYRHQLGRYGISGELAM---RPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME---TIEALGRALNNFRG 437
Cdd:cd03236 111 lkkkDERGKLDELVDQLELRHvldRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDN 190
|
....*...
gi 1189438346 438 GVILVSHD 445
Cdd:cd03236 191 YVLVVEHD 198
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
78-181 |
2.81e-09 |
|
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: 57.75 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 78 EADKAPARASVILAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AIL-WLENYLQTWP 153
Cdd:COG1120 112 AEDREAVEEALERTGLE---HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqlEVLeLLRRLARERG 188
|
90 100
....*....|....*....|....*...
gi 1189438346 154 STILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:COG1120 189 RTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
283-422 |
2.90e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.69 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 283 KHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG---------IRHAHRNL--KIGYFSQHHVEQLDLNV 351
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiQHYASKEVarRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 352 SavELLAR-KFPGRP---------EEEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 421
Cdd:PRK10253 99 Q--ELVARgRYPHQPlftrwrkedEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
.
gi 1189438346 422 M 422
Cdd:PRK10253 176 I 176
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
270-444 |
3.02e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.21 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVIFSRLSVSADLE----SRICVVGENGAGKSTMLKLLLGDLAPVRG-----------------IR 328
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEvkkgSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdivvsstskqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 329 HAHRnlKIGYFSQHHVEQL--DLNVSAVELLARKFPGRPEEEYR---HQLGRYGISGELAMRPLASLSGGQKSRVAFAQM 403
Cdd:PRK13643 81 PVRK--KVGVVFQFPESQLfeETVLKDVAFGPQNFGIPKEKAEKiaaEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438346 404 TMPCPNFYILDEPTNHLDMET---IEALGRALNNFRGGVILVSH 444
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
290-465 |
3.47e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.89 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 290 LSVSADLESRICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLK-----IGYFSQHHVEQL-------DLNV 351
Cdd:PRK13652 23 INFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPtsgsvlIRGEPITKENIRevrkfVGLVFQNPDDQIfsptveqDIAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 352 SAVELlarkfpGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEA 427
Cdd:PRK13652 103 GPINL------GLDEETVAHRvssaLHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1189438346 428 LGRALNNF--RGG--VILVSHDERFIRLVCRELWVCEGGGVT 465
Cdd:PRK13652 176 LIDFLNDLpeTYGmtVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
284-444 |
4.07e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 284 HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGdLA------------PVRGIRHA-HRNLK-IGyfsqhHVEQLDL 349
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-LArpdagevlwqgePIRRQRDEyHQDLLyLG-----HQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 350 NVSAVELL--ARKFPGRPEEEYRHQ-LGRYGISG-ELAmrPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI 425
Cdd:PRK13538 88 ELTALENLrfYQRLHGPGDDEALWEaLAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|..
gi 1189438346 426 EALGRALNNF--RGG-VILVSH 444
Cdd:PRK13538 166 ARLEALLAQHaeQGGmVILTTH 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
271-463 |
4.80e-09 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 55.24 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLlGDLAPVRG---IRHAHRNLkigYFsqhhveql 347
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWGSgriGMPEGEDL---LF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 348 dlnvsavellarkFPGRPeeeyrhqlgrYGISGELA---MRPLAS-LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME 423
Cdd:cd03223 69 -------------LPQRP----------YLPLGTLReqlIYPWDDvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438346 424 TIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGG 463
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGG 165
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
271-424 |
5.68e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 58.60 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI------------RHAHRNLkIGY 338
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEillngfslkdidRHTLRQF-INY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQhhvEQLDLNVSAVE-LLARKFPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSRVAFAQMTMPC 407
Cdd:TIGR01193 553 LPQ---EPYIFSGSILEnLLLGAKENVSQDEIWAACEIAEIKDDIENMPLgyqtelseegSSISGGQKQRIALARALLTD 629
|
170
....*....|....*..
gi 1189438346 408 PNFYILDEPTNHLDMET 424
Cdd:TIGR01193 630 SKVLILDESTSNLDTIT 646
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
94-161 |
5.84e-09 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 56.33 E-value: 5.84e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 94 GFTPKMQQQPTRE-------FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSH 161
Cdd:cd03248 131 SFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
271-470 |
6.17e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 56.34 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKH-VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIGY 338
Cdd:cd03252 1 ITFEHVRFRYKPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghdlalADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQhhvEQLDLNVSAVELLARKFPGRPEEEY--------RHQ------LGRYGISGELAmrplASLSGGQKSRVAFAQMT 404
Cdd:cd03252 81 VLQ---ENVLFNRSIRDNIALADPGMSMERVieaaklagAHDfiselpEGYDTIVGEQG----AGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 405 MPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLVCRELwVCEGGGVtrVEGG 470
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAHRLSTVKNADRII-VMEKGRI--VEQG 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
78-181 |
6.30e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 56.29 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 78 EADKAPARASVILAGLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPT---NMLDVRAILWLENYLQTWPS 154
Cdd:cd03219 116 EEREARERAEELLERVGLADLADR-PAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGI 194
|
90 100
....*....|....*....|....*..
gi 1189438346 155 TILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:cd03219 195 TVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
276-478 |
6.50e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.20 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 276 VDFYY--DPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLL-----------LGDLAPVRGIRHAHRNLKIGYFSQH 342
Cdd:TIGR00958 484 VSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptggqvLLDGVPLVQYDHHYLHRQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 343 HV-----------------EQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTM 405
Cdd:TIGR00958 564 PVlfsgsvreniaygltdtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG----------SQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 406 PCPNFYILDEPTNHLDMEtIEALGRALNNFRG-GVILVSHDERFIR-----LVCRELWVCEGGGVTRVEGGFDQYRALL 478
Cdd:TIGR00958 634 RKPRVLILDEATSALDAE-CEQLLQESRSRASrTVLLIAHRLSTVEradqiLVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
271-421 |
7.83e-09 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. 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: 213265 [Multi-domain] Cd Length: 211 Bit Score: 55.58 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYdpkHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAH------------- 331
Cdd:cd03298 1 VRLDKIRFSY---GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPqsgrvlINGVDVTAappadrpvsmlfq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 332 -RNLkigyFSQHHVEQ-LDLNVSavellarkfPG---RPEEEYRHQ--LGRYGISGELAMRPlASLSGGQKSRVAFAQMT 404
Cdd:cd03298 78 eNNL----FAHLTVEQnVGLGLS---------PGlklTAEDRQAIEvaLARVGLAGLEKRLP-GELSGGERQRVALARVL 143
|
170
....*....|....*..
gi 1189438346 405 MPCPNFYILDEPTNHLD 421
Cdd:cd03298 144 VRDKPVLLLDEPFAALD 160
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
98-162 |
8.96e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 8.96e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 98 KMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYL-QTWPSTILVVSHD 162
Cdd:PRK09473 154 RMKMYP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELkREFNTAIIMITHD 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
73-162 |
9.63e-09 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (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: 213262 [Multi-domain] Cd Length: 242 Bit Score: 55.77 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 73 KLEEIEADKAPARASVILAGLGFTPK--MQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILWLE-- 146
Cdd:cd03295 101 KLLKWPKEKIRERADELLALVGLDPAefADRYP-HELSGGQQQRVGVARALAADPPLLLMDEPFGALDpiTRDQLQEEfk 179
|
90
....*....|....*.
gi 1189438346 147 NYLQTWPSTILVVSHD 162
Cdd:cd03295 180 RLQQELGKTIVFVTHD 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
80-176 |
1.02e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.79 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 80 DKAPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAIlwleNYLQTW 152
Cdd:PRK11124 116 DQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSII----RELAET 190
|
90 100
....*....|....*....|....
gi 1189438346 153 PSTILVVSHDRNFLNAIATDIIHL 176
Cdd:PRK11124 191 GITQVIVTHEVEVARKTASRVVYM 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
73-162 |
1.16e-08 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213266 [Multi-domain] Cd Length: 235 Bit Score: 55.80 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 73 KLEEIEADKAPARASVILAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTW 152
Cdd:cd03299 97 KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKI 175
|
90
....*....|....
gi 1189438346 153 PS----TILVVSHD 162
Cdd:cd03299 176 RKefgvTVLHVTHD 189
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
102-162 |
1.18e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 54.93 E-value: 1.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 102 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHD 162
Cdd:NF040873 115 RQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
84-162 |
1.33e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 84 ARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRA-ILWLENYLQ-TWPSTILVV 159
Cdd:PRK15134 403 QQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAqILALLKSLQqKHQLAYLFI 482
|
...
gi 1189438346 160 SHD 162
Cdd:PRK15134 483 SHD 485
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
271-445 |
1.34e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.99 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVI----FSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI----------RHAHRNLK- 335
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTitiagyhitpETGNKNLKk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 336 ----IGYFSQHHVEQLDLN--VSAVELLARKFpGRPEEEYRHQ----LGRYGISGELAMRPLASLSGGQKSRVAFAQMTM 405
Cdd:PRK13641 83 lrkkVSLVFQFPEAQLFENtvLKDVEFGPKNF-GFSEDEAKEKalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1189438346 406 PCPNFYILDEPTNHLDMETIEALGRALNNF-RGG--VILVSHD 445
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGhtVILVTHN 204
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
267-473 |
1.44e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.70 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDPKHVIFSrlsVSADLESR--ICVVGENGAGKSTMLKLLLGDLAPVRGI----------------- 327
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRD---VSFDLYPGevLGIVGESGSGKTTLLNALSARLAPDAGEvhyrmrdgqlrdlyals 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 328 ----RHAHRNlKIGYFSQHHVEQLDLNVSA----VELL----ARKFpGRPEEEYRHQLGRYGI-SGELAMRPlASLSGGQ 394
Cdd:PRK11701 80 eaerRRLLRT-EWGFVHQHPRDGLRMQVSAggniGERLmavgARHY-GDIRATAGDWLERVEIdAARIDDLP-TTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 395 KSRVAFAQMTMPCPNFYILDEPTNHLDMeTIEAlgRALNNFRG-------GVILVSHDERFIRLVCRELWVCEGGGVtrV 467
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDV-SVQA--RLLDLLRGlvrelglAVVIVTHDLAVARLLAHRLLVMKQGRV--V 231
|
....*..
gi 1189438346 468 EGGF-DQ 473
Cdd:PRK11701 232 ESGLtDQ 238
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
270-445 |
1.68e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.47 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL-----KI 336
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGevlikgepIKYDKKSLlevrkTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 337 GYFSQHHVEQL-------DLNVSAVELlarkfpGRPEEEY----RHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTM 405
Cdd:PRK13639 81 GIVFQNPDDQLfaptveeDVAFGPLNL------GLSKEEVekrvKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1189438346 406 PCPNFYILDEPTNHLDMETIEALGRALN--NFRGGVILVS-HD 445
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYdlNKEGITIIIStHD 196
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
302-452 |
2.21e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.07 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLG-------------------DLAPvrgirhAHR-NLKIGYFSQHHVE----------QLDLN- 350
Cdd:COG0396 31 IMGPNGSGKSTLAKVLMGhpkyevtsgsilldgedilELSP------DERaRAGIFLAFQYPVEipgvsvsnflRTALNa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 351 VSAVELLARKFpgrpEEEYRHQLGRYGISGELAMRPL-ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALG 429
Cdd:COG0396 105 RRGEELSAREF----LKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVA 180
|
170 180
....*....|....*....|....*.
gi 1189438346 430 RALNNFRG---GVILVSHDERFIRLV 452
Cdd:COG0396 181 EGVNKLRSpdrGILIITHYQRILDYI 206
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
290-450 |
2.27e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.87 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 290 LSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRnlkigyFSQHHVEQLDlnvsavellarkfpgrpeeey 369
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPK------FSRNKLIFID--------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 370 rhQLGRY---GIsGELAM-RPLASLSGGQKSRVAFAQM--TMPCPNFYILDEPTNHLDMETIEALgraLNNFRG------ 437
Cdd:cd03238 67 --QLQFLidvGL-GYLTLgQKLSTLSGGELQRVKLASElfSEPPGTLFILDEPSTGLHQQDINQL---LEVIKGlidlgn 140
|
170
....*....|...
gi 1189438346 438 GVILVSHDERFIR 450
Cdd:cd03238 141 TVILIEHNLDVLS 153
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
304-444 |
2.46e-08 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 54.30 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 304 GENGAGKSTMLKLLLGDLAP------VRGIRhAHRN-----LKIGYFSQHhvEQLDLNVSAVELLArkFPGRPEEEYRHQ 372
Cdd:cd03266 38 GPNGAGKTTTLRMLAGLLEPdagfatVDGFD-VVKEpaearRRLGFVSDS--TGLYDRLTARENLE--YFAGLYGLKGDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 373 L--------GRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VIL 441
Cdd:cd03266 113 LtarleelaDRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgkcILF 191
|
...
gi 1189438346 442 VSH 444
Cdd:cd03266 192 STH 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
106-139 |
2.57e-08 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 55.44 E-value: 2.57e-08
10 20 30
....*....|....*....|....*....|....
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 139
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
270-445 |
2.65e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGY 338
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrVKVMGREVnaenekwvrsKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQHHVEQL-------DLNVSAVEL-LARKFPGRPEEEYRHQLGRYgisgELAMRPLASLSGGQKSRVAFAQMTMPCPNF 410
Cdd:PRK13647 84 VFQDPDDQVfsstvwdDVAFGPVNMgLDKDEVERRVEEALKAVRMW----DFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1189438346 411 YILDEPTNHLD---METIEALGRALNNFRGGVILVSHD 445
Cdd:PRK13647 160 IVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
302-445 |
2.73e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.33 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPvrgirhahrNLK-----------IGYFS----QHHVEQL---DLNVS----AVELLAR 359
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKP---------NLGdydeepswdevLKRFRgtelQDYFKKLangEIKVAhkpqYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 360 KFPGRPEE--EYRHQLGRY-GISGELAM-----RPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM-ETIEAlGR 430
Cdd:COG1245 175 VFKGTVREllEKVDERGKLdELAEKLGLenildRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyQRLNV-AR 253
|
170
....*....|....*...
gi 1189438346 431 ALNNFRGG---VILVSHD 445
Cdd:COG1245 254 LIRELAEEgkyVLVVEHD 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
302-445 |
2.80e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPvrgirhahrNLK-----------IGYFS----QHHVEQL---DLNVS----AVELLAR 359
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIP---------NLGdyeeepswdevLKRFRgtelQNYFKKLyngEIKVVhkpqYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 360 KFPGRPEEEYRH--QLGRYG-ISGELAM-----RPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM-ETIEA--L 428
Cdd:PRK13409 175 VFKGKVRELLKKvdERGKLDeVVERLGLenildRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrQRLNVarL 254
|
170
....*....|....*..
gi 1189438346 429 GRALNNFRgGVILVSHD 445
Cdd:PRK13409 255 IRELAEGK-YVLVVEHD 270
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
89-162 |
3.05e-08 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 55.50 E-value: 3.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 89 ILAGLGFTPkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL-WLENYLQTWPSTILVVSHD 162
Cdd:TIGR02142 115 VIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkYEILpYLERLHAEFGIPILYVSHS 191
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
292-462 |
3.11e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 54.81 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 292 VSADLESRICV--VGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIGYFSQHHVEQLDLNV------SAV--ELLARK 360
Cdd:TIGR02769 30 VSLSIEEGETVglLGRSGCGKSTLARLLLGLEKPAQGtVSFRGQDLYQLDRKQRRAFRRDVQLvfqdspSAVnpRMTVRQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 361 FPGRPEEEY------------RHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETI 425
Cdd:TIGR02769 110 IIGEPLRHLtsldeseqkariAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqAVI 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 1189438346 426 EALGRALNNfRGGV--ILVSHDERFIRLVCRELWVCEGG 462
Cdd:TIGR02769 190 LELLRKLQQ-AFGTayLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-162 |
3.28e-08 |
|
thiol reductant ABC exporter, CydC 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.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 55.83 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 20 QEVAGDDTPALQSVLESD------SVREDLLrrereltaqIAAGRAEGSEAAELAEiYAKLEEIeADKAPARASVILAGL 93
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDahlfdtTVRENLR---------LARPDATDEELWAALE-RVGLADW-LRALPDGLDTVLGEG 468
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 94 GftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAIL-WLENYLQTWPS-TILVVSHD 162
Cdd:TIGR02868 469 G----------ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
84-174 |
3.32e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.68 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 84 ARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDvrAI-----------LWLENYLqtw 152
Cdd:PRK11247 112 DAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALD--ALtriemqdliesLWQQHGF--- 185
|
90 100
....*....|....*....|..
gi 1189438346 153 psTILVVSHDRNFLNAIATDII 174
Cdd:PRK11247 186 --TVLLVTHDVSEAVAMADRVL 205
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
108-168 |
3.41e-08 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 55.91 E-value: 3.41e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAILwlenYLQTWPSTILVVSHDRNFLNA 168
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIR----ALKARGATVVVITHRPSLLAA 532
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
93-162 |
3.41e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 55.49 E-value: 3.41e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 93 LGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILwleNYLQTWPST----ILVVSHD 162
Cdd:COG4148 121 LGIGHLLDRRPAT-LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkAEIL---PYLERLRDEldipILYVSHS 193
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
302-445 |
3.97e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 55.15 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL---------KIGYFSQH-----H--VEQldlNVSAVelLARKFPGR 364
Cdd:COG1118 33 LLGPSGSGKTTLLRIIAGLETPDSGrIVLNGRDLftnlpprerRVGFVFQHyalfpHmtVAE---NIAFG--LRVRPPSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 365 PE--EEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD------METIeaLGRALNNFR 436
Cdd:COG1118 108 AEirARVEELLELVQLEG-LADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRRW--LRRLHDELG 184
|
....*....
gi 1189438346 437 GGVILVSHD 445
Cdd:COG1118 185 GTTVFVTHD 193
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
74-138 |
4.21e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 53.98 E-value: 4.21e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 74 LEEIEADKAPARASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:COG4181 115 LELAGRRDARARARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
103-197 |
4.54e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.28 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 103 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHDRNFLNAIATDIIHLHSQR 180
Cdd:PRK14246 150 PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGE 229
|
90
....*....|....*..
gi 1189438346 181 LDGYRGDFETFIKSKQE 197
Cdd:PRK14246 230 LVEWGSSNEIFTSPKNE 246
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
379-485 |
4.72e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 379 SGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWV 458
Cdd:PLN03073 334 TPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILH 413
|
90 100
....*....|....*....|....*..
gi 1189438346 459 CEGGGVTRVEGGFDQYRALLQEQFRRE 485
Cdd:PLN03073 414 LHGQKLVTYKGDYDTFERTREEQLKNQ 440
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
31-174 |
4.73e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.59 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 31 QSVLESDSVREDLLRRERELTAQIAAG-----RAEGSEAAELAEIYAKLEEIEADkapARASVILAGLGFTPKMQQQPTR 105
Cdd:PRK11308 77 QDLLKADPEAQKLLRQKIQIVFQNPYGslnprKKVGQILEEPLLINTSLSAAERR---EKALAMMAKVGLRPEHYDRYPH 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV--RA-ILWLENYLQTWPSTILV-VSHDRNFLNAIATDII 174
Cdd:PRK11308 154 MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVsvQAqVLNLMMDLQQELGLSYVfISHDLSVVEHIADEVM 226
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
77-171 |
4.95e-08 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 53.55 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 77 IEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWP 153
Cdd:TIGR02324 120 VPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTASLDAanrQVVVELIAEAKARG 199
|
90
....*....|....*...
gi 1189438346 154 STILVVSHDRNFLNAIAT 171
Cdd:TIGR02324 200 AALIGIFHDEEVRELVAD 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
82-181 |
6.65e-08 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 53.18 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 82 APARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILV 158
Cdd:cd03292 113 IRKRVPAALELVGLSHKHRALPA-ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDpdtTWEIMNLLKKINKAGTTVVV 191
|
90 100
....*....|....*....|...
gi 1189438346 159 VSHDRNFLNAIATDIIHLHSQRL 181
Cdd:cd03292 192 ATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
273-444 |
6.80e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.87 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 273 LDEVDFYYDPKhVIFSRL-----SVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIGYfSQHHVEQ 346
Cdd:PRK13634 5 FQKVEHRYQYK-TPFERRalydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtVTIGERVITAGK-KNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 347 LDLNVSAVellaRKFP--------------------GRPEEE----YRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQ 402
Cdd:PRK13634 83 LRKKVGIV----FQFPehqlfeetvekdicfgpmnfGVSEEDakqkAREMIELVGLPEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 403 MTMPCPNFYILDEPTNHLD-------METIEALGRalnnfRGG--VILVSH 444
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDpkgrkemMEMFYKLHK-----EKGltTVLVTH 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-240 |
7.39e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.12 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 22 VAGDDTpalqSVLESDSVREdlLRRER--------ELTAQIAAgraegSEAAELAEIYAKLEEieaDKAPARASVILAGL 93
Cdd:PRK10535 67 VAGQDV----ATLDADALAQ--LRREHfgfifqryHLLSHLTA-----AQNVEVPAVYAGLER---KQRLLRAQELLQRL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 94 GFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILwleNYLQTWPSTILVVSHDRNfLN 167
Cdd:PRK10535 133 GLEDRVEYQPS-QLSGGQQQRVSIARALMNGGQVILADEPTGALDshsgeeVMAIL---HQLRDRGHTVIIVTHDPQ-VA 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 168 AIATDIIHLHsqrldgyrgDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFR------YNANRASQVQSKLKML 240
Cdd:PRK10535 208 AQAERVIEIR---------DGEIVRNPPAQEKVNVAGGTEPVVNTASGWRQFVSGFRealtmaWRAMAANKMRTLLTML 277
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
45-181 |
7.43e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 53.66 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 45 RRERELTAQ--IAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALF 122
Cdd:TIGR02769 87 RRDVQLVFQdsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALA 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 123 ARPDLLLLDEPTNMLDV----RAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:TIGR02769 167 VKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
78-177 |
7.44e-08 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 53.50 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 78 EADKAPARASVILAGLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPT---NMLDVRAIL-WLENYLQTWP 153
Cdd:COG0411 125 EEREARERAEELLERVGLADRADE-PAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAeLIRRLRDERG 203
|
90 100
....*....|....*....|....
gi 1189438346 154 STILVVSHDRNFLNAIATDIIHLH 177
Cdd:COG0411 204 ITILLIEHDMDLVMGLADRIVVLD 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
84-161 |
7.68e-08 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 53.16 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 84 ARASVILAGLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTW----PSTILVV 159
Cdd:COG1119 121 ERARELLELLGLAHLADR-PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaegAPTLVLV 199
|
..
gi 1189438346 160 SH 161
Cdd:COG1119 200 TH 201
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
271-421 |
8.28e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.05 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVifsRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG------IRHAH------------- 331
Cdd:PRK10771 2 LKLTDITWLYHHLPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGsltlngQDHTTtppsrrpvsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 332 -RNLkigyFSQHHVEQ---LDLNvsavellarkfPG-RPEEEYRHQL----GRYGISGELAMRPlASLSGGQKSRVAFAQ 402
Cdd:PRK10771 79 eNNL----FSHLTVAQnigLGLN-----------PGlKLNAAQREKLhaiaRQMGIEDLLARLP-GQLSGGQRQRVALAR 142
|
170
....*....|....*....
gi 1189438346 403 MTMPCPNFYILDEPTNHLD 421
Cdd:PRK10771 143 CLVREQPILLLDEPFSALD 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
261-462 |
8.70e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 261 DGFEKFSPPILQLDEVDF--YYDPKHVIfsrlsvsadlesricvVGENGAGKSTMLKLLLGDLAPVRGI---------RH 329
Cdd:PRK09700 9 AGIGKSFGPVHALKSVNLtvYPGEIHAL----------------LGENGAGKSTLMKVLSGIHEPTKGTitinninynKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 330 AHR---NLKIGYFSQHH--VEQLDL--NVSAVELLARKFPGRPEEEYRHQ-------LGRYGISGELAMRpLASLSGGQK 395
Cdd:PRK09700 73 DHKlaaQLGIGIIYQELsvIDELTVleNLYIGRHLTKKVCGVNIIDWREMrvraammLLRVGLKVDLDEK-VANLSISHK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 396 SRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG---GVILVSHDERFIRLVCRELWVCEGG 462
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
38-161 |
8.90e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.66 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 38 SVREDLLrrereltaqiAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVilaglgftpkmqqqptREFSGGWRMRLAL 117
Cdd:PRK13537 96 TVRENLL----------VFGRYFGLSAAAARALVPPLLEFAKLENKADAKV----------------GELSGGMKRRLTL 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1189438346 118 ARALFARPDLLLLDEPTNMLD--VRAILW--LENYLQTwPSTILVVSH 161
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDpqARHLMWerLRSLLAR-GKTILLTTH 196
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
107-176 |
9.59e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.14 E-value: 9.59e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHL 176
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYIKPDRVHV 177
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
267-462 |
9.74e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.66 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI----------RHAHRNLKI 336
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVV-DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSislcgepvpsRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 337 GYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQ---LGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYIL 413
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 414 DEPTNHLDMETIEALGRALNNF--RGGVILVSHD--ERFIRLvCRELWVCEGG 462
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLlaRGKTILLTTHfmEEAERL-CDRLCVIEEG 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
105-177 |
9.99e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.43 E-value: 9.99e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL-QTWPSTILV-VSHdRNFLNAIATDIIHLH 177
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELPGTTVIsVGH-RSTLAAFHDRVLELT 557
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
288-445 |
1.01e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.92 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 288 SRLS-VSADLES--RICVVGENGAGKSTMLKLLLG-------------DLAPVRGIRHAHRNlkiGYFSQHHVEQLDLNV 351
Cdd:COG4138 10 GRLGpISAQVNAgeLIHLIGPNGAGKSTLLARMAGllpgqgeillngrPLSDWSAAELARHR---AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 352 saVELLARKFPGRPEEEYRHQL-----GRYGISGELaMRPLASLSGGQKSRVAFAQMTM-------PCPNFYILDEPTNH 419
Cdd:COG4138 87 --FQYLALHQPAGASSEAVEQLlaqlaEALGLEDKL-SRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNS 163
|
170 180
....*....|....*....|....*....
gi 1189438346 420 LDMETIEALGRALNNFR---GGVILVSHD 445
Cdd:COG4138 164 LDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
302-445 |
1.04e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRG----------------IRHahrnlKIGYFSQHHVEQLdlnVSA-VEL-----LAR 359
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGqiiidgdllteenvwdIRH-----KIGMVFQNPDNQF---VGAtVEDdvafgLEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 360 KfpGRPEEEYR----HQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD----METIEALGRA 431
Cdd:PRK13650 110 K--GIPHEEMKervnEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGI 186
|
170
....*....|....
gi 1189438346 432 LNNFRGGVILVSHD 445
Cdd:PRK13650 187 RDDYQMTVISITHD 200
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
300-457 |
1.14e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.47 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLG----DLAPVRGI-----------RHAHRNLKIGYFSQHHVEQLDLN-VSAVELLARkFPG 363
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGlddgSSGEVSLVgqplhqmdeeaRAKLRAKHVGFVFQSFMLIPTLNaLENVELPAL-LRG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 364 RPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGRALN-NF 435
Cdd:PRK10584 118 ESSRQSRNGakalLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkIADLLFSLNrEH 196
|
170 180
....*....|....*....|....*....
gi 1189438346 436 RGGVILVSHDE-------RFIRLVCRELW 457
Cdd:PRK10584 197 GTTLILVTHDLqlaarcdRRLRLVNGQLQ 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
106-139 |
1.33e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.20 E-value: 1.33e-07
10 20 30
....*....|....*....|....*....|....
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 139
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDV 190
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
106-199 |
1.34e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.73 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWP----STILVVSHDRNFLNAIAtdiihlhsqrl 181
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSRLS----------- 218
|
90
....*....|....*...
gi 1189438346 182 dgyrgDFETFIKSKQERL 199
Cdd:PRK14258 219 -----DFTAFFKGNENRI 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
271-442 |
1.35e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.95 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLG-----------DLAPVRGIRHA--------- 330
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGyypltegeirlDGRPLSSLSHSvlrqgvamv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 331 -----------HRNLKIGY-FSQHHVEQLdlnVSAVEL--LARKFPGrpeeeyrhqlGRYGISGELAmrplASLSGGQKS 396
Cdd:PRK10790 421 qqdpvvladtfLANVTLGRdISEEQVWQA---LETVQLaeLARSLPD----------GLYTPLGEQG----NNLSVGQKQ 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189438346 397 RVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILV 442
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLV 529
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
301-453 |
1.40e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.87 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 301 CVVGENGAGKSTMLKLLLGDLAP-------------VRGIRHAHRnLKIGYFSQHhveqLDL--NVSAVE--LLARkFPG 363
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPdsgeilldgepvrFRSPRDAQA-AGIAIIHQE----LNLvpNLSVAEniFLGR-EPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 364 RP--------EEEYRHQLGRYGISGELAmRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF 435
Cdd:COG1129 108 RGglidwramRRRARELLARLGLDIDPD-TPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL 186
|
170 180
....*....|....*....|...
gi 1189438346 436 RG---GVILVSH--DErfIRLVC 453
Cdd:COG1129 187 KAqgvAIIYISHrlDE--VFEIA 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
300-445 |
1.52e-07 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 52.08 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL------KIGYFSQHHV-------EQLDLNVSAVellarkFPGRP 365
Cdd:TIGR01184 14 ISLIGHSGCGKSTLLNLISGLAQPTSGgVILEGKQItepgpdRMVVFQNYSLlpwltvrENIALAVDRV------LPDLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 366 EEEYR----HQLGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRAL----NNFRG 437
Cdd:TIGR01184 88 KSERRaiveEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRV 166
|
....*...
gi 1189438346 438 GVILVSHD 445
Cdd:TIGR01184 167 TVLMVTHD 174
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
99-163 |
1.68e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.30 E-value: 1.68e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 99 MQQQPTR---EFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILWLE--NYLQTWPSTILVVSHDR 163
Cdd:PRK11607 139 MQEFAKRkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
298-481 |
1.82e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.70 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 298 SRICVVGENGAGKSTMLKLLLGDLaPVRGirhahrNLKIGyfsqhHVE--QLDL-----------------------NVs 352
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLGFL-PYQG------SLKIN-----GIElrELDPeswrkhlswvgqnpqlphgtlrdNV- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 353 aveLLARkfPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM 422
Cdd:PRK11174 444 ---LLGN--PDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 423 ETIEALGRALNNFRGG--VILVSHDERFIRlVCRELWVCEGGGVtrVEGGfdQYRALLQEQ 481
Cdd:PRK11174 519 HSEQLVMQALNAASRRqtTLMVTHQLEDLA-QWDQIWVMQDGQI--VQQG--DYAELSQAG 574
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
101-162 |
1.92e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.78 E-value: 1.92e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 101 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL-WLENYLQTWPSTILVVSHD 162
Cdd:COG4586 149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIReFLKEYNRERGTTILLTSHD 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
302-445 |
1.99e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.24 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDL----------APVRGIRHAHRNLKIGYFSQH-------HVEQ-LDLNVSAvellarkfpG 363
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLpgsgsiqfagQPLEAWSAAELARHRAYLSQQqtppfamPVFQyLTLHQPD---------K 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 364 RPEEEYRHQL----GRYGISGELAmRPLASLSGGQKSRVAFAQMTM-------PCPNFYILDEPTNHLDMETIEALGRAL 432
Cdd:PRK03695 98 TRTEAVASALnevaEALGLDDKLG-RSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQQAALDRLL 176
|
170
....*....|....*.
gi 1189438346 433 NNF---RGGVILVSHD 445
Cdd:PRK03695 177 SELcqqGIAVVMSSHD 192
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
73-195 |
2.15e-07 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. 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: 213225 [Multi-domain] Cd Length: 233 Bit Score: 51.81 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 73 KLEEIEADKAPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAIL-WLENY 148
Cdd:cd03258 108 EIAGVPKAEIEERVLELLELVGLEDKADAYPA-QLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTQSILaLLRDI 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1189438346 149 LQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSK 195
Cdd:cd03258 187 NRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
85-181 |
2.30e-07 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. 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: 213265 [Multi-domain] Cd Length: 211 Bit Score: 51.34 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 85 RASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRA---ILWLENYLQTwPSTILVV 159
Cdd:cd03298 108 AIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDpaLRAemlDLVLDLHAET-KMTVLMV 185
|
90 100
....*....|....*....|..
gi 1189438346 160 SHDRNFLNAIATDIIHLHSQRL 181
Cdd:cd03298 186 THQPEDAKRLAQRVVFLDNGRI 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
270-456 |
2.38e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEV-DFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG------------IRHAHRNLki 336
Cdd:TIGR01257 1937 ILRLNELtKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagksiltnISDVHQNM-- 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 337 GYFSQHH-VEQLDLNVSAVELLARkFPGRPEEEYRhQLGRYGISG----ELAMRPLASLSGGQKSRVAFAQMTMPCPNFY 411
Cdd:TIGR01257 2015 GYCPQFDaIDDLLTGREHLYLYAR-LRGVPAEEIE-KVANWSIQSlglsLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438346 412 ILDEPTNHLDMETIEALGRALNN-FRGG--VILVSHDERFIRLVCREL 456
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSiIREGraVVLTSHSMEECEALCTRL 2140
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
268-417 |
2.52e-07 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 51.52 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 268 PPILQLDEVDFYYDPKHVIFSrlsVSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLK--------- 335
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHG---VSLEVEegEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRFDGEDITglpphriar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 336 --IGY-------FSQHHVEQ-LDLnVSAVELLARKFPGRPEE---------EYRHQLGrygisgelamrplASLSGGQKS 396
Cdd:COG0410 78 lgIGYvpegrriFPSLTVEEnLLL-GAYARRDRAEVRADLERvyelfprlkERRRQRA-------------GTLSGGEQQ 143
|
170 180
....*....|....*....|.
gi 1189438346 397 RVAFAQMTMPCPNFYILDEPT 417
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPS 164
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
108-161 |
2.66e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.19 E-value: 2.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAilwlENYLQTWPS----TILVVSH 161
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAEC----EQLLQESRSrasrTVLLIAH 672
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
300-445 |
3.05e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRGirhahrNLKIGYFSQHHV-EQLDLNVSAVELLARK---------FPGRPEEEY 369
Cdd:PRK11247 41 VAVVGRSGCGKSTLLRLLAGLETPSAG------ELLAGTAPLAEArEDTRLMFQDARLLPWKkvidnvglgLKGQWRDAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 370 RHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET-------IEALGRAlNNFRggVILV 442
Cdd:PRK11247 115 LQALAAVGLADRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTriemqdlIESLWQQ-HGFT--VLLV 190
|
...
gi 1189438346 443 SHD 445
Cdd:PRK11247 191 THD 193
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
303-445 |
3.08e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.01 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 303 VGENGAGKSTMLKLLLGDLAP------VRGI---RHAHRNLK-IGY-FSQHhvEQLDLNVSAVE--LLARKFPGRPEEEY 369
Cdd:COG4586 54 IGPNGAGKSTTIKMLTGILVPtsgevrVLGYvpfKRRKEFARrIGVvFGQR--SQLWWDLPAIDsfRLLKAIYRIPDAEY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 370 RHQLGRY----GIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETIEALGRALNNFRGG-VIL 441
Cdd:COG4586 132 KKRLDELvellDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYNRERGTtILL 210
|
....
gi 1189438346 442 VSHD 445
Cdd:COG4586 211 TSHD 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-481 |
3.09e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.14 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRG------------IRHAHRnlKIGYFSQhhVEQLDLNVSAVELL---ARKF--PGR 364
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGkitvlgvpvparARLARA--RIGVVPQ--FDNLDLEFTVRENLlvfGRYFgmSTR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 365 PEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF--RGGVILV 442
Cdd:PRK13536 148 EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGKTILL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1189438346 443 SHD--ERFIRLvCRELWVCEgGGVTRVEGGFDqyrALLQEQ 481
Cdd:PRK13536 228 TTHfmEEAERL-CDRLCVLE-AGRKIAEGRPH---ALIDEH 263
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
105-176 |
3.25e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 50.23 E-value: 3.25e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHdRNFLNAIATDIIHL 176
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDL 160
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
302-446 |
3.29e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 50.94 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAP---VRG-IRHAHRNL--------KIGYFSQ------HhveqldLNVsaVELLARKFPG 363
Cdd:COG4136 32 LMGPSGSGKSTLLAAIAGTLSPafsASGeVLLNGRRLtalpaeqrRIGILFQddllfpH------LSV--GENLAFALPP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 364 RPEEEYRHQ-----LGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGR----ALNN 434
Cdd:COG4136 104 TIGRAQRRArveqaLEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREfvfeQIRQ 182
|
170
....*....|..
gi 1189438346 435 FRGGVILVSHDE 446
Cdd:COG4136 183 RGIPALLVTHDE 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
271-446 |
3.38e-07 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 51.10 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNlkIGYF 339
Cdd:cd03301 1 VELENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGriyiggrdvtdLPPKDRD--IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 340 SQHHVEQLDLNVS---AVELLARKFPGRPEEEYRHQLGR-YGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDE 415
Cdd:cd03301 78 FQNYALYPHMTVYdniAFGLKLRKVPKDEIDERVREVAElLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1189438346 416 PTNHLD----METIEALGRALNNFRGGVILVSHDE 446
Cdd:cd03301 157 PLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
284-445 |
3.41e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.75 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 284 HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDL--------APVRG--------------IRHAHRNlkiGYFSQ 341
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGdvtlngeplaaidaPRLARLR---AVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 342 HHVEQLDLNVSAVELLARKFPGRPEEEYRHQ--------LGRYGISGeLAMRPLASLSGGQKSRVAFAQM---------T 404
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGRYPHARRAGALTHRdgeiawqaLALAGATA-LVGRDVTTLSGGELARVQFARVlaqlwpphdA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438346 405 MPCPNFYILDEPTNHLD-------METIEALGRalnNFRGGVILVSHD 445
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
271-461 |
3.77e-07 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 50.63 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYdpKHVIFsRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG---------IRHAHRNLKIGYFSQ 341
Cdd:TIGR01277 1 LALDKVRYEY--EHLPM-EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGsikvndqshTGLAPYQRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 342 HHVEQLDLNVSAVELLARKfPGRP----EEEYRHQLGR-YGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEP 416
Cdd:TIGR01277 78 ENNLFAHLTVRQNIGLGLH-PGLKlnaeQQEKVVDAAQqVGIADYLDRLP-EQLSGGQRQRVALARCLVRPNPILLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1189438346 417 TNHLD----METIEALGRALNNFRGGVILVSHD-ERFIRLVCRELWVCEG 461
Cdd:TIGR01277 156 FSALDpllrEEMLALVKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQG 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
90-162 |
3.79e-07 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 50.93 E-value: 3.79e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 90 LAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILWlENYLQTWPS---TILVVSHD 162
Cdd:TIGR01184 99 IALVGLTEAADKRPG-QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDalTRGNLQ-EELMQIWEEhrvTVLMVTHD 174
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
38-134 |
3.86e-07 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). 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.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 50.90 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 38 SVREDLLrrereLTAQIaagRAEGSEAAELAEIYA---KLEEieadkaparasvilaglgftpkMQQQPTREFSGGWRMR 114
Cdd:cd03224 91 TVEENLL-----LGAYA---RRRAKRKARLERVYElfpRLKE----------------------RRKQLAGTLSGGEQQM 140
|
90 100
....*....|....*....|
gi 1189438346 115 LALARALFARPDLLLLDEPT 134
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPS 160
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
60-176 |
3.96e-07 |
|
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: 52.29 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 60 EGSEAAELAeiyakLEEIEADKAPARASVILAGL-GFT---PKMQQQPT----REFSGGWRMRLALARALFARPDLLLLD 131
Cdd:TIGR02857 409 AGTIAENIR-----LARPDASDAEIREALERAGLdEFVaalPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 132 EPTNMLD------VRAIlwLENYLQTwpSTILVVSHDRNfLNAIATDIIHL 176
Cdd:TIGR02857 484 EPTAHLDaeteaeVLEA--LRALAQG--RTVLLVTHRLA-LAALADRIVVL 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
106-470 |
4.21e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 52.38 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWPST-ILVVSHDRNFLNAIATDIIHLHsqrl 181
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqAQILDLLKDLQRELGMaLLLITHDLGVVRRFADRVAVMR---- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 182 DGY---RGDFETFIKSkqerllnqqreyeAQQQYRQHiqvfidrfrynanrasqvqsklkMLEKLPELKPVDKESEvvmk 258
Cdd:COG4172 232 QGEiveQGPTAELFAA-------------PQHPYTRK-----------------------LLAAEPRGDPRPVPPD---- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 259 fpdgfekfSPPILQLDEVDFYYDPKHVIFSRL--------SVSADL---ESrICVVGENGAGKSTMLKLLLGdLAPVRG- 326
Cdd:COG4172 272 --------APPLLEARDLKVWFPIKRGLFRRTvghvkavdGVSLTLrrgET-LGLVGESGSGKSTLGLALLR-LIPSEGe 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 327 ---------------IRHAHRNLKI------GYFS-QHHVEQLdlnVSavELLARKFPGRPEEEYRHQ----LGRYGISG 380
Cdd:COG4172 342 irfdgqdldglsrraLRPLRRRMQVvfqdpfGSLSpRMTVGQI---IA--EGLRVHGPGLSAAERRARvaeaLEEVGLDP 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 381 ELAMRPLASLSGGQKSRVAFAQ-MTMPcPNFYILDEPTNHLDMeTIEA----LGRALNNFRG-GVILVSHDERFIRLVCR 454
Cdd:COG4172 417 AARHRYPHEFSGGQRQRIAIARaLILE-PKLLVLDEPTSALDV-SVQAqildLLRDLQREHGlAYLFISHDLAVVRALAH 494
|
410
....*....|....*.
gi 1189438346 455 ELWVCEGGGVtrVEGG 470
Cdd:COG4172 495 RVMVMKDGKV--VEQG 508
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
72-181 |
4.30e-07 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. 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: 213231 [Multi-domain] Cd Length: 211 Bit Score: 50.65 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 72 AKLEEIEADKAPARASVILAGLGFTPKmQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQT 151
Cdd:cd03264 97 AWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSE 175
|
90 100 110
....*....|....*....|....*....|..
gi 1189438346 152 WPS--TILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:cd03264 176 LGEdrIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
304-448 |
4.58e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 304 GENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLK--------IGYFSQHHVEQLDLnvsAVELLARKFPGRP---- 365
Cdd:PRK11288 37 GENGAGKSTLLKILSGNYQPdagsilIDGQEMRFASTTaalaagvaIIYQELHLVPEMTV---AENLYLGQLPHKGgivn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 366 ----EEEYRHQLGRYGISGELAMrPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFR--GGV 439
Cdd:PRK11288 114 rrllNYEAREQLEHLGVDIDPDT-PLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRaeGRV 192
|
170
....*....|..
gi 1189438346 440 IL-VSH--DERF 448
Cdd:PRK11288 193 ILyVSHrmEEIF 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
263-449 |
5.36e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.64 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 263 FEKFSPPIL----QLDEVDFYYDPKHVIFsrlsvsadlesricVVGENGAGKSTMLKLLLGDLAPVRG---------IRH 329
Cdd:PRK10908 4 FEHVSKAYLggrqALQGVTFHMRPGEMAF--------------LTGHSGAGKSTLLKLICGIERPSAGkiwfsghdiTRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 330 AHRNL-----KIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQ----LGRYGISGELAMRPLaSLSGGQKSRVAF 400
Cdd:PRK10908 70 KNREVpflrrQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRvsaaLDKVGLLDKAKNFPI-QLSGGEQQRVGI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 401 AQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF-RGG--VILVSHDERFI 449
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFnRVGvtVLMATHDIGLI 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
104-181 |
5.64e-07 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 50.33 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 104 TREFSGGWRMRLALARALFARPDLLLLDEPTNMLD----VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQ 179
Cdd:cd03301 128 PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
..
gi 1189438346 180 RL 181
Cdd:cd03301 208 QI 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
106-162 |
5.67e-07 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. 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: 213267 [Multi-domain] Cd Length: 232 Bit Score: 50.70 E-value: 5.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR----AILWLENYLQTWPSTILVVSHD 162
Cdd:cd03300 130 QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKlrkdMQLELKRLQKELGITFVFVTHD 190
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
101-162 |
6.38e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 6.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 101 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWL----ENYLQTWPSTILVVSHD 162
Cdd:PRK09544 115 DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
300-424 |
6.92e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 50.63 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRnlkIGYFSQHH-------VEQLDLNVSAVEL----------LARKF 361
Cdd:cd03291 66 LAITGSTGSGKTSLLMLILGELEPSEGkIKHSGR---ISFSSQFSwimpgtiKENIIFGVSYDEYryksvvkacqLEEDI 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 362 PGRPEEEYRhQLGRYGISgelamrplasLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET 424
Cdd:cd03291 143 TKFPEKDNT-VLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
68-177 |
7.60e-07 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 49.84 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 68 AEIYAKLEEIEAdkaparasviLAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV----RAIL 143
Cdd:cd03220 117 KEIDEKIDEIIE----------FSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAafqeKCQR 183
|
90 100 110
....*....|....*....|....*....|....
gi 1189438346 144 WLENYLQTwPSTILVVSHDRNFLNAIATDIIHLH 177
Cdd:cd03220 184 RLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLE 216
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
384-470 |
7.66e-07 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 49.77 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 384 MRPLASLSGGQKSRVA----FA-QMTMPCPnFYILDEPTNHLDMETIEALGRALNNFRGGV--ILVSHDERFIRlVCREL 456
Cdd:cd03278 108 VQRLSLLSGGEKALTAlallFAiFRVRPSP-FCVLDEVDAALDDANVERFARLLKEFSKETqfIVITHRKGTME-AADRL 185
|
90
....*....|....
gi 1189438346 457 WvceggGVTRVEGG 470
Cdd:cd03278 186 Y-----GVTMQESG 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
271-444 |
8.63e-07 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. 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: 213218 [Multi-domain] Cd Length: 234 Bit Score: 49.92 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHV-IFSRLSVSADLESRICVVGENGAGKSTMLKLL-----------LGDLAPVRGIRHAHRNLKIGY 338
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdsgriLIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQ-----------------HHVEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISgelamrplasLSGGQKSRVAFA 401
Cdd:cd03251 81 VSQdvflfndtvaeniaygrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVK----------LSGGQRQRIAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1189438346 402 QMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSH 444
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNrtTFVIAH 195
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
106-163 |
9.24e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 9.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAIL--WLENYLQTWPSTILVVSHDR 163
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDaqVRKELrrWLRQLHEELKFTSVFVTHDQ 197
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
106-162 |
9.28e-07 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). 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: 213263 [Multi-domain] Cd Length: 239 Bit Score: 50.03 E-value: 9.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAIL--WLENYLQTWPSTILVVSHD 162
Cdd:cd03296 136 QLSGGQRQRVALARALAVEPKVLLLDEPFGALDakVRKELrrWLRRLHDELHVTTVFVTHD 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
269-445 |
9.48e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.13 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 269 PILQLDEVDFYYDPKHVI-FSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlKIgYFSQHHVEQL 347
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--------EI-FYNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 348 DLNvsavELlaRKFPG----RPEEEYRHQLGRYGIS---------------------GELAMRPLA-----SLSGGQKSR 397
Cdd:PRK13648 77 NFE----KL--RKHIGivfqNPDNQFVGSIVKYDVAfglenhavpydemhrrvsealKQVDMLERAdyepnALSGGQKQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 398 VAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG----VILVSHD 445
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnitIISITHD 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
96-200 |
9.58e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 96 TPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPSTILVVSHDRNFLNAIATD 172
Cdd:PRK10762 386 TPSMEQ-AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAkkeIYQLINQFKAEGLSIILVSSEMPEVLGMSDR 464
|
90 100
....*....|....*....|....*...
gi 1189438346 173 IIHLHSQRLdgyRGDFETfIKSKQERLL 200
Cdd:PRK10762 465 ILVMHEGRI---SGEFTR-EQATQEKLM 488
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
302-465 |
9.75e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.09 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLK------------LLLGDL------APVRGIRhahrnLKIGY-FSQHHveqLDLNVSAVELLA---R 359
Cdd:PRK09493 32 IIGPSGSGKSTLLRcinkleeitsgdLIVDGLkvndpkVDERLIR-----QEAGMvFQQFY---LFPHLTALENVMfgpL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 360 KFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI-EALG--RAL 432
Cdd:PRK09493 104 RVRGASKEEAEKQarelLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRhEVLKvmQDL 182
|
170 180 190
....*....|....*....|....*....|...
gi 1189438346 433 NNFRGGVILVSHDERFIRLVCRELWVCEGGGVT 465
Cdd:PRK09493 183 AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
107-161 |
9.93e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 51.32 E-value: 9.93e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILW-LENYLQTwpSTILVVSH 161
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTeteALIQEaLERLMKG--RTTIVIAH 533
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
105-163 |
1.13e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 50.48 E-value: 1.13e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILWLE--NYLQTWPSTILVVSHDR 163
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDakLREEMREElrRLQRELGITFIYVTHDQ 196
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
304-446 |
1.22e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 304 GENGAGKSTMLKLLLGDLAPVRGirhahrnlKIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQL--------GR 375
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKG--------EILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENClydihfspGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 376 YGIS--------GELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFR---GGVILVSH 444
Cdd:PRK13540 106 VGITelcrlfslEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSH 185
|
..
gi 1189438346 445 DE 446
Cdd:PRK13540 186 QD 187
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
302-424 |
1.23e-06 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. 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: 213232 [Multi-domain] Cd Length: 220 Bit Score: 49.29 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLK--IGYFSQHhvEQLDLNVSA---VELLARKF--PGRPE 366
Cdd:cd03265 31 LLGPNGAGKTTTIKMLTTLLKPTSGratvaghdVVREPREVRrrIGIVFQD--LSVDDELTGwenLYIHARLYgvPGAER 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 367 EEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET 424
Cdd:cd03265 109 RERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
267-445 |
1.27e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 50.48 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDPKHVIfsrLSVSADLESR--ICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------K 335
Cdd:COG3842 2 AMPALELENVSKRYGDVTAL---DDVSLSIEPGefVALLGPSGCGKTTLLRMIAGFETPDSGrILLDGRDVtglppekrN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 336 IGYFSQH-----H--VEQldlNVsAVELLARKFPgRPEEEYR--HQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMP 406
Cdd:COG3842 79 VGMVFQDyalfpHltVAE---NV-AFGLRMRGVP-KAEIRARvaELLELVGLEGLADRYP-HQLSGGQQQRVALARALAP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1189438346 407 CPNFYILDEPTNHLD----METIEALGRALNNFRGGVILVSHD 445
Cdd:COG3842 153 EPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHD 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
270-464 |
1.28e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYdPKHVIFSRLSVSADLeSRIC-VVGENGAGKSTMLKLL-----------LGDLAPVRGIRHAHRNLKIG 337
Cdd:PRK10575 11 TFALRNVSFRV-PGRTLLHPLSLTFPA-GKVTgLIGHNGSGKSTLLKMLgrhqppsegeiLLDAQPLESWSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 338 YFSQHHVEQLDLNVSavELLA-RKFPgrpeeeYRHQLGRYGISGE---------LAMRPLA-----SLSGGQKSRVAFAQ 402
Cdd:PRK10575 89 YLPQQLPAAEGMTVR--ELVAiGRYP------WHGALGRFGAADRekveeaislVGLKPLAhrlvdSLSGGERQRAWIAM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 403 MTMPCPNFYILDEPTNHLDME---TIEALGRALNNFRG-GVILVSHDERFIRLVCRELWVCEGGGV 464
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
270-444 |
1.42e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.90 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLlGDLAPVR-GIRHAHRNLKIGYFSQHHV---- 344
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYgGRLTKPAKGKLFYVPQRPYmtlg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 345 ---EQLDLNVSAVELLARKFPGRPEEEY------RHQLGRYGisGELAMRPLAS-LSGGQKSRVAFAQMTMPCPNFYILD 414
Cdd:TIGR00954 530 tlrDQIIYPDSSEDMKRRGLSDKDLEQIldnvqlTHILEREG--GWSAVQDWMDvLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|
gi 1189438346 415 EPTNHLDMETIEALGRALNNFRGGVILVSH 444
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
300-461 |
1.54e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlkigyfsqhhVEQLDLNVSAVellarkfpgRPEEeyrhqlgrygis 379
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGD-----------------NDEWDGITPVY---------KPQY------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 380 gelamrplASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF----RGGVILVSHDERFIRLVCRE 455
Cdd:cd03222 70 --------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDR 141
|
....*.
gi 1189438346 456 LWVCEG 461
Cdd:cd03222 142 IHVFEG 147
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
292-446 |
1.58e-06 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). 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: 213263 [Multi-domain] Cd Length: 239 Bit Score: 49.26 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 292 VSADLES--RICVVGENGAGKSTMLKLLLGDLAPVRG---------IRHAHRNLKIGYFSQH-----HVEQLDlNVsAVE 355
Cdd:cd03296 21 VSLDIPSgeLVALLGPSGSGKTTLLRLIAGLERPDSGtilfggedaTDVPVQERNVGFVFQHyalfrHMTVFD-NV-AFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 356 LLARKFPGRP-EEEYRHQ----LGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGR 430
Cdd:cd03296 99 LRVKPRSERPpEAEIRAKvhelLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRR 177
|
170 180
....*....|....*....|
gi 1189438346 431 ALNNFRGGV----ILVSHDE 446
Cdd:cd03296 178 WLRRLHDELhvttVFVTHDQ 197
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
38-134 |
1.70e-06 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 49.21 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 38 SVREDLlrrerELTAQIAAGRAEGSEAaeLAEIYA---KLEEieadkaparasvilaglgftpkMQQQPTREFSGGWRMR 114
Cdd:COG0410 94 TVEENL-----LLGAYARRDRAEVRAD--LERVYElfpRLKE----------------------RRRQRAGTLSGGEQQM 144
|
90 100
....*....|....*....|
gi 1189438346 115 LALARALFARPDLLLLDEPT 134
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPS 164
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
267-443 |
1.71e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLKIGY 338
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisilgqpTRQALQKNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQHhvEQLDLN----VSAVELLAR----KFPGRPEEEYRH----QLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMP 406
Cdd:PRK15056 83 VPQS--EEVDWSfpvlVEDVVMMGRyghmGWLRRAKKRDRQivtaALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438346 407 CPNFYILDEPTNHLDMET---IEALGRALNNfRGGVILVS 443
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTearIISLLRELRD-EGKTMLVS 198
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
290-465 |
1.72e-06 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 50.11 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 290 LSVSADLES--RICVVGENGAGKSTMLKLLLGDLAPVRGIRH----------------AHRNlKIGYFSQHHVEQLDLNV 351
Cdd:TIGR02142 14 LDADFTLPGqgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsrkgiflpPEKR-RIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 352 SAVELLARKFPGRPEEEYRHQ--LGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM----ETI 425
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFErvIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438346 426 EALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVT 465
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
269-473 |
1.72e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 269 PILQLDEVDFYYDPK--HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP-------VRG----------IRH 329
Cdd:PLN03232 613 PAISIKNGYFSWDSKtsKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaetssvvIRGsvayvpqvswIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 330 AHRNLKIGYFSQHHVEQL--DLNVSAVELLARKFPGRPeeeyRHQLGRYGISgelamrplasLSGGQKSRVAFAQMTMPC 407
Cdd:PLN03232 693 ATVRENILFGSDFESERYwrAIDVTALQHDLDLLPGRD----LTEIGERGVN----------ISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 408 PNFYILDEPTNHLDMETIEALGRAL--NNFRGGV-ILVSHDERFIRLVCRELWVCEggGVTRVEGGFDQ 473
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDSCmkDELKGKTrVLVTNQLHFLPLMDRIILVSE--GMIKEEGTFAE 825
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
301-444 |
1.83e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 301 CVVGENGAGKSTMLKLLLGDLAP------VRG----IRHAH--RNLKIGYFSQHH--VEQLdlnvSAVE--LLA---RKF 361
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPdsgeilIDGkpvrIRSPRdaIALGIGMVHQHFmlVPNL----TVAEniVLGlepTKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 362 PGRPEEEYRHQL----GRYGISGELAmRPLASLSGGQKSRV----AFAQmtmpCPNFYILDEPTNHLDMETIEALGRALN 433
Cdd:COG3845 111 GRLDRKAARARIrelsERYGLDVDPD-AKVEDLSVGEQQRVeilkALYR----GARILILDEPTAVLTPQEADELFEILR 185
|
170
....*....|....
gi 1189438346 434 NFRG---GVILVSH 444
Cdd:COG3845 186 RLAAegkSIIFITH 199
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
302-470 |
2.15e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.80 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLG--------------DLA--PVRGIRHAHRnlKIGYFSQHhveqldLNvsaveLLARK----- 360
Cdd:PRK11153 36 VIGASGAGKSTLIRCINLlerptsgrvlvdgqDLTalSEKELRKARR--QIGMIFQH------FN-----LLSSRtvfdn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 361 --FP----GRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEA 427
Cdd:PRK11153 103 vaLPlelaGTPKAEIKARvtelLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsILE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438346 428 LGRALNNFRG-GVILVSHDERFIRLVCRELWVCEGGGVtrVEGG 470
Cdd:PRK11153 182 LLKDINRELGlTIVLITHEMDVVKRICDRVAVIDAGRL--VEQG 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
105-161 |
2.28e-06 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 47.69 E-value: 2.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL--QTWPSTILVVSH 161
Cdd:cd03247 97 RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfeVLKDKTLIWITH 155
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
85-162 |
2.35e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.62 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 85 RASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILWLENylQTWPSTILV 158
Cdd:PRK10584 126 GAKALLEQLGLGKRLDHLPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqtgdkIADLLFSLN--REHGTTLIL 202
|
....
gi 1189438346 159 VSHD 162
Cdd:PRK10584 203 VTHD 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
292-446 |
2.49e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 49.31 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 292 VSADLES--RICVVGENGAGKSTMLKLLLG--------------DLAPVrgirHAhRNLKIGYFSQH-----HVEQLDlN 350
Cdd:PRK10851 21 ISLDIPSgqMVALLGPSGSGKTTLLRIIAGlehqtsghirfhgtDVSRL----HA-RDRKVGFVFQHyalfrHMTVFD-N 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 351 VS-AVELLARKfpGRPEEEYRH----------QLGRygisgeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNH 419
Cdd:PRK10851 95 IAfGLTVLPRR--ERPNAAAIKakvtqllemvQLAH------LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190
....*....|....*....|....*....|.
gi 1189438346 420 LDMETIEALGRALNN----FRGGVILVSHDE 446
Cdd:PRK10851 167 LDAQVRKELRRWLRQlheeLKFTSVFVTHDQ 197
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
90-179 |
2.62e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.56 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 90 LAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAIlwLENYLQTWPSTILVVSHDR 163
Cdd:PRK10247 121 LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkhnVNEI--IHRYVREQNIAVLWVTHDK 198
|
90
....*....|....*.
gi 1189438346 164 NFLNAiATDIIHLHSQ 179
Cdd:PRK10247 199 DEINH-ADKVITLQPH 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
303-421 |
2.62e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.97 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 303 VGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRN-------LKIGYFSQHHVEQL--DLNVSAVELLARKFPGRP 365
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLHVPTQGsvrvddtlITSTSKNkdikqirKKVGLVFQFPESQLfeETVLKDVAFGPQNFGVSQ 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 366 EEE---YRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 421
Cdd:PRK13649 119 EEAealAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
90-140 |
2.87e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.86 E-value: 2.87e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 90 LAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 140
Cdd:PRK13635 125 LRQVGMEDFLNREPHR-LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
80-174 |
2.92e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.01 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 80 DKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPS-T 155
Cdd:PRK13646 119 DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqVMRLLKSLQTDENkT 198
|
90
....*....|....*....
gi 1189438346 156 ILVVSHDRNFLNAIATDII 174
Cdd:PRK13646 199 IILVSHDMNEVARYADEVI 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
390-445 |
2.99e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 2.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 390 LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME-TIEALG--RALNNFRGGVILVSHD 445
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEifDNLNKQGKTIILVTHD 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
84-164 |
3.29e-06 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. 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: 213261 [Multi-domain] Cd Length: 269 Bit Score: 48.41 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 84 ARASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRA-----ILWLENYLQtwpSTI 156
Cdd:cd03294 139 ERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALDplIRRemqdeLLRLQAELQ---KTI 214
|
....*...
gi 1189438346 157 LVVSHDRN 164
Cdd:cd03294 215 VFITHDLD 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
272-482 |
3.39e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.57 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 272 QLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLL-----------LGDLAPVRGI-----RHAhrnlk 335
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqsgriLIDGTDIRTVtraslRRN----- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 336 IGYFSQhhvEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPLA----------SLSGGQKSRVAFAQMTM 405
Cdd:PRK13657 411 IAVVFQ---DAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGydtvvgergrQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 406 PCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLVCRELwVCEGGGVtrVE-GGFDQ-------YR 475
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGrtTFIIAHRLSTVRNADRIL-VFDNGRV--VEsGSFDElvarggrFA 564
|
....*..
gi 1189438346 476 ALLQEQF 482
Cdd:PRK13657 565 ALLRAQG 571
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
68-177 |
3.48e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.15 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 68 AEIYAKLEEIEAdkaparasviLAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEptnMLDV-------R 140
Cdd:COG1134 121 KEIDEKFDEIVE----------FAELG---DFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE---VLAVgdaafqkK 184
|
90 100 110
....*....|....*....|....*....|....*..
gi 1189438346 141 AILWLENYLQTwPSTILVVSHDRNFLNAIATDIIHLH 177
Cdd:COG1134 185 CLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLE 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
270-448 |
3.53e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 48.57 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVIFSrlsVSADLES-RIC-VVGENGAGKSTMLKLLLGDLAP------VRG--IRHAHRNlKIGY- 338
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDD---VSFTVPKgEIFgLLGPNGAGKTTTIRIILGILAPdsgevlWDGepLDPEDRR-RIGYl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 ------FSQHHV-EQLdlnvsaVELLARKfpGRPEEEYRHQ----LGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPC 407
Cdd:COG4152 77 peerglYPKMKVgEQL------VYLARLK--GLSKAEAKRRadewLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1189438346 408 PNFYILDEPTNHLD---METIEALGRALNNfRG-GVILVSHD----ERF 448
Cdd:COG4152 148 PELLILDEPFSGLDpvnVELLKDVIRELAA-KGtTVIFSSHQmelvEEL 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
270-444 |
3.56e-06 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 48.24 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYD--PKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLL-----------LGDLAPVRGIRHAHRNLKI 336
Cdd:cd03248 11 IVKFQNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqggqvLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 337 GYFSQHHV---EQLDLNVS--------------AVELLARKFPGRPEEEYRHQLGRYGisgelamrplASLSGGQKSRVA 399
Cdd:cd03248 91 SLVGQEPVlfaRSLQDNIAyglqscsfecvkeaAQKAHAHSFISELASGYDTEVGEKG----------SQLSGGQKQRVA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1189438346 400 FAQMTMPCPNFYILDEPTNHLDMETIEALGRAL--NNFRGGVILVSH 444
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALydWPERRTVLVIAH 207
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
300-479 |
3.60e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.94 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRGirHAHRNLKIGYFSQHHVEQLDlnvsavELLARKFPGRPEEE--YRHQLGRYG 377
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEG--HVHMKGSVAYVPQQAWIQND------SLRENILFGKALNEkyYQQVLEACA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 378 ISGELAMRPLA----------SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM--------ETIEALGRALNNFRggv 439
Cdd:TIGR00957 739 LLPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvgkhifeHVIGPEGVLKNKTR--- 815
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438346 440 ILVSHDERFIRLVcRELWVCEGGGVTrvEGGfdQYRALLQ 479
Cdd:TIGR00957 816 ILVTHGISYLPQV-DVIIVMSGGKIS--EMG--SYQELLQ 850
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
107-176 |
3.87e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 48.03 E-value: 3.87e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHL 176
Cdd:TIGR01978 145 FSGGEKKRNEILQMALLEPKLAILDEIDSGLDIdalKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
108-138 |
3.95e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 47.86 E-value: 3.95e-06
10 20 30
....*....|....*....|....*....|.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:COG4136 135 SGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
292-443 |
4.16e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 47.65 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 292 VSADLES--RICVVGENGAGKSTMLKLLLG---DLAPVRG-IRHAHRNLKIGYFSQH--HVEQLDLNVS----------- 352
Cdd:cd03234 26 VSLHVESgqVMAILGSSGSGKTTLLDAISGrveGGGTTSGqILFNGQPRKPDQFQKCvaYVRQDDILLPgltvretltyt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 353 AVELLARKFPgrpeEEYRHQLGRYGISGELAMRPLA-----SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEA 427
Cdd:cd03234 106 AILRLPRKSS----DAIRKKRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170
....*....|....*...
gi 1189438346 428 LGRALNNF--RGGVILVS 443
Cdd:cd03234 182 LVSTLSQLarRNRIVILT 199
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
84-138 |
4.38e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 48.32 E-value: 4.38e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 84 ARASVILAGLGFTpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:COG4525 113 ARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
89-174 |
4.45e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 89 ILAGLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV-------RAIlwlENYLQTWPSTILVVSH 161
Cdd:PRK13409 437 IIKPLQLERLLDK-NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlavaKAI---RRIAEEREATALVVDH 512
|
90
....*....|...
gi 1189438346 162 DRNFLNAIATDII 174
Cdd:PRK13409 513 DIYMIDYISDRLM 525
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
270-445 |
4.64e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.17 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVI--FSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI------RHAHRNL-----KI 336
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKvkidgeLLTAENVwnlrrKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 337 GYFSQHHVEQ-LDLNVSAVELLARKFPGRPEEEYRHQLGRYGISG---ELAMRPLASLSGGQKSRVAFAQMTMPCPNFYI 412
Cdd:PRK13642 84 GMVFQNPDNQfVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVnmlDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1189438346 413 LDEPTNHLD----METIEALGRALNNFRGGVILVSHD 445
Cdd:PRK13642 164 LDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
300-452 |
4.66e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.82 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLL------------LGDLA-----PVRGIRHAHRNLK--IGYFSQH-----HVEQLDlNVSAVE 355
Cdd:PRK11264 32 VAIIGPSGSGKTTLLRCInlleqpeagtirVGDITidtarSLSQQKGLIRQLRqhVGFVFQNfnlfpHRTVLE-NIIEGP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 356 LLARKFP-GRPEEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI-EALG--RA 431
Cdd:PRK11264 111 VIVKGEPkEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVgEVLNtiRQ 189
|
170 180
....*....|....*....|.
gi 1189438346 432 LNNFRGGVILVSHDERFIRLV 452
Cdd:PRK11264 190 LAQEKRTMVIVTHEMSFARDV 210
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
44-140 |
4.94e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 44 LRRERELTAQIAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTReFSGGWRMRLALARALFA 123
Cdd:NF000106 83 LRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAK-YSGGMRRRLDLAASMIG 161
|
90
....*....|....*..
gi 1189438346 124 RPDLLLLDEPTNMLDVR 140
Cdd:NF000106 162 RPAVLYLDEPTTGLDPR 178
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
106-162 |
5.85e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.16 E-value: 5.85e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHD 162
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
108-161 |
5.97e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 47.72 E-value: 5.97e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRA-------ILWL-ENYlqtwpsTILVVSH 161
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakieelILELkKDY------TIVIVTH 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
38-161 |
6.05e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.29 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 38 SVREDLLrrereltaqiAAGRAEGSEAAELAEI------YAKLEeieaDKAPARASvilaglgftpkmqqqptrEFSGGW 111
Cdd:PRK13536 130 TVRENLL----------VFGRYFGMSTREIEAVipslleFARLE----SKADARVS------------------DLSGGM 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 112 RMRLALARALFARPDLLLLDEPTNMLD--VRAILWLE-NYLQTWPSTILVVSH 161
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDphARHLIWERlRSLLARGKTILLTTH 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
108-161 |
7.47e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.95 E-value: 7.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL-WLENYLQTWPSTILVVSH 161
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkRELLpYLERLAREINIPILYVSH 187
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
106-183 |
8.49e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.35 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQ-TWPSTILVVSHDRNFLNAIATDIIHLHSQR- 180
Cdd:PRK13637 144 ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeILNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGKc 223
|
....
gi 1189438346 181 -LDG 183
Cdd:PRK13637 224 eLQG 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
102-146 |
8.51e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 47.91 E-value: 8.51e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1189438346 102 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV-RAILWLE 146
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLE 180
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
108-169 |
8.82e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 8.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 108 SGGWRM------RLALARALFARPDLLLLDEPTNMLD---VRAIL--WLENYLQTWPSTILVVSHDRNFLNAI 169
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenIEESLaeIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
264-421 |
9.32e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 264 EKFSPPILQLDEVDFY-YDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNL-------- 334
Cdd:PTZ00243 653 SERSAKTPKMKTDDFFeLEPK-VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIayvpqqaw 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 335 --------KIGYFSQHHVEQLD--LNVSAVELLARKFPGRPEEEyrhqLGRYGISgelamrplasLSGGQKSRVAFAQMT 404
Cdd:PTZ00243 732 imnatvrgNILFFDEEDAARLAdaVRVSQLEADLAQLGGGLETE----IGEKGVN----------LSGGQKARVSLARAV 797
|
170
....*....|....*..
gi 1189438346 405 MPCPNFYILDEPTNHLD 421
Cdd:PTZ00243 798 YANRDVYLLDDPLSALD 814
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
301-430 |
9.42e-06 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 46.15 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 301 CVVGENGAGKSTMLKLLLGdlapVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKfpgrpeeeyRHQLGRYGISG 380
Cdd:cd03239 26 AIVGPNGSGKSNIVDAICF----VLGGKAAKLRRGSLLFLAGGGVKAGINSASVEITFDK---------SYFLVLQGKVE 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 381 ELamrplasLSGGQKSRVAFA-----QMTMPCPnFYILDEPTNHLDMETIEALGR 430
Cdd:cd03239 93 QI-------LSGGEKSLSALAlifalQEIKPSP-FYVLDEIDAALDPTNRRRVSD 139
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
300-464 |
9.66e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 46.99 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIGYFSQHHVEQLDLN------VSAVEllARKFPGRP-EEEYRH 371
Cdd:PRK10419 41 VALLGRSGCGKSTLARLLVGLESPSQGnVSWRGEPLAKLNRAQRKAFRRDIQmvfqdsISAVN--PRKTVREIiREPLRH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 372 --------QLGR-------YGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM----ETIEALGRAL 432
Cdd:PRK10419 119 llsldkaeRLARasemlraVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQ 198
|
170 180 190
....*....|....*....|....*....|..
gi 1189438346 433 NNFRGGVILVSHDERFIRLVCRELWVCEGGGV 464
Cdd:PRK10419 199 QQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
105-139 |
9.85e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.23 E-value: 9.85e-06
10 20 30
....*....|....*....|....*....|....*
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 139
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
302-448 |
1.04e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNlKIGYFS----QHHVEQ------LDL----------NVSAVELLARKF 361
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGERQSQFS-HITRLSfeqlQKLVSDewqrnnTDMlspgeddtgrTTAEIIQDEVKD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 362 PGRPEEeYRHQLGrygISGELAmRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF-RGGVI 440
Cdd:PRK10938 113 PARCEQ-LAQQFG---ITALLD-RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLhQSGIT 187
|
....*...
gi 1189438346 441 LVSHDERF 448
Cdd:PRK10938 188 LVLVLNRF 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
300-444 |
1.04e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.00 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRG-----------------IRHahrnlKIGYFSQHHVEQLdlnVSA-VELLARKF 361
Cdd:PRK13633 39 LVILGRNGSGKSTIAKHMNALLIPSEGkvyvdgldtsdeenlwdIRN-----KAGMVFQNPDNQI---VATiVEEDVAFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 362 P---GRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEA 427
Cdd:PRK13633 111 PenlGIPPEEIRERvdesLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrrevVNTIKE 189
|
170
....*....|....*..
gi 1189438346 428 LGRalnNFRGGVILVSH 444
Cdd:PRK13633 190 LNK---KYGITIILITH 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
86-176 |
1.05e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.00 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 86 ASVILAGLGftpkmqQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV--RAILWlENYLQTWPST---ILVVS 160
Cdd:PRK11248 114 KKVGLEGAE------KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAftREQMQ-TLLLKLWQETgkqVLLIT 186
|
90
....*....|....*.
gi 1189438346 161 HDRNFLNAIATDIIHL 176
Cdd:PRK11248 187 HDIEEAVFMATELVLL 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
102-188 |
1.31e-05 |
|
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: 46.41 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 102 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL----QTWPSTILVVSHDRNFLNAIATDIIHLH 177
Cdd:cd03256 140 QRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrinREEGITVIVSLHQVDLAREYADRIVGLK 219
|
90
....*....|...
gi 1189438346 178 SQRL--DGYRGDF 188
Cdd:cd03256 220 DGRIvfDGPPAEL 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
270-468 |
1.34e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.53 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVifsrL-SVSADLE--SRICVVGENGAGKSTMLKLL--L-----GDLApVRGIR--HAHRNL--- 334
Cdd:COG1126 1 MIEIENLHKSFGDLEV----LkGISLDVEkgEVVVIIGPSGSGKSTLLRCInlLeepdsGTIT-VDGEDltDSKKDInkl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 335 --KIGYFSQH-----H--VEQldlNVsaveLLA-RKFPGRP----EEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAF 400
Cdd:COG1126 76 rrKVGMVFQQfnlfpHltVLE---NV----TLApIKVKKMSkaeaEERAMELLERVGLADKADAYP-AQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 401 AQMTMPCPNFYILDEPTNHLD-------METIEALGRalnnfRG-GVILVSHDERFIRLVCRELWVCEGGGVtrVE 468
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDpelvgevLDVMRDLAK-----EGmTMVVVTHEMGFAREVADRVVFMDGGRI--VE 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
106-445 |
1.43e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPST-ILVVSHDRNFLNAIATDIIHLHsQRL 181
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMY-QGE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 182 DGYRGDFETFIKSkqerllnqqreyeAQQQYRQHIQVFIDRFryNANRASQVQSKLKMLEkLPELKPVDKESEVVMKFPd 261
Cdd:PRK10261 247 AVETGSVEQIFHA-------------PQHPYTRALLAAVPQL--GAMKGLDYPRRFPLIS-LEHPAKQEPPIEQDTVVD- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 262 gfekfSPPILQLDEVDFYYDPKHVIFSRLS--------VSADL--ESRICVVGENGAGKSTMLKLLLG------------ 319
Cdd:PRK10261 310 -----GEPILQVRNLVTRFPLRSGLLNRVTrevhavekVSFDLwpGETLSLVGESGSGKSTTGRALLRlvesqggeiifn 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 320 ----DLAPVRGIRHAHRNlkIGYFSQHHVEQLD----LNVSAVELLARKFPGRPEEEYRH---QLGRYGISGELAMRPLA 388
Cdd:PRK10261 385 gqriDTLSPGKLQALRRD--IQFIFQDPYASLDprqtVGDSIMEPLRVHGLLPGKAAAARvawLLERVGLLPEHAWRYPH 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 389 SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM----ETIEALGRALNNFRGGVILVSHD 445
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHD 523
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
80-138 |
1.55e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.14 E-value: 1.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 80 DKAPARASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:COG1126 111 AEAEERAMELLERVGLADKADAYP-AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
300-444 |
1.61e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.58 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLK-------IGYFSQHHVEQL-------DLNVSAVELlar 359
Cdd:PRK13637 36 VGLIGHTGSGKSTLIQHLNGLLKPtsgkiiIDGVDITDKKVKlsdirkkVGLVFQYPEYQLfeetiekDIAFGPINL--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 360 kfpGRPEEEYRHQLGR----YGISGE-LAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEA 427
Cdd:PRK13637 113 ---GLSEEEIENRVKRamniVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKE 189
|
170
....*....|....*..
gi 1189438346 428 LGRALNNfrgGVILVSH 444
Cdd:PRK13637 190 LHKEYNM---TIILVSH 203
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
60-142 |
1.75e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II 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. In members of 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: 213182 [Multi-domain] Cd Length: 182 Bit Score: 45.50 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 60 EGSEAAELAEIYAKLEEIEA------DKAPARASV---ILAGLGFTPK-------MQQQPTRE-------FSGGWRMRLA 116
Cdd:cd03215 35 VGNGQTELAEALFGLRPPASgeitldGKPVTRRSPrdaIRAGIAYVPEdrkreglVLDLSVAEnialsslLSGGNQQKVV 114
|
90 100
....*....|....*....|....*.
gi 1189438346 117 LARALFARPDLLLLDEPTNMLDVRAI 142
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAK 140
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
108-138 |
1.80e-05 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 45.99 E-value: 1.80e-05
10 20 30
....*....|....*....|....*....|.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
287-464 |
1.84e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.54 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 287 FSRLSVSAdlesricVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL-----KIGYFSQHHVEQL---DLN 350
Cdd:PRK13638 24 FSLSPVTG-------LVGANGCGKSTLFMNLSGLLRPQKGavlwqgkpLDYSKRGLlalrqQVATVFQDPEQQIfytDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 351 vSAVELLARKFpGRPEEE----------------YRHQlgrygisgelamrPLASLSGGQKSRVAFAQMTMPCPNFYILD 414
Cdd:PRK13638 97 -SDIAFSLRNL-GVPEAEitrrvdealtlvdaqhFRHQ-------------PIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 415 EPTNHLD----METIEALGRALNNFRgGVILVSHDERFIRLVCRELWVCEGGGV 464
Cdd:PRK13638 162 EPTAGLDpagrTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
388-450 |
2.19e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 2.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 388 ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG----VILVSHDERFIR 450
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenriTIIIAHRLSTIR 644
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
108-161 |
2.26e-05 |
|
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: 44.73 E-value: 2.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSH 161
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
85-183 |
2.26e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.64 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 85 RASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSH 161
Cdd:PRK10908 117 RVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATH 195
|
90 100
....*....|....*....|..
gi 1189438346 162 DRNFLNAIATDIIHLHSQRLDG 183
Cdd:PRK10908 196 DIGLISRRSYRMLTLSDGHLHG 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
108-162 |
2.34e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.93 E-value: 2.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHD 162
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
83-141 |
2.58e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 2.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 83 PARASVIL----AGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 141
Cdd:PRK15439 376 PARENAVLeryrRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
31-161 |
2.59e-05 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 46.66 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 31 QSVLESDSVREDLLRRERELTAQiaagrAEGSEAAELAEIYAKLEEIEadkaparasvilagLGFTPKMQQQPTrEFSGG 110
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKENVSQ-----DEIWAACEIAEIKDDIENMP--------------LGYQTELSEEGS-SISGG 615
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 111 WRMRLALARALFARPDLLLLDEPTNMLDV---RAIlwLENYLQTWPSTILVVSH 161
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTiteKKI--VNNLLNLQDKTIIFVAH 667
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
297-444 |
2.73e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.93 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 297 ESRICV-VGENGAGKSTMLKLLLGDLAPVRGI-----RHAHRNL-----KIGYFSQHHVEQLDLNVSAVELLARKFPGRP 365
Cdd:TIGR01257 955 ENQITAfLGHNGAGKTTTLSILTGLLPPTSGTvlvggKDIETNLdavrqSLGMCPQHNILFHHLTVAEHILFYAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 366 EEEYRHQL-------GRYGISGELAMrplaSLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG 438
Cdd:TIGR01257 1035 WEEAQLEMeamledtGLHHKRNEEAQ----DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
....*...
gi 1189438346 439 --VILVSH 444
Cdd:TIGR01257 1111 rtIIMSTH 1118
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
78-162 |
2.81e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 45.52 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 78 EADKApaRASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEP---------TNMLD-VRAIlwlen 147
Cdd:COG3840 104 AEQRA--QVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPILLLDEPfsaldpalrQEMLDlVDEL----- 175
|
90
....*....|....*
gi 1189438346 148 yLQTWPSTILVVSHD 162
Cdd:COG3840 176 -CRERGLTVLMVTHD 189
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
76-139 |
3.27e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 45.85 E-value: 3.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 76 EIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 139
Cdd:PRK15079 131 KLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
72-162 |
3.28e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 46.18 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 72 AKLEEIEADKAPARASVIL--AGLgftpkMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRA-I 142
Cdd:PRK11000 103 AGAKKEEINQRVNQVAEVLqlAHL-----LDRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqMRIeI 176
|
90 100
....*....|....*....|
gi 1189438346 143 LWLENYLQtwpSTILVVSHD 162
Cdd:PRK11000 177 SRLHKRLG---RTMIYVTHD 193
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
99-162 |
3.33e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.49 E-value: 3.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 99 MQQQPTRE---FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQT----WPSTILVVSHD 162
Cdd:PRK13650 130 MQDFKEREparLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD 200
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
105-138 |
3.34e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 44.85 E-value: 3.34e-05
10 20 30
....*....|....*....|....*....|....
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:cd03213 110 RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
98-162 |
3.40e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.47 E-value: 3.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 98 KMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHD 162
Cdd:PRK14271 156 RLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
52-162 |
3.50e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 45.09 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 52 AQIAAGR---AEGSEAAELAEIYAKLEEIEAD-KAPARA--SVILAGLGFTP----------KMQQ---QPTREFSGGWR 112
Cdd:cd03237 42 IKMLAGVlkpDEGDIEIELDTVSYKPQYIKADyEGTVRDllSSITKDFYTHPyfkteiakplQIEQildREVPELSGGEL 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 113 MRLALARALFARPDLLLLDEPTNMLDV-------RAIlwlENYLQTWPSTILVVSHD 162
Cdd:cd03237 122 QRVAIAACLSKDADIYLLDEPSAYLDVeqrlmasKVI---RRFAENNEKTAFVVEHD 175
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
271-445 |
3.63e-05 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (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: 213262 [Multi-domain] Cd Length: 242 Bit Score: 44.98 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGYF 339
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGeIFIDGEDIreqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 340 SQH-----H--VEQldlNVSAVEllarKFPGRPEEEYRHQ----LGRYGI-SGELAMRPLASLSGGQKSRVAFAQMTMPC 407
Cdd:cd03295 81 IQQiglfpHmtVEE---NIALVP----KLLKWPKEKIRERadelLALVGLdPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1189438346 408 PNFYILDEPTNHLDMETIEALGRALNNF----RGGVILVSHD 445
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLqqelGKTIVFVTHD 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
105-140 |
4.00e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.97 E-value: 4.00e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 140
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
101-141 |
4.27e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.78 E-value: 4.27e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1189438346 101 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 141
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGA 429
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
98-174 |
4.87e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.93 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 98 KMQQQPTREFSGGWRMRLALARALfARP-DLLLLDEPTNMLDV-------RAIlwlENYLQTWPSTILVVSHDRNFLNAI 169
Cdd:COG1245 447 KLLDKNVKDLSGGELQRVAIAACL-SRDaDLYLLDEPSAHLDVeqrlavaKAI---RRFAENRGKTAMVVDHDIYLIDYI 522
|
....*
gi 1189438346 170 ATDII 174
Cdd:COG1245 523 SDRLM 527
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
107-161 |
5.15e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.83 E-value: 5.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSH 161
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
265-421 |
5.61e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.32 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 265 KFSPPILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI------------RHAHR 332
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDA-KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTllfegedistlkPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 333 NlKIGYFSQHHV---EQLDLNVsavellarKFP-----GRPEEE-YRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQM 403
Cdd:PRK10247 81 Q-QVSYCAQTPTlfgDTVYDNL--------IFPwqirnQQPDPAiFLDDLERFALPDTILTKNIAELSGGEKQRISLIRN 151
|
170
....*....|....*...
gi 1189438346 404 TMPCPNFYILDEPTNHLD 421
Cdd:PRK10247 152 LQFMPKVLLLDEITSALD 169
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
75-138 |
5.78e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.10 E-value: 5.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 75 EEIEADKAPARASVILAGlgftpkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:PRK11432 111 EERKQRVKEALELVDLAG------FEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
105-181 |
5.81e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 44.76 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 105 REFSGGWRMRLALARAL------FARPDLLLLDEPTNMLDVR---AILWL-ENYLQTWPSTILVVSHDRNFLNAIATDII 174
Cdd:PRK13548 133 PQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAhqhHVLRLaRQLAHERGLAVIVVLHDLNLAARYADRIV 212
|
....*..
gi 1189438346 175 HLHSQRL 181
Cdd:PRK13548 213 LLHQGRL 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
105-138 |
6.15e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 45.06 E-value: 6.15e-05
10 20 30
....*....|....*....|....*....|....
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:COG3839 132 KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
108-140 |
6.63e-05 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. 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: 213218 [Multi-domain] Cd Length: 234 Bit Score: 44.14 E-value: 6.63e-05
10 20 30
....*....|....*....|....*....|...
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDVR 140
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALDTE 172
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
264-423 |
6.70e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.84 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 264 EKFSPPILQLDEVDFYYDpKHVIFsrlsvsadlesriCVVGENGAGKSTMLKLLLGDLAPVRG----------------- 326
Cdd:PRK13631 33 EKQENELVALNNISYTFE-KNKIY-------------FIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 327 --IRHAHRNLK--------IGYFSQHHVEQL-------DLNVSAVELLARKFPGRPEEEYrhQLGRYGISGELAMRPLAS 389
Cdd:PRK13631 99 liTNPYSKKIKnfkelrrrVSMVFQFPEYQLfkdtiekDIMFGPVALGVKKSEAKKLAKF--YLNKMGLDDSYLERSPFG 176
|
170 180 190
....*....|....*....|....*....|....
gi 1189438346 390 LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME 423
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
304-416 |
7.06e-05 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 44.07 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 304 GENGAGKSTMLKLLLGDLAPVRG--------IRHAH----RNLKIGYFSQHH-------VEQldlNVSAVELLARKFPGR 364
Cdd:cd03218 33 GPNGAGKTTTFYMIVGLVKPDSGkilldgqdITKLPmhkrARLGIGYLPQEAsifrkltVEE---NILAVLEIRGLSKKE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 365 PEEEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEP 416
Cdd:cd03218 110 REEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
103-142 |
7.49e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 43.71 E-value: 7.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1189438346 103 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAI 142
Cdd:PRK13539 124 PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
108-140 |
7.70e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.22 E-value: 7.70e-05
10 20 30
....*....|....*....|....*....|...
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDVR 140
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
283-452 |
8.46e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.19 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 283 KHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKI-----GYFSQHHVEQLDLNVSAVEL 356
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGsIVVNGQTINLvrdkdGQLKVADKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 357 LARKFP-------------------GRPEEEYRHQLGRY----GISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYIL 413
Cdd:PRK10619 97 VFQHFNlwshmtvlenvmeapiqvlGLSKQEARERAVKYlakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1189438346 414 DEPTNHLDMETIEALGRALNNFR---GGVILVSHDERFIRLV 452
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHV 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
78-162 |
8.65e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 44.29 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 78 EADKApARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV----RAILWLENYLQTWP 153
Cdd:PRK10419 124 KAERL-ARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFG 202
|
....*....
gi 1189438346 154 STILVVSHD 162
Cdd:PRK10419 203 TACLFITHD 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
108-143 |
9.09e-05 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. 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: 213220 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 9.09e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL 143
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDThteREIQ 177
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
108-133 |
9.19e-05 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 43.61 E-value: 9.19e-05
10 20
....*....|....*....|....*.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEP 133
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
69-134 |
9.43e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 9.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 69 EIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPT 134
Cdd:NF033858 361 ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDS-LPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
70-133 |
9.63e-05 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 43.69 E-value: 9.63e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 70 IYAKLEEIEADKAPA--RASVILAGLGFTpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEP 133
Cdd:cd03218 96 ILAVLEIRGLSKKEReeKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
164-445 |
9.67e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.30 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 164 NFLNAIAtdiiHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFID---RFRYNANRASQVQSklkml 240
Cdd:pfam13304 14 NLLEALR----FLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEdgvRYRYGLDLEREDVE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 241 EKLPELKPVDKESEVVMKF-PDGFEKFSPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLG 319
Cdd:pfam13304 85 EKLSSKPTLLEKRLLLREDsEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 320 DLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELL--ARKFPGRPEEEYRHQLGRYGISGELAMRPLASLSGGQKSR 397
Cdd:pfam13304 165 DWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLgeGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 398 VAFA---QMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VILVSHD 445
Cdd:pfam13304 245 LALLaalLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNgaqLILTTHS 298
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
105-139 |
9.87e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.95 E-value: 9.87e-05
10 20 30
....*....|....*....|....*....|....*
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 139
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
99-164 |
1.04e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.85 E-value: 1.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 99 MQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPSTILVVSHDRN 164
Cdd:PRK11231 131 LADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHDLN 199
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
267-421 |
1.07e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.00 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 267 SPPILQLDEVDFYYDPKHVIFSrlsVSADLESR--ICVVGENGAGKSTMLKLL--LGDLAP---VRG-IRHAHRNLkigY 338
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNS---VSLDFYPNeiTALIGPSGSGKSTLLRSInrMNDLNPevtITGsIVYNGHNI---Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 339 FSQHHVEQLDLNVSAVELLARKFP-------------------GRPEEEYRHQLGRYGISGELAMRPLAS---LSGGQKS 396
Cdd:PRK14239 76 SPRTDTVDLRKEIGMVFQQPNPFPmsiyenvvyglrlkgikdkQVLDEAVEKSLKGASIWDEVKDRLHDSalgLSGGQQQ 155
|
170 180
....*....|....*....|....*
gi 1189438346 397 RVAFAQMTMPCPNFYILDEPTNHLD 421
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALD 180
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
108-138 |
1.09e-04 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 43.96 E-value: 1.09e-04
10 20 30
....*....|....*....|....*....|.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
108-138 |
1.12e-04 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 43.63 E-value: 1.12e-04
10 20 30
....*....|....*....|....*....|.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
80-140 |
1.20e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 43.86 E-value: 1.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 80 DKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 140
Cdd:PRK13634 119 EDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
271-423 |
1.20e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.46 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSrlsVSADLESRICVV--GENGAGKSTMLKLL-------------------LGDLAPVRGIRH 329
Cdd:PRK11124 3 IQLNGINCFYGAHQALFD---ITLDCPQGETLVllGPSGAGKSSLLRVLnllemprsgtlniagnhfdFSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 330 AHRNLKIgYFSQHHveqLDLNVSAVELLAR---KFPGRPEEEYRHQ----LGRYGISgELAMR-PLaSLSGGQKSRVAFA 401
Cdd:PRK11124 80 LRRNVGM-VFQQYN---LWPHLTVQQNLIEapcRVLGLSKDQALARaeklLERLRLK-PYADRfPL-HLSGGQQQRVAIA 153
|
170 180
....*....|....*....|..
gi 1189438346 402 QMTMPCPNFYILDEPTNHLDME 423
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPE 175
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
301-445 |
1.22e-04 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 43.89 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 301 CVVGENGAGKSTMLKLLLGDLAP---VRG-IRHAHRNL-------------------------------KIGyfsqhhvE 345
Cdd:COG0444 35 GLVGESGSGKSTLARAILGLLPPpgiTSGeILFDGEDLlklsekelrkirgreiqmifqdpmtslnpvmTVG-------D 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 346 QLD------LNVS-------AVELLAR-KFPgRPEE---EYRHQLgrygisgelamrplaslSGGQKSRVAFAQMTMPCP 408
Cdd:COG0444 108 QIAeplrihGGLSkaearerAIELLERvGLP-DPERrldRYPHEL-----------------SGGMRQRVMIARALALEP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1189438346 409 NFYILDEPTNHLDMeTIEA----LGRALNNFRG-GVILVSHD 445
Cdd:COG0444 170 KLLIADEPTTALDV-TIQAqilnLLKDLQRELGlAILFITHD 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
271-423 |
1.26e-04 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 43.46 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSrlsVSADLESRICVV--GENGAGKSTMLKLL-LGDLaPVRGIRH---------------AHR 332
Cdd:COG4161 3 IQLKNINCFYGSHQALFD---INLECPSGETLVllGPSGAGKSSLLRVLnLLET-PDSGQLNiaghqfdfsqkpsekAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 333 NL--KIGY-FSQHH------VEQlDLNVSAVELLarkfpGRPEEEYRHQ----LGRYGISGELAMRPLAsLSGGQKSRVA 399
Cdd:COG4161 79 LLrqKVGMvFQQYNlwphltVME-NLIEAPCKVL-----GLSKEQAREKamklLARLRLTDKADRFPLH-LSGGQQQRVA 151
|
170 180
....*....|....*....|....
gi 1189438346 400 FAQMTMPCPNFYILDEPTNHLDME 423
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPE 175
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
385-464 |
1.31e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 385 RPLASLSGGQKSRVAFAQ--------MTmpcpnfYILDEPTNHL---DMETIEALGRALNNFRGGVILVSHDERFIRLVC 453
Cdd:PRK00635 472 RALATLSGGEQERTALAKhlgaeligIT------YILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVEHDEQMISLAD 545
|
90
....*....|.
gi 1189438346 454 RELWVCEGGGV 464
Cdd:PRK00635 546 RIIDIGPGAGI 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
108-161 |
1.31e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.62 E-value: 1.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTwPSTILVVSH 161
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTeseRAIQAALDELQK-NRTSLVIAH 537
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
265-433 |
1.39e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 44.43 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 265 KFSPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKigyfsqhH 343
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGrILIDGQDIR-------D 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 344 VEQLDL--------------NVSAVELLARkfpGRP---EEEYRH-----QLGRYGIS---------GElamRPLaSLSG 392
Cdd:COG5265 425 VTQASLraaigivpqdtvlfNDTIAYNIAY---GRPdasEEEVEAaaraaQIHDFIESlpdgydtrvGE---RGL-KLSG 497
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1189438346 393 GQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALN 433
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
300-445 |
1.40e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 44.33 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLlGDL-APVRGI-RHAHRNLK--------------IGY-FSQHHveqLDLNVSA---VELLAr 359
Cdd:PRK10535 37 VAIVGASGSGKSTLMNIL-GCLdKPTSGTyRVAGQDVAtldadalaqlrrehFGFiFQRYH---LLSHLTAaqnVEVPA- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 360 KFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETIEALGRAL 432
Cdd:PRK10535 112 VYAGLERKQRLLRaqelLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDShsgEEVMAILHQL 190
|
170
....*....|...
gi 1189438346 433 NNFRGGVILVSHD 445
Cdd:PRK10535 191 RDRGHTVIIVTHD 203
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
302-470 |
1.44e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.91 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLL-----------------LGDLAPvRGIRHAHRnlKIGYFSQHhveqldlnvsaVELLARK---- 360
Cdd:COG1135 36 IIGYSGAGKSTLIRCInllerptsgsvlvdgvdLTALSE-RELRAARR--KIGMIFQH-----------FNLLSSRtvae 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 361 ---FP----GRPEEEyRHQ-----LGRYGISGELAMRPlASLSGGQKSRVAFAQ--MTMPcpnfYIL--DEPTNHLDMET 424
Cdd:COG1135 102 nvaLPleiaGVPKAE-IRKrvaelLELVGLSDKADAYP-SQLSGGQKQRVGIARalANNP----KVLlcDEATSALDPET 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 425 ---IEALGRALNNfRGG--VILVSHDERFIRLVCRELWVCEGGGVtrVEGG 470
Cdd:COG1135 176 trsILDLLKDINR-ELGltIVLITHEMDVVRRICDRVAVLENGRI--VEQG 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
300-421 |
1.63e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.15 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 300 ICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNlkIGYFSQH-------HVEQldlNVSA-------VE---LLA--- 358
Cdd:COG1101 35 VTVIGSNGAGKSTLLNAIAGSLPPDSGsILIDGKD--VTKLPEYkrakyigRVFQ---DPMMgtapsmtIEenlALAyrr 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 359 -RKFPGRP------EEEYRHQLGRYGISGELAMR-PLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 421
Cdd:COG1101 110 gKRRGLRRgltkkrRELFRELLATLGLGLENRLDtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
77-139 |
1.67e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 1.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 77 IEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 139
Cdd:PRK10261 434 LPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
75-138 |
1.87e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 43.78 E-value: 1.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 75 EEIEADKAPARASVILAGLGftpkmQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:PRK09452 119 AEITPRVMEALRMVQLEEFA-----QRKPHQ-LSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
70-133 |
2.15e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 42.71 E-value: 2.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 70 IYAKLEEIEADKA--PARASVILAGLGFTpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEP 133
Cdd:COG1137 99 ILAVLELRKLSKKerEERLEELLEEFGIT-HLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
106-199 |
2.21e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.07 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA----ILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
90
....*....|....*...
gi 1189438346 182 DGYRGDFETFikSKQERL 199
Cdd:PRK13645 230 ISIGSPFEIF--SNQELL 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
103-161 |
2.22e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 42.98 E-value: 2.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 103 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSH 161
Cdd:PRK14247 143 PAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
77-161 |
2.44e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.18 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 77 IEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWP 153
Cdd:PRK13643 115 IPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSG 194
|
....*...
gi 1189438346 154 STILVVSH 161
Cdd:PRK13643 195 QTVVLVTH 202
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
77-162 |
2.45e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.76 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 77 IEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV----RAILWLENYLQTW 152
Cdd:PRK10418 111 KPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKR 190
|
90
....*....|
gi 1189438346 153 PSTILVVSHD 162
Cdd:PRK10418 191 ALGMLLVTHD 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
108-143 |
2.59e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.14 E-value: 2.59e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAIL 143
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDpetTRSIL 180
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
389-421 |
2.94e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.50 E-value: 2.94e-04
10 20 30
....*....|....*....|....*....|...
gi 1189438346 389 SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 421
Cdd:TIGR00955 166 GLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
75-173 |
2.97e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 42.76 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 75 EEIEADKAPARASVILAGLgftpkmQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQT 151
Cdd:PRK13639 112 EEVEKRVKEALKAVGMEGF------ENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNK 185
|
90 100
....*....|....*....|..
gi 1189438346 152 WPSTILVVSHDRNFLNAIATDI 173
Cdd:PRK13639 186 EGITIIISTHDVDLVPVYADKV 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
264-446 |
3.02e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 42.90 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 264 EKFSPPILQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHA---HR 332
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGqimldgvdLSHVppyQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 333 NLKIGY-----FSQHHVEQldlNVsAVELLARKFPgRPEEEYR-HQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMP 406
Cdd:PRK11607 92 PINMMFqsyalFPHMTVEQ---NI-AFGLKQDKLP-KAEIASRvNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1189438346 407 CPNFYILDEPTNHLD--------METIEALGRAlnnfrgGV--ILVSHDE 446
Cdd:PRK11607 167 RPKLLLLDEPMGALDkklrdrmqLEVVDILERV------GVtcVMVTHDQ 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
105-138 |
3.44e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 3.44e-04
10 20 30
....*....|....*....|....*....|....
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
102-141 |
3.62e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 3.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1189438346 102 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 141
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGA 439
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
271-443 |
3.65e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 42.87 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGdLAP-VRGIRHAHRNLKIGYFSQH-HVEQLD 348
Cdd:COG4178 363 LALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIARPAGARVLFLPQRpYLPLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 349 LnvsaVELLArkFPGRPE----EEYRHQLGRYGIsGELAMRPLAS------LSGGQKSRVAFAQMTMPCPNFYILDEPTN 418
Cdd:COG4178 442 L----REALL--YPATAEafsdAELREALEAVGL-GHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180
....*....|....*....|....*
gi 1189438346 419 HLDMETIEALGRALNNFRGGVILVS 443
Cdd:COG4178 515 ALDEENEAALYQLLREELPGTTVIS 539
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
302-428 |
3.83e-04 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 41.38 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVR--------GIRHAHRNLK--IGYFSQHhvEQLDLNVSAVELLArkfpgrpeeeyrh 371
Cdd:cd03213 40 IMGPSGAGKSTLLNALAGRRTGLGvsgevlinGRPLDKRSFRkiIGYVPQD--DILHPTLTVRETLM------------- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 372 qlgrygISGElamrpLASLSGGQKSRVAFA-QMTMPcPNFYILDEPTNHLD-------METIEAL 428
Cdd:cd03213 105 ------FAAK-----LRGLSGGERKRVSIAlELVSN-PSLLFLDEPTSGLDsssalqvMSLLRRL 157
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
106-161 |
3.85e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.88 E-value: 3.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRA-ILWL-ENYLQTWPSTILVVSH 161
Cdd:PRK10771 129 QLSGGQRQRVALARCLVREQPILLLDEPFSALDpaLRQeMLTLvSQVCQERQLTLLMVSH 188
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
270-445 |
3.94e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 41.99 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 270 ILQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLKIGYFSQHH 343
Cdd:PRK11248 1 MLQISHLYADYGGKPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYqhgsitLDGKPVEGPGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 344 VEQLDLNVSAVELLARKFPGRPEEEYRHQ----LGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNH 419
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIahqmLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|
gi 1189438346 420 LDMETIEA----LGRALNNFRGGVILVSHD 445
Cdd:PRK11248 159 LDAFTREQmqtlLLKLWQETGKQVLLITHD 188
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
108-138 |
4.02e-04 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 41.87 E-value: 4.02e-04
10 20 30
....*....|....*....|....*....|.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:cd03234 145 SGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
64-174 |
4.08e-04 |
|
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: 40.82 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 64 AAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA-- 141
Cdd:smart00382 23 ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK-----ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQea 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1189438346 142 -------ILWLENYLQTWPSTILVVSHDRNFLNAIATDII 174
Cdd:smart00382 98 llllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
75-145 |
4.30e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.48 E-value: 4.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 75 EEIEAdkapaRASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWL 145
Cdd:PRK11153 115 AEIKA-----RVTELLELVGLSDKADRYPA-QLSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSILEL 182
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
103-149 |
4.30e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.33 E-value: 4.30e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1189438346 103 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL 149
Cdd:PRK13538 126 PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
103-174 |
4.66e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.48 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 103 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---------AILWLENYLqtwpsTILVVSHDRNFLNAIATDI 173
Cdd:COG2401 133 RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrvarnlQKLARRAGI-----TLVVATHHYDVIDDLQPDL 207
|
.
gi 1189438346 174 I 174
Cdd:COG2401 208 L 208
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
385-428 |
4.76e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 4.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1189438346 385 RPLASLSGGQKSRVAFA-QMTMPC--PNFYILDEPTNHLDMETIEAL 428
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAyELLAPSkkPTLYVLDEPTTGLHTHDIKAL 851
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-161 |
4.87e-04 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 42.78 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 5 RSLRvpAHISLlhVEQEVagddtpalqsVLESDSVredllrrerelTAQIAAGRAEGseaaelaeiyAKLEEIEADKAPA 84
Cdd:TIGR02203 402 ASLR--RQVAL--VSQDV----------VLFNDTI-----------ANNIAYGRTEQ----------ADRAEIERALAAA 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 85 RASVILAGLgftPKMQQQPTRE----FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAI-LWLENYLQTwpSTI 156
Cdd:TIGR02203 447 YAQDFVDKL---PLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNeseRLVqAALERLMQG--RTT 521
|
....*
gi 1189438346 157 LVVSH 161
Cdd:TIGR02203 522 LVIAH 526
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
271-446 |
5.49e-04 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. 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: 213267 [Multi-domain] Cd Length: 232 Bit Score: 41.45 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 271 LQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------KIGYFSQ 341
Cdd:cd03300 1 IELENVSKFYGGFVAL-DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGeILLDGKDItnlpphkrPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 342 HHVEQLDLNVSAVELLARKFPGRPEEEYRHQLGRY----GISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPT 417
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEAldlvQLEG-YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|...
gi 1189438346 418 NHLDMETIEALGRALNNFRGGV----ILVSHDE 446
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELgitfVFVTHDQ 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
89-181 |
5.60e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 41.71 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 89 ILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPS-TILVVSHDRN 164
Cdd:PRK13640 127 VLADVGMLDYIDSEPA-NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqILKLIRKLKKKNNlTVISITHDID 205
|
90
....*....|....*..
gi 1189438346 165 FLNaIATDIIHLHSQRL 181
Cdd:PRK13640 206 EAN-MADQVLVLDDGKL 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
80-181 |
6.74e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 41.74 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 80 DKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWL----ENYlQTWPST 155
Cdd:PRK13641 119 DEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMmqlfKDY-QKAGHT 197
|
90 100
....*....|....*....|....*.
gi 1189438346 156 ILVVSHDRNFLNAIATDIIHLHSQRL 181
Cdd:PRK13641 198 VILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
106-198 |
7.09e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.63 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAIL----WLENYLQTWPSTILVVSHDRNFLNAIAtDIIHLhsqrL 181
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLnaarAIRRLSEEGKKTALVVEHDLAVLDYLS-DRIHV----F 145
|
90
....*....|....*..
gi 1189438346 182 DGYRGDFETFIKSKQER 198
Cdd:cd03222 146 EGEPGVYGIASQPKGTR 162
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
101-142 |
7.18e-04 |
|
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: 40.80 E-value: 7.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1189438346 101 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAI 142
Cdd:TIGR01189 122 DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
384-421 |
7.53e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 7.53e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1189438346 384 MRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 421
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
303-453 |
8.69e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.91 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 303 VGENGAGKSTMLKLL-------------LGDLAPVRGIRHAhRNLKIGYFSQhhveQLDL--NVSAVE--LLARKFPGR- 364
Cdd:PRK10762 36 VGENGAGKSTMMKVLtgiytrdagsilyLGKEVTFNGPKSS-QEAGIGIIHQ----ELNLipQLTIAEniFLGREFVNRf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 365 -------PEEEYRHQLGRYGISGElAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHL-DMETiEALGRALNNFR 436
Cdd:PRK10762 111 gridwkkMYAEADKLLARLNLRFS-SDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET-ESLFRVIRELK 188
|
170 180
....*....|....*....|
gi 1189438346 437 G---GVILVSHDERFIRLVC 453
Cdd:PRK10762 189 SqgrGIVYISHRLKEIFEIC 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
289-445 |
8.80e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 41.62 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 289 RLSVSADLESR-ICVV-GENGAGKSTMLKLLLGDLAPVRG-IR---------HAHRNLK-----IGYFSQH-----Hveq 346
Cdd:COG4148 15 TLDVDFTLPGRgVTALfGPSGSGKTTLLRAIAGLERPDSGrIRlggevlqdsARGIFLPphrrrIGYVFQEarlfpH--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 347 ldLNVSAVELLARKFPGRPEEEYRHQ-----LGrygISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 421
Cdd:COG4148 92 --LSVRGNLLYGRKRAPRAERRISFDevvelLG---IGHLLDRRP-ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180
....*....|....*....|....*...
gi 1189438346 422 M----ETIEALGRALNNFRGGVILVSHD 445
Cdd:COG4148 166 LarkaEILPYLERLRDELDIPILYVSHS 193
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
98-180 |
9.18e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 41.26 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 98 KMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILWLenyLQTWPSTILVVSHDRNFLNAIAT 171
Cdd:PRK13647 130 DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgqetLMEILDR---LHNQGKTVIVATHDVDLAAEWAD 206
|
....*....
gi 1189438346 172 DIIHLHSQR 180
Cdd:PRK13647 207 QVIVLKEGR 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
80-162 |
9.36e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 40.99 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 80 DKAPARASVILAGLGFTPkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAIL----WLENYLQTWPST 155
Cdd:PRK13636 116 DEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSeimkLLVEMQKELGLT 194
|
....*..
gi 1189438346 156 ILVVSHD 162
Cdd:PRK13636 195 IIIATHD 201
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
302-447 |
1.03e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.78 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLG-------------------DLAPVRgirHAHRNLKIGYfsQHHVEQLdlNVSAVELL----- 357
Cdd:CHL00131 38 IMGPNGSGKSTLSKVIAGhpaykilegdilfkgesilDLEPEE---RAHLGIFLAF--QYPIEIP--GVSNADFLrlayn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 358 -ARKFPGRPE-------EEYRHQLGRYGISGELAMRPL-ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEAL 428
Cdd:CHL00131 111 sKRKFQGLPEldpleflEIINEKLKLVGMDPSFLSRNVnEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKII 190
|
170 180
....*....|....*....|..
gi 1189438346 429 GRALNNFRG---GVILVSHDER 447
Cdd:CHL00131 191 AEGINKLMTsenSIILITHYQR 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
386-445 |
1.06e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 386 PLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG---GVILVSHD 445
Cdd:PRK10762 392 AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeglSIILVSSE 454
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
108-138 |
1.07e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 40.84 E-value: 1.07e-03
10 20 30
....*....|....*....|....*....|.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
387-446 |
1.10e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 40.74 E-value: 1.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 387 LASLSGGQKSRVAFAQ-MTM----PCPnFYILDEPTNHLDMETIEALGRAL-NNFRGG-VILVSHDE 446
Cdd:cd03273 164 LTELSGGQRSLVALSLiLALllfkPAP-MYILDEVDAALDLSHTQNIGRMIkTHFKGSqFIVVSLKE 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
108-138 |
1.14e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.53 E-value: 1.14e-03
10 20 30
....*....|....*....|....*....|.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
107-166 |
1.19e-03 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 40.39 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR--------AILwleNYLQTWPSTILVVSHDRNFL 166
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlmqeGIL---KFLQDDKRTLVLVTHKLQYL 205
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
105-141 |
1.22e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including 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: 213199 [Multi-domain] Cd Length: 192 Bit Score: 39.92 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 141
Cdd:cd03232 107 RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
41-162 |
1.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 41 EDLLRRERELTAQIAAGRAEGSEAA-----ELA-EIYAKLEE-------IEADKAPARASVILAGlgftpkmQQQPTREF 107
Cdd:PRK03918 717 EKALERVEELREKVKKYKALLKERAlskvgEIAsEIFEELTEgkysgvrVKAEENKVKLFVVYQG-------KERPLTFL 789
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 108 SGGWRM------RLALARALFARPDLLLLDEPTNMLD----VRAILWLENYLQTWPSTIlVVSHD 162
Cdd:PRK03918 790 SGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDeerrRKLVDIMERYLRKIPQVI-IVSHD 853
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
107-140 |
1.25e-03 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. 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: 213221 [Multi-domain] Cd Length: 229 Bit Score: 40.29 E-value: 1.25e-03
10 20 30
....*....|....*....|....*....|....
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 140
Cdd:cd03254 140 LSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
107-164 |
1.33e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 1.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQT--WPSTILVVSHDRN 164
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAHRLN 1431
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
70-200 |
1.38e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 41.54 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 70 IYAKLEEIEADKAPARASVILAGLGFTpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL 149
Cdd:TIGR01257 2035 LYARLRGVPAEEIEKVANWSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 150 QTW---PSTILVVSHDRNFLNAIAT--------------DIIHLHSQRLDGYRGDFEtfIKSKQERLL 200
Cdd:TIGR01257 2114 VSIireGRAVVLTSHSMEECEALCTrlaimvkgafqclgTIQHLKSKFGDGYIVTMK--IKSPKDDLL 2179
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
77-161 |
1.40e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 40.50 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 77 IEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWP 153
Cdd:PRK13649 116 VSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPkgrKELMTLFKKLHQSG 195
|
....*...
gi 1189438346 154 STILVVSH 161
Cdd:PRK13649 196 MTIVLVTH 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
107-139 |
1.44e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 41.43 E-value: 1.44e-03
10 20 30
....*....|....*....|....*....|...
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDV 139
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
106-175 |
1.45e-03 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 40.43 E-value: 1.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR-----AILWLEnyLQTWPSTILVVSHDRNFLNAIAtDIIH 175
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlnaARLIRE--LAEDDNYVLVVEHDLAVLDYLS-DYIH 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
106-162 |
1.47e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.52 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEP-------TNMLDVRAILWLENYLQTwpsTILVVSHD 162
Cdd:PRK11831 143 ELSGGMARRAALARAIALEPDLIMFDEPfvgqdpiTMGVLVKLISELNSALGV---TCVVVSHD 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
390-482 |
1.49e-03 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 40.94 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 390 LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI----EALGRALNNFRGGVILVSHDERFI-RLVCRELWVcEGGGV 464
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIeDLSDKAIWL-ENGEI 247
|
90
....*....|....*...
gi 1189438346 465 TRvEGGFDQYRALLQEQF 482
Cdd:TIGR03269 248 KE-EGTPDEVVAVFMEGV 264
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
108-162 |
1.59e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 40.50 E-value: 1.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQ-TWPSTILVVSHD 162
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDArqnLLDLVRKVKsEHNITIISITHD 202
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
302-326 |
1.64e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 40.94 E-value: 1.64e-03
10 20
....*....|....*....|....*
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRG 326
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESG 387
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
108-138 |
1.66e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.46 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
386-445 |
1.77e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 40.03 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 386 PLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG--GVILVSHD 445
Cdd:PRK14246 150 PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
299-445 |
1.84e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 40.82 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 299 RICVVGENGAGKS----TMLKLLLGDLAPVRG-IRHAHRNL--------------KIGYFSQ---------HHVEQ---- 346
Cdd:COG4172 38 TLALVGESGSGKSvtalSILRLLPDPAAHPSGsILFDGQDLlglserelrrirgnRIAMIFQepmtslnplHTIGKqiae 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 347 ---LDLNVS-------AVELLAR---KFPGRPEEEYRHQLgrygisgelamrplaslSGGQKSRVAFAqMTMPC-PNFYI 412
Cdd:COG4172 118 vlrLHRGLSgaaararALELLERvgiPDPERRLDAYPHQL-----------------SGGQRQRVMIA-MALANePDLLI 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1189438346 413 LDEPTNHLDMeTIEA----LGRALNNFRG-GVILVSHD 445
Cdd:COG4172 180 ADEPTTALDV-TVQAqildLLKDLQRELGmALLLITHD 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
105-145 |
1.86e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.02 E-value: 1.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1189438346 105 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWL 145
Cdd:PLN03211 205 RGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
87-166 |
1.88e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.23 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 87 SVILAGLGFTPKMQQQPTreFSGGWRMRLALARALFARPD--LLLLDEPTNMLDVRAILWLENYLQTW---PSTILVVSH 161
Cdd:cd03238 70 FLIDVGLGYLTLGQKLST--LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEH 147
|
....*
gi 1189438346 162 DRNFL 166
Cdd:cd03238 148 NLDVL 152
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
289-451 |
1.92e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 40.24 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 289 RLSVSADLESR-ICVV-GENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------------KIGYFSQHhveqldlnv 351
Cdd:PRK11144 14 CLTVNLTLPAQgITAIfGRSGAGKTSLINAISGLTRPQKGrIVLNGRVLfdaekgiclppekrRIGYVFQD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 352 savellARKFPgrpeeEYRHQlG--RYGISGE-----------LAMRPL-----ASLSGGQKSRVAFAQMTMPCPNFYIL 413
Cdd:PRK11144 85 ------ARLFP-----HYKVR-GnlRYGMAKSmvaqfdkivalLGIEPLldrypGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438346 414 DEPTNHLDM----ETIEALGRALNNFRGGVILVSH--DErFIRL 451
Cdd:PRK11144 153 DEPLASLDLprkrELLPYLERLAREINIPILYVSHslDE-ILRL 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
103-183 |
2.08e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.58 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 103 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQ 179
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
....
gi 1189438346 180 RLDG 183
Cdd:TIGR02633 480 KLKG 483
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
81-180 |
2.09e-03 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. 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: 213236 [Multi-domain] Cd Length: 210 Bit Score: 39.57 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 81 KAPARASV--ILAGLGFTPKmQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPST 155
Cdd:cd03269 102 KEEARRRIdeWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKT 180
|
90 100
....*....|....*....|....*
gi 1189438346 156 ILVVSHDRNFLNAIATDIIHLHSQR 180
Cdd:cd03269 181 VILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
388-433 |
2.20e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.39 E-value: 2.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1189438346 388 ASLSGGQKSRVAFAQMTM-PCPnFYILDEPTNHLDMETIEALGRALN 433
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLrDSP-ILILDEATSALDTESERAIQAALD 524
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
108-139 |
2.28e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 39.84 E-value: 2.28e-03
10 20 30
....*....|....*....|....*....|..
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDV 139
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
106-162 |
2.61e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.02 E-value: 2.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS----TILVVSHD 162
Cdd:PRK10070 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
382-467 |
2.62e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 40.01 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 382 LAMRPLAsLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD------MET-IEALGRALNNfrgGVILVSHDERFIRLVCR 454
Cdd:PRK11000 127 LDRKPKA-LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqMRIeISRLHKRLGR---TMIYVTHDQVEAMTLAD 202
|
90
....*....|...
gi 1189438346 455 ELWVCEGGGVTRV 467
Cdd:PRK11000 203 KIVVLDAGRVAQV 215
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
381-458 |
2.78e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 381 ELAMRplASLSGGQKS------RVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRAL----------NNFRggVILVSH 444
Cdd:TIGR00606 1193 ALDMR--GRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITH 1268
|
90
....*....|....
gi 1189438346 445 DERFIRLVCRELWV 458
Cdd:TIGR00606 1269 DEDFVELLGRSEYV 1282
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
107-140 |
2.82e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.49 E-value: 2.82e-03
10 20 30
....*....|....*....|....*....|....
gi 1189438346 107 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 140
Cdd:PLN03130 1375 FSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
93-164 |
2.88e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 39.53 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 93 LGFTPKMQQqPTREFSGG-W-RMRLALA-----RALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHD 162
Cdd:PRK03695 114 LGLDDKLGR-SVNQLSGGeWqRVRLAAVvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSHD 192
|
..
gi 1189438346 163 RN 164
Cdd:PRK03695 193 LN 194
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
84-139 |
3.02e-03 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 39.01 E-value: 3.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 84 ARASVILAGLGFTPKMQqqptreFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 139
Cdd:cd03231 109 ALARVGLNGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
391-445 |
3.18e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 39.71 E-value: 3.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 391 SGGQKSRVAFAqMTMPC-PNFYILDEPTNHLDMeTIEALGRALNN-----FRGGVILVSHD 445
Cdd:PRK09473 163 SGGMRQRVMIA-MALLCrPKLLIADEPTTALDV-TVQAQIMTLLNelkreFNTAIIMITHD 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
302-462 |
3.19e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 39.11 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLG----------------DLAPVrgirHAHRNLKIGYFSQHH--VEQLDL--NVSAVeLLARKF 361
Cdd:PRK10895 34 LLGPNGAGKTTTFYMVVGivprdagniiiddediSLLPL----HARARRGIGYLPQEAsiFRRLSVydNLMAV-LQIRDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 362 PGRPEEEYRHQ--LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG-- 437
Cdd:PRK10895 109 LSAEQREDRANelMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDsg 187
|
170 180
....*....|....*....|....*.
gi 1189438346 438 -GVILVSHDERFIRLVCRELWVCEGG 462
Cdd:PRK10895 188 lGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
90-138 |
3.37e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 3.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1189438346 90 LAGLGFTPKMQQQPTREFSGGwRMRLAL-ARALFARPDLLLLDEPTNMLD 138
Cdd:PRK10938 385 LDILGIDKRTADAPFHSLSWG-QQRLALiVRALVKHPTLLILDEPLQGLD 433
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
100-138 |
3.52e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 39.22 E-value: 3.52e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1189438346 100 QQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:PRK13638 130 RHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
368-421 |
4.09e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 4.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 368 EYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 421
Cdd:PTZ00265 1347 KYDTNVGPYG----------KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
108-143 |
4.15e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 39.80 E-value: 4.15e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL 143
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSrteRAIQ 534
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
302-444 |
4.23e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 38.74 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLL--LGDLAP---VRG-------------IRHAHRNLKIGYFSQHHVEQLDL--NVSAVELLARKF 361
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFnrLIELYPearVSGevyldgqdifkmdVIELRRRVQMVFQIPNPIPNLSIfeNVALGLKLNRLV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 362 PGRPE--EEYRHQLGRYGISGELAMR---PLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGRALN 433
Cdd:PRK14247 114 KSKKElqERVRWALEKAQLWDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELK 193
|
170
....*....|.
gi 1189438346 434 NfRGGVILVSH 444
Cdd:PRK14247 194 K-DMTIVLVTH 203
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
385-451 |
4.25e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.78 E-value: 4.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438346 385 RPLASLSGGQKSRVAFA-QMTMPCPN-FYILDEPT-------NHLDMETIEALgRALNNfrgGVILVSHDERFIRL 451
Cdd:cd03270 133 RSAPTLSGGEAQRIRLAtQIGSGLTGvLYVLDEPSiglhprdNDRLIETLKRL-RDLGN---TVLVVEHDEDTIRA 204
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
98-215 |
4.52e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 98 KMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDII 174
Cdd:PRK13545 135 KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqtfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKAL 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1189438346 175 HLHSQRLDGYrGD-------FETFIK-----SKQERllnqQREYEAQQQYRQH 215
Cdd:PRK13545 215 WLHYGQVKEY-GDikevvdhYDEFLKkynqmSVEER----KDFREEQISQFQH 262
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
385-451 |
4.69e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 385 RPLASLSGGQKSRVAFA-----QMT--MpcpnfYILDEPT-------NHLDMETIEALgRALNNfrgGVILVSHDERFIR 450
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLAtqigsGLTgvL-----YVLDEPSiglhqrdNRRLINTLKRL-RDLGN---TLIVVEHDEDTIR 554
|
.
gi 1189438346 451 L 451
Cdd:TIGR00630 555 A 555
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
307-445 |
5.01e-03 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II 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. In members of 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: 213182 [Multi-domain] Cd Length: 182 Bit Score: 38.18 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 307 GAGKSTMLKLLLGDLAPVRG-IR-----------HAHRNLKIGYFsqhhveqldlnvsavellarkfpgrPEEeyRHQLG 374
Cdd:cd03215 36 GNGQTELAEALFGLRPPASGeITldgkpvtrrspRDAIRAGIAYV-------------------------PED--RKREG 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438346 375 ---RYGISGELAMRPLasLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFR---GGVILVSHD 445
Cdd:cd03215 89 lvlDLSVAENIALSSL--LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSE 163
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
279-480 |
5.06e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 39.51 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 279 YYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLgDLAPVRGirhahrNLKIGYFSQHHVeQLDLNVSAVELLA 358
Cdd:TIGR01271 1227 YTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEG------EIQIDGVSWNSV-TLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 359 RK---FPGR------PEEEYRHQlGRYGISGELAMRPLAS----------------LSGGQKSRVAFAQMTMPCPNFYIL 413
Cdd:TIGR01271 1299 QKvfiFSGTfrknldPYEQWSDE-EIWKVAEEVGLKSVIEqfpdkldfvlvdggyvLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 414 DEPTNHLDMETIEALGRAL-NNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRveggFDQYRALLQE 480
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ----YDSIQKLLNE 1441
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
291-422 |
5.13e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 38.62 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 291 SVSADLESR--ICVVGENGAGKSTMLKLLLGDLAPVRGI-----------RHAHRNLKIGYFSQHHVEQLDLNVSAVELL 357
Cdd:PRK15112 31 PLSFTLREGqtLAIIGENGSGKSTLAKMLAGMIEPTSGElliddhplhfgDYSYRSQRIRMIFQDPSTSLNPRQRISQIL 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 358 arKFPGR-------PEEEYR--HQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM 422
Cdd:PRK15112 111 --DFPLRlntdlepEQREKQiiETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
302-447 |
5.19e-03 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 39.01 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 302 VVGENGAGKSTMLKLLLGDLAPVRG----------IRHAHRNlKIGYFSQHH-------VEQldlNVsAVELLARKFPgR 364
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGsimldgedvtNVPPHLR-HINMVFQSYalfphmtVEE---NV-AFGLKMRKVP-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 365 PE--EEYRHQLGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF--RGGV- 439
Cdd:TIGR01187 75 AEikPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIqeQLGIt 153
|
....*....
gi 1189438346 440 -ILVSHDER 447
Cdd:TIGR01187 154 fVFVTHDQE 162
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
381-446 |
5.31e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 39.16 E-value: 5.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 381 ELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD------MET-IEALGRALN-NFrggvILVSHDE 446
Cdd:PRK09452 136 EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrkqMQNeLKALQRKLGiTF----VFVTHDQ 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
85-204 |
5.36e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 38.63 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 85 RASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA----ILWLENYLQTWPSTILVVS 160
Cdd:PRK13652 117 RVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGvkelIDFLNDLPETYGMTVIFST 195
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1189438346 161 HDRNFLNAIATDIIHLHSQRLDGYRGDFETFIkskQERLLNQQR 204
Cdd:PRK13652 196 HQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL---QPDLLARVH 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
108-138 |
5.45e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 39.26 E-value: 5.45e-03
10 20 30
....*....|....*....|....*....|.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
106-162 |
5.50e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 38.71 E-value: 5.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 106 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPSTILVVSHD 162
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHN 201
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
391-449 |
5.76e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.62 E-value: 5.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 391 SGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VILVSHDERFI 449
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkrsFIIVTHYQRIL 208
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
384-470 |
6.13e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.18 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 384 MRPLASLSGGQKSRVA----FA-QMTMPCPnFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFI----RLV 452
Cdd:pfam02463 1072 VKNLDLLSGGEKTLVAlaliFAiQKYKPAP-FYLLDEIDAALDDQNVSRVANLLKELSKNaqFIVISLREEMLekadKLV 1150
|
90
....*....|....*...
gi 1189438346 453 crelwvceggGVTRVEGG 470
Cdd:pfam02463 1151 ----------GVTMVENG 1158
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
390-449 |
6.16e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 6.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438346 390 LSGGQKSRVAFA-----QMTMPCPnFYILDEPTNHLDMETIEALGRALNNfrggvilVSHDERFI 449
Cdd:cd03272 159 LSGGQKSLVALAlifaiQKCDPAP-FYLFDEIDAALDAQYRTAVANMIKE-------LSDGAQFI 215
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
81-138 |
6.50e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 39.16 E-value: 6.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438346 81 KAPARASVILAGLGFTPKMQQQPTRE----FSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:TIGR00957 731 QQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
101-142 |
6.98e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 38.85 E-value: 6.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1189438346 101 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAI 142
Cdd:COG3845 397 DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAI 438
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
279-481 |
7.34e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 38.30 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 279 YYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLL------GDLA---------PVRGIRHAHRNL--KIGYFSQ 341
Cdd:cd03289 12 YTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQidgvswnsvPLQKWRKAFGVIpqKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 342 HHVEQLD----------LNVS---AVELLARKFPGrpeeeyrhQLGRYGISGELAmrplasLSGGQKSRVAFAQMTMPCP 408
Cdd:cd03289 92 TFRKNLDpygkwsdeeiWKVAeevGLKSVIEQFPG--------QLDFVLVDGGCV------LSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438346 409 NFYILDEPTNHLDMETIEALGRALNN-FRGGVILVSHDERFIRLVCRELWVCEGGGVTRveggFDQYRALLQEQ 481
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHRIEAMLECQRFLVIEENKVRQ----YDSIQKLLNEK 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
108-164 |
7.39e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 38.43 E-value: 7.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438346 108 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQ-TWPSTILVVSHDRN 164
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGkreIKKIMVDLRkTRKKTLISITHDMD 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
101-162 |
7.96e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 38.15 E-value: 7.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438346 101 QQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAILWLENylqTWPSTILVVSHD 162
Cdd:PRK13642 136 REPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrqeiMRVIHEIKE---KYQLTVLSITHD 200
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
386-445 |
8.34e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.68 E-value: 8.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438346 386 PLASLSGGQKSRVAFAQMTMpcpnfYILDepTNHLDMETIEALGRALNNFRggviLVSHD 445
Cdd:COG0419 155 PIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA----IITHV 203
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
105-140 |
8.72e-03 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 37.79 E-value: 8.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1189438346 105 REFSGGWRMRLALARAL-------FARPDLLLLDEPTNMLDVR 140
Cdd:COG4559 132 QTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLA 174
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
81-138 |
8.95e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 38.29 E-value: 8.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438346 81 KAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 138
Cdd:PRK13631 151 EAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| |
