|
Name |
Accession |
Description |
Interval |
E-value |
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
682-1082 |
0e+00 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 814.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 682 HQPSYTMYKMFDDMIILAKGGLTVYHGSVKKIEEYFADIGITVPDRVNPPDHYIDILEGIVKP--DGDITIEQLPVRWML 759
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEGIVKPstSSGVDYKQLPVRWML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 760 HNGYPVPHDMLKFCDGLPSSS-TGSAQEDSTH-----NSFSNDLWQDVKTNVEITKDQLQHNYSNSHDNSNRVTPTVGRQ 833
Cdd:pfam19055 81 HNGYPVPPDMLQNADGIAASSgENSSNGTNPGvgseeQSFAGELWQDVKSNVELKRDHIRHNFLKSKDLSNRRTPGVFRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 834 YRYFVGRVGKQRLREARLQALDFLILLVAGACLGTLAKVNDETIDTLGYTYTIIAVSLLCKISALRSFSVDKLQYWRESA 913
Cdd:pfam19055 161 YRYFLGRVGKQRLREARIQAVDYLILLLAGACLGTLAKVSDETFGALGYTYTIIAVSLLCKIAALRSFSLDKLQYWRESA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 914 AGISSLAHFMAKDTMDHLNTIMKPLVYLSMFYFFNNPRSSFEDNYIVLVCLVYCVTGMAYIFAILYSPSAAQLLSVLVPV 993
Cdd:pfam19055 241 SGMSSLAYFLAKDTIDHFNTVIKPLVYLSMFYFFNNPRSSFADNYIVLLCLVYCVTGIAYALAIFFEPGPAQLWSVLLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 994 VMTLIANQDKESMVLKYLGSFCYPKWTLEAFVLSNAQRYSGVWVVTRCSSLSQNGYDLSDWILCLIVLVLMGLICRFIAY 1073
Cdd:pfam19055 321 VLTLIATQTNDSKFLKVLANLCYPKWALEAFVIANAERYSGVWLITRCGALMKSGYDLHDWGLCLVILILYGVLSRIIAF 400
|
....*....
gi 1063705934 1074 FCMVTFQKK 1082
Cdd:pfam19055 401 FCMVTFQKK 409
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
482-708 |
1.44e-84 |
|
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: 271.73 E-value: 1.44e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVAFKDLTLTLKGK----HKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILINGRNDSINSYK 557
Cdd:cd03213 2 VTLSFRNLTVTVKSSpsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KITGFVPQDDVVHGNLTVEENLRFSARCrlsaymskadkvliiervieslglqhvrdslvgtiekRGISGGQRKRVNVGV 637
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFAAKL-------------------------------------RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 638 EMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMYKMFDDMIILAKGGlTVYHG 708
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGR-VIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
498-1076 |
3.47e-75 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 260.75 E-value: 3.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGK-ATGCTRTGLILINGRNDSINSYKKITGFVPQDDVVHGNLTVE 576
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRsPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 577 ENLRFSARCRLSAYMSKADKVLIIERVIESLGLQHVRDSLVGTI-EKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGL 655
Cdd:TIGR00955 118 EHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 656 DSASSQLLLRALRREALEGVNICMVVHQPSYTMYKMFDDMIILAKGGlTVYHGSVKKIEEYFADIGITVPDRVNPPDHYI 735
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGR-VAYLGSPDQAVPFFSDLGHPCPENYNPADFYV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 736 DILEGIvkpDGDitieQLPVRWMLHngypvphdmlKFCDGLPSSstgsaqedsthnSFSNDLWQDVKTNVEITKDQLQHN 815
Cdd:TIGR00955 277 QVLAVI---PGS----ENESRERIE----------KICDSFAVS------------DIGRDMLVNTNLWSGKAGGLVKDS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 816 YSNshdNSNRVTPTVGRQYRYFVGRVGKQRLREARLQALDFLILLVAGACLGTL--AKVNDE--TIDTLGYTYTIIA-VS 890
Cdd:TIGR00955 328 ENM---EGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIylGQGLTQkgVQNINGALFLFLTnMT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 891 LLCKISALRSFSVDKLQYWRESAAGISSL-AHFMAKDTMDHLNTIMKPLVYLSMFYFFNNPRSSFeDNYIVLVCLVYCVT 969
Cdd:TIGR00955 405 FQNVFPVINVFTAELPVFLRETRSGLYRVsAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGA-THFLTFLFLVTLVA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 970 GMAYIFAILYS---PSAAQLLSVLVPVVMTLIA------NQDKESMVLKYLGSFCYPKWTLEAFVLSnaqRYSGVWVV-- 1038
Cdd:TIGR00955 484 NVATSFGYLIScafSSTSMALTVGPPFVIPFLLfggffiNSDSIPVYFKWLSYLSWFRYGNEGLLIN---QWSDVDNIec 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1063705934 1039 TRCSS-----------LSQNGYDLSDWILCLIVLVLMGLICRFIAYFCM 1076
Cdd:TIGR00955 561 TSANTtgpcpssgeviLETLSFRNADLYLDLIGLVILIFFFRLLAYFAL 609
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
496-1076 |
5.61e-58 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 212.43 E-value: 5.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 496 KHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILINGRNDSINSYKKiTGFVPQDDVVHGNLTV 575
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKR-TGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EENLRFSARCRLSAYMSKADKVLIIERVIESLGLQHVRDSLVGTIEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGL 655
Cdd:PLN03211 158 RETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 656 DSASSQLLLRALRREALEGVNICMVVHQPSYTMYKMFDDMIILAKGGlTVYHGSVKKIEEYFADIGITVPDRVNPPDHYI 735
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR-CLFFGKGSDAMAYFESVGFSPSFPMNPADFLL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 736 DILEGIVKPDGDITIEQLPVRWMLHNGYpvphdmlkfcDGLPSSSTGSAQEdsthnsfsndlwqdVKTNVEITKDQLQHN 815
Cdd:PLN03211 317 DLANGVCQTDGVSEREKPNVKQSLVASY----------NTLLAPKVKAAIE--------------MSHFPQANARFVGSA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 816 YSNSHDNSNRVT-PTVGRQYRYFVGRVGKQRLREArLQALDFLILLVAGACLGTLAKVND--ETIDTLGYTYTI-IAVSL 891
Cdd:PLN03211 373 STKEHRSSDRISiSTWFNQFSILLQRSLKERKHES-FNTLRVFQVIAAALLAGLMWWHSDfrDVQDRLGLLFFIsIFWGV 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 892 LCKISALRSFSVDKLQYWRESAAGISSL-AHFMAKDTMDHLNTIMKPLVYLSMFYFFNNPRSSFEDNYIVLVCLVYCV-- 968
Cdd:PLN03211 452 FPSFNSVFVFPQERAIFVKERASGMYTLsSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVlv 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 969 ---TGMAYIFAILYSPSAAQLLSV-LVPVVMT--LIANQDKESMV-LKYLGS--FCYPkwtleafVLSNAQRYSGVWVVT 1039
Cdd:PLN03211 532 sqgLGLALGAAIMDAKKASTIVTVtMLAFVLTggFYVHKLPSCMAwIKYISTtfYSYR-------LLINVQYGEGKRISS 604
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 1040 R--CSSLSQN------------GYDLSDWIlCLIVLVLMGLICRFIAYFCM 1076
Cdd:PLN03211 605 LlgCSLPHGSdrasckfveedvAGQISPAT-SVSVLIFMFVGYRLLAYLAL 654
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
494-708 |
7.09e-58 |
|
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: 199.03 E-value: 7.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 494 KGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRT-GLILINGRNDSINSYKKITGFVPQDDVVHGN 572
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTsGQILFNGQPRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 573 LTVEENLRFSARCRLSAYMSKADKVLIIERVIES-LGLQHVRDSLVgtiekRGISGGQRKRVNVGVEMVMEPSLLILDEP 651
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRdLALTRIGGNLV-----KGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705934 652 TTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMYKMFDDMIILAKGGLtVYHG 708
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI-VYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
486-708 |
4.99e-56 |
|
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: 192.46 E-value: 4.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTL--KGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILINGRNDSINsYKKITGFV 563
Cdd:cd03232 6 WKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDKN-FQRSTGYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 564 PQDDVVHGNLTVEENLRFSARCRlsaymskadkvliiervieslglqhvrdslvgtiekrGISGGQRKRVNVGVEMVMEP 643
Cdd:cd03232 85 EQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705934 644 SLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMYKMFDDMIILAKGGLTVYHG 708
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
487-730 |
6.40e-52 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 199.95 E-value: 6.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLT--LKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKAT-GCTRTGLILINGRN-DSinSYKKITGF 562
Cdd:TIGR00956 763 RNLTYEvkIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtGVITGGDRLVNGRPlDS--SFQRSIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 563 VPQDDVVHGNLTVEENLRFSARCRLSAYMSKADKVLIIERVIESLGLQHVRDSLVGTIEKrGISGGQRKRVNVGVEMVME 642
Cdd:TIGR00956 841 VQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGE-GLNVEQRKRLTIGVELVAK 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 643 PSLLI-LDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMYKMFDDMIILAKGGLTVYHGSV----KKIEEYF 717
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLgensHTIINYF 999
|
250
....*....|....
gi 1063705934 718 ADIGIT-VPDRVNP 730
Cdd:TIGR00956 1000 EKHGAPkCPEDANP 1013
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
482-720 |
5.41e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 165.24 E-value: 5.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN--DSINSYK 557
Cdd:COG1131 1 IEV--RGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllRPTS----GEVRVLGEDvaRDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KITGFVPQDDVVHGNLTVEENLRFSARcrlsAY-MSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVG 636
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFAR----LYgLPRKEARERIDELLELFGLTDAADRKVGTL-----SGGMKQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 637 VEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSyTMYKMFDDMIILAKGGLtVYHGSVKKI--- 713
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLE-EAERLCDRVAIIDKGRI-VADGTPDELkar 221
|
....*....
gi 1063705934 714 --EEYFADI 720
Cdd:COG1131 222 llEDVFLEL 230
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
500-730 |
4.46e-45 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 178.12 E-value: 4.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILINGRNDSINSYKKITGFVPQDDVVHGNLTVEENL 579
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 580 RFSARCRLSAYMSKADKVLIIERVIESLGLQHVRDSLVGTIEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSAS 659
Cdd:PLN03140 975 IYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705934 660 SQLLLRALRREALEGVNICMVVHQPSYTMYKMFDDMIILAKGGLTVYHGSV----KKIEEYFADI-GI-TVPDRVNP 730
Cdd:PLN03140 1055 AAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLgrnsHKIIEYFEAIpGVpKIKEKYNP 1131
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
491-715 |
1.59e-37 |
|
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: 141.15 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSINSY---KKItGFVPQ 565
Cdd:COG4555 7 LSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllKPD----SGSILIDGEDVRKEPRearRQI-GVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 566 DDVVHGNLTVEENLRFSARCRLsayMSKADKVLIIERVIESLGLQHVRDSLVGtiekrGISGGQRKRVNVGVEMVMEPSL 645
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 646 LILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPsYTMYKMFDDMIILAKGGLtVYHGSVKKIEE 715
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKV-VAQGSLDELRE 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
483-732 |
5.80e-37 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 151.80 E-value: 5.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTR--TGLILING--RNDSINSYKK 558
Cdd:TIGR00956 59 TRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIgvEGVITYDGitPEEIKKHYRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 559 ITGFVPQDDVVHGNLTVEENLRFSARCRlsaymSKADKVLIIER----------VIESLGLQHVRDSLVGTIEKRGISGG 628
Cdd:TIGR00956 139 DVVYNAETDVHFPHLTVGETLDFAARCK-----TPQNRPDGVSReeyakhiadvYMATYGLSHTRNTKVGNDFVRGVSGG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 629 QRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRrealEGVNIC-----MVVHQPSYTMYKMFDDMIILAKgGL 703
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALK----TSANILdttplVAIYQCSQDAYELFDKVIVLYE-GY 288
|
250 260
....*....|....*....|....*....
gi 1063705934 704 TVYHGSVKKIEEYFADIGITVPDRVNPPD 732
Cdd:TIGR00956 289 QIYFGPADKAKQYFEKMGFKCPDRQTTAD 317
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
476-717 |
1.72e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 138.30 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 476 MRTRPVIEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSi 553
Cdd:COG1121 1 MMMMPAIEL--ENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGllPPT----SGTVRLFGKPPR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 554 NSYKKItGFVPQDDVVHGN--LTVEE--NLRFSARCRLSAYMSKADKvLIIERVIESLGLQHVRDSLVGTiekrgISGGQ 629
Cdd:COG1121 72 RARRRI-GYVPQRAEVDWDfpITVRDvvLMGRYGRRGLFRRPSRADR-EAVDEALERVGLEDLADRPIGE-----LSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 630 RKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSyTMYKMFDDMIILAKGglTVYHGS 709
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLNRG--LVAHGP 221
|
....*...
gi 1063705934 710 VkkiEEYF 717
Cdd:COG1121 222 P---EEVL 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
491-708 |
1.14e-35 |
|
First domain of the pleiotropic drug resistance-like 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: 213200 [Multi-domain] Cd Length: 202 Bit Score: 134.31 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKH-ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTR-TGLILINGRN--DSINSYKKITGFVPQD 566
Cdd:cd03233 12 TTGKGRSKIpILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSvEGDIHYNGIPykEFAEKYPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 567 DVVHGNLTVEENLRFSARCRLSAYMskadkvliiervieslglqhvrdslvgtiekRGISGGQRKRVNVGVEMVMEPSLL 646
Cdd:cd03233 92 DVHFPTLTVRETLDFALRCKGNEFV-------------------------------RGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705934 647 ILDEPTTGLDSASSQLLLRALRR--EALEGVNIcMVVHQPSYTMYKMFDDMIILAKGGLtVYHG 708
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTmaDVLKTTTF-VSLYQASDEIYDLFDKVLVLYEGRQ-IYYG 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
486-701 |
1.27e-33 |
|
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: 128.74 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRN---DSINSYKKIT 560
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGllGPT----SGEVLVDGKDltkLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 561 GFV---PQDDVVhgNLTVEENLRFSARcrlSAYMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGV 637
Cdd:cd03225 78 GLVfqnPDDQFF--GPTVEEEVAFGLE---NLGLPEEEIEERVEEALELVGLEGLRDRSPFTL-----SGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705934 638 EMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYtMYKMFDDMIILAKG 701
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL-LLELADRVIVLEDG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
487-670 |
2.01e-33 |
|
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: 128.78 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRND--SINSYKKITGF 562
Cdd:cd03263 4 RNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGelRPT----SGTAYINGYSIrtDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 563 VPQDDVVHGNLTVEENLRFSarCRLSAYmSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVME 642
Cdd:cd03263 80 CPQFDALFDELTVREHLRFY--ARLKGL-PKSEIKEEVELLLRVLGLTDKANKRARTL-----SGGMKRKLSLAIALIGG 151
|
170 180
....*....|....*....|....*...
gi 1063705934 643 PSLLILDEPTTGLDSASSQLLLRALRRE 670
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEV 179
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
487-713 |
6.32e-33 |
|
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: 128.24 E-value: 6.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNdsINSYK-----KI 559
Cdd:COG1120 5 ENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGllKPSS----GEVLLDGRD--LASLSrrelaRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 TGFVPQDDVVHGNLTVEENL---RFSARCRLSAyMSKADKVlIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVG 636
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELValgRYPHLGLFGR-PSAEDRE-AVEEALERTGLEHLADRPVDEL-----SGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 637 veMVM--EPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHQPS----YtmykmFDDMIILAKGGLtVYHGS 709
Cdd:COG1120 150 --RALaqEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlaarY-----ADRLVLLKDGRI-VAQGP 221
|
....
gi 1063705934 710 VKKI 713
Cdd:COG1120 222 PEEV 225
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
500-727 |
1.88e-32 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 137.28 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTR-TGLILINGRNdsINSY--KKITGFVPQDDVVHGNLTVE 576
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKvSGEITYNGYR--LNEFvpRKTSAYISQNDVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 577 ENLRFSARCR--------LSAY-----------------------MSKADKVLIIERVIESLGLQHVRDSLVGTIEKRGI 625
Cdd:PLN03140 258 ETLDFSARCQgvgtrydlLSELarrekdagifpeaevdlfmkataMEGVKSSLITDYTLKILGLDICKDTIVGDEMIRGI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 626 SGGQRKRVNVGvEMVMEPS-LLILDEPTTGLDSASSQLLLRALRREA-LEGVNICMVVHQPSYTMYKMFDDMIILAKGGL 703
Cdd:PLN03140 338 SGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVhLTEATVLMSLLQPAPETFDLFDDIILLSEGQI 416
|
250 260
....*....|....*....|....
gi 1063705934 704 tVYHGSVKKIEEYFADIGITVPDR 727
Cdd:PLN03140 417 -VYQGPRDHILEFFESCGFKCPER 439
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
484-719 |
5.21e-32 |
|
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: 124.75 E-value: 5.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSINSYKKI-- 559
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKPT----SGEVLVDGKDITKKNLRELrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 -TGFVPQD-D--VVhgNLTVEENLRFSARcRLSayMSKADkvlIIERVIESL---GLQHVRD----SLvgtiekrgiSGG 628
Cdd:COG1122 76 kVGLVFQNpDdqLF--APTVEEDVAFGPE-NLG--LPREE---IRERVEEALelvGLEHLADrpphEL---------SGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 629 QRKRVNV-GVeMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYtMYKMFDDMIILAKGGLtVYH 707
Cdd:COG1122 139 QKQRVAIaGV-LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRI-VAD 215
|
250
....*....|..
gi 1063705934 708 GSVkkiEEYFAD 719
Cdd:COG1122 216 GTP---REVFSD 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
501-653 |
8.49e-32 |
|
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: 121.60 E-value: 8.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGctRTGLILINGR---NDSINSYKKITGFVPQDDVVHGNLTVEE 577
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP--TEGTILLDGQdltDDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 578 NLRFSARCRlsAYMSKADKVlIIERVIESLGLQHVRDSLVGTIEKrGISGGQRKRVNVGVEMVMEPSLLILDEPTT 653
Cdd:pfam00005 79 NLRLGLLLK--GLSKREKDA-RAEEALEKLGLGDLADRPVGERPG-TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
486-684 |
1.58e-31 |
|
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: 122.59 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKgkhkhilrsvtgkimPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN--DSINSYKKITG 561
Cdd:COG4133 18 FSGLSFTLA---------------AGEALALTGPNGSGKTTLLRILAGllPPSA----GEVLWNGEPirDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 562 FVPQDDVVHGNLTVEENLRFSARCRlSAYMSKADkvliIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVM 641
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALY-GLRADREA----IDEALEAVGLAGLADLPVRQL-----SAGQKRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063705934 642 EPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQP 684
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
486-708 |
1.78e-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: 122.64 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSiNSYKKItGFV 563
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllKPT----SGSIRVFGKPLE-KERKRI-GYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 564 PQDDVVHGN--LTVEE--NLRFSARCRLSAYMSKADKVLIIErVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEM 639
Cdd:cd03235 74 PQRRSIDRDfpISVRDvvLMGLYGHKGLFRRLSKADKAKVDE-ALERVGLSELADRQIGEL-----SGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705934 640 VMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMYKmFDDMIILAKGGltVYHG 708
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEY-FDRVLLLNRTV--VASG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
480-704 |
4.92e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.99 E-value: 4.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 480 PVIEVafKDLTLTLK-GKHK-HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILING------- 548
Cdd:COG1136 3 PLLEL--RNLTKSYGtGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGldRPT----SGEVLIDGqdissls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 549 -------RNDSInsykkitGFVPQDdvvH---GNLTVEENLRFSARCrlsAYMSKADKVLIIERVIESLGLQHVRDSLVG 618
Cdd:COG1136 77 erelarlRRRHI-------GFVFQF---FnllPELTALENVALPLLL---AGVSRKERRERARELLERVGLGDRLDHRPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 619 TiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHQPSytMYKMFDDMII 697
Cdd:COG1136 144 Q-----LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE--LAARADRVIR 216
|
....*..
gi 1063705934 698 LAKGGLT 704
Cdd:COG1136 217 LRDGRIV 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
482-703 |
1.71e-29 |
|
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: 115.57 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN--DSINSYK 557
Cdd:cd03230 1 IEV--RNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGllKPDS----GEIKVLGKDikKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KITGFVPQDDVVHGNLTVEENLRFsarcrlsaymskadkvliiervieslglqhvrdslvgtiekrgiSGGQRKRVNVGV 637
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENLKL--------------------------------------------SGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 638 EMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSyTMYKMFDDMIILAKGGL 703
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGRI 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
491-708 |
5.42e-29 |
|
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: 115.37 E-value: 5.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGrVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSIN--SYKKITGFVPQDDV 568
Cdd:cd03264 6 LTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP--PSSGTIRIDGQDVLKQpqKLRRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 569 VHGNLTVEENLRFSARcrLSAYMSK-ADKvlIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLI 647
Cdd:cd03264 83 VYPNFTVREFLDYIAW--LKGIPSKeVKA--RVDEVLELVNLGDRAKKKIGSL-----SGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 648 LDEPTTGLDSAsSQLLLRALRREALEGVNICMVVHQPSYTMYkMFDDMIILAKGGLtVYHG 708
Cdd:cd03264 154 VDEPTAGLDPE-ERIRFRNLLSELGEDRIVILSTHIVEDVES-LCNQVAVLNKGKL-VFEG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
499-682 |
2.14e-28 |
|
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: 114.46 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 499 HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNdsinsykkITGFVPQDDVVHG----- 571
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGflRPTS----GSVLFDGED--------ITGLPPHEIARLGigrtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 572 -------NLTVEENLRFSARCR-----LSAYMSKADKVLI--IERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGV 637
Cdd:cd03219 82 qiprlfpELTVLENVMVAAQARtgsglLLARARREEREARerAEELLERVGLADLADRPAGEL-----SYGQQRRLEIAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063705934 638 EMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH 201
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
482-713 |
5.83e-28 |
|
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: 113.37 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN-------DS 552
Cdd:cd03261 1 IEL--RGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGllRPDS----GEVLIDGEDisglseaEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 553 INSYKKItGFVPQDDVVHGNLTVEENLRFSARcrlsaYMSKADKVLIIERVIESL---GLQHVRDSLVGTIekrgiSGGQ 629
Cdd:cd03261 73 YRLRRRM-GMLFQSGALFDSLTVFENVAFPLR-----EHTRLSEEEIREIVLEKLeavGLRGAEDLYPAEL-----SGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 630 RKRVNVGVEMVMEPSLLILDEPTTGLDSASS---QLLLRALRREalEGVNICMVVHQPSyTMYKMFDDMIILAKGGLtVY 706
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASgviDDLIRSLKKE--LGLTSIMVTHDLD-TAFAIADRIAVLYDGKI-VA 217
|
....*..
gi 1063705934 707 HGSVKKI 713
Cdd:cd03261 218 EGTPEEL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
479-713 |
9.98e-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: 118.85 E-value: 9.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 479 RPVIEVafKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKA-TGCTRTGLILINGRN---DSIN 554
Cdd:COG1123 2 TPLLEV--RDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLpHGGRISGEVLLDGRDlleLSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 555 SYKKITGFVPQDDVVHGN-LTVEENLRFSARCRLsayMSKADkvlIIERVIESL---GLQHVRDSLVGTIekrgiSGGQR 630
Cdd:COG1123 80 LRGRRIGMVFQDPMTQLNpVTVGDQIAEALENLG---LSRAE---ARARVLELLeavGLERRLDRYPHQL-----SGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 631 KRVNVGVEMVMEPSLLILDEPTTGLDSASSQL---LLRALRREalEGVNICMVVHQPSYTMYkmFDDMIILAKGGLTVYH 707
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEildLLRELQRE--RGTTVLLITHDLGVVAE--IADRVVVMDDGRIVED 224
|
....*.
gi 1063705934 708 GSVKKI 713
Cdd:COG1123 225 GPPEEI 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
478-715 |
6.52e-27 |
|
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: 110.45 E-value: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 478 TRPVIEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNdsINS 555
Cdd:COG1127 2 SEPMIEV--RNLTKSFGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRPD----SGEILVDGQD--ITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 556 Y---------KKItGFVPQddvvHG----NLTVEENLRFSARCRLSayMSKAdkvLIIERVIESL---GLQHVRDSLVGt 619
Cdd:COG1127 72 LsekelyelrRRI-GMLFQ----GGalfdSLTVFENVAFPLREHTD--LSEA---EIRELVLEKLelvGLPGAADKMPS- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 620 iEkrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQL---LLRALRREAleGVNICMVVHQPSyTMYKMFDDMI 696
Cdd:COG1127 141 -E---LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVideLIRELRDEL--GLTSVVVTHDLD-SAFAIADRVA 213
|
250
....*....|....*....
gi 1063705934 697 ILAKGGLtVYHGSVKKIEE 715
Cdd:COG1127 214 VLADGKI-IAEGTPEELLA 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
499-680 |
7.09e-27 |
|
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: 109.83 E-value: 7.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 499 HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN-DSINSYKKIT---GFVPQDDVVHGNLT 574
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP--PRSGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 575 VEENLRFSARCRlsaymSKADKVLIIERVIESL-GLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTT 653
Cdd:cd03224 92 VEENLLLGAYAR-----RRAKRKARLERVYELFpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180
....*....|....*....|....*..
gi 1063705934 654 GLDSASSQLLLRALRREALEGVNICMV 680
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEGVTILLV 188
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
486-701 |
8.57e-27 |
|
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: 109.15 E-value: 8.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN-DSINSYKKITGF 562
Cdd:cd03259 3 LKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDS----GEILIDGRDvTGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 563 VPQDDVVHGNLTVEENLRFSARCRLsayMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVME 642
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRG---VPKAEIRARVRELLELVGLEGLLNRYPHEL-----SGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 643 PSLLILDEPTTGLDSASSQLL---LRALRREAleGVNICMVVHQPSYTMyKMFDDMIILAKG 701
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELreeLKELQREL--GITTIYVTHDQEEAL-ALADRIAVMNEG 207
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
487-706 |
1.10e-26 |
|
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: 107.91 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTrtGLILINGRNdsINSYK-----KITG 561
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS--GEILLDGKD--LASLSpkelaRKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 562 FVPQddvvhgnltveenlrfsarcrlsaymskadkvliierVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVM 641
Cdd:cd03214 77 YVPQ-------------------------------------ALELLGLAHLADRPFNEL-----SGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 642 EPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHQPSYTmYKMFDDMIILAKGGLTVY 706
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLA-ARYADRVILLKDGRIVAQ 179
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
484-685 |
1.22e-26 |
|
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: 109.12 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLK--GKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSINSYKKI 559
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldRPT----SGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 T-------GFVPQDDVVHGNLTVEENLRFSarCRLSAyMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKR 632
Cdd:cd03255 77 AafrrrhiGFVFQSFNLLPDLTALENVELP--LLLAG-VPKKERRERAEELLERVGLGDRLNHYPSEL-----SGGQQQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063705934 633 VNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREA-LEGVNICMVVHQPS 685
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
487-670 |
1.29e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 108.72 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG-KATGCTRTGLILINGRN-DSINSYKKITGFVP 564
Cdd:COG4136 5 ENLTITLGGRP--LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAFSASGEVLLNGRRlTALPAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 565 QDDVVHGNLTVEENLRFSarcrLSAYMSKADKVLIIERVIESLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPS 644
Cdd:COG4136 83 QDDLLFPHLSVGENLAFA----LPPTIGRAQRRARVEQALEEAGLAGFADRDPAT-----LSGGQRARVALLRALLAEPR 153
|
170 180
....*....|....*....|....*.
gi 1063705934 645 LLILDEPTTGLDSAssqllLRALRRE 670
Cdd:COG4136 154 ALLLDEPFSKLDAA-----LRAQFRE 174
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
491-703 |
7.56e-26 |
|
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: 106.53 E-value: 7.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN--DSINSYKKI------T 560
Cdd:cd03268 6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGliKPDS----GEITFDGKSyqKNIEALRRIgalieaP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 561 GFVPqddvvhgNLTVEENLRFSARcrlsaYMSKADKvlIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMV 640
Cdd:cd03268 82 GFYP-------NLTARENLRLLAR-----LLGIRKK--RIDEVLDVVGLKDSAKKKVKGF-----SLGMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705934 641 MEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSyTMYKMFDDMIILAKGGL 703
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKL 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
484-701 |
9.13e-26 |
|
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: 104.77 E-value: 9.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILING---RNDSINSYKK 558
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlyDPT----SGEILIDGvdlRDLDLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 559 ITGFVPQDDVVHgNLTVEENLrfsarcrlsaymskadkvliiervieslglqhvrdslvgtiekrgISGGQRKRVNVGVE 638
Cdd:cd03228 77 NIAYVPQDPFLF-SGTIRENI---------------------------------------------LSGGQRQRIAIARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705934 639 MVMEPSLLILDEPTTGLDSASSQLLLRALRReALEGVNICMVVHQPSytMYKMFDDMIILAKG 701
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRA-LAKGKTVIVIAHRLS--TIRDADRIIVLDDG 170
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
499-682 |
9.68e-26 |
|
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: 107.43 E-value: 9.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 499 HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNdsinsykkITGfVPQDDVVH------ 570
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGfyRPTS----GRILFDGRD--------ITG-LPPHRIARlgiart 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 571 -------GNLTVEENLRFSARCRLSAYMSKADKVL------------IIERVIESLGLQHVRDSLVGTiekrgISGGQRK 631
Cdd:COG0411 85 fqnprlfPELTVLENVLVAAHARLGRGLLAALLRLprarreereareRAEELLERVGLADRADEPAGN-----LSYGQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063705934 632 RVNVGVEMVMEPSLLILDEPTTGLDSASSQLL---LRALRREalEGVNICMVVH 682
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELaelIRRLRDE--RGITILLIEH 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
498-682 |
1.93e-25 |
|
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: 105.73 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG---KATGCTRTGLILINGRN-----DSINSYKKITGFVPQD-DV 568
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndLIPGAPDEGEVLLDGKDiydldVDVLELRRRVGMVFQKpNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 569 VHGnlTVEENLRFSARCRLSAYMSKADKvlIIERVIESLGL-QHVRDSLVGtiekRGISGGQRKRVNVGVEMVMEPSLLI 647
Cdd:cd03260 93 FPG--SIYDNVAYGLRLHGIKLKEELDE--RVEEALRKAALwDEVKDRLHA----LGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063705934 648 LDEPTTGLDSASSQ---LLLRALRREalegVNICMVVH 682
Cdd:cd03260 165 LDEPTSALDPISTAkieELIAELKKE----YTIVIVTH 198
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
501-684 |
2.23e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.62 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATG--CTRTGLILIngrndsinsykkitGFVPQ----DDVVhgN 572
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvlRPTSgtVRRAGGARV--------------AYVPQrsevPDSL--P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 573 LTVEENLRFS--ARCRLSAYMSKADKvLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDE 650
Cdd:NF040873 72 LTVRDLVAMGrwARRGLWRRLTRDDR-AAVDDALERVGLADLAGRQLGEL-----SGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|....
gi 1063705934 651 PTTGLDSASSQLLLRALRREALEGVNICMVVHQP 684
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
498-701 |
3.10e-25 |
|
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: 104.67 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSINSYKKItGFVPQDDVVHGNLTV 575
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiiLPD----SGEVLFDGKPLDIAARNRI-GYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EENLRFSARCRlsaYMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGL 655
Cdd:cd03269 88 IDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRVEEL-----SKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063705934 656 DSASSQLLLRALRREALEGVNICMVVHQPSyTMYKMFDDMIILAKG 701
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQME-LVEELCDRVLLLNKG 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
487-704 |
6.21e-25 |
|
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: 103.49 E-value: 6.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLTLKGKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSYKKITGFVP 564
Cdd:cd03226 3 ENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGliKESS----GSILLNGKPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 565 QDdvVHGNL---TVEENLRFSARcRLSAYMSKADKVLiierviESLGL-----QHVRDslvgtiekrgISGGQRKRVNVG 636
Cdd:cd03226 78 QD--VDYQLftdSVREELLLGLK-ELDAGNEQAETVL------KDLDLyalkeRHPLS----------LSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705934 637 VEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYtMYKMFDDMIILAKGGLT 704
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGAIV 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
486-701 |
7.06e-25 |
|
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: 101.94 E-value: 7.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINS---YKKITGF 562
Cdd:cd00267 2 IENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDIAKLPleeLRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 563 VPQddvvhgnltveenlrfsarcrlsaymskadkvliiervieslglqhvrdslvgtiekrgISGGQRKRVNVGVEMVME 642
Cdd:cd00267 78 VPQ-----------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705934 643 PSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMYKmFDDMIILAKG 701
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELA-ADRVIVLKDG 156
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
482-685 |
8.81e-25 |
|
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: 110.23 E-value: 8.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVAFKDLTLTLkGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGctRTGLILING---RNDSINSYKK 558
Cdd:COG4988 335 PSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP--YSGSILINGvdlSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 559 ITGFVPQDDVV-HGnlTVEENLRFSARCrlsayMSKADkvliIERVIESLGLQHVRDSL-------VGtiEK-RGISGGQ 629
Cdd:COG4988 412 QIAWVPQNPYLfAG--TIRENLRLGRPD-----ASDEE----LEAALEAAGLDEFVAALpdgldtpLG--EGgRGLSGGQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 630 RKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRReALEGVNICMVVHQPS 685
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLA 533
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
484-701 |
1.40e-24 |
|
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: 103.46 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGkHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALagkatgcTR-----TGLILING---RNDSINS 555
Cdd:cd03253 1 IEFENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL-------FRfydvsSGSILIDGqdiREVTLDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 556 YKKITGFVPQDDVVHgNLTVEENLRFSarcRLSAY---MSKADKVLIIERVIESLGLQHvrDSLVGtieKRG--ISGGQR 630
Cdd:cd03253 73 LRRAIGVVPQDTVLF-NDTIGYNIRYG---RPDATdeeVIEAAKAAQIHDKIMRFPDGY--DTIVG---ERGlkLSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 631 KRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRReALEGVNICMVVHQPSYTMYKmfDDMIILAKG 701
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRD-VSKGRTTIVIAHRLSTIVNA--DKIIVLKDG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
510-703 |
2.04e-24 |
|
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: 102.37 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 510 PGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGR--NDS-----INSYKKITGFVPQDDVVHGNLTVEENLR 580
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPDG----GTIVLNGTvlFDSrkkinLPPQQRKIGLVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 581 FSARcrlsaymSKADKVLII--ERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSA 658
Cdd:cd03297 98 FGLK-------RKRNREDRIsvDELLDLLGLDHLLNRYPAQL-----SGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063705934 659 SSQLLLRALrREALEGVNICM--VVHQPSyTMYKMFDDMIILAKGGL 703
Cdd:cd03297 166 LRLQLLPEL-KQIKKNLNIPVifVTHDLS-EAEYLADRIVVMEDGRL 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
484-682 |
2.93e-24 |
|
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: 102.16 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLT--LKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRndSINSYKKI 559
Cdd:cd03293 1 LEVRNVSKTygGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGleRPTS----GEVLVDGE--PVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 TGFVPQDDVVHGNLTVEENLRFSARCRLsayMSKADKVLIIERVIESLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEM 639
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVGLSGFENAYPHQ-----LSGGMRQRVALARAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063705934 640 VMEPSLLILDEPTTGLDS---ASSQLLLRALRREalEGVNICMVVH 682
Cdd:cd03293 147 AVDPDVLLLDEPFSALDAltrEQLQEELLDIWRE--TGKTVLLVTH 190
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
484-682 |
3.82e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.05 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSINSYKKI-- 559
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeeRPT----SGQVLVNGQDLSRLKRREIpy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 ----TGFVPQDdvvHG---NLTVEENLRFSARCrlsAYMSKADkvlIIERVIESL---GLQHVRDSLVGTiekrgISGGQ 629
Cdd:COG2884 77 lrrrIGVVFQD---FRllpDRTVYENVALPLRV---TGKSRKE---IRRRVREVLdlvGLSDKAKALPHE-----LSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063705934 630 RKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
476-682 |
4.43e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.86 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 476 MRTRPVIeVAFKDLTLT--LKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRnd 551
Cdd:COG1116 1 MSAAAPA-LELRGVSKRfpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGleKPTS----GEVLVDGK-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 552 SINSYKKITGFVPQDDVVHGNLTVEENLRFSARCRlsaYMSKADKVLIIERVIESLGLQHVRDSLVGTiekrgISGGQRK 631
Cdd:COG1116 74 PVTGPGPDRGVVFQEPALLPWLTVLDNVALGLELR---GVPKAERRERARELLELVGLAGFEDAYPHQ-----LSGGMRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063705934 632 RVNVGVEMVMEPSLLILDEPTTGLDS---ASSQLLLRALRREalEGVNICMVVH 682
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDAltrERLQDELLRLWQE--TGKTVLFVTH 197
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
496-701 |
8.14e-24 |
|
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: 99.57 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 496 KHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNdsINSYKKI-------TGFVPQDDV 568
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE--PDSGSILIDGED--LTDLEDElpplrrrIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 569 VHGNLTVEENLRFsarcrlsaymskadkvliiervieslglqhvrdslvgtiekrGISGGQRKRVNVGVEMVMEPSLLIL 648
Cdd:cd03229 87 LFPHLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 649 DEPTTGLDSASS---QLLLRALRREalEGVNICMVVHQPSYTMYkMFDDMIILAKG 701
Cdd:cd03229 125 DEPTSALDPITRrevRALLKSLQAQ--LGITVVLVTHDLDEAAR-LADRVVVLRDG 177
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
491-703 |
8.99e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 100.28 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTrtGLILINGRN-DSIN--SYKKITGFVPQDD 567
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS--GEIYLDGKPlSAMPppEWRRQVAYVPQEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 568 VVHGNlTVEENLRFSARCRLSAY-MSKADKVLiierviESLGLQHvrDSLVGTIEKrgISGGQRKRVNVGVEMVMEPSLL 646
Cdd:COG4619 84 ALWGG-TVRDNLPFPFQLRERKFdRERALELL------ERLGLPP--DILDKPVER--LSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 647 ILDEPTTGLDSASSQL---LLRALRREalEGVNICMVVHQPSYTMyKMFDDMIILAKGGL 703
Cdd:COG4619 153 LLDEPTSALDPENTRRveeLLREYLAE--EGRAVLWVSHDPEQIE-RVADRVLTLEAGRL 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
483-709 |
1.51e-23 |
|
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: 107.23 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILING---RNDSINSYK 557
Cdd:COG2274 473 DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlyEPT----SGRILIDGidlRQIDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KITGFVPQDDVV-HGnlTVEENLRFSAR----------CRLSAymskadkvliIERVIESL--GLqhvrDSLVGtiEK-R 623
Cdd:COG2274 549 RQIGVVLQDVFLfSG--TIRENITLGDPdatdeeiieaARLAG----------LHDFIEALpmGY----DTVVG--EGgS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 624 GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRReALEGVNICMVVHQPSyTMyKMFDDMIILAKGGL 703
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRR-LLKGRTVIIIAHRLS-TI-RLADRIIVLDKGRI 687
|
....*.
gi 1063705934 704 tVYHGS 709
Cdd:COG2274 688 -VEDGT 692
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
501-682 |
4.74e-23 |
|
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: 98.60 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILING---RNDSINSYKKItGFVPQDDVVHGNLTV 575
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllKPTS----GRATVAGhdvVREPREVRRRI-GIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EENLRFSARcrLSAYM-SKADKVliIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTG 654
Cdd:cd03265 91 WENLYIHAR--LYGVPgAERRER--IDELLDFVGLLEAADRLVKTY-----SGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190
....*....|....*....|....*....|.
gi 1063705934 655 LDSASSQLL---LRALRREalEGVNICMVVH 682
Cdd:cd03265 162 LDPQTRAHVweyIEKLKEE--FGMTILLTTH 190
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
493-708 |
9.83e-23 |
|
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: 97.82 E-value: 9.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 493 LKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSINSY--KKITGFVPQDDV 568
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllEPD----AGFATVDGFDVVKEPAeaRRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 569 VHGNLTVEENLRFSARCrlsaYMSKADKVLI-IERVIESLGLQHVRDSLVGtiekrGISGGQRKRVNVGVEMVMEPSLLI 647
Cdd:cd03266 89 LYDRLTARENLEYFAGL----YGLKGDELTArLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 648 LDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSyTMYKMFDDMIILAKgGLTVYHG 708
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHR-GRVVYEG 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
486-719 |
1.59e-22 |
|
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: 97.64 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKhKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGctRTGLILING------RNDSINSYKKI 559
Cdd:cd03256 3 VENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP--TSGSVLIDGtdinklKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 TGFVPQDDVVHGNLTVEENLRFSARCRLSAY------MSKADKVL---IIERV-IESLGLQHVrDSLvgtiekrgiSGGQ 629
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRSTWrslfglFPKEEKQRalaALERVgLLDKAYQRA-DQL---------SGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 630 RKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHQPSYTMyKMFDDMIILAKGGLtVYHG 708
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAR-EYADRIVGLKDGRI-VFDG 227
|
250
....*....|.
gi 1063705934 709 SVKKIEEYFAD 719
Cdd:cd03256 228 PPAELTDEVLD 238
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
480-709 |
2.73e-22 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 97.43 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 480 PVIEVafKDLTLTLKGkHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSYK 557
Cdd:COG3638 1 PMLEL--RNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGlvEPTS----GEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KI------TGFVPQDDVVHGNLTVEENL------RFSARCRLSAYMSKADKVLIIErVIESLGLQHVRDSLVGTIekrgi 625
Cdd:COG3638 74 ALrrlrrrIGMIFQQFNLVPRLSVLTNVlagrlgRTSTWRSLLGLFPPEDRERALE-ALERVGLADKAYQRADQL----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHQPSYTMyKMFDDMIILAKGGLt 704
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLAR-RYADRIIGLRDGRV- 225
|
....*
gi 1063705934 705 VYHGS 709
Cdd:COG3638 226 VFDGP 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
484-669 |
6.23e-22 |
|
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: 95.76 E-value: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALagkatgcTR-----TGLILING---RNDSINS 555
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI-------PRfydvdSGRILIDGhdvRDYTLAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 556 YKKITGFVPQDdVVHGNLTVEENLRFSARCRLSAYMSKADKVLIIERVIESL--GLQHVrdslvgtIEKRGI--SGGQRK 631
Cdd:cd03251 74 LRRQIGLVSQD-VFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELpeGYDTV-------IGERGVklSGGQRQ 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063705934 632 RVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRR 669
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALER 183
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
471-713 |
1.25e-21 |
|
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: 99.98 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 471 ATDTEMRTRPVIEVafKDLTLT---LKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLIL 545
Cdd:COG1123 250 AAPAAAAAEPLLEV--RNLSKRypvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllRPTS----GSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 546 INGRN------DSINSYKKITGFVPQDdvVHGNL----TVEENLRFSARcrLSAYMSKADKVLIIERVIESLGLQ-HVRD 614
Cdd:COG1123 324 FDGKDltklsrRSLRELRRRVQMVFQD--PYSSLnprmTVGDIIAEPLR--LHGLLSRAERRERVAELLERVGLPpDLAD 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 615 SLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDsASSQL----LLRALRREalEGVNICMVVHQPSyTMYK 690
Cdd:COG1123 400 RYPHEL-----SGGQRQRVAIARALALEPKLLILDEPTSALD-VSVQAqilnLLRDLQRE--LGLTYLFISHDLA-VVRY 470
|
250 260
....*....|....*....|...
gi 1063705934 691 MFDDMIILAKGGLtVYHGSVKKI 713
Cdd:COG1123 471 IADRVAVMYDGRI-VEDGPTEEV 492
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
471-685 |
1.47e-21 |
|
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: 100.05 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 471 ATDTEMRTRPVIEVAFKDLTLTLKGKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN 550
Cdd:TIGR02857 309 AGKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD--PTEGSIAVNGVP 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 551 -DSINS---YKKItGFVPQDDVVHgNLTVEENLRFSARcrlsaYMSKADkvliIERVIESLGLQHVRDSLVGTIEK---- 622
Cdd:TIGR02857 386 lADADAdswRDQI-AWVPQHPFLF-AGTIAENIRLARP-----DASDAE----IREALERAGLDEFVAALPQGLDTpige 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705934 623 --RGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRReALEGVNICMVVHQPS 685
Cdd:TIGR02857 455 ggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRLA 518
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
501-701 |
1.54e-21 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 96.31 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGCTRTglilINGRnDSINSYKKI---TGFVPQDDVVHGNLTV 575
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTllRPTSGTAR----VAGY-DVVREPRKVrrsIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EENLRFSARCrlsaY-MSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTG 654
Cdd:TIGR01188 84 RENLEMMGRL----YgLPKDEAEERAEELLELFELGEAADRPVGTY-----SGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063705934 655 LDSASSQLLLRALRREALEGVNICMVVHQpsytMY---KMFDDMIILAKG 701
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTHY----MEeadKLCDRIAIIDHG 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
501-669 |
2.27e-21 |
|
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: 94.32 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN-DSINSYKKITGFVPQDDVVHGNLTVEENL 579
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK--PDSGKILLNGKDiTNLPPEKRDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 580 RFSARCRlsaymsKADKVLIIERVIE---SLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:cd03299 93 AYGLKKR------KVDKKEIERKVLEiaeMLGIDHLLNRKPETL-----SGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170
....*....|...
gi 1063705934 657 SASSQLLLRALRR 669
Cdd:cd03299 162 VRTKEKLREELKK 174
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
482-703 |
2.92e-21 |
|
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: 91.89 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVafKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDS---INSY 556
Cdd:cd03246 1 LEV--ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGllRPTS----GRVRLDGADISqwdPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 KKITGFVPQDDvvhgnltveeNLrFSarcrlsaymskadkvliiervieslglqhvrdslvGTIEKRGISGGQRKRVNVG 636
Cdd:cd03246 75 GDHVGYLPQDD----------EL-FS-----------------------------------GSIAENILSGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705934 637 VEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTmyKMFDDMIILAKGGL 703
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETL--ASADRILVLEDGRV 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
498-701 |
3.23e-21 |
|
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: 92.98 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN-----DSINSYKKITGFVPQDDVVH 570
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLleEPDS----GTIIIDGLKltddkKNINELRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 571 GNLTVEENLRFSARCRLSayMSKADKVLIIERVIESLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPSLLILDE 650
Cdd:cd03262 89 PHLTVLENITLAPIKVKG--MSKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 651 PTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTmYKMFDDMIILAKG 701
Cdd:cd03262 162 PTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFA-REVADRVIFMDDG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
483-703 |
4.55e-21 |
|
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: 93.04 E-value: 4.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN----DSINSY 556
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlyKPTS----GSVLLDGTDirqlDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 KKItGFVPQDDV-VHGnlTVEENLRFSARcrlsaymsKADKVLIIeRVIESLGL-----QHVR--DSLVGtiEK-RGISG 627
Cdd:cd03245 78 RNI-GYVPQDVTlFYG--TLRDNITLGAP--------LADDERIL-RAAELAGVtdfvnKHPNglDLQIG--ERgRGLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 628 GQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREaLEGVNICMVVHQPSytMYKMFDDMIILAKGGL 703
Cdd:cd03245 144 GQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPS--LLDLVDRIIVMDSGRI 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
482-701 |
4.61e-21 |
|
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: 93.71 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVafKDLTLT--LKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGctRTGLILINGR---NDSINSY 556
Cdd:COG1124 2 LEV--RNLSVSygQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP--WSGEVTFDGRpvtRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 KKITGFVPQD--DVVHGNLTVEENLRFSARCrlsayMSKADKVLIIERVIESLGL-QHVRDSLVGTIekrgiSGGQRKRV 633
Cdd:COG1124 78 RRRVQMVFQDpyASLHPRHTVDRILAEPLRI-----HGLPDREERIAELLEQVGLpPSFLDRYPHQL-----SGGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 634 NVGVEMVMEPSLLILDEPTTGLDsASSQ---L-LLRALRREalEGVNICMVVHQPSYtMYKMFDDMIILAKG 701
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALD-VSVQaeiLnLLKDLREE--RGLTYLFVSHDLAV-VAHLCDRVAVMQNG 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
491-682 |
7.23e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 95.55 E-value: 7.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKH-----ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNdsINS---YKKIT 560
Cdd:COG3842 6 LELENVSKRygdvtALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTPDS----GRILLDGRD--VTGlppEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 561 GFVPQDDVVHGNLTVEENLRFSARCRLsayMSKADkvlIIERVIESL---GLQHVRDSLVGTiekrgISGGQRKRVNVGV 637
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMRG---VPKAE---IRARVAELLelvGLEGLADRYPHQ-----LSGGQQQRVALAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063705934 638 EMVMEPSLLILDEPTTGLDS---ASSQLLLRALRREAleGVNICMVVH 682
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAklrEEMREELRRLQREL--GITFIYVTH 194
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
499-680 |
7.39e-21 |
|
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: 92.74 E-value: 7.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 499 HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KAtgctRTGLILINGRN-DSINSYKKIT---GFVPQDDVVHGN 572
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGllPP----RSGSIRFDGEDiTGLPPHRIARlgiGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 573 LTVEENLRFSARCRLSAYMSKADkvliIERVIEsL--GLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPSLLILDE 650
Cdd:COG0410 93 LTVEENLLLGAYARRDRAEVRAD----LERVYE-LfpRLKERRRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190
....*....|....*....|....*....|..
gi 1063705934 651 PTTGLdsASS--QLLLRALRREALEGVNICMV 680
Cdd:COG0410 163 PSLGL--APLivEEIFEIIRRLNREGVTILLV 192
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
486-713 |
8.07e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.51 E-value: 8.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKHKHIlrSVTgkIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNdsinsykkITGFVP- 564
Cdd:COG3840 4 LDDLTYRYGDFPLRF--DLT--IAAGERVAILGPSGAGKSTLLNLIAGFLP--PDSGRILWNGQD--------LTALPPa 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 565 --------QDDVVHGNLTVEEN--LRFSARCRLSAymskADKVLIIErVIESLGLQHVRDSLVGTiekrgISGGQRKRVN 634
Cdd:COG3840 70 erpvsmlfQENNLFPHLTVAQNigLGLRPGLKLTA----EQRAQVEQ-ALERVGLAGLLDRLPGQ-----LSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 635 VGVEMVMEPSLLILDEPTTGLDSassqlllrALRREALEGVN-IC--------MVVHQPSYTmyKMFDDMIILAKGGLTV 705
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDP--------ALRQEMLDLVDeLCrergltvlMVTHDPEDA--ARIADRVLLVADGRIA 209
|
....*...
gi 1063705934 706 YHGSVKKI 713
Cdd:COG3840 210 ADGPTAAL 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
481-708 |
9.08e-21 |
|
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: 92.18 E-value: 9.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 481 VIEVafKDLTLTL--KGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSY 556
Cdd:cd03257 1 LLEV--KNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGllKPTS----GSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 -------KKItGFVPQD--DVVHGNLTVEENLRFSARcrlSAYMSKADKvliIERVIESLGLQHVrdSLVGTIEKR---G 624
Cdd:cd03257 75 rlrkirrKEI-QMVFQDpmSSLNPRMTIGEQIAEPLR---IHGKLSKKE---ARKEAVLLLLVGV--GLPEEVLNRyphE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 625 ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDsASSQL----LLRALRREalEGVNICMVVHQPSyTMYKMFDDMIILaK 700
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALD-VSVQAqildLLKKLQEE--LGLTLLFITHDLG-VVAKIADRVAVM-Y 220
|
....*...
gi 1063705934 701 GGLTVYHG 708
Cdd:cd03257 221 AGKIVEEG 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
484-685 |
1.09e-20 |
|
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: 97.53 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRndSINSYK---- 557
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRflDPQS----GSITLGGV--DLRDLDeddl 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 -KITGFVPQD-DVVHGnlTVEENLRFsARCRLSaymskaDKVLI--IERV-----IESL--GLqhvrDSLVGtiEK-RGI 625
Cdd:COG4987 408 rRRIAVVPQRpHLFDT--TLRENLRL-ARPDAT------DEELWaaLERVglgdwLAALpdGL----DTWLG--EGgRRL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 626 SGGQRKRVnvGVEMVM--EPSLLILDEPTTGLDSASSQLLLRALrREALEGVNICMVVHQPS 685
Cdd:COG4987 473 SGGERRRL--ALARALlrDAPILLLDEPTEGLDAATEQALLADL-LEALAGRTVLLITHRLA 531
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
484-701 |
2.88e-20 |
|
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: 90.54 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILING------RNDSINSYK 557
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL--PTSGTIRVNGqdvsdlRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KITGFVPQDDVVHGNLTVEENLRFSARCrlsaymSKADKVLIIERV---IESLGLQHVRDSLvgtieKRGISGGQRKRVN 634
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEV------TGVPPREIRKRVpaaLELVGLSHKHRAL-----PAELSGGEQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 635 VGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSytmykMFDDM----IILAKG 701
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKE-----LVDTTrhrvIALERG 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
480-684 |
2.88e-20 |
|
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: 91.30 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 480 PVIEvaFKDLTLTLKGKHkhILRSVTGKIMPG-RVsAVMGPSGAGKTTFLSALAG---KATGCTRTglILinGR---NDS 552
Cdd:COG1119 2 PLLE--LRNVTVRRGGKT--ILDDISWTVKPGeHW-AILGPNGAGKSTLLSLITGdlpPTYGNDVR--LF--GErrgGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 553 INSYKKITGFVPQD--DVVHGNLTVEENLrfsarcrLSAYMS--------KADKVLIIERVIESLGLQHVRDSLVGTIek 622
Cdd:COG1119 73 VWELRKRIGLVSPAlqLRFPRDETVLDVV-------LSGFFDsiglyrepTDEQRERARELLELLGLAHLADRPFGTL-- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705934 623 rgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEG-VNICMVVHQP 684
Cdd:COG1119 144 ---SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHV 203
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
510-682 |
2.90e-20 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 90.68 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 510 PGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRndSINSYKKITGFVPQD---------DVVHgnlTVeenlr 580
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIP--PAKGTVKVAGA--SPGKGWRHIGYVPQRhefawdfpiSVAH---TV----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 581 FSARCRLSAYM--SKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSA 658
Cdd:TIGR03771 73 MSGRTGHIGWLrrPCVADFAAVRDALRRVGLTELADRPVGEL-----SGGQRQRVLVARALATRPSVLLLDEPFTGLDMP 147
|
170 180
....*....|....*....|....
gi 1063705934 659 SSQLLLRALRREALEGVNICMVVH 682
Cdd:TIGR03771 148 TQELLTELFIELAGAGTAILMTTH 171
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
478-701 |
3.09e-20 |
|
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: 96.47 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 478 TRPVI--EVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN--- 550
Cdd:TIGR03375 456 HRPRLqgEIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGlyQPTE----GSVLLDGVDirq 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 551 -DSINSYKKItGFVPQDDVV-HGnlTVEENLRFSARcrlsaymsKADKVLIIeRVIESLGL-----QHVR--DSLVGtiE 621
Cdd:TIGR03375 532 iDPADLRRNI-GYVPQDPRLfYG--TLRDNIALGAP--------YADDEEIL-RAAELAGVtefvrRHPDglDMQIG--E 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 622 K-RGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREaLEGVNICMVVHQPSytMYKMFDDMIILAK 700
Cdd:TIGR03375 598 RgRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTS--LLDLVDRIIVMDN 674
|
.
gi 1063705934 701 G 701
Cdd:TIGR03375 675 G 675
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
500-682 |
3.13e-20 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 89.79 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGR-----NDSINSYKKITGFVPQD-DVVHGNL 573
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLR--PQSGAVLIDGEpldysRKGLLERRQRVGLVFQDpDDQLFAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 574 TVEENLRFSARcrlSAYMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTT 653
Cdd:TIGR01166 85 DVDQDVAFGPL---NLGLSEAEVERRVREALTAVGASGLRERPTHCL-----SGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180
....*....|....*....|....*....
gi 1063705934 654 GLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
483-669 |
4.72e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 95.62 E-value: 4.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILING---RNDSINSYK 557
Cdd:COG1132 339 EIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyDPTS----GRILIDGvdiRDLTLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KITGFVPQDDVV-HGnlTVEENLRFSarcRLSAymSKAD-----KVLIIERVIESL--GLqhvrDSLVGtieKRGI--SG 627
Cdd:COG1132 414 RQIGVVPQDTFLfSG--TIRENIRYG---RPDA--TDEEveeaaKAAQAHEFIEALpdGY----DTVVG---ERGVnlSG 479
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063705934 628 GQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRR 669
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER 521
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
498-716 |
4.88e-20 |
|
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: 90.44 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN------DSINSYKKITGFVPQDDVVHG 571
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVE--PSSGSILLEGTDitklrgKKLRKLRRRIGMIFQHYNLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 572 NLTVEENL---RFSARC---RLSAYMSKADKVL---IIERV-IESLGLQHVrDSLvgtiekrgiSGGQRKRVNVGVEMVM 641
Cdd:TIGR02315 93 RLTVLENVlhgRLGYKPtwrSLLGRFSEEDKERalsALERVgLADKAYQRA-DQL---------SGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 642 EPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHQPSYTmyKMFDDMIILAKGGLTVYHGSVKKIEEY 716
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLA--KKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
510-684 |
9.82e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 9.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 510 PGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSYKKITGFVPQDDVVHGNLTVEENLRFSARCRl 587
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGllPPAA----GTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLEFWAAFL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 588 saymskADKVLIIERVIESLGLQHVRDslvgtIEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRAL 667
Cdd:PRK13539 102 ------GGEELDIAAALEAVGLAPLAH-----LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
170
....*....|....*..
gi 1063705934 668 RREALEGVNICMVVHQP 684
Cdd:PRK13539 171 RAHLAQGGIVIAATHIP 187
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
497-701 |
1.27e-19 |
|
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: 89.22 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 497 HKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN-DSINSYKKITGFVPQDDVVHGNL 573
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfeTPTS----GEILLDGKDiTNLPPHKRPVNTVFQNYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 574 TVEENLRFSARcrlsayMSKADKVLIIERVIESLGLqhVRdslVGTIEKRGI---SGGQRKRVNVGVEMVMEPSLLILDE 650
Cdd:cd03300 88 TVFENIAFGLR------LKKLPKAEIKERVAEALDL--VQ---LEGYANRKPsqlSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063705934 651 PTTGLDS---ASSQLLLRALRREAleGVNICMVVHQPSYTMyKMFDDMIILAKG 701
Cdd:cd03300 157 PLGALDLklrKDMQLELKRLQKEL--GITFVFVTHDQEEAL-TMSDRIAVMNKG 207
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
499-674 |
2.49e-19 |
|
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: 87.97 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 499 HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN-DSINSYKKIT---GFVPQDDVVHGNLT 574
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLP--VKSGSIRLDGEDiTKLPPHERARagiAYVPQGREIFPRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 575 VEENLRFSARCRlsaymsKADKVLIIERVIESLG-LQHVRDslvgtieKRG--ISGGQRKRVNVGVEMVMEPSLLILDEP 651
Cdd:TIGR03410 92 VEENLLTGLAAL------PRRSRKIPDEIYELFPvLKEMLG-------RRGgdLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180
....*....|....*....|...
gi 1063705934 652 TTGLDSASSQLLLRALRREALEG 674
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEG 181
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
501-669 |
3.18e-19 |
|
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: 88.17 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDS-INSYKKITGFVPQDDVVHGNLTVEE 577
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGleRPD----SGTILFGGEDATdVPVQERNVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NLRFSARCRLSAymSKADKVLIIERVIESLGLQHVrDSLvgtiEKR---GISGGQRKRVNVGVEMVMEPSLLILDEPTTG 654
Cdd:cd03296 94 NVAFGLRVKPRS--ERPPEAEIRAKVHELLKLVQL-DWL----ADRypaQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170
....*....|....*
gi 1063705934 655 LDSASSQLLLRALRR 669
Cdd:cd03296 167 LDAKVRKELRRWLRR 181
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
482-713 |
3.41e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.22 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAgkatgctR-----TGLILINGRNdsINSY 556
Cdd:COG4604 2 IEI--KNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS-------RllppdSGEVLVDGLD--VATT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 K-----KITGFVPQDDVVHGNLTVEENLRFS----ARCRLSAymskADKVlIIERVIESLGLQHVRDSLVGTIekrgiSG 627
Cdd:COG4604 69 PsrelaKRLAILRQENHINSRLTVRELVAFGrfpySKGRLTA----EDRE-IIDEAIAYLDLEDLADRYLDEL-----SG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 628 GQRKRVNVGveMVM--EPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHqpsytmykmfD--------DMI 696
Cdd:COG4604 139 GQRQRAFIA--MVLaqDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH----------DinfascyaDHI 206
|
250
....*....|....*..
gi 1063705934 697 ILAKGGLTVYHGSVKKI 713
Cdd:COG4604 207 VAMKDGRVVAQGTPEEI 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
496-656 |
3.41e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.16 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 496 KHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNdsinsykkIT------------G 561
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlvKPDS----GRIFLDGED--------IThlpmhkrarlgiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 562 FVPQDDVVHGNLTVEENLRFSARCRlsaYMSKADKVLIIERVIESLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVM 641
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELR---KLSKKEREERLEELLEEFGITHLRKSKAYS-----LSGGERRRVEIARALAT 153
|
170
....*....|....*
gi 1063705934 642 EPSLLILDEPTTGLD 656
Cdd:COG1137 154 NPKFILLDEPFAGVD 168
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
511-701 |
4.17e-19 |
|
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: 87.16 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 511 GRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN-DSINSYKKITGFVPQDDVVHGNLTVEEN--LRFSARCRL 587
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFET--PQSGRVLINGVDvTAAPPADRPVSMLFQENNLFAHLTVEQNvgLGLSPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 588 SAYMSKAdkvliIERVIESLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSA---SSQLLL 664
Cdd:cd03298 102 TAEDRQA-----IEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPAlraEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063705934 665 RALRREalEGVNICMVVHQPSYTMyKMFDDMIILAKG 701
Cdd:cd03298 172 LDLHAE--TKMTVLMVTHQPEDAK-RLAQRVVFLDNG 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
509-719 |
5.33e-19 |
|
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: 89.79 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 509 MPGR-VSAVMGPSGAGKTTFLSALAGkatgCTR--TGLILINGR--NDS-----INSYKKITGFVPQDDVVHGNLTVEEN 578
Cdd:TIGR02142 20 LPGQgVTAIFGRSGSGKTTLIRLIAG----LTRpdEGEIVLNGRtlFDSrkgifLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 579 LRFS-ARCRLSaymskaDKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDS 657
Cdd:TIGR02142 96 LRYGmKRARPS------ERRISFERVIELLGIGHLLGRLPGRL-----SGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705934 658 ASSQLLLRALRREALE-GVNICMVVHQPSyTMYKMFDDMIILAKGGLTvyhgSVKKIEEYFAD 719
Cdd:TIGR02142 165 PRKYEILPYLERLHAEfGIPILYVSHSLQ-EVLRLADRVVVLEDGRVA----AAGPIAEVWAS 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
498-713 |
5.99e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 88.63 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSINSYKKItGFVPQDDVVHGNLTV 575
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilAPD----SGEVLWDGEPLDPEDRRRI-GYLPEERGLYPKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EENLRFSARCRLsayMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGL 655
Cdd:COG4152 89 GEQLVYLARLKG---LSKAEAKRRADEWLERLGLGDRANKKVEEL-----SKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705934 656 DSASSQLLLRALRREALEGVNICMVVHQPSYTMyKMFDDMIILAKGGlTVYHGSVKKI 713
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELVE-ELCDRIVIINKGR-KVLSGSVDEI 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
478-709 |
7.21e-19 |
|
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: 87.21 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 478 TRPVIEVaFKDLTLTLKgkhkhilrsvtgkimPGRVSAVMGPSGAGKTTFLSALagkatgcTR-----TGLILING---R 549
Cdd:cd03249 12 SRPDVPI-LKGLSLTIP---------------PGKTVALVGSSGCGKSTVVSLL-------ERfydptSGEILLDGvdiR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 550 NDSINSYKKITGFVPQDDVVHgNLTVEENLRFSARCRLSAYMSKADKVLIIERVIESL--GLqhvrDSLVGTiekRG--I 625
Cdd:cd03249 69 DLNLRWLRSQIGLVSQEPVLF-DGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLpdGY----DTLVGE---RGsqL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRReALEGVNICMVVHQPSyTMYKMfdDMIILAKGGLTV 705
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDR-AMKGRTTIVIAHRLS-TIRNA--DLIAVLQNGQVV 216
|
....
gi 1063705934 706 YHGS 709
Cdd:cd03249 217 EQGT 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
483-709 |
8.79e-19 |
|
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: 86.51 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKHkHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRND---SINSYK 557
Cdd:cd03254 2 EIEFENVNFSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfyDPQK----GQILIDGIDIrdiSRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KITGFVPQDDVVHgNLTVEENLRFSarcRLSAYMS---KADKVLIIERVIESL--GLQHVrdslvgtIEKRG--ISGGQR 630
Cdd:cd03254 77 SMIGVVLQDTFLF-SGTIMENIRLG---RPNATDEeviEAAKEAGAHDFIMKLpnGYDTV-------LGENGgnLSQGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705934 631 KRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRReALEGVNICMVVHQPSYTMYKmfdDMIILAKGGLTVYHGS 709
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK-LMKGRTSIIIAHRLSTIKNA---DKILVLDDGKIIEEGT 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
496-656 |
1.44e-18 |
|
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: 86.06 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 496 KHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNdsinsykkIT------------G 561
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvKPDS----GKILLDGQD--------ITklpmhkrarlgiG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 562 FVPQDDVVHGNLTVEENLRFSARCRlsaYMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVM 641
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIR---GLSKKEREEKLEELLEEFHITHLRKSKASSL-----SGGERRRVEIARALAT 150
|
170
....*....|....*
gi 1063705934 642 EPSLLILDEPTTGLD 656
Cdd:cd03218 151 NPKFLLLDEPFAGVD 165
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
498-670 |
1.44e-18 |
|
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: 85.38 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGR--NDsINSYKKITGFVPQDDVVHGNL 573
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGleEPTS----GRIYIGGRdvTD-LPPKDRDIAMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 574 TVEENLRFSARCRlsaymsKADKVLIIERVIES---LGLQHVRDSLVgtiekRGISGGQRKRVNVGVEMVMEPSLLILDE 650
Cdd:cd03301 88 TVYDNIAFGLKLR------KVPKDEIDERVREVaelLQIEHLLDRKP-----KQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180
....*....|....*....|
gi 1063705934 651 PTTGLDSassqLLLRALRRE 670
Cdd:cd03301 157 PLSNLDA----KLRVQMRAE 172
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
510-670 |
1.47e-18 |
|
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: 88.62 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 510 PGRVSAVMGPSGAGKTTFLSALAGKATGCtrTGLILINGR--NDS---IN--SYKKITGFVPQDDVVHGNLTVEENLRFS 582
Cdd:COG4148 24 GRGVTALFGPSGSGKTTLLRAIAGLERPD--SGRIRLGGEvlQDSargIFlpPHRRRIGYVFQEARLFPHLSVRGNLLYG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 583 ARcRLSAYMSKADkvliIERVIESLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQL 662
Cdd:COG4148 102 RK-RAPRAERRIS----FDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170
....*....|.
gi 1063705934 663 L---LRALRRE 670
Cdd:COG4148 172 IlpyLERLRDE 182
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
484-684 |
1.53e-18 |
|
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: 90.50 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKH------ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILING---RNDSIN 554
Cdd:TIGR02868 328 VGLGKPTLELRDLSAGypgappVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGvpvSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 555 SYKKITGFVPQDDVVHGNlTVEENLRFSARCRLSAYMSKADKVLIIERVIESL--GLqhvrDSLVGTIEKRgISGGQRKR 632
Cdd:TIGR02868 406 EVRRRVSVCAQDAHLFDT-TVRENLRLARPDATDEELWAALERVGLADWLRALpdGL----DTVLGEGGAR-LSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 633 VNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALrREALEGVNICMVVHQP 684
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
478-685 |
5.00e-18 |
|
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: 84.41 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 478 TRPVIEVafKDLTLTLK-GKHK-HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILING----- 548
Cdd:COG4181 5 SAPIIEL--RGLTKTVGtGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGldRPTS----GTVRLAGqdlfa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 549 ---------RNDSInsykkitGFVPQDDVVHGNLTVEEN------LRFSARCRlsaymSKADKVLiiERVieslGLQHVR 613
Cdd:COG4181 79 ldedararlRARHV-------GFVFQSFQLLPTLTALENvmlpleLAGRRDAR-----ARARALL--ERV----GLGHRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705934 614 DSLvgtieKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQL---LLRALRREAleGVNICMVVHQPS 685
Cdd:COG4181 141 DHY-----PAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidLLFELNRER--GTTLVLVTHDPA 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
480-682 |
5.71e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.82 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 480 PVIEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNdsINSYK-- 557
Cdd:PRK13548 1 AMLEA--RNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS--PDSGEVRLNGRP--LADWSpa 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 ---KITGFVPQddvvHGNL----TVEENLRFSarcRLSAYMSKADKVLIIERVIESLGLQHVRDSLVgtiekRGISGGQR 630
Cdd:PRK13548 73 elaRRRAVLPQ----HSSLsfpfTVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDLAHLAGRDY-----PQLSGGEQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705934 631 KRVNVG-V-----EMVMEPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVH 682
Cdd:PRK13548 141 QRVQLArVlaqlwEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLH 199
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
479-685 |
7.60e-18 |
|
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: 88.27 E-value: 7.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 479 RPVIEVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNdsINSY 556
Cdd:COG4618 326 RPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGvwPPTA----GSVRLDGAD--LSQW 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 KKIT-----GFVPQDdvVH---GnlTVEENLrfsARcrlsayMSKADKvliiERVIES----------LGLQHVRDSLVG 618
Cdd:COG4618 400 DREElgrhiGYLPQD--VElfdG--TIAENI---AR------FGDADP----EKVVAAaklagvhemiLRLPDGYDTRIG 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705934 619 TiEKRGISGGQRKRV--------NvgvemvmePSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPS 685
Cdd:COG4618 463 E-GGARLSGGQRQRIglaralygD--------PRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS 528
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
498-726 |
8.06e-18 |
|
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: 84.81 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNdsINSYKKIT--------GFVPQ-- 565
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGllKPT----SGTVTIDGRD--ITAKKKKKlkdlrkkvGLVFQfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 566 ----------DDVVHG--NLTVEEnlrfsarcrlsaymSKADkvliiERVIESLglqhvrdSLVG---TIEKR---GISG 627
Cdd:TIGR04521 92 ehqlfeetvyKDIAFGpkNLGLSE--------------EEAE-----ERVKEAL-------ELVGldeEYLERspfELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 628 GQRKRVNV-GVeMVMEPSLLILDEPTTGLDSASSQLLL---RALRREalEGVNICMVVHQpsytM---YKMFDDMIILAK 700
Cdd:TIGR04521 146 GQMRRVAIaGV-LAMEPEVLILDEPTAGLDPKGRKEILdlfKRLHKE--KGLTVILVTHS----MedvAEYADRVIVMHK 218
|
250 260
....*....|....*....|....*....
gi 1063705934 701 GGLtVYHGSVKKI---EEYFADIGITVPD 726
Cdd:TIGR04521 219 GKI-VLDGTPREVfsdVDELEKIGLDVPE 246
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
516-701 |
1.36e-17 |
|
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: 85.24 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 516 VMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDS-INSYKKITGFVPQDDVVHGNLTVEENLRFSARcrlsayMSKA 594
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQ--PDSGSIMLDGEDVTnVPPHLRHINMVFQSYALFPHMTVEENVAFGLK------MRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 595 DKVLIIERVIESLGLQHVRDslVGTIEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSA---SSQLLLRALRREA 671
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEE--FADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdQMQLELKTIQEQL 150
|
170 180 190
....*....|....*....|....*....|
gi 1063705934 672 leGVNICMVVHQPSYTMyKMFDDMIILAKG 701
Cdd:TIGR01187 151 --GITFVFVTHDQEEAM-TMSDRIAIMRKG 177
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
484-709 |
1.94e-17 |
|
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: 82.92 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTfLSALAGKATGCTRtGLILINGRNDSI---NSYKKIT 560
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKST-LTKLIQRFYVPEN-GRVLVDGHDLALadpAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 561 GFVPQDDVVHgNLTVEENLrfsarcrlsaymSKADKVLIIERVIESLGLQHVR----------DSLVGTiEKRGISGGQR 630
Cdd:cd03252 79 GVVLQENVLF-NRSIRDNI------------ALADPGMSMERVIEAAKLAGAHdfiselpegyDTIVGE-QGAGLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705934 631 KRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRReALEGVNICMVVHQPSYTMYKmfdDMIILAKGGLTVYHGS 709
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHD-ICAGRTVIIIAHRLSTVKNA---DRIIVMEKGRIVEQGS 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
501-669 |
2.09e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.20 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSIN--SYKKITGFVPQDDVVHGNLTVE 576
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGleTPD----SGRIVLNGRDLFTNlpPRERRVGFVFQHYALFPHMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 577 ENLRFSARCRLSaymSKADKVLIIERVIESLGLQHvrdslvgtIEKR---GISGGQRKRVNVGVEMVMEPSLLILDEPTT 653
Cdd:COG1118 94 ENIAFGLRVRPP---SKAEIRARVEELLELVQLEG--------LADRypsQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170
....*....|....*.
gi 1063705934 654 GLDSASSQLLLRALRR 669
Cdd:COG1118 163 ALDAKVRKELRRWLRR 178
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
500-684 |
2.94e-17 |
|
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: 81.25 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGR--NDSINSYKKITGFVPQDDVVHGNLTV 575
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllRPDS----GEVRWNGTplAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EENLRFsaRCRLSAYMSKAdkvliIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGL 655
Cdd:TIGR01189 91 LENLHF--WAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQL-----SAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*....
gi 1063705934 656 DSASSQLLLRALRREALEGVNICMVVHQP 684
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
490-670 |
5.68e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.58 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 490 TLTLKGKHK-----HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNdsinsykkITGF 562
Cdd:COG3839 3 SLELENVSKsyggvEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGleDPTS----GEILIGGRD--------VTDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 563 VPQD-DV--V--------HgnLTVEENLRFSARCRlsaYMSKADKVLIIERVIESLGLQHVRDSLVgtiekRGISGGQRK 631
Cdd:COG3839 71 PPKDrNIamVfqsyalypH--MTVYENIAFPLKLR---KVPKAEIDRRVREAAELLGLEDLLDRKP-----KQLSGGQRQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063705934 632 RVNVGVEMVMEPSLLILDEPTTGLDSAssqllLRA-LRRE 670
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAK-----LRVeMRAE 175
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
487-682 |
7.25e-17 |
|
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: 80.26 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG----KATGctrtGLILINGRNdsinsykkITgf 562
Cdd:cd03217 4 KDLHVSVGGKE--ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkyEVTE----GEILFKGED--------IT-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 563 vpqddvvhgNLTVEEnlrfsaRCRLSAYMSkadkvliIERVIESLGLQhVRDSLVGTIEkrGISGGQRKRVNVGVEMVME 642
Cdd:cd03217 68 ---------DLPPEE------RARLGIFLA-------FQYPPEIPGVK-NADFLRYVNE--GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063705934 643 PSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
499-752 |
8.13e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.20 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 499 HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGR-----NDSINSYKKITGFVPQD-DVVH 570
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGilKPS----SGRILFDGKpidysRKGLMKLRESVGMVFQDpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 571 GNLTVEENLRFSArcrLSAYMSKADKVLIIERVIESLGLQHVRDSlvgtiEKRGISGGQRKRVNVGVEMVMEPSLLILDE 650
Cdd:PRK13636 96 FSASVYQDVSFGA---VNLKLPEDEVRKRVDNALKRTGIEHLKDK-----PTHCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 651 PTTGLDSASSQLLLRaLRREALEGVNICMVVHQPSYTMYKMFDDMIILAKGGLTVYHGSVKkieEYFADIGI--TVPDRV 728
Cdd:PRK13636 168 PTAGLDPMGVSEIMK-LLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK---EVFAEKEMlrKVNLRL 243
|
250 260
....*....|....*....|....*..
gi 1063705934 729 NPPDHYIDILE---GIVKPDGDITIEQ 752
Cdd:PRK13636 244 PRIGHLMEILKekdGFVFDELDLTISQ 270
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
474-797 |
1.78e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.58 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 474 TEMRTRPVIEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDS- 552
Cdd:PRK11607 12 TRKALTPLLEI--RNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ--PTAGQIMLDGVDLSh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 553 INSYKKITGFVPQDDVVHGNLTVEENLRFSARcrlsayMSKADKVLIIERVIESLGLQHVRDslvgtIEKRG---ISGGQ 629
Cdd:PRK11607 86 VPPYQRPINMMFQSYALFPHMTVEQNIAFGLK------QDKLPKAEIASRVNEMLGLVHMQE-----FAKRKphqLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 630 RKRVNVGVEMVMEPSLLILDEPTTGLDsassqlllRALR-REALEGVNI-------C-MVVHQPSYTMyKMFDDMIILAK 700
Cdd:PRK11607 155 RQRVALARSLAKRPKLLLLDEPMGALD--------KKLRdRMQLEVVDIlervgvtCvMVTHDQEEAM-TMAGRIAIMNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 701 GGLtVYHGSVKKIEEyfadigitvpdrvNPPDHY-------IDILEGIVKPDGD--ITIEQLPVRWMLH--------NGY 763
Cdd:PRK11607 226 GKF-VQIGEPEEIYE-------------HPTTRYsaefigsVNVFEGVLKERQEdgLVIDSPGLVHPLKvdadasvvDNV 291
|
330 340 350
....*....|....*....|....*....|....*....
gi 1063705934 764 PV-----PHDMLkFCDGLPSSSTGSAQEDSTHNSFSNDL 797
Cdd:PRK11607 292 PVhvalrPEKIM-LCEEPPADGCNFAVGEVIHIAYLGDL 329
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
487-725 |
2.54e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 80.62 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLTLKGKhKHILRSVTgkIMPGRVS--AVMGPSGAGKTTFLSALAGKATgcTRTGLILINGR---NDSINSYKKITG 561
Cdd:PRK13652 7 RDLCYSYSGS-KEALNNIN--FIAPRNSriAVIGPNGAGKSTLFRHFNGILK--PTSGSVLIRGEpitKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 562 FVPQ--DDVVHGNlTVEENLRFSArCRLSAymskaDKVLIIERVIESL---GLQHVRDSLvgtieKRGISGGQRKRVNVG 636
Cdd:PRK13652 82 LVFQnpDDQIFSP-TVEQDIAFGP-INLGL-----DEETVAHRVSSALhmlGLEELRDRV-----PHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 637 VEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHQPSYtMYKMFDDMIILAKGGLTVYhGSVKKI-- 713
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAY-GTVEEIfl 227
|
250
....*....|...
gi 1063705934 714 -EEYFADIGITVP 725
Cdd:PRK13652 228 qPDLLARVHLDLP 240
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
511-684 |
2.68e-16 |
|
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: 78.69 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 511 GRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDS--INSYKKITGFVPQDDVVHGNLTVEENLRFSAR-CRL 587
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSP--PLAGRVLLNGGPLDfqRDSIARGLLYLGHAPGIKTTLSVLENLRFWHAdHSD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 588 SAymskadkvliIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRAL 667
Cdd:cd03231 104 EQ----------VEEALARVGLNGFEDRPVAQL-----SAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170
....*....|....*..
gi 1063705934 668 RREALEGVNICMVVHQP 684
Cdd:cd03231 169 AGHCARGGMVVLTTHQD 185
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
482-683 |
4.68e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 80.89 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEvaFKDLTLTLKGKHK--HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNdsINSY- 556
Cdd:COG1135 2 IE--LENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLleRPT----SGSVLVDGVD--LTALs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 --------KKItGFVPQddvvHGNL----TVEENLRFSARCrlsAYMSKADkvlIIERVIESLglqhvrdSLVGTIEKRG 624
Cdd:COG1135 74 erelraarRKI-GMIFQ----HFNLlssrTVAENVALPLEI---AGVPKAE---IRKRVAELL-------ELVGLSDKAD 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705934 625 -----ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQ--L-LLRALRREaLeGVNICMVVHQ 683
Cdd:COG1135 136 aypsqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRsiLdLLKDINRE-L-GLTIVLITHE 200
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
481-683 |
6.04e-16 |
|
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: 78.39 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 481 VIEvaFKDLTLTLKGKHK--HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSINSY 556
Cdd:cd03258 1 MIE--LKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGleRPT----SGSVLVDGTDLTLLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 KKI------TGFVPQddvvHGNL----TVEENLRFSARCrlsAYMSKADkvlIIERVIESLglqhvrdSLVGTIEKRG-- 624
Cdd:cd03258 75 KELrkarrrIGMIFQ----HFNLlssrTVFENVALPLEI---AGVPKAE---IEERVLELL-------ELVGLEDKADay 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705934 625 ---ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQ---LLLRALRREAleGVNICMVVHQ 683
Cdd:cd03258 138 paqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQsilALLRDINREL--GLTIVLITHE 200
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
482-719 |
7.90e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 78.64 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSA---LAGKATGCTRTGLILINGrNDSINSYKK 558
Cdd:PRK11264 4 IEV--KNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinlLEQPEAGTIRVGDITIDT-ARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 559 I-------TGFVPQ-----------DDVVHGNLTVEENLRFSARCRLSAYMSKadkvliierviesLGLQHVRDSLvgti 620
Cdd:PRK11264 79 LirqlrqhVGFVFQnfnlfphrtvlENIIEGPVIVKGEPKEEATARARELLAK-------------VGLAGKETSY---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 621 eKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTmyKMFDDMIILAK 700
Cdd:PRK11264 142 -PRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFA--RDVADRAIFMD 218
|
250
....*....|....*....
gi 1063705934 701 GGLTVYHGSVKkieEYFAD 719
Cdd:PRK11264 219 QGRIVEQGPAK---ALFAD 234
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
468-682 |
1.09e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 468 ISMATDTEMRTRPVIEVAFKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKAtgCTRTGLILIN 547
Cdd:PRK13536 26 ISEAKASIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT--SPDAGKITVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 548 GRN--DSINSYKKITGFVPQDDVVHGNLTVEENLR-FSARCRLSAYMskadkvliIERVIESLgLQHVRDSLVGTIEKRG 624
Cdd:PRK13536 102 GVPvpARARLARARIGVVPQFDNLDLEFTVRENLLvFGRYFGMSTRE--------IEAVIPSL-LEFARLESKADARVSD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705934 625 ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
508-780 |
1.21e-15 |
|
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: 82.75 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 508 IMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN--DSINSYKKITGFVPQDDVVHGNLTVEENLRFSARC 585
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAGKSilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 586 RlsAYMSKAdkvliIERV----IESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQ 661
Cdd:TIGR01257 2040 R--GVPAEE-----IEKVanwsIQSLGLSLYADRLAGTY-----SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 662 LLLRALRREALEGVNICMVVHQPSyTMYKMFDDMIILAKGGLTVYhGSVKKIEEYFADiGITVPDRVNPPDHyiDILegi 741
Cdd:TIGR01257 2108 MLWNTIVSIIREGRAVVLTSHSME-ECEALCTRLAIMVKGAFQCL-GTIQHLKSKFGD-GYIVTMKIKSPKD--DLL--- 2179
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1063705934 742 vkPDGDitieqlPVRWMLHNGYPVP------HDMLKFcdGLPSSS 780
Cdd:TIGR01257 2180 --PDLN------PVEQFFQGNFPGSvqrerhYNMLQF--QVSSSS 2214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
512-683 |
1.25e-15 |
|
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: 82.37 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 512 RVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN--DSINSYKKITGFVPQDDVVHGNLTVEENLRFSARCRLSa 589
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLP--PTSGTVLVGGKDieTNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGR- 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 590 ymSKADKVLIIERVIESLGLQHVRDSlvgtiEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRR 669
Cdd:TIGR01257 1034 --SWEEAQLEMEAMLEDTGLHHKRNE-----EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170
....*....|....
gi 1063705934 670 EAlEGVNICMVVHQ 683
Cdd:TIGR01257 1107 YR-SGRTIIMSTHH 1119
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
491-704 |
1.71e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGR---NDSINSYKKITGFVPQDD 567
Cdd:PRK11231 8 LTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT--PQSGTVFLGDKpisMLSSRQLARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 568 VVHGNLTVEENLRFSARCRLSAY--MSKADKVLIiERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSL 645
Cdd:PRK11231 86 LTPEGITVRELVAYGRSPWLSLWgrLSAEDNARV-NQAMEQTRINHLADRRLTDL-----SGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 646 LILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH---QPSytmyKMFDDMIILAKGGLT 704
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVM 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
484-709 |
1.82e-15 |
|
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: 80.92 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALagkatgcTR-----TGLILING---RNDSINS 555
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI-------PRfyepdSGQILLDGhdlADYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 556 YKKITGFVPQDdVVHGNLTVEENLRFSARcrlsAYMSKADkvliIERVIESLGLQHVRDSL-------VGTIEKRgISGG 628
Cdd:TIGR02203 404 LRRQVALVSQD-VVLFNDTIANNIAYGRT----EQADRAE----IERALAAAYAQDFVDKLplgldtpIGENGVL-LSGG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 629 QRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRReALEGVNICMVVHQPSyTMYKMfdDMIILAKGGLTVYHG 708
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALER-LMQGRTTLVIAHRLS-TIEKA--DRIVVMDDGRIVERG 549
|
.
gi 1063705934 709 S 709
Cdd:TIGR02203 550 T 550
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
508-682 |
1.83e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 508 IMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGrnDSINSYKKIT----GFVPQDDVVHGNLTVEENLRFSA 583
Cdd:PRK13537 30 VQRGECFGLLGPNGAGKTTTLRMLLGLTH--PDAGSISLCG--EPVPSRARHArqrvGVVPQFDNLDPDFTVRENLLVFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 584 RcrlsaY--MSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQ 661
Cdd:PRK13537 106 R-----YfgLSAAAARALVPPLLEFAKLENKADAKVGEL-----SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARH 175
|
170 180
....*....|....*....|.
gi 1063705934 662 LLLRALRREALEGVNICMVVH 682
Cdd:PRK13537 176 LMWERLRSLLARGKTILLTTH 196
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
498-682 |
2.68e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.05 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN-DSINSYK--KITGFVPQDDVV--HGN 572
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP--PDSGSILIDGKDvTKLPEYKraKYIGRVFQDPMMgtAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 573 LTVEENLRFSARcR-----LSAYMSKADKVLIIERVIE-SLGLQHVRDSLVGTIekrgiSGGQRKrvnvGVEMVM----E 642
Cdd:COG1101 97 MTIEENLALAYR-RgkrrgLRRGLTKKRRELFRELLATlGLGLENRLDTKVGLL-----SGGQRQ----ALSLLMatltK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063705934 643 PSLLILDEPTTGLDSASSQLLLrALRREALEGVNIC--MVVH 682
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALVL-ELTEKIVEENNLTtlMVTH 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
484-704 |
4.18e-15 |
|
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: 74.27 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KAtgctRTGLILINGRNDSI--NSYKKI 559
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdlKP----QQGEITLDGVPVSDleKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 TGFVPQDdvVHgnltveenlRFSARCRlsaymskadkvliierviESLGLQhvrdslvgtiekrgISGGQRKRVNVGVEM 639
Cdd:cd03247 77 ISVLNQR--PY---------LFDTTLR------------------NNLGRR--------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705934 640 VMEPSLLILDEPTTGLDSASSQLLLRaLRREALEGVNICMVVHQpsYTMYKMFDDMIILAKGGLT 704
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLS-LIFEVLKDKTLIWITHH--LTGIEHMDKILFLENGKII 175
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
511-685 |
4.65e-15 |
|
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: 75.28 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 511 GRVSAVMGPSGAGKTTFLSALAGKATGCTrtGLILINGRNDSINS-YKKITGFVPQDDVVHGNLTVEENLRFSARCRLSA 589
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEPAS--GSIKVNDQSHTGLApYQRPVSMLFQENNLFAHLTVRQNIGLGLHPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 590 YMSKADKvliIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRR 669
Cdd:TIGR01277 102 NAEQQEK---VVDAAQQVGIADYLDRLPEQL-----SGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170
....*....|....*..
gi 1063705934 670 EALE-GVNICMVVHQPS 685
Cdd:TIGR01277 174 LCSErQRTLLMVTHHLS 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
479-716 |
6.15e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 479 RPVIEVafKDLTLTLKGKHkhILRSVTGKIMPG-RVsAVMGPSGAGKTTFLSALAG--KATgctrTGLILInGRNDSIns 555
Cdd:COG0488 313 KKVLEL--EGLSKSYGDKT--LLDDLSLRIDRGdRI-GLIGPNGAGKSTLLKLLAGelEPD----SGTVKL-GETVKI-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 556 ykkitGFVPQD-DVVHGNLTVEENLR--------FSARCRLSAYMSKADKVliiERVIESLglqhvrdslvgtiekrgiS 626
Cdd:COG0488 381 -----GYFDQHqEELDPDKTVLDELRdgapggteQEVRGYLGRFLFSGDDA---FKPVGVL------------------S 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 627 GGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALrrEALEGvniCMVV--HQPsYTMYKMFDDMIILAKGGLT 704
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL--DDFPG---TVLLvsHDR-YFLDRVATRILEFEDGGVR 508
|
250
....*....|..
gi 1063705934 705 VYHGSVkkiEEY 716
Cdd:COG0488 509 EYPGGY---DDY 517
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
470-682 |
1.25e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.07 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 470 MATDTEMrTRPVIEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSAL-------AgkatGCTRTG 542
Cdd:COG1117 1 MTAPAST-LEPKIEV--RNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliP----GARVEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 543 LILINGRN---DSINSY---KKItGFVPQddvvHGN---LTVEENLRFSArcRLSAYMSKADkvlIIERVIESL---GL- 609
Cdd:COG1117 72 EILLDGEDiydPDVDVVelrRRV-GMVFQ----KPNpfpKSIYDNVAYGL--RLHGIKSKSE---LDEIVEESLrkaALw 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705934 610 QHVRDSLvgtieKR---GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQL---LLRALRREalegVNICMVVH 682
Cdd:COG1117 142 DEVKDRL-----KKsalGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKieeLILELKKD----YTIVIVTH 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
499-658 |
1.84e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 499 HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGR--NDsINSYKKITGFVPQDDVVHGNLTVE 576
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLFIGEKrmND-VPPAERGVGMVFQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 577 ENLRFSARcrlsayMSKADKVLIIERV---IESLGLQHVRDSlvgtiEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTT 653
Cdd:PRK11000 94 ENMSFGLK------LAGAKKEEINQRVnqvAEVLQLAHLLDR-----KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
....*
gi 1063705934 654 GLDSA 658
Cdd:PRK11000 163 NLDAA 167
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
480-704 |
1.97e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.80 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 480 PVIEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSYKKI 559
Cdd:PRK09536 2 PMIDV--SDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT--PTAGTVLVAGDDVEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 T---GFVPQDDVVHGNLTVE---ENLRFSARCRLSAYMSKADKVliIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRV 633
Cdd:PRK09536 76 SrrvASVPQDTSLSFEFDVRqvvEMGRTPHRSRFDTWTETDRAA--VERAMERTGVAQFADRPVTSL-----SGGERQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 634 NVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMyKMFDDMIILAKGGLT 704
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAA-RYCDELVLLADGRVR 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
479-706 |
2.15e-14 |
|
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: 77.39 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 479 RPVIEVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGkATGCTRtGLILING---RNDSINS 555
Cdd:TIGR01842 312 EPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVG-IWPPTS-GSVRLDGadlKQWDRET 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 556 YKKITGFVPQD-DVVHGnlTVEENL-RFsarcrlsaymskaDKVLIIERVIES----------LGLQHVRDSLVGTiEKR 623
Cdd:TIGR01842 390 FGKHIGYLPQDvELFPG--TVAENIaRF-------------GENADPEKIIEAaklagvheliLRLPDGYDTVIGP-GGA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 624 GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTmyKMFDDMIILAKGGL 703
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLL--GCVDKILVLQDGRI 531
|
...
gi 1063705934 704 TVY 706
Cdd:TIGR01842 532 ARF 534
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
491-656 |
2.65e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.49 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHK-----HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN-----DSINSYKK 558
Cdd:COG1126 2 IEIENLHKsfgdlEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLleEPDS----GTITVDGEDltdskKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 559 ITGFVPQddvvHGNL----TVEEN----LRFSARcrlsayMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQR 630
Cdd:COG1126 78 KVGMVFQ----QFNLfphlTVLENvtlaPIKVKK------MSKAEAEERAMELLERVGLADKADAYPAQL-----SGGQQ 142
|
170 180
....*....|....*....|....*.
gi 1063705934 631 KRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
478-660 |
2.73e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 478 TRPVIEVafKDLTLTLkGKhKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKAT---GCTRTGLILINGRN---- 550
Cdd:PRK14239 2 TEPILQV--SDLSVYY-NK-KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpEVTITGSIVYNGHNiysp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 551 --DSINSYKKItGFVPQddvvHGN---LTVEENLRFSARCRlsaymSKADKVLIIERVIESLG----LQHVRDSLVGTie 621
Cdd:PRK14239 78 rtDTVDLRKEI-GMVFQ----QPNpfpMSIYENVVYGLRLK-----GIKDKQVLDEAVEKSLKgasiWDEVKDRLHDS-- 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063705934 622 KRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASS 660
Cdd:PRK14239 146 ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISA 184
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
491-713 |
2.79e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.48 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKAT------GCTRTGLILINGRN-DSINSYK--KITG 561
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprGARVTGDVTLNGEPlAAIDAPRlaRLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 562 FVPQddvvhgnlTVEENLRFSAR----------CRLSAYMSKADKVlIIERVIESLGlqhvRDSLVGTiEKRGISGGQRK 631
Cdd:PRK13547 87 VLPQ--------AAQPAFAFSAReivllgryphARRAGALTHRDGE-IAWQALALAG----ATALVGR-DVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 632 RVNVGV---------EMVMEPSLLILDEPTTGLDSASSQLLL---RALRREALEGVniCMVVHQPSytMYKMFDDMIILA 699
Cdd:PRK13547 153 RVQFARvlaqlwpphDAAQPPRYLLLDEPTAALDLAHQHRLLdtvRRLARDWNLGV--LAIVHDPN--LAARHADRIAML 228
|
250
....*....|....
gi 1063705934 700 KGGLTVYHGSVKKI 713
Cdd:PRK13547 229 ADGAIVAHGAPADV 242
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
486-656 |
2.93e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKHkhILRSVTGKIMPG-RVsAVMGPSGAGKTTFLSALAG--KATGctrtGLIlingrndSINSYKKItGF 562
Cdd:COG0488 1 LENLSKSFGGRP--LLDDVSLSINPGdRI-GLVGRNGAGKSTLLKILAGelEPDS----GEV-------SIPKGLRI-GY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 563 VPQDDVVHGNLTVEENLR---------FSARCRLSAYMSKADKVLI--------------------IERVIESLGLQHV- 612
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLdgdaelralEAELEELEAKLAEPDEDLErlaelqeefealggweaearAEEILSGLGFPEEd 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063705934 613 RDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:COG0488 146 LDRPVSEL-----SGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
501-682 |
3.50e-14 |
|
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: 73.27 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRndsinsykKITGFVPQDDVVHGN------LT 574
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQ--PTSGGVILEGK--------QITEPGPDRMVVFQNysllpwLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 575 VEENLRFSARCRLsAYMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTG 654
Cdd:TIGR01184 71 VRENIALAVDRVL-PDLSKSERRAIVEEHIALVGLTEAADKRPGQL-----SGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180
....*....|....*....|....*....
gi 1063705934 655 LDSASSQLLLRALRREALE-GVNICMVVH 682
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEhRVTVLMVTH 173
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
501-739 |
3.54e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.96 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGR-----NDSINSYKKITGFVPQ--DDVVHG 571
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGilKPT----SGEVLIKGEpikydKKSLLEVRKTVGIVFQnpDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 572 NlTVEENLRFSArcrLSAYMSKADkvlIIERVIESLGlqhvRDSLVGTIEK--RGISGGQRKRVNVGVEMVMEPSLLILD 649
Cdd:PRK13639 94 P-TVEEDVAFGP---LNLGLSKEE---VEKRVKEALK----AVGMEGFENKppHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 650 EPTTGLDSASSQLLLRALRREALEGVNICMVVHQ----PSYTmykmfDDMIILAKGGLtVYHGSVKKIeeyFADIGITVP 725
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvdlvPVYA-----DKVYVMSDGKI-IKEGTPKEV---FSDIETIRK 233
|
250
....*....|....*.
gi 1063705934 726 DRVNPP--DHYIDILE 739
Cdd:PRK13639 234 ANLRLPrvAHLIEILN 249
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
510-684 |
5.16e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 510 PGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNdsINSykkitgfvpQDDVVHGN-------------LTVE 576
Cdd:PRK13538 26 AGELVQIEGPNGAGKTSLLRILAGLAR--PDAGEVLWQGEP--IRR---------QRDEYHQDllylghqpgikteLTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 577 ENLRFSarCRLSAYMSKADKVLIIERVieslGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:PRK13538 93 ENLRFY--QRLHGPGDDEALWEALAQV----GLAGFEDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190
....*....|....*....|....*....|.
gi 1063705934 657 SASSQLLLRALRREALEGvniCMVV---HQP 684
Cdd:PRK13538 162 KQGVARLEALLAQHAEQG---GMVIlttHQD 189
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
467-715 |
5.84e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 467 VISMATDTEMRTRPVIEvAFkdlTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILI 546
Cdd:COG2401 16 VYSSVLDLSERVAIVLE-AF---GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 547 N----GRNDSInsykkITGFVPQDDVVhgnltveENLRFSARCRLSaymskaDKVLIIERVIEslglqhvrdslvgtiek 622
Cdd:COG2401 92 PdnqfGREASL-----IDAIGRKGDFK-------DAVELLNAVGLS------DAVLWLRRFKE----------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 623 rgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHQpsYTMYK-MFDDMIIlak 700
Cdd:COG2401 137 --LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHH--YDVIDdLQPDLLI--- 209
|
250
....*....|....*
gi 1063705934 701 gglTVYHGSVKKIEE 715
Cdd:COG2401 210 ---FVGYGGVPEEKR 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
494-669 |
6.80e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 72.97 E-value: 6.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 494 KGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG---KATGCtrtglILINGRndsinsykKITG------FVP 564
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGflaPSSGE-----ITLDGV--------PVTGpgadrgVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 565 QDDVVHGNLTVEENLRFSARCRlsaYMSKADKVLIIERVIESLGLQHVrdslvgtiEKRGI---SGGQRKRVNVGVEMVM 641
Cdd:COG4525 83 QKDALLPWLNVLDNVAFGLRLR---GVPKAERRARAEELLALVGLADF--------ARRRIwqlSGGMRQRVGIARALAA 151
|
170 180 190
....*....|....*....|....*....|..
gi 1063705934 642 EPSLLILDEPTTGLDSAS----SQLLLRALRR 669
Cdd:COG4525 152 DPRFLLMDEPFGALDALTreqmQELLLDVWQR 183
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
484-668 |
7.67e-14 |
|
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: 72.12 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGK-HKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRndSINSYK--- 557
Cdd:cd03248 12 VKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfyQPQG----GQVLLDGK--PISQYEhky 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 --KITGFVPQDDVVHGNlTVEENLRFS-ARCRLSAYMSKADKVLIIERVIEslgLQHVRDSLVGtiEKRG-ISGGQRKRV 633
Cdd:cd03248 86 lhSKVSLVGQEPVLFAR-SLQDNIAYGlQSCSFECVKEAAQKAHAHSFISE---LASGYDTEVG--EKGSqLSGGQKQRV 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1063705934 634 NVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALR 668
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALY 194
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
483-669 |
8.53e-14 |
|
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: 75.63 E-value: 8.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTfLSALAgkatgcTR-----TGLILING---RNDSIN 554
Cdd:COG5265 357 EVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKST-LARLL------FRfydvtSGRILIDGqdiRDVTQA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 555 SYKKITGFVPQDDVVHgNLTVEENLRFSarcRLSAymSKADkvliIERV---------IESL--GLqhvrDSLVGtieKR 623
Cdd:COG5265 429 SLRAAIGIVPQDTVLF-NDTIAYNIAYG---RPDA--SEEE----VEAAaraaqihdfIESLpdGY----DTRVG---ER 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063705934 624 G--ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRR 669
Cdd:COG5265 492 GlkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE 539
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
494-682 |
9.37e-14 |
|
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: 71.98 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 494 KGKHKHI--LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGR---NDSINSYKKITGFVPQDDV 568
Cdd:cd03267 28 KRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQ--PTSGEVRVAGLvpwKRRKKFLRRIGVVFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 569 VHGNLTVEENLRFSARC-RLSAYMSKADkvliIERVIESLGLQHVRDSLVgtiekRGISGGQRKRVNVGVEMVMEPSLLI 647
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIyDLPPARFKKR----LDELSELLDLEELLDTPV-----RQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063705934 648 LDEPTTGLDsASSQLLLRALRRE--ALEGVNICMVVH 682
Cdd:cd03267 177 LDEPTIGLD-VVAQENIRNFLKEynRERGTTVLLTSH 212
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
487-684 |
1.22e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.02 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG----KATGctrtGLILINGRNdsinsykkITGF 562
Cdd:COG0396 4 KNLHVSVEGKE--ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkyEVTS----GSILLDGED--------ILEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 563 VPQDDVVHG------------NLTVEENLRFSARCRLSAYMSKADKVLIIERVIESLGLqhvRDSLVgtieKR----GIS 626
Cdd:COG0396 70 SPDERARAGiflafqypveipGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGL---DEDFL----DRyvneGFS 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 627 GGQRKRVnvgvEM----VMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQP 684
Cdd:COG0396 143 GGEKKRN----EIlqmlLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
476-744 |
1.32e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 476 MRTRPVIEvaFKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgCTRtGLILINGRNdsins 555
Cdd:PRK09452 9 SSLSPLVE--LRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFET-PDS-GRIMLDGQD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 556 ykkITGFVPQDDVVHG---------NLTVEENLRFSARcrlsayMSKADKVLIIERVIESLGLQHvrdsLVGTIEKR--G 624
Cdd:PRK09452 78 ---ITHVPAENRHVNTvfqsyalfpHMTVFENVAFGLR------MQKTPAAEITPRVMEALRMVQ----LEEFAQRKphQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 625 ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLD---SASSQLLLRALRREAleGVNICMVVH--QPSYTMykmfDDMIILA 699
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklRKQMQNELKALQRKL--GITFVFVTHdqEEALTM----SDRIVVM 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705934 700 KGGLTVYHGSVKKIEE---------YFADIGI---TVPDRVNpPDHYIDILEGIVKP 744
Cdd:PRK09452 219 RDGRIEQDGTPREIYEepknlfvarFIGEINIfdaTVIERLD-EQRVRANVEGRECN 274
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
475-743 |
1.33e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.09 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 475 EMRTRPVIEvaFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGR--- 549
Cdd:PRK13648 1 MEDKNSIIV--FKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGieKVK----SGEIFYNNQait 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 550 NDSINSYKKITGFVPQDDvvhGNLTVEENLRFSARCRLSAYMSKADKVL-IIERVIESLGLQHVRDSlvgtiEKRGISGG 628
Cdd:PRK13648 75 DDNFEKLRKHIGIVFQNP---DNQFVGSIVKYDVAFGLENHAVPYDEMHrRVSEALKQVDMLERADY-----EPNALSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 629 QRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRR-EALEGVNICMVVHQPSYTMYKmfDDMIILAKGglTVYH 707
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKvKSEHNITIISITHDLSEAMEA--DHVIVMNKG--TVYK 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1063705934 708 -GSVKKI---EEYFADIGITVP--DRVNP----PDHYIDiLEGIVK 743
Cdd:PRK13648 223 eGTPTEIfdhAEELTRIGLDLPfpIKINQmlghQTSFLT-YEGLVD 267
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
491-682 |
1.33e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSYKKIT---GFVPQDD 567
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT--PAHGHVWLDGEHIQHYASKEVArriGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 568 VVHGNLTVEEnlrFSARCR-----LSAYMSKADKVlIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVME 642
Cdd:PRK10253 91 TTPGDITVQE---LVARGRyphqpLFTRWRKEDEE-AVTKAMQATGITHLADQSVDTL-----SGGQRQRAWIAMVLAQE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063705934 643 PSLLILDEPTTGLDsASSQL----LLRALRREalEGVNICMVVH 682
Cdd:PRK10253 162 TAIMLLDEPTTWLD-ISHQIdlleLLSELNRE--KGYTLAAVLH 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
495-683 |
1.33e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.92 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 495 GKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTrtGLILINGRNDSInsykkitgfVPQDDvvhGNLT 574
Cdd:PRK10619 16 GEHE-VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSE--GSIVVNGQTINL---------VRDKD---GQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 575 V--EENLRFsARCRLS---------AYMSKADKVLiiERVIESLGL--QHVRDSLVGTIEKRGI------------SGGQ 629
Cdd:PRK10619 81 VadKNQLRL-LRTRLTmvfqhfnlwSHMTVLENVM--EAPIQVLGLskQEARERAVKYLAKVGIderaqgkypvhlSGGQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063705934 630 RKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQ 683
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
497-714 |
2.07e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 497 HKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGL-ILINGRN--------DSINSYKKITGFVPQDD 567
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShIELLGRTvqregrlaRDIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 568 VVHGNLTVEENLRFSA-------RCRLSaYMSKADKvliiERVIESL---GLQHVRDSLVGTIekrgiSGGQRKRVNVGV 637
Cdd:PRK09984 96 NLVNRLSVLENVLIGAlgstpfwRTCFS-WFTREQK----QRALQALtrvGMVHFAHQRVSTL-----SGGQQQRVAIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705934 638 EMVMEPSLLILDEPTTGLDSASSQLLLRALRR-EALEGVNICMVVHQPSYTMykMFDDMIILAKGGLTVYHGSVKKIE 714
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYAL--RYCERIVALRQGHVFYDGSSQQFD 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
501-682 |
2.25e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSYKK-----ItGFVPQDDVVHGNL 573
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGvyQPDS----GEILLDGEPVRFRSPRDaqaagI-AIIHQELNLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 574 TVEENL---RFSARCRL---SAYMSKADKVLiierviESLGLqHVR-DSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLL 646
Cdd:COG1129 95 SVAENIflgREPRRGGLidwRAMRRRARELL------ARLGL-DIDpDTPVGDL-----SVAQQQLVEIARALSRDARVL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063705934 647 ILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
481-670 |
2.56e-13 |
|
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: 72.39 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 481 VIEVafKDLTLTLKGKHK--HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGCTrTGLILINGRN------ 550
Cdd:COG0444 1 LLEV--RNLKVYFPTRRGvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllPPPGIT-SGEILFDGEDllklse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 551 DSINSY--KKItGFVPQD-----DVVHgnlTVEENLRFSARCRLSayMSKADkvlIIERVIESLglqhvrdSLVGtI--- 620
Cdd:COG0444 78 KELRKIrgREI-QMIFQDpmtslNPVM---TVGDQIAEPLRIHGG--LSKAE---ARERAIELL-------ERVG-Lpdp 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 621 EKRG------ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDsASSQL----LLRALRRE 670
Cdd:COG0444 141 ERRLdrypheLSGGMRQRVMIARALALEPKLLIADEPTTALD-VTIQAqilnLLKDLQRE 199
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
484-705 |
2.69e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.89 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTltlkgKH---KHILRSVTGKIMPGRVSAVMGPSGAGKTTFL---SALAGKATGCTRTGLILINGRNDSINSYK 557
Cdd:PRK09493 2 IEFKNVS-----KHfgpTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEEITSGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KITGFVPQDDVVHGNLTVEENLRFSARcRLSAyMSKADKVLIIERVIESLGLQ----HVRDSLvgtiekrgiSGGQRKRV 633
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGPL-RVRG-ASKEEAEKQARELLAKVGLAerahHYPSEL---------SGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 634 NVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMyKMFDDMIILAKGGLTV 705
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAE-KVASRLIFIDKGRIAE 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
486-683 |
4.15e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.34 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKHKHILrSVTGKIMPGRVS---------AVMGPSGAGKTTFLSALAGKAtgcTRTGLILING---RNDSI 553
Cdd:PRK11174 343 ASNDPVTIEAEDLEIL-SPDGKTLAGPLNftlpagqriALVGPSGAGKTSLLNALLGFL---PYQGSLKINGielRELDP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 554 NSYKKITGFVPQD-DVVHGnlTVEENLRFSarcRLSAYMSKADKVLIIERVIE-----SLGLQHvrdslvgTIEKR--GI 625
Cdd:PRK11174 419 ESWRKHLSWVGQNpQLPHG--TLRDNVLLG---NPDASDEQLQQALENAWVSEflpllPQGLDT-------PIGDQaaGL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALrREALEGVNICMVVHQ 683
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL-NAASRRQTTLMVTHQ 543
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
484-702 |
5.73e-13 |
|
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: 69.04 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKH---ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKatgctrtgLILINGrndSINSYKKIt 560
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGE--------LEKLSG---SVSVPGSI- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 561 GFVPQDDVVHgNLTVEENLRFSARCRLSAYmskadkvliiERVIESLGLQhvRD---------SLVGtieKRGI--SGGQ 629
Cdd:cd03250 69 AYVSQEPWIQ-NGTIRENILFGKPFDEERY----------EKVIKACALE--PDleilpdgdlTEIG---EKGInlSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705934 630 RKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLL-RALRREALEGVNICMVVHQPSYTMYKmfdDMIILAKGG 702
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPHA---DQIVVLDNG 203
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
491-682 |
7.72e-13 |
|
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: 67.45 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHK-----HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSykkitgfv 563
Cdd:cd03216 1 LELRGITKrfggvKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlyKPDS----GEILVDGKEVSFAS-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 564 PQDDVVHGnltveenlrfsarcrlsaymskadkvliiervieslglqhvrdslVGTIEKrgISGGQRKRVNVGVEMVMEP 643
Cdd:cd03216 69 PRDARRAG---------------------------------------------IAMVYQ--LSVGERQMVEIARALARNA 101
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063705934 644 SLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISH 140
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
479-680 |
8.57e-13 |
|
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: 67.84 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 479 RPVIEV-------AFKDLTLTLKgkhkhilrsvtgkimPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRND 551
Cdd:cd03215 2 EPVLEVrglsvkgAVRDVSFEVR---------------AGEIVGIAGLVGNGQTELAEALFGLRP--PASGEITLDGKPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 552 SINSYKKIT----GFVPQDDVVHG---NLTVEENLrfSARCRLSaymskadkvliiervieslglqhvrdslvgtiekrg 624
Cdd:cd03215 65 TRRSPRDAIragiAYVPEDRKREGlvlDLSVAENI--ALSSLLS------------------------------------ 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 625 isGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMV 680
Cdd:cd03215 107 --GGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLI 160
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
513-680 |
8.81e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 513 VSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGR--NDS---IN--SYKKITGFVPQDDVVHGNLTVEENLRFSarc 585
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTR--PQKGRIVLNGRvlFDAekgIClpPEKRRIGYVFQDARLFPHYKVRGNLRYG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 586 rlsayMSKADKVLIiERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLR 665
Cdd:PRK11144 101 -----MAKSMVAQF-DKIVALLGIEPLLDRYPGSL-----SGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170
....*....|....*
gi 1063705934 666 ALRREALEgVNICMV 680
Cdd:PRK11144 170 YLERLARE-INIPIL 183
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
498-684 |
9.68e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.69 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG----KATGCTRTGLILINGRN----DSINSYKKItGFVPQDDVV 569
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiYDSKIKVDGKVLYFGKDifqiDAIKLRKEV-GMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 570 HGNLTVEENLRFSARCRlsAYMSKADKVLIIERVIESLGL-QHVRDSLVGTIEKrgISGGQRKRVNVGVEMVMEPSLLIL 648
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSH--GIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQ--LSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063705934 649 DEPTTGLDSASSQL---LLRALRREalegVNICMVVHQP 684
Cdd:PRK14246 178 DEPTSMIDIVNSQAiekLITELKNE----IAIVIVSHNP 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
484-725 |
1.34e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.44 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG----KATGCTRTGLILINGRNDSINSYKKI 559
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 TGFVPQD-DVVHGNLTVEENLRFSARCRlsaYMSKADKVLIIERVIESLGLQHVRDSlvgtiEKRGISGGQRKRVNVGVE 638
Cdd:PRK13640 86 VGIVFQNpDNQFVGATVGDDVAFGLENR---AVPRPEMIKIVRDVLADVGMLDYIDS-----EPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 639 MVMEPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHQPSYTmyKMFDDMIILAKGGLtVYHGSVKKI---E 714
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA--NMADQVLVLDDGKL-LAQGSPVEIfskV 234
|
250
....*....|.
gi 1063705934 715 EYFADIGITVP 725
Cdd:PRK13640 235 EMLKEIGLDIP 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
486-706 |
1.52e-12 |
|
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: 68.33 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSInsykkI---T 560
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiyPPD----SGTVTVRGRVSSL-----LglgG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 561 GFvpqddvvHGNLTVEENLRFsaRCRLSAyMSKADKVLIIERVIESLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMV 640
Cdd:cd03220 94 GF-------NPELTGRENIYL--NGRLLG-LSRKEIDEKIDEIIEFSELGDFIDLPVKT-----YSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 641 MEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSyTMYKMFDDMIILAKGGLTVY 706
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS-SIKRLCDRALVLEKGKIRFD 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
497-669 |
1.52e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.11 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 497 HKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDS-INSYKKITGFVPQDDVVHGNLTV 575
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEH--QTSGHIRFHGTDVSrLHARDRKVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EENLRFS-----ARCRLSAYMSKAdKVLiieRVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDE 650
Cdd:PRK10851 92 FDNIAFGltvlpRRERPNAAAIKA-KVT---QLLEMVQLAHLADRYPAQL-----SGGQKQRVALARALAVEPQILLLDE 162
|
170
....*....|....*....
gi 1063705934 651 PTTGLDSASSQLLLRALRR 669
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQ 181
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
496-713 |
1.78e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 496 KHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSI----NSYKKITGFVPQDDVVHG 571
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP--RDAGNIIIDDEDISLlplhARARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 572 NLTVEENLRfsARCRLSAYMSKADKVLIIERVIESLGLQHVRDSLvgtieKRGISGGQRKRVNVGVEMVMEPSLLILDEP 651
Cdd:PRK10895 92 RLSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 652 TTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMyKMFDDMIILAKGGLtVYHGSVKKI 713
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHL-IAHGTPTEI 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
508-683 |
2.85e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.68 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 508 IMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINS-YKKITGFVPQDDVVHGNLTVEEN--LRFSAR 584
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLT--PASGSLTLNGQDHTTTPpSRRPVSMLFQENNLFSHLTVAQNigLGLNPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 585 CRLSAYmSKADKVLIIERVieslGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSassqlll 664
Cdd:PRK10771 100 LKLNAA-QREKLHAIARQM----GIEDLLARLPGQ-----LSGGQRQRVALARCLVREQPILLLDEPFSALDP------- 162
|
170 180
....*....|....*....|....*...
gi 1063705934 665 rALRREALEGVN-IC--------MVVHQ 683
Cdd:PRK10771 163 -ALRQEMLTLVSqVCqerqltllMVSHS 189
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
501-706 |
3.40e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGctrTGLILINGRN---DSINSYKKITGFVPQDDVVHGNLTVEE 577
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG---SGSIQFAGQPleaWSAAELARHRAYLSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NLRFSarcrLSAYMSKADKVLIIERVIESLGLQHVRDSLVGTiekrgISGGQRKRVN-VGVEMVMEPS------LLILDE 650
Cdd:PRK03695 89 YLTLH----QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQ-----LSGGEWQRVRlAAVVLQVWPDinpagqLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 651 PTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTmYKMFDDMIILAKGGLTVY 706
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHT-LRHADRVWLLKQGKLLAS 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
482-753 |
5.43e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.74 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVAFKDLTLTLKGK---HKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KAT-GCTRTG--LILINGRNDSI 553
Cdd:PRK13634 1 MDITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGllQPTsGTVTIGerVITAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 554 NSYKKITGFV---PQDDVVHGnlTVEENLRFSArcrLSAYMSKADKVLIIERVIESLGLQHvrdslvgTIEKRG---ISG 627
Cdd:PRK13634 81 KPLRKKVGIVfqfPEHQLFEE--TVEKDICFGP---MNFGVSEEDAKQKAREMIELVGLPE-------ELLARSpfeLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 628 GQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLR---ALRREAleGVNICMVVHQ----PSYTmykmfDDMIILAK 700
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHKEK--GLTTVLVTHSmedaARYA-----DQIVVMHK 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705934 701 GGLtVYHGSVKKI---EEYFADIGITVPDRVNppdhYIDILE---GIVKPDGDITIEQL 753
Cdd:PRK13634 222 GTV-FLQGTPREIfadPDELEAIGLDLPETVK----FKRALEekfGISFPKPCLTLEEL 275
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
484-682 |
6.34e-12 |
|
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: 66.56 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLKGKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALagkatgcTR-----TGLILINGRN----DSIN 554
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-------NRlieptSGEIFIDGEDireqDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 555 SYKKItGFVPQDDVVHGNLTVEENLRfsarcrLSAYMSKADKVLIIERVIESLGLQHVRDSLVGTIEKRGISGGQRKRVN 634
Cdd:cd03295 73 LRRKI-GYVIQQIGLFPHMTVEENIA------LVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 635 VGVEMVMEPSLLILDEPTTGLDS---ASSQLLLRALRREAleGVNICMVVH 682
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPitrDQLQEEFKRLQQEL--GKTIVFVTH 194
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
483-667 |
1.21e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.51 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALagkatgcTR-----TGLILINGRNdsINSYK 557
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLL-------TRfydidEGEILLDGHD--LRDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 -----KITGFVPQDdvVH-GNLTVEENLRFSARCRLSAY-MSKADKVLIIERVIEslGLQHVRDSLVGtieKRGI--SGG 628
Cdd:PRK11176 412 laslrNQVALVSQN--VHlFNDTIANNIAYARTEQYSREqIEEAARMAYAMDFIN--KMDNGLDTVIG---ENGVllSGG 484
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063705934 629 QRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRAL 667
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL 523
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
481-708 |
1.28e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.30 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 481 VIEVafKDLTLTLKgKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSYKKIT 560
Cdd:PRK13647 4 IIEV--EDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYL--PQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 561 GFV------PQDDVVHGnlTVEENLRFSAR-CRLSAymskaDKVLiiERVIESL---GLQHVRDSlvgtiEKRGISGGQR 630
Cdd:PRK13647 79 SKVglvfqdPDDQVFSS--TVWDDVAFGPVnMGLDK-----DEVE--RRVEEALkavRMWDFRDK-----PPYHLSYGQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705934 631 KRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMykMFDDMIILAKGGLTVYHG 708
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA--EWADQVIVLKEGRVLAEG 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
500-683 |
1.40e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSYKKITGF----VPQDDVVHGNLTV 575
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP--PDSGTLEIGGNPCARLTPAKAHQLgiylVPQEPLLFPNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EENLRFsarcRLSAYMSKADKVliiERVIESLGLQHVRDSLVGTIEKrgisgGQRKRVNVGVEMVMEPSLLILDEPTTGL 655
Cdd:PRK15439 104 KENILF----GLPKRQASMQKM---KQLLAALGCQLDLDSSAGSLEV-----ADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180
....*....|....*....|....*...
gi 1063705934 656 DSASSQLLLRALRREALEGVNICMVVHQ 683
Cdd:PRK15439 172 TPAETERLFSRIRELLAQGVGIVFISHK 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
506-736 |
1.46e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 506 GKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRndsInSYKkitgfvPQ---DDVvhgNLTVEENLR 580
Cdd:PRK13409 360 GEIYEGEVIGIVGPNGIGKTTFAKLLAGvlKPDE----GEVDPELK---I-SYK------PQyikPDY---DGTVEDLLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 581 FSArcrlSAYMSKADKVLIIERviesLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASS 660
Cdd:PRK13409 423 SIT----DDLGSSYYKSEIIKP----LQLERLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 661 QLLLRALRREALEGVNICMVVHQPSYtMYKMFDDMIILAKGGLTVY---HGSVKKIE---EYFADIGITV---PD----R 727
Cdd:PRK13409 490 LAVAKAIRRIAEEREATALVVDHDIY-MIDYISDRLMVFEGEPGKHghaSGPMDMREgmnRFLKELGITFrrdEEtgrpR 568
|
....*....
gi 1063705934 728 VNPPDHYID 736
Cdd:PRK13409 569 VNKPGSYLD 577
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
494-720 |
1.64e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.49 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 494 KGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRndsinsykkI-------TGFvp 564
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGilEPT----SGRVEVNGR---------VsallelgAGF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 565 qddvvHGNLTVEENLRFSARcrlsAY-MSKADKVLIIERVIESLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEP 643
Cdd:COG1134 100 -----HPELTGRENIYLNGR----LLgLSRKEIDEKFDEIVEFAELGDFIDQPVKT-----YSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705934 644 SLLILDEPT-TGlDSASSQLLLRALRREALEGVNICMVVHQPSyTMYKMFDDMIILAKGGLtVYHGSVKK-IEEYFADI 720
Cdd:COG1134 166 DILLVDEVLaVG-DAAFQKKCLARIRELRESGRTVIFVSHSMG-AVRRLCDRAIWLEKGRL-VMDGDPEEvIAAYEALL 241
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
501-701 |
2.53e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILINGRNDSINSYKKI----TGFVPQDDVVHGNLT 574
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGdpRAT----SGRIVFDGKDITDWQTAKImreaVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 575 VEENLR----FSARcrlSAYMSKadkvliIERVIESLG-LQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILD 649
Cdd:PRK11614 97 VEENLAmggfFAER---DQFQER------IKWVYELFPrLHERRIQRAGTM-----SGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 650 EPTTGLDSASSQLLLRALRREALEGVNIcMVVHQPSYTMYKMFDDMIILAKG 701
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTI-FLVEQNANQALKLADRGYVLENG 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
501-682 |
4.07e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.15 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG---KATGCTRTGLILING--RNDSINSYKKITGFV---PQDDVVHGn 572
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGlhvPTQGSVRVDDTLITStsKNKDIKQIRKKVGLVfqfPESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 573 lTVEENLRFSARcrlSAYMSKADKVLIIErviESLGLQHVRDSLvgtIEKR--GISGGQRKRVNVGVEMVMEPSLLILDE 650
Cdd:PRK13649 102 -TVLKDVAFGPQ---NFGVSQEEAEALAR---EKLALVGISESL---FEKNpfELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190
....*....|....*....|....*....|..
gi 1063705934 651 PTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
486-709 |
5.57e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.39 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALagkatgcTR-----TGLILINGRNdsINSY---- 556
Cdd:PRK11160 341 LNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL-------TRawdpqQGEILLNGQP--IADYseaa 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 -KKITGFVPQDdvVH-GNLTVEENLRFSARcrlsaymSKADKVLIieRVIESLGLqhvrDSLVGTIEK---------RGI 625
Cdd:PRK11160 412 lRQAISVVSQR--VHlFSATLRDNLLLAAP-------NASDEALI--EVLQQVGL----EKLLEDDKGlnawlgeggRQL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREAlEGVNICMVVHQpSYTMYKMfdDMIILAKGGLTV 705
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHR-LTGLEQF--DRICVMDNGQII 552
|
....
gi 1063705934 706 YHGS 709
Cdd:PRK11160 553 EQGT 556
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
483-670 |
5.77e-11 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C 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-resistance 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: 213211 [Multi-domain] Cd Length: 221 Bit Score: 63.28 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTrtGLILINGRNdsINSY------ 556
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSS--GSILIDGVD--ISKIglhdlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 KKITgFVPQDDVVHGNlTVEENLRFSARCRLSAYMSKADKVLIIERVIESLGLqhvrdsLVGTIEKRG--ISGGQRKRVN 634
Cdd:cd03244 78 SRIS-IIPQDPVLFSG-TIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGG------LDTVVEEGGenLSVGQRQLLC 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063705934 635 VGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRRE 670
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTIREA 185
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
498-671 |
6.02e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.95 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSYKKitGFVPQDDVVHGNLTVEE 577
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP--YQHGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NLRFSARCrlsAYMSKADKVLIIERVIESLGLQHVrdslvgtiEKRGI---SGGQRKRVNVGVEMVMEPSLLILDEPTTG 654
Cdd:PRK11248 90 NVAFGLQL---AGVEKMQRLEIAHQMLKKVGLEGA--------EKRYIwqlSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180
....*....|....*....|.
gi 1063705934 655 LDSASSQ----LLLRALRREA 671
Cdd:PRK11248 159 LDAFTREqmqtLLLKLWQETG 179
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
482-682 |
6.64e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.72 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVafKDLTLTLKGK---HKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALagKATGCTRTGLILINGRNDSINSYKK 558
Cdd:PRK13651 3 IKV--KNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHL--NALLLPDTGTIEWIFKDEKNKKKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 559 ITGFVPQDDVVHGNL----------------------------TVEENLRFSARcrlSAYMSKADKVLIIERVIESLGLQ 610
Cdd:PRK13651 79 EKEKVLEKLVIQKTRfkkikkikeirrrvgvvfqfaeyqlfeqTIEKDIIFGPV---SMGVSKEEAKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705934 611 hvrdslVGTIEKR--GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:PRK13651 156 ------ESYLQRSpfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
482-751 |
6.88e-11 |
|
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: 65.98 E-value: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 482 IEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILINGRNDSINSYKKITG 561
Cdd:TIGR03269 1 IEV--KNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 562 FVPQDDVVHGNLTVEENLRF-----SARCRLS---AYMSKADKVL-----IIERVIESLG----------------LQHV 612
Cdd:TIGR03269 77 KVGEPCPVCGGTLEPEEVDFwnlsdKLRRRIRkriAIMLQRTFALygddtVLDNVLEALEeigyegkeavgravdlIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 613 RDSLVGTIEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALrREALEGVNICMVV--HQPSyTMYK 690
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNAL-EEAVKASGISMVLtsHWPE-VIED 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 691 MFDDMIILAKGGL----------TVYHGSVKKIE-EYFADIGITVPDRVNPPDHYIDILEGIVKPDGDITIE 751
Cdd:TIGR03269 235 LSDKAIWLENGEIkeegtpdevvAVFMEGVSEVEkECEVEVGEPIIKVRNVSKRYISVDRGVVKAVDNVSLE 306
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
501-725 |
7.87e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.30 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILING-----RNDSINSYKKITGFV---PQDDVVH 570
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllKPT----SGKIIIDGvditdKKVKLSDIRKKVGLVfqyPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 571 GnlTVEENLRFSARcRLSayMSKADkvlIIERVIESLglqhvrdSLVG----TIEKRG---ISGGQRKRVNVGVEMVMEP 643
Cdd:PRK13637 99 E--TIEKDIAFGPI-NLG--LSEEE---IENRVKRAM-------NIVGldyeDYKDKSpfeLSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 644 SLLILDEPTTGLDSASSQLLL---RALRREalEGVNICMVVHqpsyTMykmfDDMIILAKGGLTVYHGSVK---KIEEYF 717
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILnkiKELHKE--YNMTIILVSH----SM----EDVAKLADRIIVMNKGKCElqgTPREVF 233
|
250
....*....|....
gi 1063705934 718 ------ADIGITVP 725
Cdd:PRK13637 234 kevetlESIGLAVP 247
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
476-679 |
8.18e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.51 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 476 MRTRPVIEVafKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILINGRNdsins 555
Cdd:CHL00131 2 NKNKPILEI--KNLHASVNENE--ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGES----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 556 ykkITGFVPQDDVVHG------------NLTVEENLRFSARCRLSAY-MSKADKVLIIERVIESLGLQHVRDSLVGTIEK 622
Cdd:CHL00131 73 ---ILDLEPEERAHLGiflafqypieipGVSNADFLRLAYNSKRKFQgLPELDPLEFLEIINEKLKLVGMDPSFLSRNVN 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705934 623 RGISGGQRKRvNVGVEM-VMEPSLLILDEPTTGLDsassqllLRALRREAlEGVNICM 679
Cdd:CHL00131 150 EGFSGGEKKR-NEILQMaLLDSELAILDETDSGLD-------IDALKIIA-EGINKLM 198
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
483-667 |
8.91e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.75 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKhKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALagkatgcTR-----TGLILING---RNDSIN 554
Cdd:PRK13657 334 AVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-------QRvfdpqSGRILIDGtdiRTVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 555 SYKKITGFVPQDDVVHgNLTVEENLRF------SARCRLSAYMSKADKvlIIERviESLGLqhvrDSLVGtieKRG--IS 626
Cdd:PRK13657 406 SLRRNIAVVFQDAGLF-NRSIEDNIRVgrpdatDEEMRAAAERAQAHD--FIER--KPDGY----DTVVG---ERGrqLS 473
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063705934 627 GGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRAL 667
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL 514
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
506-737 |
9.10e-11 |
|
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: 63.58 E-value: 9.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 506 GKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINgrNDSInSYKkitgfvPQDDVVHGNLTVEENLRFSA 583
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGvlKPDE----GDIEIE--LDTV-SYK------PQYIKADYEGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 584 R--CRLSAYMSKADKVLIIERVIEslglQHVRDslvgtiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQ 661
Cdd:cd03237 87 KdfYTHPYFKTEIAKPLQIEQILD----REVPE----------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 662 LLLRALRREALEGVNICMVVHQPSYtMYKMFDDMIILAKGGLTVY------HGSVKKIEEYFADIGITV---PD----RV 728
Cdd:cd03237 153 MASKVIRRFAENNEKTAFVVEHDII-MIDYLADRLIVFEGEPSVNgvanppQSLRSGMNRFLKNLDITFrrdPEtgrpRI 231
|
....*....
gi 1063705934 729 NPPDHYIDI 737
Cdd:cd03237 232 NKLGSVKDR 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
480-736 |
1.31e-10 |
|
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: 65.19 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 480 PVIEVAFKDLTLTLKGkhkhilrsvtGKIMPGRVSAVMGPSGAGKTTFLSALAGKAT---GCTRTGLILingrndsinSY 556
Cdd:COG1245 345 PDLTKSYGGFSLEVEG----------GEIREGEVLGIVGPNGIGKTTFAKILAGVLKpdeGEVDEDLKI---------SY 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 KkitgfvPQDDVVHGNLTVEENLRfsarcrlSAYMSKADKVLIIERVIESLGLQHVRDSLVgtiekRGISGGQRKRVNVG 636
Cdd:COG1245 406 K------PQYISPDYDGTVEEFLR-------SANTDDFGSSYYKTEIIKPLGLEKLLDKNV-----KDLSGGELQRVAIA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 637 VEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHqpSYTMYKMFDDMIILAKGGLTVY---HGSVKK 712
Cdd:COG1245 468 ACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDH--DIYLIDYISDRLMVFEGEPGVHghaSGPMDM 545
|
250 260 270
....*....|....*....|....*....|....
gi 1063705934 713 IE---EYFADIGITV---PD----RVNPPDHYID 736
Cdd:COG1245 546 REgmnRFLKELGITFrrdEEtgrpRINKPGSYLD 579
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
501-682 |
1.44e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSykkitgfvPQDDV------VH-- 570
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGlyQPDS----GEILIDGKPVRIRS--------PRDAIalgigmVHqh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 571 ----GNLTVEENLRFSARCRLSAYMSKADKVLIIERVIESLGLqHVR-DSLVGTiekrgISGGQRKRvnvgVEMV----M 641
Cdd:COG3845 89 fmlvPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGL-DVDpDAKVED-----LSVGEQQR----VEILkalyR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063705934 642 EPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
476-670 |
1.72e-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: 64.71 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 476 MRTRPVIEVafKDLTLTLK--GKHKHILRSVTGKIMPGRVSAVMGPSGAGKT-TFLSAL------AGKATGCtrtglILI 546
Cdd:COG4172 1 MMSMPLLSV--EDLSVAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpdpAAHPSGS-----ILF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 547 NGRN------DSINSY--KKItGFVPQD-----DVVHgnlTVE----ENLRFSARcrlsayMSKADkvlIIERVIESLGL 609
Cdd:COG4172 74 DGQDllglseRELRRIrgNRI-AMIFQEpmtslNPLH---TIGkqiaEVLRLHRG------LSGAA---ARARALELLER 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 610 QHVRDSlvgtiEKR------GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDsASSQL----LLRALRRE 670
Cdd:COG4172 141 VGIPDP-----ERRldayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALD-VTVQAqildLLKDLQRE 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
498-701 |
2.11e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGcTRTGLILINGRndsinsykkiTGFVPQDDVVHgNLTVEE 577
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-AETSSVVIRGS----------VAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NLRFSARCRLSAYMskadkvliieRVIESLGLQHVRDSLVG----TIEKRG--ISGGQRKRVNVGVEMVMEPSLLILDEP 651
Cdd:PLN03232 698 NILFGSDFESERYW----------RAIDVTALQHDLDLLPGrdltEIGERGvnISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063705934 652 TTGLDSASSQLLLRALRREALEGVNICMVVHQPSYtmYKMFDDMIILAKG 701
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF--LPLMDRIILVSEG 815
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
487-656 |
2.17e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.50 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILINGRNdsinsykkITGFVPQD 566
Cdd:PRK09580 5 KDLHVSVEDKA--ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKD--------LLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 567 DV----------------VHGNLTVEENLRFSARCRLSAYMSKADKVLIIERVIESLGLQhvRDSLVGTIEKrGISGGQR 630
Cdd:PRK09580 75 RAgegifmafqypveipgVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMP--EDLLTRSVNV-GFSGGEK 151
|
170 180
....*....|....*....|....*.
gi 1063705934 631 KRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLD 177
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
478-663 |
2.67e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 64.36 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 478 TRPVIEVaFKDLTLTLKgkhkhilrsvtgkimPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILING---RNDS 552
Cdd:TIGR00958 490 NRPDVPV-LKGLTFTLH---------------PGEVVALVGPSGSGKSTVAALLQNlyQPTG----GQVLLDGvplVQYD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 553 INSYKKITGFVPQDDVVHGNlTVEENLRFSARCRLSAYMSKADKVLIIERVIesLGLQHVRDSLVGtiEKRG-ISGGQRK 631
Cdd:TIGR00958 550 HHYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFI--MEFPNGYDTEVG--EKGSqLSGGQKQ 624
|
170 180 190
....*....|....*....|....*....|..
gi 1063705934 632 RVNVGVEMVMEPSLLILDEPTTGLDSASSQLL 663
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
491-725 |
3.10e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.33 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG-------------KATGCTRTGLILIngRNDSINSYK 557
Cdd:PRK13638 7 LWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllrpqkgavlwqgKPLDYSKRGLLAL--RQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KitgfvPQDDVVHGNltVEENLRFSARcrlSAYMSKADkvlIIERVIESLGL---QHVRDSLVgtiekRGISGGQRKRVN 634
Cdd:PRK13638 85 D-----PEQQIFYTD--IDSDIAFSLR---NLGVPEAE---ITRRVDEALTLvdaQHFRHQPI-----QCLSHGQKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 635 VGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYtMYKMFDDMIILAKGGLTVYH--GSVKK 712
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGapGEVFA 225
|
250
....*....|...
gi 1063705934 713 IEEYFADIGITVP 725
Cdd:PRK13638 226 CTEAMEQAGLTQP 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
498-682 |
3.16e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILING------RNDSINSYKKITGFVPQDDVVHG 571
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIER--PSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 572 NLTVEENLRF----------SARCRLSAYMskaDKVLIIERViESLGLQhvrdslvgtiekrgISGGQRKRVNVGVEMVM 641
Cdd:PRK10908 93 DRTVYDNVAIpliiagasgdDIRRRVSAAL---DKVGLLDKA-KNFPIQ--------------LSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063705934 642 EPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
500-713 |
3.44e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.85 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSA------LAGKATgctRTGLILINGRN----DSINSYKKITgFVPQDDVV 569
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlieLYPEAR---VSGEVYLDGQDifkmDVIELRRRVQ-MVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 570 HGNLTVEENLRFSARC-RLSAymSKADkvlIIERVIESLG----LQHVRDSLVGTIEKrgISGGQRKRVNVGVEMVMEPS 644
Cdd:PRK14247 94 IPNLSIFENVALGLKLnRLVK--SKKE---LQERVRWALEkaqlWDEVKDRLDAPAGK--LSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 645 LLILDEPTTGLD---SASSQLLLRALRREalegVNICMVVHQPSYTmyKMFDDMIILAKGGLTVYHGSVKKI 713
Cdd:PRK14247 167 VLLADEPTANLDpenTAKIESLFLELKKD----MTIVLVTHFPQQA--ARISDYVAFLYKGQIVEWGPTREV 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
500-713 |
3.58e-10 |
|
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: 63.99 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILING---RNDSINSYKKITGFVPQDDVVHGNlTVE 576
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ--ARSGEILLNGfslKDIDRHTLRQFINYLPQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 577 ENLRFSARCRLSAYM-SKADKVLIIERVIE--SLGLQhvrDSLvgTIEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTT 653
Cdd:TIGR01193 566 ENLLLGAKENVSQDEiWAACEIAEIKDDIEnmPLGYQ---TEL--SEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 654 GLDSASSQLLLRALRReaLEGVNICMVVHQpsYTMYKMFDDMIILAKGGLtVYHGSVKKI 713
Cdd:TIGR01193 641 NLDTITEKKIVNNLLN--LQDKTIIFVAHR--LSVAKQSDKIIVLDHGKI-IEQGSHDEL 695
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
463-685 |
4.43e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 463 TFSGVISMATDTEMRTRPVIE-----VAFKDLTLTLkGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG---K 534
Cdd:COG4178 337 GFEEALEAADALPEAASRIETsedgaLALEDLTLRT-PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpY 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 535 ATGCtrtglILINGRNDSInsykkitgFVPQDD-VVHGNLtveenlrfsaRCRLsAYMSKADKV--LIIERVIESLGLQH 611
Cdd:COG4178 416 GSGR-----IARPAGARVL--------FLPQRPyLPLGTL----------REAL-LYPATAEAFsdAELREALEAVGLGH 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705934 612 VRDSLvgTIEK---RGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREaLEGVNICMVVHQPS 685
Cdd:COG4178 472 LAERL--DEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE-LPGTTVISVGHRST 545
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
495-656 |
5.67e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.80 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 495 GKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN---------DSINSYKKITGFVPQ 565
Cdd:COG4161 13 GSHQ-ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLET--PDSGQLNIAGHQfdfsqkpseKAIRLLRQKVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 566 DDVVHGNLTVEENLrFSARCRLsAYMSKADKVLIIERVIESLGLQHVRDSLvgtieKRGISGGQRKRVNVGVEMVMEPSL 645
Cdd:COG4161 90 QYNLWPHLTVMENL-IEAPCKV-LGLSKEQAREKAMKLLARLRLTDKADRF-----PLHLSGGQQQRVAIARALMMEPQV 162
|
170
....*....|.
gi 1063705934 646 LILDEPTTGLD 656
Cdd:COG4161 163 LLFDEPTAALD 173
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
498-685 |
6.92e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.21 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgctRTGLILINGRNDSINS--YKK---ITGFVPQDDVVHGN 572
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE---LESEVRVEGRVEFFNQniYERrvnLNRLRRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 573 -----LTVEENLRFSARcrLSAYMSKADKVLIIERVIESLGLQhvrDSLVGTIEKRGI--SGGQRKRVNVGVEMVMEPSL 645
Cdd:PRK14258 97 pnlfpMSVYDNVAYGVK--IVGWRPKLEIDDIVESALKDADLW---DEIKHKIHKSALdlSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063705934 646 LILDEPTTGLDSASS---QLLLRALR-REALEGVNICMVVHQPS 685
Cdd:PRK14258 172 LLMDEPCFGLDPIASmkvESLIQSLRlRSELTMVIVSHNLHQVS 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
507-755 |
7.84e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.29 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 507 KIMPGRVSAVMGPSGAGKTTFLSALAG---KATGCTRTGLILING--RNDSINSYKKITGFV---PQDDVVHGnlTVEEN 578
Cdd:PRK13643 28 EVKKGSYTALIGHTGSGKSTLLQHLNGllqPTEGKVTVGDIVVSStsKQKEIKPVRKKVGVVfqfPESQLFEE--TVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 579 LRFSARcrlSAYMSKADKVLIIERVIESLGLQHvrdslvGTIEKR--GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:PRK13643 106 VAFGPQ---NFGIPKEKAEKIAAEKLEMVGLAD------EFWEKSpfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 657 SASSQLLLRALRREALEGVNICMVVHqpsyTMYKMFD--DMIILAKGGLTVYHGSVKKIeeyFADIGITVPDRVNPPD-- 732
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTH----LMDDVADyaDYVYLLEKGHIISCGTPSDV---FQEVDFLKAHELGVPKat 249
|
250 260
....*....|....*....|...
gi 1063705934 733 HYIDILEgivkPDGDITIEQLPV 755
Cdd:PRK13643 250 HFADQLQ----KTGAVTFEKLPI 268
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
478-688 |
1.07e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 478 TRPVIEVafKDLTLTLKGkhkhiLRSVTG---KIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGrnds 552
Cdd:PRK11300 2 SQPLLSV--SGLMMRFGG-----LLAVNNvnlEVREQEIVSLIGPNGAGKTTVFNCLTGfyKPTG----GTILLRG---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 553 insyKKITGFVPQDDVVHG------------NLTVEENLR-----------FSARCRLSAYMSKADKVLiiERV---IES 606
Cdd:PRK11300 67 ----QHIEGLPGHQIARMGvvrtfqhvrlfrEMTVIENLLvaqhqqlktglFSGLLKTPAFRRAESEAL--DRAatwLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 607 LGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASS---QLLLRALRREalEGVNICMVVHQ 683
Cdd:PRK11300 141 VGLLEHANRQAGNL-----AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETkelDELIAELRNE--HNVTVLLIEHD 213
|
....*
gi 1063705934 684 PSYTM 688
Cdd:PRK11300 214 MKLVM 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
497-656 |
1.09e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.83 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 497 HKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN-DSINSYKKIT------GFVPQDDVV 569
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT--PTSGDVIFNGQPmSKLSSAAKAElrnqklGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 570 HGNLTVEENLRfsarcrLSAYMSKADKVLIIERVIESLglqhvrdSLVGtIEKRG------ISGGQRKRVNVGVEMVMEP 643
Cdd:PRK11629 99 LPDFTALENVA------MPLLIGKKKPAEINSRALEML-------AAVG-LEHRAnhrpseLSGGERQRVAIARALVNNP 164
|
170
....*....|...
gi 1063705934 644 SLLILDEPTTGLD 656
Cdd:PRK11629 165 RLVLADEPTGNLD 177
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
498-711 |
1.12e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLIlINGRndsinsykkiTGFVPQDDVVHgNLTVEE 577
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-IRGT----------VAYVPQVSWIF-NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NLRFSARCRLSAYmskadkvliiERVIESLGLQHVRDSLVG----TIEKRG--ISGGQRKRVNVGVEMVMEPSLLILDEP 651
Cdd:PLN03130 698 NILFGSPFDPERY----------ERAIDVTALQHDLDLLPGgdltEIGERGvnISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 652 TTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMYKmfdDMIILakggltVYHGSVK 711
Cdd:PLN03130 768 LSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV---DRIIL------VHEGMIK 818
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
508-701 |
1.26e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.27 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 508 IMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSYKK--ITgFVPQDDVVHGNLTVEENLRFSA 583
Cdd:PRK11432 29 IKQGTMVTLLGPSGCGKTTVLRLVAGleKPTE----GQIFIDGEDVTHRSIQQrdIC-MVFQSYALFPHMSLGENVGYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 584 RcrlsayMSKADKVLIIERVIESLGLQhvrdSLVGtIEKR---GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSAss 660
Cdd:PRK11432 104 K------MLGVPKEERKQRVKEALELV----DLAG-FEDRyvdQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063705934 661 qlLLRALR---REALEGVNIC--MVVHQPSyTMYKMFDDMIILAKG 701
Cdd:PRK11432 171 --LRRSMRekiRELQQQFNITslYVTHDQS-EAFAVSDTVIVMNKG 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
486-668 |
1.48e-09 |
|
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: 57.46 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 486 FKDLTLTLKGKHkhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKatgctrtgLILINGrndSINSYKKIT-GFVP 564
Cdd:cd03221 3 LENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE--------LEPDEG---IVTWGSTVKiGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 565 QddvvhgnltveenlrfsarcrlsaymskadkvliiervieslglqhvrdslvgtiekrgISGGQRKRVNVGVEMVMEPS 644
Cdd:cd03221 70 Q-----------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180
....*....|....*....|....
gi 1063705934 645 LLILDEPTTGLDSASSQLLLRALR 668
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALK 114
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
459-667 |
1.52e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 459 NKNLTFSGVISMATDTEMRTRPVIEVaFKDLTLTLKGKhkhilrsvtgkimpgRVSAVMGPSGAGKTTFLSAL------- 531
Cdd:PTZ00265 1158 NKNDIKGKIEIMDVNFRYISRPNVPI-YKDLTFSCDSK---------------KTTAIVGETGSGKSTVMSLLmrfydlk 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 532 ---------------------------------------------AGKATGCTRTGLILINGRN---DSINSYKKITGFV 563
Cdd:PTZ00265 1222 ndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsGEDSTVFKNSGKILLDGVDicdYNLKDLRNLFSIV 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 564 PQDDVVHgNLTVEENLRFSARCRLSAYMSKADKVLIIERVIESLGLQHvrDSLVGTIEKrGISGGQRKRVNVGVEMVMEP 643
Cdd:PTZ00265 1302 SQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKY--DTNVGPYGK-SLSGGQKQRIAIARALLREP 1377
|
250 260
....*....|....*....|....
gi 1063705934 644 SLLILDEPTTGLDSASSQLLLRAL 667
Cdd:PTZ00265 1378 KILLLDEATSSLDSNSEKLIEKTI 1401
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
624-745 |
1.87e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.63 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 624 GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSYTMyKMFDDMIILAKGGL 703
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKGKI 254
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1063705934 704 tVYHGSVKKI---EEYFADIGITVPdrvnppdHYIDILEGIVKPD 745
Cdd:PRK13631 255 -LKTGTPYEIftdQHIINSTSIQVP-------RVIQVINDLIKKD 291
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
485-682 |
1.88e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.11 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 485 AFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALA---GKATGCTRTGLILINGRndSINSYKKITG 561
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmnDKVSGYRYSGDVLLGGR--SIFNYRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 562 FVPQDDVVHGN-----LTVEENLRfsARCRLSAYMSKADKVLIIERVIESLGL-QHVRDSLVGTIEKrgISGGQRKRVNV 635
Cdd:PRK14271 99 FRRRVGMLFQRpnpfpMSIMDNVL--AGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSPFR--LSGGQQQLLCL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063705934 636 GVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREAlEGVNICMVVH 682
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTH 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
499-685 |
2.12e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.47 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 499 HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSA---LAGKATGCTRTGLILINGRN------DSINSYKKItGFVPQDDVV 569
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARVEGEVRLFGRNiyspdvDPIEVRREV-GMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 570 HGNLTVEENLRFSARCRlSAYMSKADKVLIIERVIESLGL-QHVRDSLvgTIEKRGISGGQRKRVNVGVEMVMEPSLLIL 648
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLN-GLVKSKKELDERVEWALKKAALwDEVKDRL--NDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063705934 649 DEPTTGLD---SASSQLLLRALRREalegVNICMVVHQPS 685
Cdd:PRK14267 174 DEPTANIDpvgTAKIEELLFELKKE----YTIVLVTHSPA 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
488-670 |
2.29e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.51 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 488 DLTLTLKGKHKhILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSYKKITGFVPQDD 567
Cdd:PRK15056 11 DVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVR--LASGKISILGQPTRQALQKNLVAYVPQSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 568 VVHGNLTV-EENLRFSARCRLSAYM--SKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPS 644
Cdd:PRK15056 88 EVDWSFPVlVEDVVMMGRYGHMGWLrrAKKRDRQIVTAALARVDMVEFRHRQIGEL-----SGGQKKRVFLARAIAQQGQ 162
|
170 180
....*....|....*....|....*....
gi 1063705934 645 LLILDEPTTGLD---SASSQLLLRALRRE 670
Cdd:PRK15056 163 VILLDEPFTGVDvktEARIISLLRELRDE 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
501-725 |
2.40e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.62 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN----DSINSYKKITGFVPQD-DVVHGNLTV 575
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR--PQKGKVLVSGIDtgdfSKLQGIRKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EENLRFSAR--CRLSAYMSKadkvlIIERVIESLGLQHVRDSlvgtiEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTT 653
Cdd:PRK13644 96 EEDLAFGPEnlCLPPIEIRK-----RVDRALAEIGLEKYRHR-----SPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705934 654 GLDSASSQLLLRALRREALEGVNICMVVHQpsytMYKMFD-DMIILAKGGLTVYHGSVKKI--EEYFADIGITVP 725
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHN----LEELHDaDRIIVMDRGKIVLEGEPENVlsDVSLQTLGLTPP 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
498-698 |
3.62e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLsalagkatgctRTGLILINGRNDSINSYKKI-TGFVPQDdvVHGN---- 572
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLV-----------RVVLGLVAPDEGVIKRNGKLrIGYVPQK--LYLDttlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 573 LTVEenlRFsarCRLSAYMSKADKVLIIERVIESLGLQHVRDSLvgtiekrgiSGGQRKRVNVGVEMVMEPSLLILDEPT 652
Cdd:PRK09544 84 LTVN---RF---LRLRPGTKKEDILPALKRVQAGHLIDAPMQKL---------SGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063705934 653 TGLDsASSQL----LLRALRREAleGVNICMVVHQPSYTMYKMfDDMIIL 698
Cdd:PRK09544 149 QGVD-VNGQValydLIDQLRREL--DCAVLMVSHDLHLVMAKT-DEVLCL 194
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
481-683 |
3.81e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.81 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 481 VIEvaFKDLTLTLKGKHKHI--LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSY 556
Cdd:PRK11153 1 MIE--LKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLleRPTS----GRVLVDGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 KKIT------GFVPQddvvHGNL----TVEENLRFSARCrlsAYMSKADkvlIIERVIESLglqhvrdSLVGTIEKRG-- 624
Cdd:PRK11153 75 KELRkarrqiGMIFQ----HFNLlssrTVFDNVALPLEL---AGTPKAE---IKARVTELL-------ELVGLSDKADry 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705934 625 ---ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQ--L-LLRALRREAleGVNICMVVHQ 683
Cdd:PRK11153 138 paqLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRsiLeLLKDINREL--GLTIVLITHE 200
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
478-680 |
4.24e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 478 TRPVIEVafKDLTLTLKGKhkhiLRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGkaTGCTRTGLILINGRNDSINS-- 555
Cdd:PRK09700 262 HETVFEV--RNVTSRDRKK----VRDISFSVCRGEILGFAGLVGSGRTELMNCLFG--VDKRAGGEIRLNGKDISPRSpl 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 556 --YKKITGFVPQ---DDVVHGNLTVEENLRFSARCRLSAY------MSKADKVLIIERVIESLGLQhvrdslVGTIEKR- 623
Cdd:PRK09700 334 daVKKGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDGGYkgamglFHEVDEQRTAENQRELLALK------CHSVNQNi 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705934 624 -GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMV 680
Cdd:PRK09700 408 tELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV 465
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
507-734 |
4.86e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.87 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 507 KIMPGRVSAVMGPSGAGKTTFLSALAG---KATGCTRTGLILINGRNDSINSYKKI---TGFV---PQDDVVHGnlTVEE 577
Cdd:PRK13645 33 TFKKNKVTCVIGTTGSGKSTMIQLTNGliiSETGQTIVGDYAIPANLKKIKEVKRLrkeIGLVfqfPEYQLFQE--TIEK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NLRFSArcrlsaYMSKADKVLIIERVIESLGLQHVRDSLVgtieKRG---ISGGQRKRVNVGVEMVMEPSLLILDEPTTG 654
Cdd:PRK13645 111 DIAFGP------VNLGENKQEAYKKVPELLKLVQLPEDYV----KRSpfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 655 LDSASSQLLLRA-LRREALEGVNICMVVHQPSYTMyKMFDDMIILAKGGLTvyhgSVKKIEEYFADIGITVPDRVNPPDH 733
Cdd:PRK13645 181 LDPKGEEDFINLfERLNKEYKKRIIMVTHNMDQVL-RIADEVIVMHEGKVI----SIGSPFEIFSNQELLTKIEIDPPKL 255
|
.
gi 1063705934 734 Y 734
Cdd:PRK13645 256 Y 256
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
479-680 |
4.96e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 479 RPVIEVafKDLTltlkgkHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSY 556
Cdd:COG1129 254 EVVLEV--EGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGadPADS----GEIRLDGKPVRIRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 K-----KItGFVPQDDVVHG---NLTVEENLRFSARCRLSA--YMSKADKVLIIERVIESLGlqhVR----DSLVGTIek 622
Cdd:COG1129 322 RdairaGI-AYVPEDRKGEGlvlDLSIRENITLASLDRLSRggLLDRRRERALAEEYIKRLR---IKtpspEQPVGNL-- 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705934 623 rgiSGG-QRKrVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMV 680
Cdd:COG1129 396 ---SGGnQQK-VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI 450
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
499-714 |
6.31e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 499 HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN----DSINSYKKITGFVPQDDVVHGNLT 574
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--PTKGTITINNINynklDHKLAAQLGIGIIYQELSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 575 VEENLrFSARCRLSAYM-----------SKADKVLIIerviesLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEP 643
Cdd:PRK09700 97 VLENL-YIGRHLTKKVCgvniidwremrVRAAMMLLR------VGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 644 SLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQpsYTMYKMFDDMIILAKGGLTVYHGSVKKIE 714
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK--LAEIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
484-728 |
9.64e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTL-KGK--HKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATgctrTGLILING-------RND 551
Cdd:PRK13646 3 IRFDNVSYTYqKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllKPT----TGTVTVDDitithktKDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 552 SINSYKKITGFV---PQDDVVHGNltVEENLRFSAR---CRLSAYMSKADKVLIiervieSLGLQhvRDslVGTIEKRGI 625
Cdd:PRK13646 79 YIRPVRKRIGMVfqfPESQLFEDT--VEREIIFGPKnfkMNLDEVKNYAHRLLM------DLGFS--RD--VMSQSPFQM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALE-GVNICMVVHQPSyTMYKMFDDMIILAKGGLt 704
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMN-EVARYADEVIVMKEGSI- 224
|
250 260
....*....|....*....|....*..
gi 1063705934 705 VYHGSVKKI---EEYFADIGITVPDRV 728
Cdd:PRK13646 225 VSQTSPKELfkdKKKLADWHIGLPEIV 251
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
491-670 |
1.25e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.39 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDS------INSYKKITGF 562
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGleSPSQ----GNVSWRGEPLAklnraqRKAFRRDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 563 VPQDDV--VHGNLTVEENLRFSARCRLSayMSKADKvliIERVIESLGLQHVRDSLVgtiEKR--GISGGQRKRVNVGVE 638
Cdd:PRK10419 94 VFQDSIsaVNPRKTVREIIREPLRHLLS--LDKAER---LARASEMLRAVDLDDSVL---DKRppQLSGGQLQRVCLARA 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1063705934 639 MVMEPSLLILDEPTTGLD---SASSQLLLRALRRE 670
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDlvlQAGVIRLLKKLQQQ 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
511-680 |
1.56e-08 |
|
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: 58.30 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 511 GRVSAVMGPSGAGKTTFLSALAGKATGcTRTGLILINGRNDSI-NSYKKITG---FVPQDDVVHG---------NLTVEE 577
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALFGAYPG-KFEGNVFINGKPVDIrNPAQAIRAgiaMVPEDRKRHGivpilgvgkNITLSV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NLRFSARCRLSAymskADKVLIIERVIESLGLQHVRDSLVGTiekrGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDS 657
Cdd:TIGR02633 365 LKSFCFKMRIDA----AAELQIIGSAIQRLKVKTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180
....*....|....*....|...
gi 1063705934 658 ASSQLLLRALRREALEGVNICMV 680
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVV 459
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
493-701 |
1.96e-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: 56.74 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 493 LKGKHKH--ILRSVTGKIMPGRVSAVMGPSGAGKTTF---LSALAGKATGCTR-TGLILINGRNDSINSYKKITGFVPQD 566
Cdd:TIGR02769 17 LFGAKQRapVLTNVSLSIEEGETVGLLGRSGCGKSTLarlLLGLEKPAQGTVSfRGQDLYQLDRKQRRAFRRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 567 --DVVHGNLTVEENLRFSARCRLSayMSKADKvliIERVIESLGLQHVRDSLVGTIeKRGISGGQRKRVNVGVEMVMEPS 644
Cdd:TIGR02769 97 spSAVNPRMTVRQIIGEPLRHLTS--LDESEQ---KARIAELLDMVGLRSEDADKL-PRQLSGGQLQRINIARALAVKPK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 645 LLILDEPTTGLD---SASSQLLLRALRREAleGVNICMVVHQPSyTMYKMFDDMIILAKG 701
Cdd:TIGR02769 171 LIVLDEAVSNLDmvlQAVILELLRKLQQAF--GTAYLFITHDLR-LVQSFCQRVAVMDKG 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
501-682 |
2.13e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.47 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSYKKIT------------GFVPQddv 568
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLA--PDAGEVHYRMRDGQLRDLYALSeaerrrllrtewGFVHQ--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 569 vhgnltveeNLRFSARCRLSAYMSkadkvlIIERVIeSLGLQH---VRDSLVGTIEK------------RGISGGQRKRV 633
Cdd:PRK11701 97 ---------HPRDGLRMQVSAGGN------IGERLM-AVGARHygdIRATAGDWLERveidaariddlpTTFSGGMQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 634 NVGVEMVMEPSLLILDEPTTGLD-SASSQLL--LRALRREAleGVNICMVVH 682
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDvSVQARLLdlLRGLVREL--GLAVVIVTH 210
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
508-667 |
3.97e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 508 IMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSYKKITGFVPQDDVVHGNLTVEENLRFsaRCRL 587
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLH--VESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHF--LCGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 588 SAYMSK--ADKVLIIerviesLGLQHVRDSLVgtiekRGISGGQRKRVNVGvEMVMEPS-LLILDEPTTGLDSASSQLLL 664
Cdd:PRK13543 110 HGRRAKqmPGSALAI------VGLAGYEDTLV-----RQLSAGQKKRLALA-RLWLSPApLWLLDEPYANLDLEGITLVN 177
|
...
gi 1063705934 665 RAL 667
Cdd:PRK13543 178 RMI 180
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
518-677 |
8.04e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 518 GPSGAGKTT-------FLSALAGKATGCTRTglilINGRNdsINSYKKItGFVPQDDVVHGNLTVEENLRFSARC-RLSA 589
Cdd:NF033858 299 GSNGCGKSTtmkmltgLLPASEGEAWLFGQP----VDAGD--IATRRRV-GYMSQAFSLYGELTVRQNLELHARLfHLPA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 590 YMSKADkvliIERVIESLGLQHVRDSLVGtiekrGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASS----QLLLR 665
Cdd:NF033858 372 AEIAAR----VAEMLERFDLADVADALPD-----SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARdmfwRLLIE 442
|
170
....*....|..
gi 1063705934 666 aLRREalEGVNI 677
Cdd:NF033858 443 -LSRE--DGVTI 451
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
478-669 |
1.16e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.64 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 478 TRPVIEVafKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSY- 556
Cdd:PRK13635 2 KEEIIRV--EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL--PEAGTITVGGMVLSEETVw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 ---KKItGFVPQ--DDVVHGNlTVEENLRFSARCRlsaYMSKADkvlIIERVIESLGLQHVRDSLvgTIEKRGISGGQRK 631
Cdd:PRK13635 78 dvrRQV-GMVFQnpDNQFVGA-TVQDDVAFGLENI---GVPREE---MVERVDQALRQVGMEDFL--NREPHRLSGGQKQ 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063705934 632 RVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRR 669
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQ 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
484-685 |
1.27e-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: 52.54 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 484 VAFKDLTLTLkGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSInsykkitgFV 563
Cdd:cd03223 1 IELENLSLAT-PDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP--WGSGRIGMPEGEDLL--------FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 564 PQddvvhgnltveenlrfsarcrlSAYMSKAdkvliiervieSLglqhvRDSLVGTIEKRgISGGQRKRVNVGVEMVMEP 643
Cdd:cd03223 70 PQ----------------------RPYLPLG-----------TL-----REQLIYPWDDV-LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063705934 644 SLLILDEPTTGLDSASSQLLLRALRRealEGVNICMVVHQPS 685
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE---LGITVISVGHRPS 149
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
510-701 |
1.49e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 510 PGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSYKKIT----GFVPQDDVVHGNLTVEENLrFSARC 585
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYT--RDAGSILYLGKEVTFNGPKSSQeagiGIIHQELNLIPQLTIAENI-FLGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 586 RLSAY-------M-SKADKVLiierviESLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDS 657
Cdd:PRK10762 106 FVNRFgridwkkMyAEADKLL------ARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063705934 658 ASSQLLLRALRREALEGVNICMVVHQpsytMYKMF---DDMIILAKG 701
Cdd:PRK10762 175 TETESLFRVIRELKSQGRGIVYISHR----LKEIFeicDDVTVFRDG 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
511-738 |
1.53e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.00 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 511 GRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN------DSINSYKKITGFVPQDDVVHGNLTVEENLRFSAR 584
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIA--PDHGEILFDGENipamsrSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 585 --CRLSAYMSKADKVLIIERVieslGLQHVRDslvgtIEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQL 662
Cdd:PRK11831 111 ehTQLPAPLLHSTVMMKLEAV----GLRGAAK-----LMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 663 LLRALRR--EALeGVNiCMVVHQPSYTMYKMFDDMIILAkGGLTVYHGSVKKIEE-------YFADiGIT---VPDRVNP 730
Cdd:PRK11831 182 LVKLISElnSAL-GVT-CVVVSHDVPEVLSIADHAYIVA-DKKIVAHGSAQALQAnpdprvrQFLD-GIAdgpVPFRYPA 257
|
....*...
gi 1063705934 731 PDHYIDIL 738
Cdd:PRK11831 258 GDYHADLL 265
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
500-656 |
2.56e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.09 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALagKATGCTRTGLILINGRN---------DSINSYKKITGFVPQDDVVH 570
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVL--NLLEMPRSGTLNIAGNHfdfsktpsdKAIRELRRNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 571 GNLTVEENLrFSARCRL-----SAYMSKADKVLiierviESLGLQHVRDSLvgtieKRGISGGQRKRVNVGVEMVMEPSL 645
Cdd:PRK11124 95 PHLTVQQNL-IEAPCRVlglskDQALARAEKLL------ERLRLKPYADRF-----PLHLSGGQQQRVAIARALMMEPQV 162
|
170
....*....|.
gi 1063705934 646 LILDEPTTGLD 656
Cdd:PRK11124 163 LLFDEPTAALD 173
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
510-698 |
2.74e-07 |
|
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: 54.79 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 510 PGRVSAVMGPSGAGKTTFLSALAGkatgctrtglILI-N-GRNDSINSYKKI----TGFVPQD---DVVHGNLTVE---- 576
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSG----------ELKpNlGDYDEEPSWDEVlkrfRGTELQDyfkKLANGEIKVAhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 577 --ENLRFSARCRLSAYMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTG 654
Cdd:COG1245 168 yvDLIPKVFKGTVRELLEKVDERGKLDELAEKLGLENILDRDISEL-----SGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063705934 655 LD------SAssqlllRALRREALEGVNICMVVHqpsytmykmfdDMIIL 698
Cdd:COG1245 243 LDiyqrlnVA------RLIRELAEEGKYVLVVEH-----------DLAIL 275
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
516-656 |
2.76e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.08 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 516 VM-GPSGAGKTTFLSALAGKATgcTRTGLILINGRNdsinsykkITGFVPQD-DV--VHGN------LTVEENLRFSARC 585
Cdd:PRK11650 34 VLvGPSGCGKSTLLRMVAGLER--ITSGEIWIGGRV--------VNELEPADrDIamVFQNyalyphMSVRENMAYGLKI 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705934 586 RlsaYMSKADkvlIIERVieslglQHVRDSLvgTIEK------RGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:PRK11650 104 R---GMPKAE---IEERV------AEAARIL--ELEPlldrkpRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
501-719 |
2.82e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.29 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFL---SALAGKATG-CTRTGL-ILINGRNDSINSYKKITGFVPQ---------- 565
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLKPSSGtITIAGYhITPETGNKNLKKLRKKVSLVFQfpeaqlfent 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 566 --DDVVHGNLtveeNLRFSARCRLSAYMSKADKVLIIERVIESLGLQhvrdslvgtiekrgISGGQRKRVNVGVEMVMEP 643
Cdd:PRK13641 103 vlKDVEFGPK----NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFE--------------LSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 644 SLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPSyTMYKMFDDMIILAKGGLtVYHGSVKKIeeyFAD 719
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMD-DVAEYADDVLVLEHGKL-IKHASPKEI---FSD 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
487-669 |
3.09e-07 |
|
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: 54.92 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 487 KDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKAtgcTRTGLILING---RNDSINSYKKITGFV 563
Cdd:TIGR01271 1221 QGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL---STEGEIQIDGvswNSVTLQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 564 PQDDVVhgnltveenLRFSARCRLSAYMSKADKVliIERVIESLGLQHV----RDSLVGTIEKRG--ISGGQRKRVNVGV 637
Cdd:TIGR01271 1298 PQKVFI---------FSGTFRKNLDPYEQWSDEE--IWKVAEEVGLKSVieqfPDKLDFVLVDGGyvLSNGHKQLMCLAR 1366
|
170 180 190
....*....|....*....|....*....|..
gi 1063705934 638 EMVMEPSLLILDEPTTGLDSASSQLLLRALRR 669
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
500-683 |
3.48e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN--DSINSYKKITGFVPQDDVVHGNLTVEE 577
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLN--PEKGEILFERQSikKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NlrfsarCRLSAYMSKADkvLIIERVIESLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDS 657
Cdd:PRK13540 94 N------CLYDIHFSPGA--VGITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 1063705934 658 ASSQLLLRALRREALEGVNICMVVHQ 683
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
501-702 |
3.74e-07 |
|
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: 52.33 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSYKKiTGFVPQDDVVHG-------NL 573
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ--TLEGKVHWSNKNESEPSFEA-TRSRNRYSVAYAaqkpwllNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 574 TVEENLRFSARCRLSAYmskadkvliiERVIESLGLQHVRDSL----VGTIEKRGI--SGGQRKRVNVGVEMVMEPSLLI 647
Cdd:cd03290 94 TVEENITFGSPFNKQRY----------KAVTDACSLQPDIDLLpfgdQTEIGERGInlSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705934 648 LDEPTTGLDSASSQLLLRALRREAL--EGVNICMVVHQPSYTMYKmfdDMIILAKGG 702
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHA---DWIIAMKDG 217
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
485-718 |
4.23e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.17 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 485 AFKDLtltLKGKHKHI--LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRN---DSINSYK 557
Cdd:COG4586 23 ALKGL---FRREYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilVPTS----GEVRVLGYVpfkRRKEFAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 558 KITgfvpqddVVHGN-------LTVEENLRfsarcrLSAYMSKADKVLIIERV---IESLGLQHVRDSLVgtiekRGISG 627
Cdd:COG4586 96 RIG-------VVFGQrsqlwwdLPAIDSFR------LLKAIYRIPDAEYKKRLdelVELLDLGELLDTPV-----RQLSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 628 GQRKRVNVGVEMVMEPSLLILDEPTTGLDsASSQL----LLRALRREalEGVNICMVVHqpsytmykmfdDM-------- 695
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLD-VVSKEaireFLKEYNRE--RGTTILLTSH-----------DMddiealcd 223
|
250 260
....*....|....*....|....*
gi 1063705934 696 --IILAKGGLtVYHGSVKKIEEYFA 718
Cdd:COG4586 224 rvIVIDHGRI-IYDGSLEELKERFG 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
510-682 |
4.54e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 510 PGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGR-------NDSINS-----YKKITgFVPqddvvhgNLTVEE 577
Cdd:PRK11288 29 AGQVHALMGENGAGKSTLLKILSGNYQ--PDAGSILIDGQemrfastTAALAAgvaiiYQELH-LVP-------EMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NLRFSarcRLSAYMSKADKVLIIERVIESlgLQHVRDSLVGTIEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDS 657
Cdd:PRK11288 99 NLYLG---QLPHKGGIVNRRLLNYEAREQ--LEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180
....*....|....*....|....*
gi 1063705934 658 ASSQLLLRALRREALEGVNICMVVH 682
Cdd:PRK11288 174 REIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
494-684 |
4.82e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 494 KGKHK-HILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGctRTGLILINGRN-DSINSYK------KITGFVPQ 565
Cdd:PRK10584 18 QGEHElSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDG--SSGEVSLVGQPlHQMDEEAraklraKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 566 DDVVHGNLTVEENLRFSARCR-LSAYMSKADKVLIIERviesLGLQHVRDSLVGTiekrgISGGQRKRVNVGVEMVMEPS 644
Cdd:PRK10584 96 SFMLIPTLNALENVELPALLRgESSRQSRNGAKALLEQ----LGLGKRLDHLPAQ-----LSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063705934 645 LLILDEPTTGLDSASSQL---LLRALRREalEGVNICMVVHQP 684
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKiadLLFSLNRE--HGTTLILVTHDL 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
480-656 |
5.62e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 52.30 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 480 PVIEvaFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILING---RNDSIN 554
Cdd:PRK13632 6 VMIK--VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGllKPQS----GEIKIDGitiSKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 555 SYKKITGFVPQ--DDVVHGnLTVEENLRFSA--RCRLSAYMSKadkvlIIERVIESLGLQHVRDSlvgtiEKRGISGGQR 630
Cdd:PRK13632 80 EIRKKIGIIFQnpDNQFIG-ATVEDDIAFGLenKKVPPKKMKD-----IIDDLAKKVGMEDYLDK-----EPQNLSGGQK 148
|
170 180
....*....|....*....|....*.
gi 1063705934 631 KRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
501-682 |
5.83e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFL---SALAGKATGCTRTGLILINGRN------DSINSYKKItGFVPQDDVVHG 571
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGFRVEGKVTFHGKNlyapdvDPVEVRRRI-GMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 572 NlTVEENLRFSARcrLSAYMSKADKVliIERVIESLGL-QHVRDSLvgTIEKRGISGGQRKRVNVGVEMVMEPSLLILDE 650
Cdd:PRK14243 105 K-SIYDNIAYGAR--INGYKGDMDEL--VERSLRQAALwDEVKDKL--KQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|..
gi 1063705934 651 PTTGLDSASSqLLLRALRREALEGVNICMVVH 682
Cdd:PRK14243 178 PCSALDPIST-LRIEELMHELKEQYTIIIVTH 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
497-680 |
5.95e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 497 HKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGcTRTGLILINGRNDSINSY--------------KKITGF 562
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPG-RWEGEIFIDGKPVKIRNPqqaiaqgiamvpedRKRDGI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 563 VPQDDVVHgNLTVEENLRFSARCRLSAymskADKVLIIERVIESLglqHVRDSlvgTIEKR--GISGGQRKRVNVGVEMV 640
Cdd:PRK13549 353 VPVMGVGK-NITLAALDRFTGGSRIDD----AAELKTILESIQRL---KVKTA---SPELAiaRLSGGNQQKAVLAKCLL 421
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063705934 641 MEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMV 680
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
501-656 |
8.94e-07 |
|
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: 51.49 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGctrtGLILINGRNDSINSYKKIT-------GFVPQDDVVHG 571
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRliEPTS----GKVLIDGQDIAAMSRKELRelrrkkiSMVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 572 NLTVEENLRFSarcrLS-AYMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDE 650
Cdd:cd03294 116 HRTVLENVAFG----LEvQGVPRAEREERAAEALELVGLEGWEHKYPDEL-----SGGMQQRVGLARALAVDPDILLMDE 186
|
....*.
gi 1063705934 651 PTTGLD 656
Cdd:cd03294 187 AFSALD 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
625-670 |
1.03e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 1.03e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1063705934 625 ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLD-SASSQL--LLRALRRE 670
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDvSVQAQIlqLLRELQQE 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
626-670 |
1.13e-06 |
|
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: 1.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLD-SASSQL--LLRALRRE 670
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDvSVQAQIldLLRDLQRE 474
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
626-682 |
1.16e-06 |
|
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: 50.90 E-value: 1.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQL---LLRALRRealEGVNICMVVH 682
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVvveLIEEAKA---RGTAIIGIFH 210
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
501-656 |
1.32e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAG-KATgctRTGLILING--------RNDSinsYKKItGFVPQddvvhG 571
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGaRKI---QQGRVEVLGgdmadarhRRAV---CPRI-AYMPQ-----G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 572 -------NLTVEENLRFSARcrLSAyMSKADKVLIIERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPS 644
Cdd:NF033858 85 lgknlypTLSVFENLDFFGR--LFG-QDAAERRRRIDELLRATGLAPFADRPAGKL-----SGGMKQKLGLCCALIHDPD 156
|
170
....*....|..
gi 1063705934 645 LLILDEPTTGLD 656
Cdd:NF033858 157 LLILDEPTTGVD 168
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
397-667 |
1.38e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 397 NLTKMMKSMEENPSNNEGFNvgtgskpgKKPQAPKGKQLHTQSQIFKYAYgqiekekameqnnKNLTFsgvismatdtEM 476
Cdd:PTZ00265 344 NITEYMKSLEATNSLYEIIN--------RKPLVENNDDGKKLKDIKKIQF-------------KNVRF----------HY 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 477 RTRPVIEVaFKDLTLTLKgkhkhilrsvtgkimPGRVSAVMGPSGAGKTTFLSaLAGKATGCTRtGLILINGRND----S 552
Cdd:PTZ00265 393 DTRKDVEI-YKDLNFTLT---------------EGKTYAFVGESGCGKSTILK-LIERLYDPTE-GDIIINDSHNlkdiN 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 553 INSYKKITGFVPQDDVVHGNlTVEENLRFS------------------------ARCRLSAYMSKADKVLIIERVIESLG 608
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSN-SIKNNIKYSlyslkdlealsnyynedgndsqenKNKRNSCRAKCAGDLNDMSNTTDSNE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 609 LQHVR-------------------------------DSLVGTIEKRgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDS 657
Cdd:PTZ00265 534 LIEMRknyqtikdsevvdvskkvlihdfvsalpdkyETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
330
....*....|
gi 1063705934 658 ASSQLLLRAL 667
Cdd:PTZ00265 613 KSEYLVQKTI 622
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
510-709 |
1.42e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 510 PGRVSAVMGPSGAGKTTFLSALaGKATGCTrTGLILINGRN-DSINS--YKKITGFVPQDDVVHGNLTVEENL---RFSA 583
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPlESWSSkaFARKVAYLPQQLPAAEGMTVRELVaigRYPW 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 584 RCRLSAYmSKADKVLIiERVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLL 663
Cdd:PRK10575 114 HGALGRF-GAADREKV-EEAISLVGLKPLAHRLVDSL-----SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063705934 664 LRALRREALE-GVNICMVVHqpSYTMYKMFDDMIILAKGGLTVYHGS 709
Cdd:PRK10575 187 LALVHRLSQErGLTVIAVLH--DINMAARYCDYLVALRGGEMIAQGT 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
500-684 |
2.03e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.03 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALagkatGC---TRTGLILINGRN------DSINSYKKIT-GFVPQDDVV 569
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-----GCldkPTSGTYRVAGQDvatldaDALAQLRREHfGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 570 HGNLTVEENLRFSArcrLSAYMSKADKvliIERVIESLGlqhvRDSLVGTIEKR--GISGGQRKRVNVGvEMVMEPSLLI 647
Cdd:PRK10535 98 LSHLTAAQNVEVPA---VYAGLERKQR---LLRAQELLQ----RLGLEDRVEYQpsQLSGGQQQRVSIA-RALMNGGQVI 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063705934 648 L-DEPTTGLDSASSQLLLRALRREALEGVNICMVVHQP 684
Cdd:PRK10535 167 LaDEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
474-680 |
2.18e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 474 TEMRTRPVIEV------AFKDLTLTLKgkhkhilrsvtgkimPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILIN 547
Cdd:PRK15439 261 QQAAGAPVLTVedltgeGFRNISLEVR---------------AGEILGLAGVVGAGRTELAETLYGLRP--ARGGRIMLN 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 548 GRNdsINSYKKIT----GFV--PQDDVVHGnLTVEENLRFSArC-----RLSAYMSKADKVLIIERVIESLG--LQHVRD 614
Cdd:PRK15439 324 GKE--INALSTAQrlarGLVylPEDRQSSG-LYLDAPLAWNV-CalthnRRGFWIKPARENAVLERYRRALNikFNHAEQ 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 615 SLvgtiekRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMV 680
Cdd:PRK15439 400 AA------RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI 459
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
498-669 |
2.22e-06 |
|
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: 51.47 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGctrtglilINGRNDSINSYKkiTGFVPQDDVVHGNLTVEE 577
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD--------FNGEARPQPGIK--VGYLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NL------------RFSArcrLSAYMSKAD---KVLI-----IERVIESLGLQHVR---------------DSLVGTIek 622
Cdd:TIGR03719 88 NVeegvaeikdaldRFNE---ISAKYAEPDadfDKLAaeqaeLQEIIDAADAWDLDsqleiamdalrcppwDADVTKL-- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063705934 623 rgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRR 669
Cdd:TIGR03719 163 ---SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
497-670 |
2.41e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.63 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 497 HKHILRSVTGKIMPGRVSAVMGPSGAGKTT----FLSALAGKatgctrtGLILINGRNDSINSYKKITGFVPQDDVVHGN 572
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDGQPLHNLNRRQLLPVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 573 --------LTV----EENLRFSARcrlsaYMSKADKVLIIERVIESLGLQHvrdslvgtiEKR-----GISGGQRKRVNV 635
Cdd:PRK15134 371 pnsslnprLNVlqiiEEGLRVHQP-----TLSAAQREQQVIAVMEEVGLDP---------ETRhrypaEFSGGQRQRIAI 436
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063705934 636 GVEMVMEPSLLILDEPTTGLD-SASSQL--LLRALRRE 670
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDkTVQAQIlaLLKSLQQK 474
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
428-681 |
2.55e-06 |
|
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: 51.47 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 428 QAPKGKQLHTQSQIfkYAYGQIEKEKAMEQNNKNltfsgvismatdtEMRTRP-------VIEVafKDLTltlKG-KHKH 499
Cdd:TIGR03719 277 QSPKGRQAKSKARL--ARYEELLSQEFQKRNETA-------------EIYIPPgprlgdkVIEA--ENLT---KAfGDKL 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKAT---GCTRTGlilingrnDSInsykKItGFVPQD-DVVHGNLTV 575
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQpdsGTIEIG--------ETV----KL-AYVDQSrDALDPNKTV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EE------------NLRFSARCRLSAYMSK-ADKvliiervieslglqhvrDSLVGTIekrgiSGGQRKRVNVGVEMVME 642
Cdd:TIGR03719 404 WEeisggldiiklgKREIPSRAYVGRFNFKgSDQ-----------------QKKVGQL-----SGGERNRVHLAKTLKSG 461
|
250 260 270
....*....|....*....|....*....|....*....
gi 1063705934 643 PSLLILDEPTTGLDSASsqllLRALrREALEGVNICMVV 681
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVET----LRAL-EEALLNFAGCAVV 495
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
483-683 |
4.83e-06 |
|
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: 49.47 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKAtgcTRTGLILINGRN---DSINSYKKI 559
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL---NTEGDIQIDGVSwnsVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 TGFVPQDDVVhgnltveenlrFSA--RCRLSAYMSKADKVLIieRVIESLGLQHVRDSLVG----TIEKRG--ISGGQRK 631
Cdd:cd03289 79 FGVIPQKVFI-----------FSGtfRKNLDPYGKWSDEEIW--KVAEEVGLKSVIEQFPGqldfVLVDGGcvLSHGHKQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063705934 632 RVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALrREALEGVNICMVVHQ 683
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTL-KQAFADCTVILSEHR 196
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
626-682 |
5.32e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.72 E-value: 5.32e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLD---SASSQLLLRALRREAleGVNICMVVH 682
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvQAQIMTLLNELKREF--NTAIIMITH 220
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
491-669 |
6.10e-06 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.15 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLS-----ALAGKATG-------CTR-TGL------ILIN---- 547
Cdd:cd03271 1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypALARRLHLkkeqpgnHDRiEGLehidkvIVIDqspi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 548 GRNDSINS--YKKITGFVPQD--DVVHG---------------------NLTVEENLRFSARC-RLSAYMskadkvliie 601
Cdd:cd03271 81 GRTPRSNPatYTGVFDEIRELfcEVCKGkrynretlevrykgksiadvlDMTVEEALEFFENIpKIARKL---------- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 602 RVIESLGLQHVRDSLVGTIekrgISGGQRKRVNVGVEMVME---PSLLILDEPTTGLDSASSQLLLRALRR 669
Cdd:cd03271 151 QTLCDVGLGYIKLGQPATT----LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQR 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
498-665 |
6.22e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 498 KHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILINGRNDS---INSYKKITGFVpqddvvhgnlt 574
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRGSgetIWDIKKHIGYV----------- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 575 veenlrfSARCRLSAYMSKADKVLIIERVIESLGL-QHVRD----------SLVGTIEK------RGISGGQRKRVNVGV 637
Cdd:PRK10938 342 -------SSSLHLDYRVSTSVRNVILSGFFDSIGIyQAVSDrqqklaqqwlDILGIDKRtadapfHSLSWGQQRLALIVR 414
|
170 180
....*....|....*....|....*...
gi 1063705934 638 EMVMEPSLLILDEPTTGLDSASSQLLLR 665
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRR 442
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
510-673 |
6.70e-06 |
|
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: 46.98 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 510 PGRVSAVMGPSGAGKTTFLSALAGKAtGCTRTGLILINGrndsinsykkitgfvpqddvvhgnltveenlrfsarcrlsa 589
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAREL-GPPGGGVIYIDG----------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 590 ymskadkvliierviESLGLQHVRDSLVGTIEKRGISGGQRKRVNVGVEMVME--PSLLILDEPTTGLDSASSQLLLRAL 667
Cdd:smart00382 39 ---------------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKlkPDVLILDEITSLLDAEQEALLLLLE 103
|
....*.
gi 1063705934 668 RREALE 673
Cdd:smart00382 104 ELRLLL 109
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
490-682 |
7.22e-06 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 48.64 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 490 TLTLKGKHK-----HILRSVTGKIMPGRVSAVMGPSGAGKTTFLS-------------ALAGKATGCTRTGliliNGRND 551
Cdd:COG4598 8 ALEVRDLHKsfgdlEVLKGVSLTARKGDVISIIGSSGSGKSTFLRcinlletpdsgeiRVGGEEIRLKPDR----DGELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 552 SINSyKKIT------GFVPQddvvHGNL----TVEENLRFSARCRLSayMSKADKVLIIERVIESLGLQHVRDSLVGTIe 621
Cdd:COG4598 84 PADR-RQLQrirtrlGMVFQ----SFNLwshmTVLENVIEAPVHVLG--RPKAEAIERAEALLAKVGLADKRDAYPAHL- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 622 krgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:COG4598 156 ----SGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
481-669 |
9.69e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.57 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 481 VIEVafKDLTLTLK-GKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGctRTGLILINGR---NDSINSY 556
Cdd:PRK13650 4 IIEV--KNLTFKYKeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEA--ESGQIIIDGDlltEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 557 KKITGFVPQD-DVVHGNLTVEENLRFSARCRLSAYmskadkVLIIERVIESLGLQHVRDslVGTIEKRGISGGQRKRVNV 635
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPH------EEMKERVNEALELVGMQD--FKEREPARLSGGQKQRVAI 151
|
170 180 190
....*....|....*....|....*....|....
gi 1063705934 636 GVEMVMEPSLLILDEPTTGLDSASSQLLLRALRR 669
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKG 185
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
500-656 |
1.29e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 500 ILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINS---YKKITGFVPQDDVVHGNlTVE 576
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS--PTSGTLLFEGEDISTLKpeiYRQQVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 577 ENLRFSARCRLSAYMSKAdkvliierVIESLglqhVRDSLVGTIEKRGI---SGGQRKRVNVGVEMVMEPSLLILDEPTT 653
Cdd:PRK10247 99 DNLIFPWQIRNQQPDPAI--------FLDDL----ERFALPDTILTKNIaelSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
...
gi 1063705934 654 GLD 656
Cdd:PRK10247 167 ALD 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
501-702 |
1.60e-05 |
|
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: 49.17 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKAtgctrtglilingrnDSINSYKKITG---FVPQDDVVHgNLTVEE 577
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM---------------DKVEGHVHMKGsvaYVPQQAWIQ-NDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 578 NLRFSARCRLSAYMSkadkvliierVIESLGLQHVRDSLVG----TIEKRGI--SGGQRKRVNVGVEMVMEPSLLILDEP 651
Cdd:TIGR00957 718 NILFGKALNEKYYQQ----------VLEACALLPDLEILPSgdrtEIGEKGVnlSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063705934 652 TTGLDSASSQLLLRAL--RREALEGVNICMVVHQPSYTMYKmfdDMIILAKGG 702
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVigPEGVLKNKTRILVTHGISYLPQV---DVIIVMSGG 837
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
501-667 |
1.86e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.78 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRN---DSINSYKKITGFVPQD-DVVHGNLTVE 576
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE--EFEGKVKIDGELltaENVWNLRRKIGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 577 ENLRFSARCRlsaymsKADKVLIIERVIESLGLQHVRDslVGTIEKRGISGGQRKRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:PRK13642 101 DDVAFGMENQ------GIPREEMIKRVDEALLAVNMLD--FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170
....*....|.
gi 1063705934 657 SASSQLLLRAL 667
Cdd:PRK13642 173 PTGRQEIMRVI 183
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
494-725 |
1.91e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.77 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 494 KGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTF---LSALAGKATGC------------------TRTGLILINGRNds 552
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSEGKvyvdgldtsdeenlwdirNKAGMVFQNPDN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 553 insykKITGFVPQDDVVHG--NLTVE-ENLRfsarcrlsaymskadkvliiERVIESLglqhvrdSLVGTIEKRG----- 624
Cdd:PRK13633 97 -----QIVATIVEEDVAFGpeNLGIPpEEIR--------------------ERVDESL-------KKVGMYEYRRhaphl 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 625 ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASsqlllralRREAL---------EGVNICMVVHqpsYTMYKMFDDM 695
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG--------RREVVntikelnkkYGITIILITH---YMEEAVEADR 213
|
250 260 270
....*....|....*....|....*....|...
gi 1063705934 696 IILAKGGLTVYHGSVKKI---EEYFADIGITVP 725
Cdd:PRK13633 214 IIVMDSGKVVMEGTPKEIfkeVEMMKKIGLDVP 246
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
626-670 |
6.62e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 46.26 E-value: 6.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLD-SASSQL--LLRALRRE 670
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDvSIQAQVlnLLEDLQDE 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
501-683 |
8.04e-05 |
|
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: 46.36 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 501 LRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATGCTRTGLILING-----RNDSINSYKKITgFVPQDDVVHGNLTV 575
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGsplkaSNIRDTERAGIV-IIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 EENLRFSARCRLSAY-MSKADKVLIIERVIESLGLQHVRDSL-VGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTT 653
Cdd:TIGR02633 96 AENIFLGNEITLPGGrMAYNAMYLRAKNLLRELQLDADNVTRpVGDY-----GGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190
....*....|....*....|....*....|
gi 1063705934 654 GLDSASSQLLLRALRREALEGVNICMVVHQ 683
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
504-670 |
8.73e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 45.85 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 504 VTGKIMPGRVSAVMGPSGAGKTTFLSALAG--KATGCTRT--GLILINGRNDSINSYKKITGFVPQDDVVHGN--LTV-- 575
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGlvKATDGEVAwlGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNprMTIge 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 576 --EENLRfsarcrlsAYMSKADKVLIIERVIE---SLGLqhvrdsLVGTIEK--RGISGGQRKRVNVGVEMVMEPSLLIL 648
Cdd:PRK15079 120 iiAEPLR--------TYHPKLSRQEVKDRVKAmmlKVGL------LPNLINRypHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180
....*....|....*....|....*
gi 1063705934 649 DEPTTGLD-SASSQL--LLRALRRE 670
Cdd:PRK15079 186 DEPVSALDvSIQAQVvnLLQQLQRE 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
491-702 |
1.03e-04 |
|
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: 44.24 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 491 LTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSAlAGKATGCTRtgliLINGRndSINSYKKITgFVPQddvvh 570
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-GLYASGKAR----LISFL--PKFSRNKLI-FIDQ----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 571 gnltveenLRFsarcrlsaymskadkvlIIERVIESLGLQHVRDSLvgtiekrgiSGGQRKRVNVGVEMVMEP--SLLIL 648
Cdd:cd03238 68 --------LQF-----------------LIDVGLGYLTLGQKLSTL---------SGGELQRVKLASELFSEPpgTLFIL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063705934 649 DEPTTGLDSASSQLLLRALRREALEGVNICMVVHQPsyTMYKMFDDMIILAKGG 702
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFGPGS 165
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
507-694 |
1.31e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 507 KIMPGRVSAVMGPSGAGKTTFLSALAGKatgctrtgLILING-RNDSIN-----SYKKITGFVPQ--------------D 566
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGE--------LPLLSGeRQSQFShitrlSFEQLQKLVSDewqrnntdmlspgeD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 567 DVvhGNLTVE---ENLRFSARCrlsaymskadkvliiERVIESLGLQHVrdslvgtIEKRGI--SGGQRKRVNVGVEMVM 641
Cdd:PRK10938 97 DT--GRTTAEiiqDEVKDPARC---------------EQLAQQFGITAL-------LDRRFKylSTGETRKTLLCQALMS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063705934 642 EPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQpsytmykmFDD 694
Cdd:PRK10938 153 EPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNR--------FDE 197
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
626-682 |
1.64e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 1.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQ 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
470-675 |
1.93e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.62 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 470 MATDTEMRTRPVIEVafKDLTLTLKGKHKHI--LRSVTGKIMPGRVSAVMGPSGAGKT-TFLS--ALAGKATGCTRTGLI 544
Cdd:PRK10261 1 MPHSDELDARDVLAV--ENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvTALAlmRLLEQAGGLVQCDKM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 545 LINGRND--------SINSYKKITG----FVPQDDVVHGN--LTVEENLRFSARcrLSAYMSKADKVLIIERVieslgLQ 610
Cdd:PRK10261 79 LLRRRSRqvielseqSAAQMRHVRGadmaMIFQEPMTSLNpvFTVGEQIAESIR--LHQGASREEAMVEAKRM-----LD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 611 HVRDSLVGTIEKR---GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLD-SASSQL--LLRALRREALEGV 675
Cdd:PRK10261 152 QVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvTIQAQIlqLIKVLQKEMSMGV 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
469-670 |
2.51e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 469 SMATDTEMRTRPVI------EVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgcTRTG 542
Cdd:PLN03232 1214 SEATAIIENNRPVSgwpsrgSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE--LEKG 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 543 LILINGRNDS---INSYKKITGFVPQDDVVHGNlTVEENLR-FSARcrlsaymSKADkvliierVIESLGLQHVRD---- 614
Cdd:PLN03232 1292 RIMIDDCDVAkfgLTDLRRVLSIIPQSPVLFSG-TVRFNIDpFSEH-------NDAD-------LWEALERAHIKDvidr 1356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 615 ---SLVGTIEKRG--ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRRE 670
Cdd:PLN03232 1357 npfGLDAEVSEGGenFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREE 1417
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
480-656 |
2.79e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 480 PVIEVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAGKATgctRT-GLILINGRNDSINSykk 558
Cdd:PRK10762 247 PRLDKAPGEVRLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP---RTsGYVTLDGHEVVTRS--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 559 itgfvPQDDVVHG---------------NLTVEENLRFSARCRLSAYMSK---ADKVLIIERVIESLGLQH-VRDSLVGT 619
Cdd:PRK10762 321 -----PQDGLANGivyisedrkrdglvlGMSVKENMSLTALRYFSRAGGSlkhADEQQAVSDFIRLFNIKTpSMEQAIGL 395
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063705934 620 IekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:PRK10762 396 L-----SGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
480-701 |
3.70e-04 |
|
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: 44.94 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 480 PVIEVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALAgkATGCTRTGLILINGRNDSI----NS 555
Cdd:TIGR00957 1281 PRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF--RINESAEGEIIIDGLNIAKiglhDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 556 YKKITgFVPQDDVVHGNltveenlrfSARCRLSAYMSKADkvliiERVIESLGLQHVRDSLVGTIEK---------RGIS 626
Cdd:TIGR00957 1359 RFKIT-IIPQDPVLFSG---------SLRMNLDPFSQYSD-----EEVWWALELAHLKTFVSALPDKldhecaeggENLS 1423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705934 627 GGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREaLEGVNICMVVHQPSYTMykMFDDMIILAKG 701
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQ-FEDCTVLTIAHRLNTIM--DYTRVIVLDKG 1495
|
|
| DUF4674 |
pfam15719 |
Domain of unknown function (DUF4674); This family of proteins is found in eukaryotes. Proteins ... |
303-414 |
4.20e-04 |
|
Domain of unknown function (DUF4674); This family of proteins is found in eukaryotes. Proteins in this family are typically between 126 and 221 amino acids in length.
Pssm-ID: 464823 Cd Length: 191 Bit Score: 42.46 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 303 SLSLLMIMVYNCSDQvlaTREKRQAKSREAAARHAKETTQARERWKTAKGVAKNQKMGLSAQLSQTFSRMKSARK----- 377
Cdd:pfam15719 71 SKSVLLITCKSCNKT---TRHPGKSRSFLTALKSNPSTPQSRSSLKTPDRKTKSSKKNKPTPVSKSNSKGKSPALtfrtp 147
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1063705934 378 ---DATPVKASGKSKDKKKEPSNLtKMMKSMEENPSNNEG 414
Cdd:pfam15719 148 tsgQSTPSSSSKPGSKKKFHFSQL-KRLLKLEESQKTPKG 186
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
626-663 |
4.85e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.41 E-value: 4.85e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1063705934 626 SGGQRKRVNVGVEMVMEPSLLILDEPTTGLD-SASSQLL 663
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQVL 194
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
515-711 |
5.30e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 515 AVMGPSGAGKTTFLSALAGKATGCTRTglilingrndSINSYKKITGFVPQDDVVHGNLTVEEnLRFSARCRLSAYMSKA 594
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGT----------VFRSAKVRMAVFSQHHVDGLDLSSNP-LLYMMRCFPGVPEQKL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 595 DKVLIIERVIESLGLQHVRDslvgtiekrgISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALrreALEG 674
Cdd:PLN03073 608 RAHLGSFGVTGNLALQPMYT----------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL---VLFQ 674
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063705934 675 VNICMVVHQpSYTMYKMFDDMIILAKGGLTVYHGSVK 711
Cdd:PLN03073 675 GGVLMVSHD-EHLISGSVDELWVVSEGKVTPFHGTFH 710
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
515-668 |
7.90e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.55 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 515 AVMGPSGAGKTTFLSALAGKATgcTRTGLILINGRNDSINSY---KKITGFVPQDDVVHGNltveenlRFSARCRLSAYM 591
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYP--LTEGEIRLDGRPLSSLSHsvlRQGVAMVQQDPVVLAD-------TFLANVTLGRDI 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 592 SKaDKVLiieRVIESLGLQHVRDSLVGTIEKR------GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLR 665
Cdd:PRK10790 442 SE-EQVW---QALETVQLAELARSLPDGLYTPlgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQ 517
|
...
gi 1063705934 666 ALR 668
Cdd:PRK10790 518 ALA 520
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
511-535 |
1.29e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.23 E-value: 1.29e-03
10 20
....*....|....*....|....*
gi 1063705934 511 GRVSAVMGPSGAGKTTFLSALAGKA 535
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPEL 109
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
625-723 |
1.56e-03 |
|
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: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 625 ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLDSASSQLLLRALRREALEGVNICMVVHQpSYTMYKMFDDMIILAKGGLT 704
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEH-DLAVLDYLSDRIHVFEGEPG 150
|
90 100
....*....|....*....|....*
gi 1063705934 705 VY------HGSVKKIEEYFADIGIT 723
Cdd:cd03222 151 VYgiasqpKGTREGINRFLRGYLIT 175
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
483-663 |
1.80e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.43 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 483 EVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFlsALAGKATGCTRTGLILINGRNDS---INSYKKI 559
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISklpLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 560 TGFVPQDDVVHGNlTVEENLRFSARCRLSAyMSKADKVLIIERVIESL--GLqhvrDSLVgTIEKRGISGGQRKRVNVGV 637
Cdd:cd03288 97 LSIILQDPILFSG-SIRFNLDPECKCTDDR-LWEALEIAQLKNMVKSLpgGL----DAVV-TEGGENFSVGQRQLFCLAR 169
|
170 180
....*....|....*....|....*.
gi 1063705934 638 EMVMEPSLLILDEPTTGLDSASSQLL 663
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENIL 195
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
448-658 |
2.74e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 448 QIEKEKAMEqnnKNLTFSGVISMATDTEMRTRPVI--EVAFKDLTLTLKGKHKHILRSVTGKIMPGRVSAVMGPSGAGKT 525
Cdd:PTZ00243 1274 ALERRTGMA---ADVTGTVVIEPASPTSAAPHPVQagSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKS 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 526 TFLSALAGKATGCtrTGLILINGRNdsINSY-----KKITGFVPQDDVVHGNlTVEENLR-FsarcrLSAymSKADkvli 599
Cdd:PTZ00243 1351 TLLLTFMRMVEVC--GGEIRVNGRE--IGAYglrelRRQFSMIPQDPVLFDG-TVRQNVDpF-----LEA--SSAE---- 1414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 600 IERVIESLGLQHVRDSLVGTIEKRGISGGQRKRVNVGVEMVMEPSLL-------ILDEPTTGLDSA 658
Cdd:PTZ00243 1415 VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkkgsgfiLMDEATANIDPA 1480
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
457-656 |
2.85e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 457 QNNKNLTFSGVISMATDTEMRTR-PVIEVAFKDLTLTLKG---KHKHILRSVTGKIMPGRVSAVMGPSGAGKTTFLSALA 532
Cdd:PRK10982 216 QPLAGLTMDKIIAMMVGRSLTQRfPDKENKPGEVILEVRNltsLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLF 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 533 GKATgcTRTGLILINGrndsinsyKKITGFVPQDDVVHGNLTVEENLRFSArcrLSAYMSKADKVLI--IERVIESLGL- 609
Cdd:PRK10982 296 GIRE--KSAGTITLHG--------KKINNHNANEAINHGFALVTEERRSTG---IYAYLDIGFNSLIsnIRNYKNKVGLl 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705934 610 ---------QHVRDSL-VGTIEKR----GISGGQRKRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:PRK10982 363 dnsrmksdtQWVIDSMrVKTPGHRtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
508-656 |
3.81e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.79 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 508 IMPGRVSAVMGPSGAGKTTFLSALaGKATGCTRtGLILINGRNDSINS-------YKKITGFVPQDDVVHGNLTVEENLR 580
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLL-NRLIEPTR-GQVLIDGVDIAKISdaelrevRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705934 581 FSARCRLSAYMSKADKVLiieRVIESLGLQHVRDSLVGTIekrgiSGGQRKRVNVGVEMVMEPSLLILDEPTTGLD 656
Cdd:PRK10070 129 FGMELAGINAEERREKAL---DALRQVGLENYAHSYPDEL-----SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
625-670 |
4.59e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 4.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1063705934 625 ISGGQRKRVNVGVEMVMEPSLLILDEPTTGLD-SASSQ---LLLRALRRE 670
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQiieLLLELQQKE 203
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
511-544 |
5.98e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.06 E-value: 5.98e-03
10 20 30
....*....|....*....|....*....|....
gi 1063705934 511 GRVSAVMGPSGAGKTTFLSALAGKATgcTRTGLI 544
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPELD--LRTGEI 137
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
572-682 |
6.68e-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: 40.77 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705934 572 NLTVEENLRFsarcrlsaymskADKVLIIERVIESL---GLQHVRDSLVGTIekrgISGGQRKRVNVGVEM---VMEPSL 645
Cdd:TIGR00630 790 DMTVEEAYEF------------FEAVPSISRKLQTLcdvGLGYIRLGQPATT----LSGGEAQRIKLAKELskrSTGRTL 853
|
90 100 110
....*....|....*....|....*....|....*..
gi 1063705934 646 LILDEPTTGLDSASSQLLLRALRREALEGVNICMVVH 682
Cdd:TIGR00630 854 YILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| |
