|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-468 |
3.82e-111 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 339.35 E-value: 3.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 6 LNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR--VPVDYLPQIQAPSPQ---- 78
Cdd:COG0488 1 LENLSKSFGGRPLLDdVS-LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkgLRIGYLPQEPPLDDDltvl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 79 --------------------------------------------------------------------------SGGEAT 84
Cdd:COG0488 80 dtvldgdaelraleaeleeleaklaepdedlerlaelqeefealggweaearaeeilsglgfpeedldrpvselSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 85 ITAL-QPLFVWPkSLLILDEPTANLDLDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRLSVYKGNYTDYL 163
Cdd:COG0488 160 RVALaRALLSEP-DLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 164 KLQENKRAKQWQDYYQYQDRLQRLQASAQKRLDRAQSFKKkkasiswsdykvnnfagkydaqekamaksAKALERRMNRL 243
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQ-----------------------------AQSRIKALEKL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 244 EKVDKPVKEKRYTLKalghLSDPS---NTLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK------ 314
Cdd:COG0488 290 EREEPPRRDKTVEIR----FPPPErlgKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKllagel 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 315 ----GMVSRSlpgyyyDQLSVGYFSQNFDQLDLNQSILENVTQDSVQSMTL-VRNLLAGLGFNIDKLDQRISTLSGGERV 389
Cdd:COG0488 366 epdsGTVKLG------ETVKIGYFDQHQEELDPDKTVLDELRDGAPGGTEQeVRGYLGRFLFSGDDAFKPVGVLSGGEKA 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092676368 390 RLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQFIKECVNRRYYIKDQQLlnEQQDTDYSD 468
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGV--REYPGGYDD 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-442 |
4.64e-57 |
|
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: 199.01 E-value: 4.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 28 PQDRIGLVGANGSGKSTLLRMIMGMDTDYQG--RIDLRVPVDYLPQ---------------------------------- 71
Cdd:TIGR03719 30 PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGeaRPQPGIKVGYLPQepqldptktvrenveegvaeikdaldrfneisak 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 ---------------------IQA-------------------PSPQ------SGGEATITALQPLFVWPKSLLILDEPT 105
Cdd:TIGR03719 110 yaepdadfdklaaeqaelqeiIDAadawdldsqleiamdalrcPPWDadvtklSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 106 ANLDLDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRLSVYKGNYTDYLKlQENKRAKQWQdyyqyqdrlq 185
Cdd:TIGR03719 190 NHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLE-QKQKRLEQEE---------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 186 RLQASAQKRLDR-----AQSFK----KKKASISwsdykvnnfagKYDAQekamakSAKALERRMNRLEkVDKPVKEKryt 256
Cdd:TIGR03719 259 KEESARQKTLKRelewvRQSPKgrqaKSKARLA-----------RYEEL------LSQEFQKRNETAE-IYIPPGPR--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 257 lkaLGhlsdpsNTLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP-------GyyyDQL 329
Cdd:TIGR03719 318 ---LG------DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPdsgtieiG---ETV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 330 SVGYFSQNFDQLDLNQSILENVT--QDSVQSMTLVRNLLAGLG-FNIDKLDQ--RISTLSGGERVRLSLAKVLLADHHLL 404
Cdd:TIGR03719 386 KLAYVDQSRDALDPNKTVWEEISggLDIIKLGKREIPSRAYVGrFNFKGSDQqkKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
490 500 510
....*....|....*....|....*....|....*...
gi 1092676368 405 FLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQFI 442
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFL 503
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-441 |
4.14e-54 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 191.10 E-value: 4.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGMDTDYQG--RIDLRVPVDYLPQ-------------------------------------- 71
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGeaRPAPGIKVGYLPQepqldpektvrenveegvaevkaaldrfneiyaayaep 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 -----------------IQA-------------------PSPQ------SGGEATITALQPLFVWPKSLLILDEPTANLD 109
Cdd:PRK11819 116 dadfdalaaeqgelqeiIDAadawdldsqleiamdalrcPPWDakvtklSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 110 LDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRLSVYKGNYTDYLKlQENKRAKQWQdyyqyqdrlqRLQA 189
Cdd:PRK11819 196 AESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLE-QKAKRLAQEE----------KQEA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 190 SAQKRLDR-----AQSFK----KKKASISwsdykvnnfagKYDAqekaMAKSAkalERRMNRLEKVDKPVKEKrytlkaL 260
Cdd:PRK11819 265 ARQKALKRelewvRQSPKarqaKSKARLA-----------RYEE----LLSEE---YQKRNETNEIFIPPGPR------L 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 261 GhlsdpsNTLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP-------GyyyDQLSVGY 333
Cdd:PRK11819 321 G------DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPdsgtikiG---ETVKLAY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 334 FSQNFDQLDLNQSILENVT--QDSVQSMTLVRNLLAGLG-FNIDKLDQ--RISTLSGGERVRLSLAKVLLADHHLLFLDE 408
Cdd:PRK11819 392 VDQSRDALDPNKTVWEEISggLDIIKVGNREIPSRAYVGrFNFKGGDQqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDE 471
|
490 500 510
....*....|....*....|....*....|...
gi 1092676368 409 PTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQF 441
Cdd:PRK11819 472 PTNDLDVETLRALEEALLEFPGCAVVISHDRWF 504
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-151 |
2.33e-45 |
|
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: 155.68 E-value: 2.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL--RVPVDYLPQiqapspQSGG 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ------LSGG 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 82 EATITALQPLFVWPKSLLILDEPTANLDLDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRR 151
Cdd:cd03221 75 EKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
70-478 |
8.84e-45 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 166.88 E-value: 8.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 70 PQIQAP-SPQSGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIE 148
Cdd:PRK10636 141 EQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 149 QRRLSVYKGNYTDYlKLQENKRAKQWQDYYQYQdrlqrlqasaQKRLDRAQSFkkkkasiswsdykVNNFagkydaqeKA 228
Cdd:PRK10636 221 QQSLFEYTGNYSSF-EVQRATRLAQQQAMYESQ----------QERVAHLQSY-------------IDRF--------RA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 229 MAKSAKALERRMNRLEK--------VDKPVkekRYTLKALGHLSDPsntLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVG 300
Cdd:PRK10636 269 KATKAKQAQSRIKMLERmeliapahVDNPF---HFSFRAPESLPNP---LLKMEKVSAGYGDRIILDSIKLNLVPGSRIG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 301 LLGPNKAGKTTFLKGMVSRSLPGYYYDQLS----VGYFSQN-FDQLDLNQSILENVTQDSVQSM-TLVRNLLAGLGFNID 374
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgikLGYFAQHqLEFLRADESPLQHLARLAPQELeQKLRDYLGGFGFQGD 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 375 KLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQFIKECVNRRYYIKD 454
Cdd:PRK10636 423 KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHD 502
|
410 420
....*....|....*....|....
gi 1092676368 455 QQLlnEQQDTDYSDrSQQTLSLLQ 478
Cdd:PRK10636 503 GKV--EPFDGDLED-YQQWLSDVQ 523
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
273-503 |
9.11e-45 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 164.85 E-value: 9.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 273 LQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK----------GMVSRSlPGyyydqLSVGYFSQNfDQLD 342
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKilagelepdsGEVSIP-KG-----LRIGYLPQE-PPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 343 LNQSILENVTQDSVQSMTL---------------------------------------VRNLLAGLGFNIDKLDQRISTL 383
Cdd:COG0488 74 DDLTVLDTVLDGDAELRALeaeleeleaklaepdedlerlaelqeefealggweaearAEEILSGLGFPEEDLDRPVSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 384 SGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQFIKECVNRRYYIKDQQLlnEQQD 463
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKL--TLYP 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1092676368 464 TDYSD---RSQQTLSLLQ--FKLQEAisnpevsltEIRQLQDQIQ 503
Cdd:COG0488 232 GNYSAyleQRAERLEQEAaaYAKQQK---------KIAKEEEFIR 267
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
271-456 |
1.64e-42 |
|
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: 147.98 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPGY----YYDQLSVGYFSQnfdqldlnqs 346
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEgivtWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 347 ilenvtqdsvqsmtlvrnllaglgfnidkldqristLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQ 426
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 1092676368 427 EYPGTFVLVSHDQQFIKECVNRRYYIKDQQ 456
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-509 |
1.38e-37 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 146.25 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 24 LLVQPQDRIGLVGANGSGKSTLLRMIMG---MDT---------------------------DY-------QG-------R 59
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDgriiyeqdlivarlqqdpprnvegtvyDFvaegieeQAeylkryhD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 60 IDLRVPVDY-------LPQIQAP----------------------------SPQSGGEATITALQPLFVWPKSLLILDEP 104
Cdd:PRK11147 104 ISHLVETDPseknlneLAKLQEQldhhnlwqlenrinevlaqlgldpdaalSSLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 105 TANLDLDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRLSVYKGNYTDYL-KLQENKRAKQWQDYyQYQDR 183
Cdd:PRK11147 184 TNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLlEKEEALRVEELQNA-EFDRK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 184 LqrlqasAQKRLDRAQSFKKKKAsiswsdykvnnfagkydaQEKAMAKSAKAL-ERRMNRLE---KVDKPVKEkrytlka 259
Cdd:PRK11147 263 L------AQEEVWIRQGIKARRT------------------RNEGRVRALKALrRERSERREvmgTAKMQVEE------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 260 lghlSDPSNTLI-HLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--GYYY--DQLSVGYF 334
Cdd:PRK11147 312 ----ASRSGKIVfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQAdsGRIHcgTKLEVAYF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 335 SQNFDQLDLNQSILENVTqDSVQSMTL---VRNLLAGLG---FNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDE 408
Cdd:PRK11147 388 DQHRAELDPEKTVMDNLA-EGKQEVMVngrPRHVLGYLQdflFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 409 PTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQFIKECVNRRYYIKDQQLLNE----------QQDTDYSDRSQQTLSLLQ 478
Cdd:PRK11147 467 PTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRyvggyhdarqQQAQYLALKQPAVKKKEE 546
|
570 580 590
....*....|....*....|....*....|....*...
gi 1092676368 479 FKLQEAIS--NPEVSLT-----EIRQLQDQIQDLKENI 509
Cdd:PRK11147 547 AAAPKAETvkRSSKKLSyklqrELEQLPQLLEDLEAEI 584
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
89-459 |
1.17e-36 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 142.34 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 89 QPLFVWPKSLLiLDEPTANLDLDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRLSVYKGNYTDYLklqen 168
Cdd:PRK15064 168 QALFSNPDILL-LDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYM----- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 169 krakqwqdyyqyqdrlqrlQASAQKRLDRAQSFKKKKASISWSDYKVNNFAgkydaqekAMAKSAKALERRMNRLEKVD- 247
Cdd:PRK15064 242 -------------------TAATQARERLLADNAKKKAQIAELQSFVSRFS--------ANASKAKQATSRAKQIDKIKl 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 248 ---KPV----------KEKRYTLKALghlsdpsntliHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK 314
Cdd:PRK15064 295 eevKPSsrqnpfirfeQDKKLHRNAL-----------EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 315 GMVSRSLPGY----YYDQLSVGYFSQN----FDQlDLNqsILENVTQ-----DSVQSmtlVRNLLAGLGFNIDKLDQRIS 381
Cdd:PRK15064 364 TLVGELEPDSgtvkWSENANIGYYAQDhaydFEN-DLT--LFDWMSQwrqegDDEQA---VRGTLGRLLFSQDDIKKSVK 437
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 382 TLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQFIKECVNRRYYIKDQQLLN 459
Cdd:PRK15064 438 VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-164 |
2.76e-36 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 140.97 E-value: 2.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 3 ILELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL--RVPVDYLPQ-------- 71
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDdLS-LRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgeTVKIGYFDQhqeeldpd 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 ------IQAPSPQ---------------------------SGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCLIQ 118
Cdd:COG0488 394 ktvldeLRDGAPGgteqevrgylgrflfsgddafkpvgvlSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEE 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1092676368 119 QVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRLSVYKGNYTDYLK 164
Cdd:COG0488 474 ALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
71-454 |
1.00e-28 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 120.35 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 71 QIQAPSPQSGGEATITAL-QPLFVWPkSLLILDEPTANLDLDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQ 149
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALaRALFIEP-DLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 150 RRLSVYKGNYTDYLKLQENKRAKQwqdyyqyqdrlQRLQASAQKRLDRAQSFkkkkasiswsdykVNNFagKYDAQEKAM 229
Cdd:PLN03073 417 QKLVTYKGDYDTFERTREEQLKNQ-----------QKAFESNERSRSHMQAF-------------IDKF--RYNAKRASL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 230 AKS-AKALERrmnrLEKVDKPVKEKRYTLKALGHLSDPSNTLIHLQDIDVQV-DDRLLFHLQHFKLQKGDKVGLLGPNKA 307
Cdd:PLN03073 471 VQSrIKALDR----LGHVDAVVNDPDYKFEFPTPDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGI 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 308 GKTTFLK----------GMVSRSlpgyyyDQLSVGYFSQN-FDQLDLNQSILENVTQ--DSVQSMTLvRNLLAGLGFNID 374
Cdd:PLN03073 547 GKSTILKlisgelqpssGTVFRS------AKVRMAVFSQHhVDGLDLSSNPLLYMMRcfPGVPEQKL-RAHLGSFGVTGN 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 375 KLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQFIKECVNRRYYIKD 454
Cdd:PLN03073 620 LALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSE 699
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
271-457 |
9.82e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 101.82 E-value: 9.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLPG-----YY----YDQLS-------VGYF 334
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLR-ALADLDPPtsgeiYLdgkpLSAMPppewrrqVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 335 SQNFDQLDlnQSILENVT-----QDSVQSMTLVRNLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEP 409
Cdd:COG4619 80 PQEPALWG--GTVRDNLPfpfqlRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 410 TNYLDLPTLQELEAFLQEYP----GTFVLVSHDQQFIKECVNRRYYIKDQQL 457
Cdd:COG4619 158 TSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
291-456 |
1.05e-23 |
|
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: 98.69 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--------GYYYDQLS-------VGYFSQNFD-QL-------DLNQSi 347
Cdd:cd03225 22 LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPtsgevlvdGKDLTKLSlkelrrkVGLVFQNPDdQFfgptveeEVAFG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 348 LENVTQDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQE 427
Cdd:cd03225 101 LENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK 179
|
170 180 190
....*....|....*....|....*....|..
gi 1092676368 428 YPG---TFVLVSHDQQFIKECVNRRYYIKDQQ 456
Cdd:cd03225 180 LKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
296-441 |
1.07e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 104.43 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 296 GDKVGLLGPNKAGKTTFLKGMV---------SRSLPGYyydqlSVGYFSQNfDQLDLNQSILENVtQDSVQSmtlVRNLL 366
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAgvdkefegeARPAPGI-----KVGYLPQE-PQLDPEKTVRENV-EEGVAE---VKAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 367 AGL--------------------------------GFNID-KL------------DQRISTLSGGERVRLSLAKVLLADH 401
Cdd:PRK11819 103 DRFneiyaayaepdadfdalaaeqgelqeiidaadAWDLDsQLeiamdalrcppwDAKVTKLSGGERRRVALCRLLLEKP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092676368 402 HLLFLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQF 441
Cdd:PRK11819 183 DMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYF 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-151 |
1.88e-23 |
|
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: 96.55 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 5 ELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------DLRVPVDYLPQ 71
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlidgkdiaklpleELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 IqapspqSGGE------ATITALQPlfvwpkSLLILDEPTANLDLDHKN---CLIQQVKDYPGAVLMVSHDRDFLDQTVD 142
Cdd:cd00267 81 L------SGGQrqrvalARALLLNP------DLLLLDEPTSGLDPASRErllELLRELAEEGRTVIIVTHDPELAELAAD 148
|
....*....
gi 1092676368 143 WIWAIEQRR 151
Cdd:cd00267 149 RVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
266-457 |
6.56e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 94.77 E-value: 6.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 266 PSNTLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGM----------VSRSLPGYYYDQLSVGYFS 335
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlgllpptsgtVRLFGKPPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 336 Q--NFDQ-------------LDLNQSILENVTQDSVQsmtLVRNLLA--GLGfniDKLDQRISTLSGGERVRLSLAKVLL 398
Cdd:COG1121 82 QraEVDWdfpitvrdvvlmgRYGRRGLFRRPSRADRE---AVDEALErvGLE---DLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 399 ADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG---TFVLVSHDQQFIKECVNRRYYIKDQQL 457
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
296-460 |
9.68e-22 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 98.70 E-value: 9.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 296 GDKVGLLGPNKAGKTTFL---KGMVSR-----SLPGYY-----------YDQLSVGYF---SQNFDQL--DLNQSILENV 351
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLallKNEISAdggsyTFPGNWqlawvnqetpaLPQPALEYVidgDREYRQLeaQLHDANERND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 TQ---------DSVQSMTL---VRNLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQ 419
Cdd:PRK10636 107 GHaiatihgklDAIDAWTIrsrAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092676368 420 ELEAFLQEYPGTFVLVSHDQQFIKECVNRRYYIkDQQLLNE 460
Cdd:PRK10636 187 WLEKWLKSYQGTLILISHDRDFLDPIVDKIIHI-EQQSLFE 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
291-438 |
9.56e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 91.28 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--------GYYYDQLS------VGYFSQNFDqLDLNQSILENVT---- 352
Cdd:COG1131 21 LTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtsgevrvlGEDVARDPaevrrrIGYVPQEPA-LYPDLTVRENLRffar 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 353 ---QDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYP 429
Cdd:COG1131 100 lygLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELA 178
|
170
....*....|..
gi 1092676368 430 G---TFVLVSHD 438
Cdd:COG1131 179 AegkTVLLSTHY 190
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
272-456 |
1.31e-20 |
|
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: 88.46 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 272 HLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKgMVSRslpgyyydqlsvgyfsqnfdqldlnqsiLENV 351
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLR-AIAG----------------------------LLKP 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 TQDSVQsmtlvRNLLAGLGFNIDKLDQRIST---LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEY 428
Cdd:cd00267 52 TSGEIL-----IDGKDIAKLPLEELRRRIGYvpqLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL 126
|
170 180 190
....*....|....*....|....*....|.
gi 1092676368 429 PG---TFVLVSHDQQFIKECVNRRYYIKDQQ 456
Cdd:cd00267 127 AEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
270-438 |
1.66e-20 |
|
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: 90.87 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 270 LIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMvSRSLPGY----YYD-----QLS-------VGY 333
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRAL-AGLLKPSsgevLLDgrdlaSLSrrelarrIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 334 FSQNFdQLDLNQSILENV-----------TQDSVQSMTLVRNLLAGLGfnIDKL-DQRISTLSGGERVRLSLAKVLLADH 401
Cdd:COG1120 80 VPQEP-PAPFGLTVRELValgryphlglfGRPSAEDREAVEEALERTG--LEHLaDRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092676368 402 HLLFLDEPTNYLDLP----TLQELEAFLQEYPGTFVLVSHD 438
Cdd:COG1120 157 PLLLLDEPTSHLDLAhqleVLELLRRLARERGRTVVMVLHD 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
273-438 |
1.78e-20 |
|
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: 88.65 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 273 LQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLPGyyyDQLSVGYFSQNFDQLDLNQ-----SI 347
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLK-TLAGLLKP---SSGEILLDGKDLASLSPKElarkiAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 348 LEnvtqdsvQSMTLVrnllaglgfNIDKL-DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLP----TLQELE 422
Cdd:cd03214 78 VP-------QALELL---------GLAHLaDRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAhqieLLELLR 141
|
170
....*....|....*.
gi 1092676368 423 AFLQEYPGTFVLVSHD 438
Cdd:cd03214 142 RLARERGKTVVMVLHD 157
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
268-454 |
2.19e-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: 90.53 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 268 NTLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK--------------------------------- 314
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSlitgdlpptygndvrlfgerrggedvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 315 GMVSRSLPGYYYDQLSV------GYFsqnfDQLDLNQsileNVTQDSVQsmtLVRNLLAGLGFNiDKLDQRISTLSGGER 388
Cdd:COG1119 81 GLVSPALQLRFPRDETVldvvlsGFF----DSIGLYR----EPTDEQRE---RARELLELLGLA-HLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 389 VRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG----TFVLVSHDQQFIKECVNRRYYIKD 454
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTHHVEEIPPGITHVLLLKD 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
270-445 |
5.80e-20 |
|
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: 87.92 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 270 LIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK----------GMVS------RSLPGYYYDQLsvGY 333
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRilagllppsaGEVLwngepiRDAREDYRRRL--AY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 334 FSQNfDQLDLNQSILENVT-----QDSVQSMTLVRNLLAGLGfnIDKL-DQRISTLSGGERVRLSLAKVLLADHHLLFLD 407
Cdd:COG4133 80 LGHA-DGLKPELTVRENLRfwaalYGLRADREAIDEALEAVG--LAGLaDLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092676368 408 EPTNYLDLPTLQELEAFLQEYP---GTFVLVSHDQQFIKEC 445
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
290-469 |
6.21e-20 |
|
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: 89.15 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLK----------------GMVSRSLPgyYYDQLSVGYFSQNFDqLDLNQSILENVT- 352
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTTLLRmlagllkpdsgsilidGEDVRKEP--REARRQIGVLPDERG-LYDRLTVRENIRy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 353 ------QDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQ 426
Cdd:COG4555 98 faelygLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1092676368 427 EY---PGTFVLVSHDQQFIKECVNRRYYIKDQQLLNEQQDTDYSDR 469
Cdd:COG4555 177 ALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
290-411 |
1.60e-19 |
|
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: 85.01 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLK---GMVS----------RSLPGYYYDQLS--VGYFSQNfDQLDLNQSILENV--- 351
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKliaGLLSptegtilldgQDLTDDERKSLRkeIGYVFQD-PQLFPRLTVRENLrlg 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 352 -------TQDSVQSMTLVRNLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTN 411
Cdd:pfam00005 84 lllkglsKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-152 |
2.23e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 86.41 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------DLRVPVDYLP 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkplsampppEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 71 QI--------------------QAPSPQ-----------------------SGGEATITAL------QPlfvwpkSLLIL 101
Cdd:COG4619 81 QEpalwggtvrdnlpfpfqlreRKFDREralellerlglppdildkpverlSGGERQRLALiralllQP------DVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 102 DEPTANLDLDHKNCLIQQVKDYP----GAVLMVSHDRDFLDQTVDWIWAIEQRRL 152
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
290-457 |
5.38e-19 |
|
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: 85.62 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFL----------KGMVS---RSLPGYYYDQLS------VGYFSQNFDQLDlNQSILEN 350
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLnilggldrptSGEVRvdgTDISKLSEKELAafrrrhIGFVFQSFNLLP-DLTALEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 351 V-------TQDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT----LQ 419
Cdd:cd03255 103 VelplllaGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevME 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092676368 420 ELEAFLQEYPGTFVLVSHDQQFIKECvNRRYYIKDQQL 457
Cdd:cd03255 182 LLRELNKEAGTTIVVVTHDPELAEYA-DRIIELRDGKI 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
238-457 |
2.32e-18 |
|
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: 87.90 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 238 RRMNRLEKVDKPVKEKRytlkalGHLSDPSNTLIHLQDIDVQVDDRLLFHLQH--FKLQKGDKVGLLGPNKAGKTTFLK- 314
Cdd:COG4987 307 RRLNELLDAPPAVTEPA------EPAPAPGGPSLELEDVSFRYPGAGRPVLDGlsLTLPPGERVAIVGPSGSGKSTLLAl 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 315 ---------GMVS---RSLPGYYYDQLS--VGYFSQN---FdqldlNQSILENVT--------QDSVQSMTLVR--NLLA 367
Cdd:COG4987 381 llrfldpqsGSITlggVDLRDLDEDDLRrrIAVVPQRphlF-----DTTLRENLRlarpdatdEELWAALERVGlgDWLA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 368 GLGfniDKLDQRI----STLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQE-LEAFLQEYPG-TFVLVSHDQQF 441
Cdd:COG4987 456 ALP---DGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAlLADLLEALAGrTVLLITHRLAG 532
|
250
....*....|....*.
gi 1092676368 442 IkECVNRRYYIKDQQL 457
Cdd:COG4987 533 L-ERMDRILVLEDGRI 547
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
26-167 |
2.98e-18 |
|
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: 83.92 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI---DLRVPVDYLPQI--------QAP------------------- 75
Cdd:COG1122 24 IEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdGKDITKKNLRELrrkvglvfQNPddqlfaptveedvafgpen 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 76 ---------------------------SPQ--SGGE------ATITALQPlfvwpkSLLILDEPTANLDLDHKNCLIQQV 120
Cdd:COG1122 104 lglpreeirerveealelvglehladrPPHelSGGQkqrvaiAGVLAMEP------EVLVLDEPTAGLDPRGRRELLELL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 121 KDYPGA---VLMVSHDRDFLDQTVDWIWAIEQRRLsVYKGN----YTDYLKLQE 167
Cdd:COG1122 178 KRLNKEgktVIIVTHDLDLVAELADRVIVLDDGRI-VADGTprevFSDYELLEE 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
271-484 |
3.25e-18 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 87.99 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPG-------YYYDQLSVG----------- 332
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDGipkncqiLHVEQEVVGddttalqcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 333 ----------------------YFSQNF--DQLDLNQSI---------------LENVTQDSVQSMTlvRNLLAGLGFNI 373
Cdd:PLN03073 258 tdiertqlleeeaqlvaqqrelEFETETgkGKGANKDGVdkdavsqrleeiykrLELIDAYTAEARA--ASILAGLSFTP 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 374 DKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQFIKECVNRRYYIK 453
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
250 260 270
....*....|....*....|....*....|.
gi 1092676368 454 DQQLLNEQQDTDYSDRSQQTLSLLQFKLQEA 484
Cdd:PLN03073 416 GQKLVTYKGDYDTFERTREEQLKNQQKAFES 446
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-151 |
3.80e-18 |
|
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: 82.90 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 5 ELNHIKKTW--QAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL-RVPVDYLP----------- 70
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSlkelrrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 71 ------QIQAP---------------------------------------SPQ--SGGE------ATITALQPlfvwpkS 97
Cdd:cd03225 81 fqnpddQFFGPtveeevafglenlglpeeeieerveealelvgleglrdrSPFtlSGGQkqrvaiAGVLAMDP------D 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 98 LLILDEPTANLDLDHKNCLIQQVKDYPGA---VLMVSHDRDFLDQTVDWIWAIEQRR 151
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
272-449 |
5.19e-18 |
|
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: 82.58 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 272 HLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMV--------SRSLPGY--YYDQLSVGYFSQNFD-Q 340
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgllkptsgSIRVFGKplEKERKRIGYVPQRRSiD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 341 LDLNQSILENV-----------TQDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEP 409
Cdd:cd03235 81 RDFPISVRDVVlmglyghkglfRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092676368 410 TNYLDLPTLQELEAFLQEYPG---TFVLVSHDQQFIKE------CVNRR 449
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEyfdrvlLLNRT 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
291-458 |
1.98e-17 |
|
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: 81.22 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK----------GMVS---RSLPGYYYDQLS--VGY-FsQN-FDQLdLNQSILENV-- 351
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRllngllkptsGEVLvdgKDITKKNLRELRrkVGLvF-QNpDDQL-FAPTVEEDVaf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 -------TQDSVQSMtlVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAF 424
Cdd:COG1122 100 gpenlglPREEIRER--VEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLEL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1092676368 425 LQEYPG---TFVLVSHDQQFIKECVNRRYYIKDQQLL 458
Cdd:COG1122 177 LKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
288-443 |
4.70e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 84.23 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 288 LQH--FKLQKGDKVGLLGPNKAGKTTFLKGM------------------VSR-------SLPGYYYDQLSVG-------- 332
Cdd:PRK11147 19 LDNaeLHIEDNERVCLVGRNGAGKSTLMKILngevllddgriiyeqdliVARlqqdpprNVEGTVYDFVAEGieeqaeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 333 -------------YFSQNFDQLDLNQSILENvtQDSVQSMTLVRNLLAGLGFNIDKldqRISTLSGGERVRLSLAKVLLA 399
Cdd:PRK11147 99 kryhdishlvetdPSEKNLNELAKLQEQLDH--HNLWQLENRINEVLAQLGLDPDA---ALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1092676368 400 DHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQFIK 443
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIR 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
290-454 |
4.79e-17 |
|
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: 79.61 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLK---GMVSRSLPGYYYD---------QLSVGYFSQN----------FDQLDLNQSI 347
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKilaGLIKESSGSILLNgkpikakerRKSIGYVMQDvdyqlftdsvREELLLGLKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 348 LENVTQDsvqsmtlVRNLLAGLGFNIDKlDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQEL-EAF-- 424
Cdd:cd03226 100 LDAGNEQ-------AETVLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVgELIre 171
|
170 180 190
....*....|....*....|....*....|
gi 1092676368 425 LQEYPGTFVLVSHDQQFIKECVNRRYYIKD 454
Cdd:cd03226 172 LAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
271-454 |
6.33e-17 |
|
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: 78.19 E-value: 6.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDRLLFHLQH--FKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLPGY----YYDQLSVgyfsQNFDQLDLN 344
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDvsLTIKPGEKVAIVGPSGSGKSTLLK-LLLRLYDPTsgeiLIDGVDL----RDLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 345 QSILEnVTQDSVqsmtlvrnLLAG-LGFNIdkldqristLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEA 423
Cdd:cd03228 76 KNIAY-VPQDPF--------LFSGtIRENI---------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|...
gi 1092676368 424 FLQEYPG--TFVLVSHDQQFIKECvNRRYYIKD 454
Cdd:cd03228 138 ALRALAKgkTVIVIAHRLSTIRDA-DRIIVLDD 169
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
291-457 |
2.37e-16 |
|
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: 76.67 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK---GMVSRS-----LPGYYYDQLS------VGYFSQNFDQLDlnqsilenvtqdsv 356
Cdd:cd03230 21 LTVEKGEIYGLLGPNGAGKTTLIKiilGLLKPDsgeikVLGKDIKKEPeevkrrIGYLPEEPSLYE-------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 357 qSMTLVRNLlaglgfnidkldqrisTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEY---PGTFV 433
Cdd:cd03230 87 -NLTVRENL----------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTIL 149
|
170 180
....*....|....*....|....
gi 1092676368 434 LVSHDQQFIKECVNRRYYIKDQQL 457
Cdd:cd03230 150 LSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-438 |
2.55e-16 |
|
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: 81.49 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 24 LLVQPQDRIGLVGANGSGKSTLLRMIMGM---DTDYQGRIDLR---------------------------VPVDYLPQI- 72
Cdd:COG1123 27 LTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDgrdllelsealrgrrigmvfqdpmtqlNPVTVGDQIa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 73 -------------------------------QAPSPQSGGE------ATITALQPlfvwpkSLLILDEPTANLDLDHKNC 115
Cdd:COG1123 107 ealenlglsraeararvlelleavglerrldRYPHQLSGGQrqrvaiAMALALDP------DLLIADEPTTALDVTTQAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 116 ---LIQQVKDYPG-AVLMVSHDRDFLDQTVDWIWAIEQRRLsVYKGNYTDYLklqenkrakqwqdyyqyqDRLQRLQASA 191
Cdd:COG1123 181 ildLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI-VEDGPPEEIL------------------AAPQALAAVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 192 QKRLDRaqsfkkkkasiswsdykvnnfagkyDAQEKAMAKSAKALErrmnrLEKVDKpvkekRYTLKALGHlsdpsntlI 271
Cdd:COG1123 242 RLGAAR-------------------------GRAAPAAAAAEPLLE-----VRNLSK-----RYPVRGKGG--------V 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 272 H-LQDIDvqvddrllfhlqhFKLQKGDKVGLLGPNKAGKTTFLKGMV-------------SRSLPGYYYDQL-----SVG 332
Cdd:COG1123 279 RaVDDVS-------------LTLRRGETLGLVGESGSGKSTLARLLLgllrptsgsilfdGKDLTKLSRRSLrelrrRVQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 333 YFSQN-FDQLDLNQSILENVTQ--------DSVQSMTLVRNLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHL 403
Cdd:COG1123 346 MVFQDpYSSLNPRMTVGDIIAEplrlhgllSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKL 425
|
490 500 510
....*....|....*....|....*....|....*....
gi 1092676368 404 LFLDEPTNYLDLPT----LQELEAFLQEYPGTFVLVSHD 438
Cdd:COG1123 426 LILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHD 464
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-243 |
3.34e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 81.37 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 3 ILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR--VPVDYLPQIQ------- 73
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgIKLGYFAQHQleflrad 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 74 -AP-------SPQ---------------------------SGGEATITALQpLFVWPK-SLLILDEPTANLDLDHKNCLI 117
Cdd:PRK10636 392 eSPlqhlarlAPQeleqklrdylggfgfqgdkvteetrrfSGGEKARLVLA-LIVWQRpNLLLLDEPTNHLDLDMRQALT 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 118 QQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRLSVYKGNYTDYlklqenkraKQWQDYYQYQDRlQRLQASAQKRLDR 197
Cdd:PRK10636 471 EALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY---------QQWLSDVQKQEN-QTDEAPKENNANS 540
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1092676368 198 AQSFKKKKASiswsdykvnnfAGKYDAQEKAMAKSAKALERRMNRL 243
Cdd:PRK10636 541 AQARKDQKRR-----------EAELRTQTQPLRKEIARLEKEMEKL 575
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
291-438 |
4.19e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 80.79 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK----------GMVS---RSLPGYYYDQL--SVGYFSQNfdQLDLNQSILENVT-QD 354
Cdd:TIGR02857 343 FTVPPGERVALVGPSGAGKSTLLNlllgfvdpteGSIAvngVPLADADADSWrdQIAWVPQH--PFLFAGTIAENIRlAR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 355 SVQSMTLVRN---------LLAGLGFNID-KLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAF 424
Cdd:TIGR02857 421 PDASDAEIREaleragldeFVAALPQGLDtPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA 500
|
170
....*....|....*.
gi 1092676368 425 LQEYPG--TFVLVSHD 438
Cdd:TIGR02857 501 LRALAQgrTVLLVTHR 516
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
26-151 |
5.33e-16 |
|
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: 75.50 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-----DLR-VPVDYLPQIQAPSPQ--------------SGGEATI 85
Cdd:cd03228 25 IKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvDLRdLDLESLRKNIAYVPQdpflfsgtirenilSGGQRQR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 86 TALQPLFVWPKSLLILDEPTANLDLDHKNCLIQQVKDYPG--AVLMVSHdRDFLDQTVDWIWAIEQRR 151
Cdd:cd03228 105 IAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
291-462 |
6.14e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 77.01 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFL----------KGMVS---RSLPGYYYDQLS------VGYFSQNFdQLDLNQSILENV 351
Cdd:COG1136 29 LSIEAGEFVAIVGPSGSGKSTLLnilggldrptSGEVLidgQDISSLSERELArlrrrhIGFVFQFF-NLLPELTALENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 T-------QDSVQSMTLVRNLLA--GLGfniDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT----L 418
Cdd:COG1136 108 AlplllagVSRKERRERARELLErvGLG---DRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1092676368 419 QELEAFLQEYPGTFVLVSHDQQFIKECvNRRYYIKDQQLLNEQQ 462
Cdd:COG1136 185 ELLRELNRELGTTIVMVTHDPELAARA-DRVIRLRDGRIVSDER 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-152 |
9.32e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 76.67 E-value: 9.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 1 MAILELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL--------RVPVDYLPQ 71
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEdVS-LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprraRRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 IQA--------------------------PSPQ-------------------------SGGEatitaLQPLFV------W 94
Cdd:COG1121 83 RAEvdwdfpitvrdvvlmgrygrrglfrrPSRAdreavdealervgledladrpigelSGGQ-----QQRVLLaralaqD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092676368 95 PKsLLILDEPTANLDLDHKNC---LIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRL 152
Cdd:COG1121 158 PD-LLLLDEPFAGVDAATEEAlyeLLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
291-454 |
1.33e-15 |
|
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: 74.92 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPgyyyDQLSVGYFSQNFDQLDLNQSILENVTQDSVQSMTLVRNLLAglg 370
Cdd:cd03229 21 LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP----DSGSILIDGEDLTDLEDELPPLRRRIGMVFQDFALFPHLTV--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 371 fnidkLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFL----QEYPGTFVLVSHDQQFIKECV 446
Cdd:cd03229 94 -----LENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARLA 168
|
....*...
gi 1092676368 447 NRRYYIKD 454
Cdd:cd03229 169 DRVVVLRD 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-152 |
2.05e-15 |
|
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: 73.97 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI------------DLRVPVDYLP 70
Cdd:cd03230 1 IEVRNLSKRYGKKTALDdIS-LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikkepeEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 71 QIQAPSPQ---------SGGEATITAL-QPLFVWPKsLLILDEPTANLD-------LDhkncLIQQVKDYPGAVLMVSHD 133
Cdd:cd03230 80 EEPSLYENltvrenlklSGGMKQRLALaQALLHDPE-LLILDEPTSGLDpesrrefWE----LLRELKKEGKTILLSSHI 154
|
170
....*....|....*....
gi 1092676368 134 RDFLDQTVDWIWAIEQRRL 152
Cdd:cd03230 155 LEEAERLCDRVAILNNGRI 173
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-172 |
3.56e-15 |
|
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: 78.05 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 3 ILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL--RVPVDYLPQ--------- 71
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgeTVKLAYVDQsrdaldpnk 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 -----------------IQAPSPQ-------------------SGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNC 115
Cdd:TIGR03719 402 tvweeisggldiiklgkREIPSRAyvgrfnfkgsdqqkkvgqlSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 116 LIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIE-QRRLSVYKGNYTDYlklQENKRAK 172
Cdd:TIGR03719 482 LEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEY---EEDKKRR 536
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
291-445 |
3.61e-15 |
|
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: 78.34 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLP---------GYYYDQLS-------VGYFSQNfDQLdLNQSILENVTQD 354
Cdd:COG2274 496 LTIKPGERVAIVGRSGSGKSTLLK-LLLGLYEptsgrilidGIDLRQIDpaslrrqIGVVLQD-VFL-FSGTIRENITLG 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 355 SVQ-SMTLVRNLL--AGLGFNIDKLDQRIST--------LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEA 423
Cdd:COG2274 573 DPDaTDEEIIEAArlAGLHDFIEALPMGYDTvvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILE 652
|
170 180
....*....|....*....|....
gi 1092676368 424 FLQEYPG--TFVLVSHDQQFIKEC 445
Cdd:COG2274 653 NLRRLLKgrTVIIIAHRLSTIRLA 676
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
291-440 |
3.75e-15 |
|
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: 74.46 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK---GMVSRS-----LPGY------YYDQLSVGYFSQnFDQLDLNQSILENVtqdsv 356
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKmltGELRPTsgtayINGYsirtdrKAARQSLGYCPQ-FDALFDELTVREHL----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 357 QSMTLVR------------NLLAGLGFnIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDlPTLQ-ELEA 423
Cdd:cd03263 97 RFYARLKglpkseikeeveLLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PASRrAIWD 174
|
170
....*....|....*....
gi 1092676368 424 FLQEYPG--TFVLVSHDQQ 440
Cdd:cd03263 175 LILEVRKgrSIILTTHSMD 193
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
275-438 |
4.52e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 74.25 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 275 DIDVQVDDRLL-FHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--GY-------YYD----------QLSVGYF 334
Cdd:cd03297 1 MLCVDIEKRLPdFTLKIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPdgGTivlngtvLFDsrkkinlppqQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 335 SQN---FDQLDLNQSIL-------ENVTQDSVQSMTLVrnllaglgFNIDKL-DQRISTLSGGERVRLSLAKVLLADHHL 403
Cdd:cd03297 81 FQQyalFPHLNVRENLAfglkrkrNREDRISVDELLDL--------LGLDHLlNRYPAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092676368 404 LFLDEPTNYLDLPTLQELEAFLQE----YPGTFVLVSHD 438
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHD 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
26-152 |
5.91e-15 |
|
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: 72.85 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR-VPVDYLPQIQ-----APSPQ------------------SGG 81
Cdd:cd03214 22 IEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDgKDLASLSPKElarkiAYVPQalellglahladrpfnelSGG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 82 E------ATITALQPlfvwpkSLLILDEPTANLDLDHKNCLIQQVKDYPG----AVLMVSHDrdfLDQTV---DWIWAIE 148
Cdd:cd03214 102 ErqrvllARALAQEP------PILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVLHD---LNLAAryaDRVILLK 172
|
....
gi 1092676368 149 QRRL 152
Cdd:cd03214 173 DGRI 176
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
290-409 |
1.26e-14 |
|
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: 73.35 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTT----------------FLKGMVSRSLPGYYYDQLSVGYFSQN---FDQLDLNQSI--- 347
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTtfymivglvkpdsgkiLLDGQDITKLPMHKRARLGIGYLPQEasiFRKLTVEENIlav 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 348 LENVTQDSVQSMTLVRNLLAGlgFNIDKL-DQRISTLSGGERVRLSLAKVLLADHHLLFLDEP 409
Cdd:cd03218 100 LEIRGLSKKEREEKLEELLEE--FHITHLrKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
267-414 |
2.41e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 267 SNTLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK---GMVS----------RSLPGY-YYDQLSVG 332
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRmllGLTHpdagsislcgEPVPSRaRHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 333 YFSQnFDQLDLNQSILENVT-------QDSVQSMTLVRNLL--AGLGfniDKLDQRISTLSGGERVRLSLAKVLLADHHL 403
Cdd:PRK13537 84 VVPQ-FDNLDPDFTVRENLLvfgryfgLSAAAARALVPPLLefAKLE---NKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170
....*....|.
gi 1092676368 404 LFLDEPTNYLD 414
Cdd:PRK13537 160 LVLDEPTTGLD 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
291-462 |
2.76e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.01 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLP---------GYYYDQLS----------VGYFSQNFdQLDLNQSILENV 351
Cdd:COG2884 23 LEIEKGEFVFLTGPSGAGKSTLLK-LLYGEERptsgqvlvnGQDLSRLKrreipylrrrIGVVFQDF-RLLPDRTVYENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 T-------QDSVQSMTLVRNLLA--GLGfniDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQE-- 420
Cdd:COG2884 101 AlplrvtgKSRKEIRRRVREVLDlvGLS---DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEim 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1092676368 421 --LEAFLQEypGTFVLV-SHDQQFIKECVNRRYYIKDQQLLNEQQ 462
Cdd:COG2884 178 elLEEINRR--GTTVLIaTHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
262-464 |
3.17e-14 |
|
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: 72.08 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 262 HLSDPSNTLIHLQDIDVQVddrllfhlqhfklQKGDKVGLLGPNKAGKTTFL----------KGMVS---RSLPGYYYDQ 328
Cdd:COG4181 17 TVGTGAGELTILKGISLEV-------------EAGESVAIVGASGSGKSTLLgllagldrptSGTVRlagQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 329 L------SVGYFSQNFdQLDLNQSILENVT-----QDSVQSMTLVRNLLA--GLGfniDKLDQRISTLSGGERVRLSLAK 395
Cdd:COG4181 84 RarlrarHVGFVFQSF-QLLPTLTALENVMlplelAGRRDARARARALLErvGLG---HRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 396 VLLADHHLLFLDEPTNYLDLPTLQELEAFL----QEYPGTFVLVSHDQQFIKECvNRRYYIKDQQLLNEQQDT 464
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLVTHDPALAARC-DRVLRLRAGRLVEDTAAT 231
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-165 |
6.29e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 74.51 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 31 RIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------------DLRV-PVDYLPQIQAPSPQ--------SGGE 82
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhhvdglDLSSnPLLYMMRCFPGVPEqklrahlgSFGV 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 83 ATITALQPLFVWP---KS-------------LLILDEPTANLDLDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVDWIWA 146
Cdd:PLN03073 617 TGNLALQPMYTLSggqKSrvafakitfkkphILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWV 696
|
170
....*....|....*....
gi 1092676368 147 IEQRRLSVYKGNYTDYLKL 165
Cdd:PLN03073 697 VSEGKVTPFHGTFHDYKKT 715
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
291-409 |
7.54e-14 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 71.15 E-value: 7.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTT----------------FLKGMVSRSLPGYYYDQLSVGYFSQN---FDQLDLNQSIL--- 348
Cdd:TIGR04406 22 LSVKSGEIVGLLGPNGAGKTTsfymivglvrpdagkiLIDGQDITHLPMHERARLGIGYLPQEasiFRKLTVEENIMavl 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 349 ---ENVTQDSVQSMTlvRNLLAGlgFNIDKL-DQRISTLSGGERVRLSLAKVLLADHHLLFLDEP 409
Cdd:TIGR04406 102 eirKDLDRAEREERL--EALLEE--FQISHLrDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
291-409 |
8.01e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.21 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTT----------------FLKGMVSRSLPGYYYDQLSVGYFSQN---FDQLDLNQ---SIL 348
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTtfymivglvkpdsgriFLDGEDITHLPMHKRARLGIGYLPQEasiFRKLTVEDnilAVL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 349 ENVTQDSVQSMTLVRNLLAGlgFNIDKL-DQRISTLSGGERVRLSLAKVLLADHHLLFLDEP 409
Cdd:COG1137 104 ELRKLSKKEREERLEELLEE--FGITHLrKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
291-459 |
8.19e-14 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 70.84 E-value: 8.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFL----------------KGMVSRSLPGY---YYDQLSVGYFSQnFDQLDLNQSILENV 351
Cdd:TIGR02211 26 LSIGKGEIVAIVGSSGSGKSTLLhllggldnptsgevlfNGQSLSKLSSNeraKLRNKKLGFIYQ-FHHLLPDFTALENV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 T-------QDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT------- 417
Cdd:TIGR02211 105 AmplligkKSVKEAKERAYEMLEKVGLE-HRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNakiifdl 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1092676368 418 LQELEaflQEYPGTFVLVSHDQQFIKeCVNRRYYIKDQQLLN 459
Cdd:TIGR02211 184 MLELN---RELNTSFLVVTHDLELAK-KLDRVLEMKDGQLFN 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
291-438 |
1.03e-13 |
|
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: 73.55 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMvSRSLP---------GYYYDQLS-------VGYFSQN---FDQldlnqSILEN- 350
Cdd:TIGR02868 356 LDLPPGERVAILGPSGSGKSTLLATL-AGLLDplqgevtldGVPVSSLDqdevrrrVSVCAQDahlFDT-----TVRENl 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 351 ------VTQDSVQSMtLVRnllAGLGFNIDKLDQRIST--------LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLP 416
Cdd:TIGR02868 430 rlarpdATDEELWAA-LER---VGLADWLRALPDGLDTvlgeggarLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170 180
....*....|....*....|....
gi 1092676368 417 TLQE-LEAFLQEYPG-TFVLVSHD 438
Cdd:TIGR02868 506 TADElLEDLLAALSGrTVVLITHH 529
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
26-152 |
1.17e-13 |
|
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: 73.25 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------DLRVPVDYLPQ--------------IQAPS-- 76
Cdd:COG4988 360 IPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdldpaSWRRQIAWVPQnpylfagtirenlrLGRPDas 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 77 --------------------PQ-------------SGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCLIQQVKDY 123
Cdd:COG4988 440 deeleaaleaagldefvaalPDgldtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL 519
|
170 180 190
....*....|....*....|....*....|.
gi 1092676368 124 PG--AVLMVSHDRDFLDQtVDWIWAIEQRRL 152
Cdd:COG4988 520 AKgrTVILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
291-448 |
1.32e-13 |
|
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: 70.44 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK----------------GMVSRSLPGYYYDQLSVGYFSQN--------FDQLDLNQS 346
Cdd:cd03267 42 FTIEKGEIVGFIGPNGAGKTTTLKilsgllqptsgevrvaGLVPWKRRKKFLRRIGVVFGQKTqlwwdlpvIDSFYLLAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 347 ILEnvtQDSVQSMTLVRNLLAGLgfNIDK-LDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFL 425
Cdd:cd03267 122 IYD---LPPARFKKRLDELSELL--DLEElLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFL 196
|
170 180
....*....|....*....|....*..
gi 1092676368 426 QEY----PGTFVLVSHDQQFIKECVNR 448
Cdd:cd03267 197 KEYnrerGTTVLLTSHYMKDIEALARR 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
269-438 |
1.36e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 269 TLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLkgmvsRSLPGYYY-DQLSVGYFSQNFDQLD----- 342
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLL-----RALSGELSpDSGEVRLNGRPLADWSpaela 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 343 -----LNQS--------ILENV-------TQDSVQSMTLVRNLLAGLGfnIDKLDQR-ISTLSGGERVRLSLAKVLLADH 401
Cdd:PRK13548 76 rrravLPQHsslsfpftVEEVVamgraphGLSRAEDDALVAAALAQVD--LAHLAGRdYPQLSGGEQQRVQLARVLAQLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092676368 402 H------LLFLDEPTNYLDL----PTLQELEAFLQEYPGTFVLVSHD 438
Cdd:PRK13548 154 EpdgpprWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD 200
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
291-443 |
1.53e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLkgmvsRSLPGYYYDQLSVGYFSQNFDQLDLNQSILENVtqDSVQSMTLVRNLL--AG 368
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLL-----RLLAGALKGTPVAGCVDVPDNQFGREASLIDAI--GRKGDFKDAVELLnaVG 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092676368 369 LGFNIDKLdQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQ----EYPGTFVLVSHDQQFIK 443
Cdd:COG2401 124 LSDAVLWL-RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQklarRAGITLVVATHHYDVID 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
292-414 |
1.70e-13 |
|
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: 72.89 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 292 KLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--GYYYDQLSVGYFSQ--NFDQLDLNQSILENVTQDSVQSmTLVRNLLA 367
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPdeGEVDEDLKISYKPQyiSPDYDGTVEEFLRSANTDDFGS-SYYKTEII 440
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1092676368 368 GlGFNIDKL-DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:COG1245 441 K-PLGLEKLlDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
273-438 |
2.04e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.87 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 273 LQDIDVQVDDRLL-FHLQhfkLQKGDKVGLLGPNKAGKTTFLK---GMVS---------RSLPGYYYDQLSV--GYFSQN 337
Cdd:COG4138 1 LQLNDVAVAGRLGpISAQ---VNAGELIHLIGPNGAGKSTLLArmaGLLPgqgeillngRPLSDWSAAELARhrAYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 338 ---------FDQLDLNQSilENVTQDSVQsmTLVRNLLAGLGFNiDKLDQRISTLSGGE--RVRlsLAKVLL-------A 399
Cdd:COG4138 78 qsppfampvFQYLALHQP--AGASSEAVE--QLLAQLAEALGLE-DKLSRPLTQLSGGEwqRVR--LAAVLLqvwptinP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1092676368 400 DHHLLFLDEPTNYLDLPTLQELEAFLQEYP---GTFVLVSHD 438
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
291-448 |
4.55e-13 |
|
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: 68.39 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--------GYYYDQLS-------VGYFSQNFdQLdLNQSILENVT--Q 353
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPtsgsvlldGTDIRQLDpadlrrnIGYVPQDV-TL-FYGTLRDNITlgA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 354 DSVQSMTLVRNL-LAGLGFNIDK----LDQRIS----TLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAF 424
Cdd:cd03245 103 PLADDERILRAAeLAGVTDFVNKhpngLDLQIGergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER 182
|
170 180
....*....|....*....|....*.
gi 1092676368 425 LQEYPG--TFVLVSHDQQFIkECVNR 448
Cdd:cd03245 183 LRQLLGdkTLIIITHRPSLL-DLVDR 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
291-458 |
5.03e-13 |
|
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: 71.37 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLP---GYYYDQLS--------------------VGYFSQNFDqLDLNQSI 347
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSK-IIAGVLEptsGEVNVRVGdewvdmtkpgpdgrgrakryIGILHQEYD-LYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 348 LENVTQ-------DSVQSMTLVRNLLAgLGFNIDK----LDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLP 416
Cdd:TIGR03269 383 LDNLTEaiglelpDELARMKAVITLKM-VGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1092676368 417 TLQEL-EAFL---QEYPGTFVLVSHDQQFIKECVNRRYYIKDQQLL 458
Cdd:TIGR03269 462 TKVDVtHSILkarEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
286-448 |
6.82e-13 |
|
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: 68.13 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 286 FHLQ--HFKLQKGDKVGLLGPNKAGKTTFLK---GMVSR-----SLPGYYYDQLS-----VGYFSQN---FDQLDLNQSI 347
Cdd:cd03299 13 FKLKnvSLEVERGDYFVILGPTGSGKSVLLEtiaGFIKPdsgkiLLNGKDITNLPpekrdISYVPQNyalFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 348 ---LENVTQDSVQSMTLVRNLLAGLGfnIDK-LDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT----LQ 419
Cdd:cd03299 93 aygLKKRKVDKKEIERKVLEIAEMLG--IDHlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklRE 170
|
170 180
....*....|....*....|....*....
gi 1092676368 420 ELEAFLQEYPGTFVLVSHDQQFIKECVNR 448
Cdd:cd03299 171 ELKKIRKEFGVTVLHVTHDFEEAWALADK 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
271-437 |
8.23e-13 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 66.47 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDR---LLFHLqHFKLQKGDKVGLLGPNKAGKTTFLKGM-----------------VSRSLPGYYYDQls 330
Cdd:cd03246 1 LEVENVSFRYPGAeppVLRNV-SFSIEPGESLAIIGPSGSGKSTLARLIlgllrptsgrvrldgadISQWDPNELGDH-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 331 VGYFSQNfDQLdLNQSILENVtqdsvqsmtlvrnllaglgfnidkldqristLSGGERVRLSLAKVLLADHHLLFLDEPT 410
Cdd:cd03246 78 VGYLPQD-DEL-FSGSIAENI-------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190
....*....|....*....|....*....|
gi 1092676368 411 NYLDLPT---LQELEAFLQEYPGTFVLVSH 437
Cdd:cd03246 125 SHLDVEGeraLNQAIAALKAAGATRIVIAH 154
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
291-437 |
1.00e-12 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 67.24 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPgyyyDQLSVGYFSQNFDQL--DLNQ--SILEnvTQDSVQSMTLVRNLL 366
Cdd:cd03268 21 LHVKKGEIYGFLGPNGAGKTTTMKIILGLIKP----DSGEITFDGKSYQKNieALRRigALIE--APGFYPNLTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 367 ---AGLGF---NIDKL----------DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD---LPTLQELEAFLQE 427
Cdd:cd03268 95 llaRLLGIrkkRIDEVldvvglkdsaKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpdgIKELRELILSLRD 174
|
170
....*....|
gi 1092676368 428 YPGTFVLVSH 437
Cdd:cd03268 175 QGITVLISSH 184
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
291-448 |
1.16e-12 |
|
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: 67.17 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGM---------------VSRSLPGYYYDQL--SVGYFSQNFDqLDLNQSILENVT- 352
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCInlleepdsgtiiidgLKLTDDKKNINELrqKVGMVFQQFN-LFPHLTVLENITl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 353 -QDSVQSM------TLVRNLLAGLGFnIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFL 425
Cdd:cd03262 100 aPIKVKGMskaeaeERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVM 178
|
170 180
....*....|....*....|....*.
gi 1092676368 426 QE--YPG-TFVLVSHDQQFIKECVNR 448
Cdd:cd03262 179 KDlaEEGmTMVVVTHEMGFAREVADR 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
263-457 |
1.17e-12 |
|
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: 70.17 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 263 LSDPSNTLIHLQDIDVQ-VDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK---GMVS----------RSLPGYYYDQ 328
Cdd:COG4988 329 LPAAGPPSIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNlllGFLPpysgsilingVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 329 LS--VGYFSQNfDQLdLNQSILENV-------TQDSVQS-------MTLVRNLLAGLgfnidklDQRI----STLSGGER 388
Cdd:COG4988 409 WRrqIAWVPQN-PYL-FAGTIRENLrlgrpdaSDEELEAaleaaglDEFVAALPDGL-------DTPLgeggRGLSGGQA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 389 VRLSLAKVLLADHHLLFLDEPTNYLDLPT----LQELEAFLQEYpgTFVLVSHDQQFIKECvNRRYYIKDQQL 457
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETeaeiLQALRRLAKGR--TVILITHRLALLAQA-DRILVLDDGRI 549
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
267-414 |
1.17e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 267 SNTLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTT---FLKGMVSRS----------LPGYY-YDQLSVG 332
Cdd:PRK13536 38 STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTiarMILGMTSPDagkitvlgvpVPARArLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 333 YFSQnFDQLDLNQSILENVT-------QDSVQSMTLVRNLL--AGLGfniDKLDQRISTLSGGERVRLSLAKVLLADHHL 403
Cdd:PRK13536 118 VVPQ-FDNLDLEFTVRENLLvfgryfgMSTREIEAVIPSLLefARLE---SKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170
....*....|.
gi 1092676368 404 LFLDEPTNYLD 414
Cdd:PRK13536 194 LILDEPTTGLD 204
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-166 |
1.33e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.92 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI---------------------DL 62
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqdhaydfenDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 63 RVpVDYLPQIQAPSPQ-------------------------SGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCLI 117
Cdd:PRK15064 400 TL-FDWMSQWRQEGDDeqavrgtlgrllfsqddikksvkvlSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLN 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092676368 118 QQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRLSVYKGNYTDYLKLQ 166
Cdd:PRK15064 479 MALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
26-132 |
1.57e-12 |
|
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: 65.70 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------DLRVPVDYLPQ-IQ------APSPQSGGEATI 85
Cdd:cd03246 25 IEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisqwdpnELGDHVGYLPQdDElfsgsiAENILSGGQRQR 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1092676368 86 TAL-QPLFVWPKsLLILDEPTANLDLD---HKNCLIQQVKDYPGAVLMVSH 132
Cdd:cd03246 105 LGLaRALYGNPR-ILVLDEPNSHLDVEgerALNQAIAALKAAGATRIVIAH 154
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-138 |
1.58e-12 |
|
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: 66.35 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 2 AILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR------VPVDYLPQI--- 72
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepirdAREDYRRRLayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 73 -------------------QAPSPQSGGEATITAL-----------QP----------------LFVWPKSLLILDEPTA 106
Cdd:COG4133 81 ghadglkpeltvrenlrfwAALYGLRADREAIDEAleavglagladLPvrqlsagqkrrvalarLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1092676368 107 NLDLDHKNCLIQQVKDYP---GAVLMVSHDRDFLD 138
Cdd:COG4133 161 ALDAAGVALLAELIAAHLargGAVLLTTHQPLELA 195
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-133 |
1.61e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMdTDYQGRIDLR-VPVD------------YLPQIQAPSPQ-------------- 78
Cdd:COG4138 19 VNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNgRPLSdwsaaelarhraYLSQQQSPPFAmpvfqylalhqpag 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 79 ------------------------------SGGE-------ATItaLQplfVWPK-----SLLILDEPTANLDLDHK--- 113
Cdd:COG4138 98 asseaveqllaqlaealgledklsrpltqlSGGEwqrvrlaAVL--LQ---VWPTinpegQLLLLDEPMNSLDVAQQaal 172
|
170 180
....*....|....*....|
gi 1092676368 114 NCLIQQVKDYPGAVLMVSHD 133
Cdd:COG4138 173 DRLLRELCQQGITVVMSSHD 192
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-142 |
3.10e-12 |
|
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: 68.85 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 24 LLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------DLRVPVDYLPQ------------------- 71
Cdd:TIGR02857 343 FTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadadSWRDQIAWVPQhpflfagtiaenirlarpd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 ------------------IQApSPQ-------------SGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCLIQQV 120
Cdd:TIGR02857 423 asdaeirealeragldefVAA-LPQgldtpigeggaglSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL 501
|
170 180
....*....|....*....|....*..
gi 1092676368 121 KDYPG--AVLMVSHDRDFL---DQTVD 142
Cdd:TIGR02857 502 RALAQgrTVLLVTHRLALAalaDRIVV 528
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-152 |
3.57e-12 |
|
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: 65.69 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 19 LEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------DLRVPVDYLPQ-------------- 71
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqldpaDLRRNIGYVPQdvtlfygtlrdnit 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 IQAPS----------------------PQ-------------SGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCL 116
Cdd:cd03245 100 LGAPLadderilraaelagvtdfvnkhPNgldlqigergrglSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092676368 117 IQQVKDYPG--AVLMVSHdRDFLDQTVDWIWAIEQRRL 152
Cdd:cd03245 180 KERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
270-438 |
8.11e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 65.52 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 270 LIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLPGYyydQLSVGYFSQNFDQLDLNQ---- 345
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLK-LLTGELTPS---SGEVRLNGRPLAAWSPWElarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 346 --------------SILENV-------TQDSVQSMTLVRNLLA--GLGfniDKLDQRISTLSGGERVRLSLAKVLL---- 398
Cdd:COG4559 77 ravlpqhsslafpfTVEEVValgraphGSSAAQDRQIVREALAlvGLA---HLAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092676368 399 ---ADHHLLFLDEPTNYLDLP----TLQELEAFLQEyPGTFVLVSHD 438
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDLAhqhaVLRLARQLARR-GGGVVAVLHD 199
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-158 |
8.36e-12 |
|
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: 65.26 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQG--RIDLRVPVD----------YLPQ 71
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGsiLIDGEDVRKeprearrqigVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 -------------IQAPSPQ--------------------------------SGGEATITALQPLFVWPKSLLILDEPTA 106
Cdd:COG4555 82 erglydrltvrenIRYFAELyglfdeelkkrieeliellgleefldrrvgelSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 107 NLDLDHKNCL---IQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRLsVYKGN 158
Cdd:COG4555 162 GLDVMARRLLreiLRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV-VAQGS 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
293-461 |
9.66e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 293 LQKGDKVGLLGPNKAGKTTFLKGM-------------------VSRSLPGY--YYDQL--SVGYFSQNFDqLDLNQSILE 349
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirvgditidTARSLSQQkgLIRQLrqHVGFVFQNFN-LFPHRTVLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 350 NVTQDSV--------QSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQEL 421
Cdd:PRK11264 105 NIIEGPVivkgepkeEATARARELLAKVGLA-GKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1092676368 422 EAF---LQEYPGTFVLVSHDQQFIKECVNRRYYIkDQQLLNEQ 461
Cdd:PRK11264 184 LNTirqLAQEKRTMVIVTHEMSFARDVADRAIFM-DQGRIVEQ 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
288-457 |
1.11e-11 |
|
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: 63.49 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 288 LQHFKLQ--KGDKVGLLGPNKAGKTTFLkgmvsrslpgyyydQLSVGYFSQNFDQLDLNQSILENVtQDSVQSMTLVRNL 365
Cdd:cd03247 18 LKNLSLElkQGEKIALLGRSGSGKSTLL--------------QLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 366 LAGLgFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQE-LEAFLQEYPG-TFVLVSHDQQFIk 443
Cdd:cd03247 83 RPYL-FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQlLSLIFEVLKDkTLIWITHHLTGI- 160
|
170
....*....|....
gi 1092676368 444 ECVNRRYYIKDQQL 457
Cdd:cd03247 161 EHMDKILFLENGKI 174
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
271-458 |
1.28e-11 |
|
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: 64.45 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMV------------------SRSLPGYYYDQLSVG 332
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVgllrpdsgevlidgedisGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 333 Y-FSQN--FDQLdlnqSILENV-------TQDSVQSMT-LVRNLLA--GLGfniDKLDQRISTLSGGERVRLSLAKVLLA 399
Cdd:cd03261 81 MlFQSGalFDSL----TVFENVafplrehTRLSEEEIReIVLEKLEavGLR---GAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 400 DHHLLFLDEPTNYLDLPTLQELEAFL----QEYPGTFVLVSHDQQFIKECVNRRYYIKDQQLL 458
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-137 |
1.41e-11 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 62.97 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR-VPVDYLPQIQAPS------ 76
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDLEDELPPLrrrigm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 77 -------------------PQSGGEATITALQPLFVWPKSLLILDEPTANLDLDHKN---CLIQQVKDYPG-AVLMVSHD 133
Cdd:cd03229 81 vfqdfalfphltvlenialGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRevrALLKSLQAQLGiTVVLVTHD 160
|
....
gi 1092676368 134 RDFL 137
Cdd:cd03229 161 LDEA 164
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
300-414 |
1.72e-11 |
|
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: 63.75 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 300 GLLGPNKAGKTTFLK-----------------------GMVSRSLPGY------YYDQLSVgyfsqnFDQLDLnQSILEN 350
Cdd:cd03264 29 GLLGPNGAGKTTLMRilatltppssgtiridgqdvlkqPQKLRRRIGYlpqefgVYPNFTV------REFLDY-IAWLKG 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 351 VTQDSVQSmtLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:cd03264 102 IPSKEVKA--RVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
291-439 |
1.83e-11 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 63.69 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK----------GMVS---RSLPGYYYDQLSVGYFSQNFdQLDLNQSILENV------ 351
Cdd:cd03259 21 LTVEPGEFLALLGPSGCGKTTLLRliaglerpdsGEILidgRDVTGVPPERRNIGMVFQDY-ALFPHLTVAENIafglkl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 -TQDSVQSMTLVRNLLAGLGFnIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG 430
Cdd:cd03259 100 rGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQR 178
|
170
....*....|...
gi 1092676368 431 ----TFVLVSHDQ 439
Cdd:cd03259 179 elgiTTIYVTHDQ 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-170 |
1.90e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 3 ILELNHIKKTWQaelileiDRLLVQ------PQDRI-GLVGANGSGKSTLLRMIMGMDTDYQGRIDL--RVPVDYLPQ-- 71
Cdd:PRK11819 324 VIEAENLSKSFG-------DRLLIDdlsfslPPGGIvGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgeTVKLAYVDQsr 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 ------------------------IQAPS------------PQ-------SGGEATITALQPLFVWPKSLLILDEPTANL 108
Cdd:PRK11819 397 daldpnktvweeisggldiikvgnREIPSrayvgrfnfkggDQqkkvgvlSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 109 DLDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVDWIWAIE-QRRLSVYKGNYTDYlklQENKR 170
Cdd:PRK11819 477 DVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEY---EEDKK 536
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
249-448 |
2.11e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.11 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 249 PVKEKRYTLK-ALGHLSDPSNTLIH-LQDIDvqvddrllfhlqhFKLQKGDKVGLLGPNKAGKTTFLK------------ 314
Cdd:COG4586 12 RVYEKEPGLKgALKGLFRREYREVEaVDDIS-------------FTIEPGEIVGFIGPNGAGKSTTIKmltgilvptsge 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 315 ----GMV-SRSLPGYYYdQLSV--GYFSQNF------DQLDLNQSILENVTQDSVQSMTLVRNLLaGLGfniDKLDQRIS 381
Cdd:COG4586 79 vrvlGYVpFKRRKEFAR-RIGVvfGQRSQLWwdlpaiDSFRLLKAIYRIPDAEYKKRLDELVELL-DLG---ELLDTPVR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 382 TLSGGERVRLSLAKVLLadHH--LLFLDEPTNYLDLPTLQELEAFL----QEYPGTFVLVSHDQQFIKECVNR 448
Cdd:COG4586 154 QLSLGQRMRCELAAALL--HRpkILFLDEPTIGLDVVSKEAIREFLkeynRERGTTILLTSHDMDDIEALCDR 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
271-438 |
2.75e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDidVQVDDRLLfhLQHFKLQKGDKVGLLGPNKAGKTTFLKGMV------------SRSLPGYYYDQLSV--GYFSQ 336
Cdd:PRK03695 1 MQLND--VAVSTRLG--PLSAEVRAGEILHLVGPNGAGKSTLLARMAgllpgsgsiqfaGQPLEAWSAAELARhrAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 337 N---------FDQLDLNQSILENVTQDSVQSMTLVRNLlaGLGfniDKLDQRISTLSGGE--RVRlsLAKVLLADH---- 401
Cdd:PRK03695 77 QqtppfampvFQYLTLHQPDKTRTEAVASALNEVAEAL--GLD---DKLGRSVNQLSGGEwqRVR--LAAVVLQVWpdin 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1092676368 402 ---HLLFLDEPTNYLDLPTLQELEAFLQEYP---GTFVLVSHD 438
Cdd:PRK03695 150 pagQLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
26-138 |
2.77e-11 |
|
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: 63.67 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL-------RVPVDYLPQIQA------------------------ 74
Cdd:COG1124 28 VAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrRRRKAFRRRVQMvfqdpyaslhprhtvdrilaeplr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 75 ----------------------------PSPQSGGE------ATITALQPlfvwpkSLLILDEPTANLDLDHK----NCL 116
Cdd:COG1124 108 ihglpdreeriaelleqvglppsfldryPHQLSGGQrqrvaiARALILEP------ELLLLDEPTSALDVSVQaeilNLL 181
|
170 180
....*....|....*....|..
gi 1092676368 117 IQQVKDYPGAVLMVSHDRDFLD 138
Cdd:COG1124 182 KDLREERGLTYLFVSHDLAVVA 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
291-448 |
2.80e-11 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 63.61 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLPGY----YYD-------------QLSVGYFSQN---FDQLdlnqSILEN 350
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFN-LISGFLRPTsgsvLFDgeditglppheiaRLGIGRTFQIprlFPEL----TVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 351 V----TQDSVQSMTLVRN-------------LLA--GLGfniDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTN 411
Cdd:cd03219 96 VmvaaQARTGSGLLLARArreereareraeeLLErvGLA---DLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092676368 412 YLDLPTLQELEAFLQEYPG---TFVLVSHDQQFIKECVNR 448
Cdd:cd03219 173 GLNPEETEELAELIRELRErgiTVLLVEHDMDVVMSLADR 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
330-461 |
2.98e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.26 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 330 SVGYFSQNFdQLDLNQSILENVT-------QDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHH 402
Cdd:PRK10584 89 HVGFVFQSF-MLIPTLNALENVElpallrgESSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 403 LLFLDEPTNYLDLPTLQELEAFL----QEYPGTFVLVSHDQQFIKECvNRRYYIKDQQLLNEQ 461
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQLAARC-DRRLRLVNGQLQEEA 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
290-438 |
3.22e-11 |
|
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: 63.67 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLKgmvsrslpgyyydqLSVGYFSQNFDQLDLNQSILEN------------VTQDSVQ 357
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLR--------------ALAGLERPWSGEVTFDGRPVTRrrrkafrrrvqmVFQDPYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 358 S----MTL-------------------VRNLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:COG1124 91 SlhprHTVdrilaeplrihglpdreerIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180
....*....|....*....|....*...
gi 1092676368 415 LPT----LQELEAFLQEYPGTFVLVSHD 438
Cdd:COG1124 171 VSVqaeiLNLLKDLREERGLTYLFVSHD 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
32-141 |
3.48e-11 |
|
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: 62.94 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGMDTDYQGRIDL--------RVPVDYLPQ--------------------------IQAPSP 77
Cdd:cd03235 28 LAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplekeRKRIGYVPQrrsidrdfpisvrdvvlmglyghkglFRRLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 78 Q-------------------------SGGEatitaLQPLF-----VWPKSLLILDEPTANLDLDHKNC---LIQQVKDYP 124
Cdd:cd03235 108 AdkakvdealervglseladrqigelSGGQ-----QQRVLlaralVQDPDLLLLDEPFAGVDPKTQEDiyeLLRELRREG 182
|
170 180
....*....|....*....|.
gi 1092676368 125 GAVLMVSHD----RDFLDQTV 141
Cdd:cd03235 183 MTILVVTHDlglvLEYFDRVL 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
291-448 |
3.87e-11 |
|
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: 62.91 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPgyyyDQLSVGYFSQnfDQLDLNQSILEN-------VTQDSVQS----M 359
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKP----TSGSIIFDGK--DLLKLSRRLRKIrrkeiqmVFQDPMSSlnprM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 360 T-----------------------LVRNLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLP 416
Cdd:cd03257 100 TigeqiaeplrihgklskkearkeAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1092676368 417 T----LQELEAFLQEYPGTFVLVSHDQQFIKECVNR 448
Cdd:cd03257 180 VqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADR 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
26-133 |
4.37e-11 |
|
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: 63.14 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR-VPVD------------YLPQ--------------------- 71
Cdd:COG1120 24 LPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgRDLAslsrrelarriaYVPQeppapfgltvrelvalgryph 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 ---IQAPSPQ-------------------------SGGE------ATITALQPlfvwpkSLLILDEPTANLDLDHK---- 113
Cdd:COG1120 104 lglFGRPSAEdreaveealertglehladrpvdelSGGErqrvliARALAQEP------PLLLLDEPTSHLDLAHQlevl 177
|
170 180
....*....|....*....|
gi 1092676368 114 NCLIQQVKDYPGAVLMVSHD 133
Cdd:COG1120 178 ELLRRLARERGRTVVMVLHD 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
268-475 |
7.35e-11 |
|
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: 64.54 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 268 NTLIHLQDIDVQVDDRLLFHLQH--FKLQKGDKVGLLGPNKAGKTTFLKGmVSRSLP------------GYYYDQLS--- 330
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGvsLTIAPGETVALVGESGSGKSTLALA-LMGLLPhggrisgevlldGRDLLELSeal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 331 ----VGYFSQNFD-QLD----LNQSI--LENVTQDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLA 399
Cdd:COG1123 81 rgrrIGMVFQDPMtQLNpvtvGDQIAeaLENLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 400 DHHLLFLDEPTNYLDLPT----LQELEAFLQEYPGTFVLVSHDQQFIKECVNRRYYIKDQQLLnEQQDTDYSDRSQQTLS 475
Cdd:COG1123 160 DPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV-EDGPPEEILAAPQALA 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-183 |
7.46e-11 |
|
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: 64.40 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTW--QAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------DLRVPVDY 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdldedDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 69 LPQ--------------IQAPS----------------------PQ-------------SGGEATITALQPLFVWPKSLL 99
Cdd:COG4987 414 VPQrphlfdttlrenlrLARPDatdeelwaalervglgdwlaalPDgldtwlgeggrrlSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 100 ILDEPTANLD-------LDHkncLIQQVKDypGAVLMVSHDRDFLDQtVDWIWAIEQRRLsVYKGNYTDYlkLQENKRak 172
Cdd:COG4987 494 LLDEPTEGLDaateqalLAD---LLEALAG--RTVLLITHRLAGLER-MDRILVLEDGRI-VEQGTHEEL--LAQNGR-- 562
|
250
....*....|.
gi 1092676368 173 qwqdYYQYQDR 183
Cdd:COG4987 563 ----YRQLYQR 569
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
271-440 |
9.36e-11 |
|
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: 61.81 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLPGYYY--DQLSVGYFSQNFDQLDLN---- 344
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLR-LLNRLNDLIPGapDEGEVLLDGKDIYDLDVDvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 345 --------Q-------SILENVT--------QDSVQSMTLVRNLL--AGLGFNI-DKLDQRisTLSGGERVRLSLAKVLL 398
Cdd:cd03260 80 rrrvgmvfQkpnpfpgSIYDNVAyglrlhgiKLKEELDERVEEALrkAALWDEVkDRLHAL--GLSGGQQQRLCLARALA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1092676368 399 ADHHLLFLDEPTNYLDLPTLQELEAFLQEY--PGTFVLVSHD-QQ 440
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNmQQ 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
271-437 |
9.96e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.06 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQV-DDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK----------GMVSRS-------LP-------GYY 325
Cdd:COG4178 363 LALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRaiaglwpygsGRIARPagarvlfLPqrpylplGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 326 YDQLSVGYFSQNFDQLDLNQsILENVtqdsvqsmtlvrnllaGLGFNIDKLDQRIS---TLSGGERVRLSLAKVLLADHH 402
Cdd:COG4178 443 REALLYPATAEAFSDAELRE-ALEAV----------------GLGHLAERLDEEADwdqVLSLGEQQRLAFARLLLHKPD 505
|
170 180 190
....*....|....*....|....*....|....*..
gi 1092676368 403 LLFLDEPTNYLDLPTLQEL-EAFLQEYPG-TFVLVSH 437
Cdd:COG4178 506 WLFLDEATSALDEENEAALyQLLREELPGtTVISVGH 542
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
17-137 |
1.20e-10 |
|
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: 61.12 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 17 LILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLRVP-----------------VDY----------- 68
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrksigyvmqdVDYqlftdsvreel 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 69 ---LPQIQAPSPQ---------------------SGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNC---LIQQVK 121
Cdd:cd03226 94 llgLKELDAGNEQaetvlkdldlyalkerhplslSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERvgeLIRELA 173
|
170
....*....|....*.
gi 1092676368 122 DYPGAVLMVSHDRDFL 137
Cdd:cd03226 174 AQGKAVIVITHDYEFL 189
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
291-437 |
1.39e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 63.65 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSRslpgyYYD----QLSVGyfSQNFDQLDLnQSILEN---VTQDSVQ-SMTLV 362
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVN-LLLR-----FYDptsgRILID--GVDIRDLTL-ESLRRQigvVPQDTFLfSGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 363 RNL-----------------LAGLGFNIDKL----DQRI----STLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT 417
Cdd:COG1132 432 ENIrygrpdatdeeveeaakAAQAHEFIEALpdgyDTVVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTET 511
|
170 180
....*....|....*....|....
gi 1092676368 418 ---LQE-LEAFLQEYpgTFVLVSH 437
Cdd:COG1132 512 ealIQEaLERLMKGR--TTIVIAH 533
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
271-427 |
1.45e-10 |
|
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: 61.48 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDRLLFHLQH--FKLQKGDKVGLLGPNKAGKTTFLKgMVSR--------------SLPGYYYDQL--SVG 332
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDisLDIPAGETVALVGPSGSGKSTLVN-LIPRfydvdsgrilidghDVRDYTLASLrrQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 333 YFSQnfDQLDLNQSILENV-------TQDSV-------QSMTLVRNLLAGLGFNIDkldQRISTLSGGERVRLSLAKVLL 398
Cdd:cd03251 80 LVSQ--DVFLFNDTVAENIaygrpgaTREEVeeaaraaNAHEFIMELPEGYDTVIG---ERGVKLSGGQRQRIAIARALL 154
|
170 180
....*....|....*....|....*....
gi 1092676368 399 ADHHLLFLDEPTNYLDLptlqELEAFLQE 427
Cdd:cd03251 155 KDPPILILDEATSALDT----ESERLVQA 179
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
293-414 |
1.63e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 293 LQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--GYYYDQLSVGYFSQNF--DQLDLNQSILENVTQDSVQSMtlVRNLLAG 368
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPdeGEVDPELKISYKPQYIkpDYDGTVEDLLRSITDDLGSSY--YKSEIIK 439
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1092676368 369 lGFNIDKL-DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:PRK13409 440 -PLQLERLlDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
290-448 |
2.45e-10 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 60.67 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLK----------GMVSrsLPGYYYDQLS----------VGYFSQNFDQLDlNQSILE 349
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRcinglerptsGSVL--VDGTDLTLLSgkelrkarrrIGMIFQHFNLLS-SRTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 350 NVT-------QDSVQSMTLVRNLLA--GLGfniDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQE 420
Cdd:cd03258 102 NVAlpleiagVPKAEIEERVLELLElvGLE---DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQS 178
|
170 180 190
....*....|....*....|....*....|..
gi 1092676368 421 LEAFL----QEYPGTFVLVSHDQQFIKECVNR 448
Cdd:cd03258 179 ILALLrdinRELGLTIVLITHEMEVVKRICDR 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
291-436 |
2.47e-10 |
|
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: 60.46 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK---GMVSRS-----LPGYYYDQ------LSVGYFSQN---FDQLdlnqSILENVTQ 353
Cdd:cd03266 26 FTVKPGEVTGLLGPNGAGKTTTLRmlaGLLEPDagfatVDGFDVVKepaearRRLGFVSDStglYDRL----TARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 354 -------DSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQ 426
Cdd:cd03266 102 faglyglKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR 180
|
170
....*....|..
gi 1092676368 427 EY--PGTFVLVS 436
Cdd:cd03266 181 QLraLGKCILFS 192
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
291-448 |
2.48e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 60.62 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK----------GMVSR-----SLPGyyydqLSVGyfsqnfdqLDLNQSILENV---- 351
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRllagiyppdsGTVTVrgrvsSLLG-----LGGG--------FNPELTGRENIylng 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 -----TQDSVQSMtlVRNLL--AGLGfniDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAF 424
Cdd:cd03220 110 rllglSRKEIDEK--IDEIIefSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRR 184
|
170 180
....*....|....*....|....*..
gi 1092676368 425 LQEY---PGTFVLVSHDQQFIKECVNR 448
Cdd:cd03220 185 LRELlkqGKTVILVSHDPSSIKRLCDR 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-135 |
2.75e-10 |
|
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: 60.23 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL------RVPV----------D 67
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtGVPPerrnigmvfqD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 68 Y----------------------LPQIQA------------------PSPQSGGEATITAL------QPlfvwpkSLLIL 101
Cdd:cd03259 81 YalfphltvaeniafglklrgvpKAEIRArvrellelvglegllnryPHELSGGQQQRVALaralarEP------SLLLL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092676368 102 DEPTANLDLDHKNCLIQQVKDYPGA----VLMVSHDRD 135
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRElgitTIYVTHDQE 192
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
293-438 |
2.77e-10 |
|
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: 60.88 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 293 LQKGDKVGLLGPNKAGKTTFLKGMVSRSLPG---YYYDQLSVGYFSQNF--DQLDLNQSILENVTQDSVQSMTLVRNLLA 367
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDegdIEIELDTVSYKPQYIkaDYEGTVRDLLSSITKDFYTHPYFKTEIAK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 368 GLGfnIDKL-DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPtlQELEA------FLQEYPGTFVLVSHD 438
Cdd:cd03237 102 PLQ--IEQIlDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE--QRLMAskvirrFAENNEKTAFVVEHD 175
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
272-440 |
3.63e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.80 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 272 HLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPGY------YYDQLS----------VGYFS 335
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasgevLLNGRRltalpaeqrrIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 336 QN---FDQLDLNQSIL----ENVT----QDSVQSMtLVRNLLAGLGfnidklDQRISTLSGGERVRLSLAKVLLADHHLL 404
Cdd:COG4136 83 QDdllFPHLSVGENLAfalpPTIGraqrRARVEQA-LEEAGLAGFA------DRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092676368 405 FLDEPTNYLDLPTLQELEAF----LQEYPGTFVLVSHDQQ 440
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEE 195
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
291-448 |
4.41e-10 |
|
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: 59.89 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK----------GMVS------RSLPGYYYDQL--SVGYFSQNFdQLDLNQSILENVT 352
Cdd:cd03256 22 LSINPGEFVALIGPSGAGKSTLLRclnglveptsGSVLidgtdiNKLKGKALRQLrrQIGMIFQQF-NLIERLSVLENVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 353 QDSVQSMTLVRNLLA-----------------GLgfnIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDL 415
Cdd:cd03256 101 SGRLGRRSTWRSLFGlfpkeekqralaalervGL---LDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDP 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1092676368 416 PTLQE-LEAFLQ--EYPGTFVLVS-HDQQFIKECVNR 448
Cdd:cd03256 178 ASSRQvMDLLKRinREEGITVIVSlHQVDLAREYADR 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-152 |
4.65e-10 |
|
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: 59.43 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAE----LILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI----------------DLR 63
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklsekelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 64 ------VPVDY-------------LPQIQAPSPQ---------------------------SGGE----ATITAL--QPl 91
Cdd:cd03255 81 rrhigfVFQSFnllpdltalenveLPLLLAGVPKkerreraeellervglgdrlnhypselSGGQqqrvAIARALanDP- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 92 fvwpkSLLILDEPTANLDLDHK----NCLIQQVKDYPGAVLMVSHDRDfLDQTVDWIWAIEQRRL 152
Cdd:cd03255 160 -----KIILADEPTGNLDSETGkevmELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
291-410 |
4.84e-10 |
|
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: 59.37 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK---GMVSRS-------------LPGYYYDQLSVGYFSQN---FDQLdlnqSILENV 351
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKtimGLLPPRsgsirfdgrditgLPPHERARAGIGYVPEGrriFPEL----TVEENL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 TqdsvqsMTLVRNLLAGLGFNID-----------KLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPT 410
Cdd:cd03224 97 L------LGAYARRRAKRKARLErvyelfprlkeRRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-133 |
5.06e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.77 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQaELILEIDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI----------------------- 60
Cdd:COG3840 2 LRLDDLTYRYG-DFPLRFD-LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltalppaerpvsmlfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 61 -------------------DLRVPVDYLPQIQA--------------PSPQSGGEATITALQPLFVWPKSLLILDEPTAN 107
Cdd:COG3840 80 nnlfphltvaqniglglrpGLKLTAEQRAQVEQalervglaglldrlPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190
....*....|....*....|....*....|....
gi 1092676368 108 LD-------LDhkncLIQQV-KDYPGAVLMVSHD 133
Cdd:COG3840 160 LDpalrqemLD----LVDELcRERGLTVLMVTHD 189
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
291-414 |
6.00e-10 |
|
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: 58.72 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFL------------KGMV-----SRSLPGYYYdqlSVGYFSQNfDQLDLNQSILENvtq 353
Cdd:cd03213 30 GKAKPGELTAIMGPSGAGKSTLLnalagrrtglgvSGEVlingrPLDKRSFRK---IIGYVPQD-DILHPTLTVRET--- 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092676368 354 dsvqsmtlvrnllagLGFNIdkldqRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:cd03213 103 ---------------LMFAA-----KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
291-438 |
6.56e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 59.31 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLP------------------------GYYYDQLSVGYFSQNFDQLDLnQS 346
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIK-MLTTLLKptsgratvaghdvvreprevrrriGIVFQDLSVDDELTGWENLYI-HA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 347 ILENVTQDSVQSMtlVRNLLAGLGFnIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQEL----E 422
Cdd:cd03265 99 RLYGVPGAERRER--IDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVweyiE 175
|
170
....*....|....*.
gi 1092676368 423 AFLQEYPGTFVLVSHD 438
Cdd:cd03265 176 KLKEEFGMTILLTTHY 191
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
291-438 |
6.56e-10 |
|
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: 59.62 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSRSL------------PGYYYDQL----SVGYFSQnfdQLDL--NQSILENVT 352
Cdd:cd03295 22 LEIAKGEFLVLIGPSGSGKTTTMK-MINRLIeptsgeifidgeDIREQDPVelrrKIGYVIQ---QIGLfpHMTVEENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 353 -------QDSVQSMTLVRNLLAGLGFNIDKLDQRI-STLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT---LQEL 421
Cdd:cd03295 98 lvpkllkWPKEKIRERADELLALVGLDPAEFADRYpHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITrdqLQEE 177
|
170
....*....|....*...
gi 1092676368 422 EAFLQEYPG-TFVLVSHD 438
Cdd:cd03295 178 FKRLQQELGkTIVFVTHD 195
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
293-438 |
7.16e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 58.40 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 293 LQKGDKVGLLGPNKAGKTTFLKGM---------------------------VSRSLPGYYYDQLSVGYFSQnfdqldlnQ 345
Cdd:NF040873 15 IPAGSLTAVVGPNGSGKSTLLKVLagvlrptsgtvrraggarvayvpqrseVPDSLPLTVRDLVAMGRWAR--------R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 346 SILENVTQDSVQSMT--LVRNLLAGLgfnidkLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEA 423
Cdd:NF040873 87 GLWRRLTRDDRAAVDdaLERVGLADL------AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170
....*....|....*...
gi 1092676368 424 FLQEYPG---TFVLVSHD 438
Cdd:NF040873 161 LLAEEHArgaTVVVVTHD 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
278-454 |
7.27e-10 |
|
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: 59.04 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 278 VQVDD-RLLFHLQ--HFKLQ--KGDKVGLLGPNKAGKTTFLKGMVSRSLP---GYYYDQLSVGY-----------FSQN- 337
Cdd:cd03298 1 VRLDKiRFSYGEQpmHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPqsgRVLINGVDVTAappadrpvsmlFQENn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 338 -FDQLDLNQSI---------LENVTQDSVQSmtlvrnLLAGLGfnIDKLDQRIS-TLSGGERVRLSLAKVLLADHHLLFL 406
Cdd:cd03298 81 lFAHLTVEQNVglglspglkLTAEDRQAIEV------ALARVG--LAGLEKRLPgELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 407 DEPTNYLDLPTLQELEAFL----QEYPGTFVLVSHDQQFIKECVNRRYYIKD 454
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVldlhAETKMTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-132 |
7.68e-10 |
|
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: 57.93 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 14 QAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLrvPVD----YLPQ------------IQAPSP 77
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--PEGedllFLPQrpylplgtlreqLIYPWD 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 78 Q--SGGE------ATITALQPLFVwpksllILDEPTANLDLDHKNCLIQQVKDYPGAVLMVSH 132
Cdd:cd03223 90 DvlSGGEqqrlafARLLLHKPKFV------FLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
271-439 |
8.81e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 60.16 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDrllFHLQH---FKLQKGDKVGLLGPNKAGKTTFLK---GMVSrslP--GY-------YYDQLS----- 330
Cdd:COG1118 3 IEVRNISKRFGS---FTLLDdvsLEIASGELVALLGPSGSGKTTLLRiiaGLET---PdsGRivlngrdLFTNLPprerr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 331 VGYFSQNFDqldL--NQSILENV-------------TQDSVQSM-TLVRnlLAGLGfnidklDQRISTLSGGERVRLSLA 394
Cdd:COG1118 77 VGFVFQHYA---LfpHMTVAENIafglrvrppskaeIRARVEELlELVQ--LEGLA------DRYPSQLSGGQRQRVALA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092676368 395 KVLLADHHLLFLDEPTNYLDLPTLQELEA----FLQEYPGTFVLVSHDQ 439
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRwlrrLHDELGGTTVFVTHDQ 194
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
145-255 |
9.06e-10 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 55.27 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 145 WAIEQRRLSVYKGNYTDYLKLQENKRAKQWQDYYQYQDRLQRLQASAQKrldraqsFKKKkasiswsdykvnnfagkyda 224
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDR-------FRAK-------------------- 53
|
90 100 110
....*....|....*....|....*....|.
gi 1092676368 225 qeKAMAKSAKALERRMNRLEKVDKPVKEKRY 255
Cdd:pfam12848 54 --ASKAKQAQSRIKALEKMERIEKPERDKPK 82
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
365-441 |
1.50e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 1.50e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 365 LLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSHDQQF 441
Cdd:PRK15064 138 LLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHF 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
291-440 |
1.97e-09 |
|
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: 58.12 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFL----------KGMV---SRSLPGYYYDQLSVGYFSQNFdQLDLNQSILENVT----- 352
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLrliaglerpdSGTIlfgGEDATDVPVQERNVGFVFQHY-ALFRHMTVFDNVAfglrv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 353 ------QDSVQSMTLVRNLLAGLGfnIDKLDQRI-STLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFL 425
Cdd:cd03296 102 kprserPPEAEIRAKVHELLKLVQ--LDWLADRYpAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWL 179
|
170
....*....|....*....
gi 1092676368 426 QEYPG----TFVLVSHDQQ 440
Cdd:cd03296 180 RRLHDelhvTTVFVTHDQE 198
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
286-445 |
2.50e-09 |
|
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: 57.09 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 286 FHLQ--HFKLQKGDKVGLLGPNKAGKTTFLKGMVS--RSLPGYYYDQLSVGYFSQnfdqldlnqsilenvtQDSVQSMTL 361
Cdd:cd03250 19 FTLKdiNLEVPKGELVAIVGPVGSGKSSLLSALLGelEKLSGSVSVPGSIAYVSQ----------------EPWIQNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 362 VRNLLAGLGFNIDKLDQRIS------------------------TLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT 417
Cdd:cd03250 83 RENILFGKPFDEERYEKVIKacalepdleilpdgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
170 180 190
....*....|....*....|....*....|..
gi 1092676368 418 LQEL--EAFLQE--YPGTFVLVSHDQQFIKEC 445
Cdd:cd03250 163 GRHIfeNCILGLllNNKTRILVTHQLQLLPHA 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
291-414 |
2.66e-09 |
|
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: 59.41 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKL------QKGDKVGLLGPNKAGKTTFLK----------GMVSR--------------SLPGYYYD----QLSVGYFSQ 336
Cdd:COG1245 88 FRLyglpvpKKGKVTGILGPNGIGKSTALKilsgelkpnlGDYDEepswdevlkrfrgtELQDYFKKlangEIKVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 337 NFDQL---------DLnqsiLENVTQdsvqsmtlvRNLLAGLG--FNIDK-LDQRISTLSGGERVRLSLAKVLLADHHLL 404
Cdd:COG1245 168 YVDLIpkvfkgtvrEL----LEKVDE---------RGKLDELAekLGLENiLDRDISELSGGELQRVAIAAALLRDADFY 234
|
170
....*....|
gi 1092676368 405 FLDEPTNYLD 414
Cdd:COG1245 235 FFDEPSSYLD 244
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
266-458 |
2.81e-09 |
|
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: 57.68 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 266 PSNTLIHLQDIDVQVDDRLlfHLQH--FKLQKGDKVGLLGPNKAGKTTFLKGMVsrslpGyyydQL-----SVGYFSQNF 338
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRV--VLDGvsLDVPRGEILAIIGGSGSGKSVLLKLII-----G----LLrpdsgEILVDGQDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 339 DQLDLNQ---------------------SILENV-------TQDSVQSMT-LVRNLLA--GLGfniDKLDQRISTLSGGE 387
Cdd:COG1127 70 TGLSEKElyelrrrigmlfqggalfdslTVFENVafplrehTDLSEAEIReLVLEKLElvGLP---GAADKMPSELSGGM 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 388 RVRLSLAKVLLADHHLLFLDEPTNYLDlP----TLQELEAFLQ-EYPGTFVLVSHDQQFIKECVNRRYYIKDQQLL 458
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLD-PitsaVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-166 |
3.10e-09 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 59.46 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 14 QAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-----DLR-VPVD-------YLPQ--------- 71
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgiDLRqIDPAslrrqigVVLQdvflfsgti 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 -----IQAPS----------------------PQ-------------SGGEATITAL------QPlfvwpkSLLILDEPT 105
Cdd:COG2274 566 renitLGDPDatdeeiieaarlaglhdfiealPMgydtvvgeggsnlSGGQRQRLAIarallrNP------RILILDEAT 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 106 ANLDLDHKNCLIQQVKDYPG--AVLMVSHDRDFLDQtVDWIWAIEQRRLsVYKGNYTDYLKLQ 166
Cdd:COG2274 640 SALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVLDKGRI-VEDGTHEELLARK 700
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
292-414 |
3.22e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.29 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 292 KLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPGYYYD--------------QLSVGYFSQNFDQL--------DLN-QSIL 348
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSgsvllngmpidakeMRAISAYVQQDDLFiptltvreHLMfQAHL 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 349 ---ENVTQDsvQSMTLVRNLLAGLGFnIDKLDQRIST------LSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:TIGR00955 127 rmpRRVTKK--EKRERVDEVLQALGL-RKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
291-448 |
3.30e-09 |
|
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: 57.03 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP-------------GYYYDQL-----SVGYFSQNFdQLDLNQSILENV- 351
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPtsgtirvngqdvsDLRGRAIpylrrKIGVVFQDF-RLLPDRNVYENVa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 -----TQDSVQSMT-LVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFL 425
Cdd:cd03292 101 falevTGVPPREIRkRVPAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLL 179
|
170 180
....*....|....*....|....*.
gi 1092676368 426 QEY--PGTFVLVS-HDqqfiKECVNR 448
Cdd:cd03292 180 KKInkAGTTVVVAtHA----KELVDT 201
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
270-437 |
3.61e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.74 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 270 LIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK----------GMVS-------RSLPGYYYDQLSVG 332
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRilaglarpdaGEVLwqgepirRQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 333 YfsQN--------FDQLDLNQSILENVTQDSvqsmtlVRNLLA--GL-GFnidkLDQRISTLSGGERVRLSLAKVLLADH 401
Cdd:PRK13538 81 H--QPgikteltaLENLRFYQRLHGPGDDEA------LWEALAqvGLaGF----EDVPVRQLSAGQQRRVALARLWLTRA 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092676368 402 HLLFLDEPTNYLDLPTLQELEAFLQEYP---GTFVLVSH 437
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
291-414 |
3.86e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKL------QKGDKVGLLGPNKAGKTTFLKGMVSRSLP--GYYYDQLS----VGYFSQNfdQLdlnQSILENVTQDSV-- 356
Cdd:PRK13409 88 FKLyglpipKEGKVTGILGPNGIGKTTAVKILSGELIPnlGDYEEEPSwdevLKRFRGT--EL---QNYFKKLYNGEIkv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 357 ----QSMTL--------VRNLLAGLG-----------FNIDK-LDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNY 412
Cdd:PRK13409 163 vhkpQYVDLipkvfkgkVRELLKKVDergkldevverLGLENiLDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
..
gi 1092676368 413 LD 414
Cdd:PRK13409 243 LD 244
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
282-438 |
4.53e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.69 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 282 DRLLFHLQHFKLQ------KGDKVGLLGPNKAGKTTFLkGMVSRSLP---------GYYYDQLSVG------YFSQN--F 338
Cdd:COG3840 5 DDLTYRYGDFPLRfdltiaAGERVAILGPSGAGKSTLL-NLIAGFLPpdsgrilwnGQDLTALPPAerpvsmLFQENnlF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 339 DQLDLNQSI---------LENVTQDSVQSMtLVRnllAGLGfniDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEP 409
Cdd:COG3840 84 PHLTVAQNIglglrpglkLTAEQRAQVEQA-LER---VGLA---GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190
....*....|....*....|....*....|....
gi 1092676368 410 TNYLDlPTL-QELEAFL----QEYPGTFVLVSHD 438
Cdd:COG3840 157 FSALD-PALrQEMLDLVdelcRERGLTVLMVTHD 189
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
291-460 |
5.21e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.75 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--------GYYYDQLS-----------VGYFSQnFDQLDLNQSILENV 351
Cdd:PRK11629 30 FSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPtsgdvifnGQPMSKLSsaakaelrnqkLGFIYQ-FHHLLPDFTALENV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 T-------QDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAF 424
Cdd:PRK11629 109 AmplligkKKPAEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092676368 425 LQEY---PGT-FVLVSHDQQFIKEcVNRRYYIKDQQLLNE 460
Cdd:PRK11629 188 LGELnrlQGTaFLVVTHDLQLAKR-MSRQLEMRDGRLTAE 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
291-438 |
6.03e-09 |
|
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: 57.40 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLP---------GYyyDQLSvgyfsqnfDQLDLNQSILENVTQDSV-QSMT 360
Cdd:TIGR01188 14 FKVREGEVFGFLGPNGAGKTTTIR-MLTTLLRptsgtarvaGY--DVVR--------EPRKVRRSIGIVPQYASVdEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 361 LVRNL-----LAGL--------------GFNI-DKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQE 420
Cdd:TIGR01188 83 GRENLemmgrLYGLpkdeaeeraeelleLFELgEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180
....*....|....*....|.
gi 1092676368 421 LEAFLQEYPG---TFVLVSHD 438
Cdd:TIGR01188 163 IWDYIRALKEegvTILLTTHY 183
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
290-442 |
7.05e-09 |
|
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: 56.59 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLKgMVSrslpGYY--------YD-------------QLSVGY-FsQN---FDQLdln 344
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFN-LIT----GFYrptsgrilFDgrditglpphriaRLGIARtF-QNprlFPEL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 345 qSILENV-------TQDSVQSMTL---------------VRNLLA--GLGfniDKLDQRISTLSGGERVRLSLAKVLLAD 400
Cdd:COG0411 95 -TVLENVlvaaharLGRGLLAALLrlprarreerearerAEELLErvGLA---DRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1092676368 401 HHLLFLDEPT---NyldlPTL-QELEAFLQEYPG----TFVLVSHDQQFI 442
Cdd:COG0411 171 PKLLLLDEPAaglN----PEEtEELAELIRRLRDergiTILLIEHDMDLV 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-133 |
7.87e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.48 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMdTDYQGRI-------------DLRVPVDYLPQIQAPSPQ-------------- 78
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIqfagqpleawsaaELARHRAYLSQQQTPPFAmpvfqyltlhqpdk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 79 ------------------------------SGGE-------ATItaLQplfVWPKS-----LLILDEPTANLDLDHKNCL 116
Cdd:PRK03695 98 trteavasalnevaealglddklgrsvnqlSGGEwqrvrlaAVV--LQ---VWPDInpagqLLLLDEPMNSLDVAQQAAL 172
|
170 180
....*....|....*....|
gi 1092676368 117 IQQVKDYP---GAVLMVSHD 133
Cdd:PRK03695 173 DRLLSELCqqgIAVVMSSHD 192
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
269-438 |
8.00e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.56 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 269 TLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMV--------SRSLPGYYYDQLSVGYFSQNFDQ 340
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFArlltpqsgTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 341 LDLNQSILENVT-----------------QDSVQSMTLVRNLLAGLGfnIDKL-DQRISTLSGGERVRLSLAKVLLADHH 402
Cdd:PRK11231 81 LPQHHLTPEGITvrelvaygrspwlslwgRLSAEDNARVNQAMEQTR--INHLaDRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092676368 403 LLFLDEPTNYLDLPTLQELEAFLQEYPG---TFVLVSHD 438
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHD 197
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-132 |
8.32e-09 |
|
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: 54.74 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR-VPVDYLpqiqapSPQ--- 78
Cdd:cd03216 1 LELRGITKRFGGVKALDgVS-LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgKEVSFA------SPRdar 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 79 ----------SGGEATITALQPLFVWPKSLLILDEPTANLDL---DHKNCLIQQVKDYPGAVLMVSH 132
Cdd:cd03216 74 ragiamvyqlSVGERQMVEIARALARNARLLILDEPTAALTPaevERLFKVIRRLRAQGVAVIFISH 140
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
266-437 |
8.81e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.91 E-value: 8.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 266 PSNTLIHLQDIDVQVDDRLLFHLQHFKLQ--KGDKVGLLGPNKAGKTTFLkgmvsrslpgyyydQLSVGYFSQNFDQLDL 343
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQikAGEKVALLGRTGCGKSTLL--------------QLLTRAWDPQQGEILL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 344 NQSILENVTQDSVQSM-------------TLVRNLL-----------------AGLGF---NIDKLDQRIS----TLSGG 386
Cdd:PRK11160 400 NGQPIADYSEAALRQAisvvsqrvhlfsaTLRDNLLlaapnasdealievlqqVGLEKlleDDKGLNAWLGeggrQLSGG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 387 ERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG--TFVLVSH 437
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQnkTVLMITH 532
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
290-427 |
9.10e-09 |
|
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: 56.08 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTT----------------FLKGMVSRSLPGYYYDQlSVGYFSQnfDQLDLNQSILENVT- 352
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTlinllmrfydpqkgqiLIDGIDIRDISRKSLRS-MIGVVLQ--DTFLFSGTIMENIRl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 353 QDSVQSMTLVRNLLAGLGFN--IDKLDQ--------RISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELE 422
Cdd:cd03254 100 GRPNATDEEVIEAAKEAGAHdfIMKLPNgydtvlgeNGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQ 179
|
....*
gi 1092676368 423 AFLQE 427
Cdd:cd03254 180 EALEK 184
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
34-138 |
1.02e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 54.29 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 34 LVGANGSGKSTLLR---MIMGMDTDYQGRIDLRVPVDYLPQIQAP----SPQ-SGGEATITALQPLF----VWPKSLLIL 101
Cdd:cd03227 26 ITGPNGSGKSTILDaigLALGGAQSATRRRSGVKAGCIVAAVSAEliftRLQlSGGEKELSALALILalasLKPRPLYIL 105
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1092676368 102 DEPTANLDLDHKNCLIQQVKDY--PGA-VLMVSHDRDFLD 138
Cdd:cd03227 106 DEIDRGLDPRDGQALAEAILEHlvKGAqVIVITHLPELAE 145
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
271-450 |
1.11e-08 |
|
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: 55.52 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQD-IDVQVddrllFHLQHFKLQKGDKVGLLGPNKAGKTTFLKgMVSRS-LPG----YYYDQLSV------------- 331
Cdd:COG4778 16 LHLQGgKRLPV-----LDGVSFSVAAGECVALTGPSGAGKSTLLK-CIYGNyLPDsgsiLVRHDGGWvdlaqaspreila 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 332 ------GYFSQnFdqldLN----QSILENVTQ-------DSVQSMTLVRNLLAGLGfnidkLDQRI-----STLSGGERV 389
Cdd:COG4778 90 lrrrtiGYVSQ-F----LRviprVSALDVVAEpllergvDREEARARARELLARLN-----LPERLwdlppATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 390 RLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYP--GTFVL-VSHDQQFIKECVNRRY 450
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKarGTAIIgIFHDEEVREAVADRVV 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-135 |
1.20e-08 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 55.43 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 2 AILELNHIKKTWQAEL----ILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI----------------D 61
Cdd:COG1136 3 PLLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslserelaR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 62 LR------VPVDY-------------LPQIQAPSPQ---------------------------SGGE--------ATITa 87
Cdd:COG1136 83 LRrrhigfVFQFFnllpeltalenvaLPLLLAGVSRkerrerarellervglgdrldhrpsqlSGGQqqrvaiarALVN- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 88 lQPlfvwpkSLLILDEPTANldLDHKNC-----LIQQVKDYPG-AVLMVSHDRD 135
Cdd:COG1136 162 -RP------KLILADEPTGN--LDSKTGeevleLLRELNRELGtTIVMVTHDPE 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
267-466 |
1.24e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.49 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 267 SNTLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVS----------------RSLPGYYYDQlS 330
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASlisptsgtllfegediSTLKPEIYRQ-Q 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 331 VGYFSQN--------FDQLDLNQSIlenvTQDSVQSMTLVRNLlAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHH 402
Cdd:PRK10247 83 VSYCAQTptlfgdtvYDNLIFPWQI----RNQQPDPAIFLDDL-ERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 403 LLFLDEPTNYLDLPTLQELEAFLQEY---PGTFVL-VSHDQQFIKECVNrryYIKDQQLLNEQQDTDY 466
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYvreQNIAVLwVTHDKDEINHADK---VITLQPHAGEMQEARY 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
271-438 |
1.26e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.16 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFL---KGMVSRS-----LPGYYYDQLSVGYFSQNFDQLD 342
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLraiNGTLTPTagtvlVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 343 LNQSILENVTQDSVQSM-----------------TLVRNLLAGLGfnIDKL-DQRISTLSGGERVRLSLAKVLLADHHLL 404
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtphrsrfdtwtetdrAAVERAMERTG--VAQFaDRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092676368 405 FLDEPTNYLDL----PTLqELEAFLQEYPGTFVLVSHD 438
Cdd:PRK09536 162 LLDEPTASLDInhqvRTL-ELVRRLVDDGKTAVAAIHD 198
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-148 |
1.46e-08 |
|
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: 54.50 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 23 RLLVQPQD-----RIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL-RVPVDYLPQIQApspQSGGEATITALQPLFVWPK 96
Cdd:cd03222 14 FLLVELGVvkegeVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWdGITPVYKPQYID---LSGGELQRVAIAAALLRNA 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 97 SLLILDEPTANLDLDHKNCLIQQVKDY----PGAVLMVSHDRDFLDQTVDWIWAIE 148
Cdd:cd03222 91 TFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
273-438 |
1.71e-08 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 55.48 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 273 LQDIDvqvddrllfhlqhFKLQKGDKVGLLGPNKAGKTTFLK---GMVSRS-----LPGYYYDQLS--VGYFSQN---FD 339
Cdd:COG1116 27 LDDVS-------------LTVAAGEFVALVGPSGCGKSTLLRliaGLEKPTsgevlVDGKPVTGPGpdRGVVFQEpalLP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 340 QLdlnqSILENVT-------QDSVQSMTLVRNLLA--GLGfniDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPT 410
Cdd:COG1116 94 WL----TVLDNVAlglelrgVPKAERRERARELLElvGLA---GFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
170 180 190
....*....|....*....|....*....|..
gi 1092676368 411 NYLDLPT---LQ-ELEAFLQEYPGTFVLVSHD 438
Cdd:COG1116 167 GALDALTrerLQdELLRLWQETGKTVLFVTHD 198
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
292-437 |
1.86e-08 |
|
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: 57.06 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 292 KLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPGYyyDQLSVGYFS-QNFDQLDLNQSIlENVTQDSVQ-SMTLVRNLLAGL 369
Cdd:TIGR01193 496 TIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS--GEILLNGFSlKDIDRHTLRQFI-NYLPQEPYIfSGSILENLLLGA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 370 --GFNIDKLDQRI------------------------STLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQE-LE 422
Cdd:TIGR01193 573 keNVSQDEIWAACeiaeikddienmplgyqtelseegSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKiVN 652
|
170
....*....|....*
gi 1092676368 423 AFLQEYPGTFVLVSH 437
Cdd:TIGR01193 653 NLLNLQDKTIIFVAH 667
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
376-438 |
1.95e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 56.26 E-value: 1.95e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 376 LDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTF----VLVSHD 438
Cdd:COG4148 127 LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELdipiLYVSHS 193
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-142 |
2.05e-08 |
|
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: 54.75 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGmdtDYQ------------GRIDL---------------------------RVPV------ 66
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYG---NYLpdsgsilvrhdgGWVDLaqaspreilalrrrtigyvsqflrvipRVSAldvvae 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 67 -----------------DYLPQIQAP------SPQ--SGGEAtitalQPL-----FVWPKSLLILDEPTANLDLDHKNC- 115
Cdd:COG4778 117 pllergvdreearararELLARLNLPerlwdlPPAtfSGGEQ-----QRVniargFIADPPLLLLDEPTASLDAANRAVv 191
|
170 180
....*....|....*....|....*....
gi 1092676368 116 --LIQQVKDYPGAVLMVSHDRDFLDQTVD 142
Cdd:COG4778 192 veLIEEAKARGTAIIGIFHDEEVREAVAD 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
280-440 |
2.09e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 280 VDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKgmVSRSLPGYYYDQLSVG----YFSQNFDQLDL------------ 343
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLK--VLNRLIEIYDSKIKVDgkvlYFGKDIFQIDAiklrkevgmvfq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 344 ------NQSILENVT--------QDSVQSMTLVRNLLAGLGF---NIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFL 406
Cdd:PRK14246 98 qpnpfpHLSIYDNIAyplkshgiKEKREIKKIVEECLRKVGLwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1092676368 407 DEPTNYLDLPTLQELEAFLQEYPG--TFVLVSHDQQ 440
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQ 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
293-448 |
2.27e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.86 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 293 LQKGDKVGLLGPNKAGKTTFLkgmvsRSLPGYyyDQLSVGYFS---QNFDQLDLNQSILENVTQDSV--QSMTLVRNLLA 367
Cdd:PRK10851 25 IPSGQMVALLGPSGSGKTTLL-----RIIAGL--EHQTSGHIRfhgTDVSRLHARDRKVGFVFQHYAlfRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 368 GLGF-------NIDKLDQRI-----------------STLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEA 423
Cdd:PRK10851 98 GLTVlprrerpNAAAIKAKVtqllemvqlahladrypAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRR 177
|
170 180
....*....|....*....|....*....
gi 1092676368 424 FL----QEYPGTFVLVSHDQQFIKECVNR 448
Cdd:PRK10851 178 WLrqlhEELKFTSVFVTHDQEEAMEVADR 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
291-409 |
2.34e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.90 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTT---FLKGMVSRS-------------LPGYYYDQLSVGYFSQN---------FDQLDLNQ 345
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDagniiiddedislLPLHARARRGIGYLPQEasifrrlsvYDNLMAVL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 346 SILENVTQDsvQSMTLVRNLLAGlgFNIDKL-DQRISTLSGGERVRLSLAKVLLADHHLLFLDEP 409
Cdd:PRK10895 104 QIRDDLSAE--QREDRANELMEE--FHIEHLrDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
291-438 |
2.52e-08 |
|
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: 54.40 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK----------GMVS---RSLPGYYYDqlsVGYFSQN---FDQLdlnqSILENVT-- 352
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRiiaglerptsGEVLvdgEPVTGPGPD---RGYVFQQdalLPWL----TVLDNVAlg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 353 -----QDSVQSMTLVRNLLA--GL-GFnidkLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT---LQ-E 420
Cdd:cd03293 98 lelqgVPKAEARERAEELLElvGLsGF----ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqLQeE 173
|
170
....*....|....*...
gi 1092676368 421 LEAFLQEYPGTFVLVSHD 438
Cdd:cd03293 174 LLDIWRETGKTVLLVTHD 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
269-438 |
3.37e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 269 TLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK----------GMVSRSlpgyyyDQLSVGYFSQnf 338
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRvvlglvapdeGVIKRN------GKLRIGYVPQ-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 339 dQLDLNQSI---------LENVTQDSVQSMTLVRNLLAGLgfnidkLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEP 409
Cdd:PRK09544 75 -KLYLDTTLpltvnrflrLRPGTKKEDILPALKRVQAGHL------IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190
....*....|....*....|....*....|...
gi 1092676368 410 TNYLDLP---TLQELEAFLQEYPGTFVL-VSHD 438
Cdd:PRK09544 148 TQGVDVNgqvALYDLIDQLRRELDCAVLmVSHD 180
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-135 |
3.38e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 55.54 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 1 MAIlELNHIKKTWQAE-LILEIDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL-------RVPV------ 66
Cdd:COG1118 1 MSI-EVRNISKRFGSFtLLDDVS-LEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLngrdlftNLPPrerrvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 67 ----DYL--------------PQIQAPSPQ--------------------------SGGEATITAL-QPLFVWPKSLLiL 101
Cdd:COG1118 79 fvfqHYAlfphmtvaeniafgLRVRPPSKAeirarveellelvqlegladrypsqlSGGQRQRVALaRALAVEPEVLL-L 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092676368 102 DEPTANLDLDHKNCLIQQV----KDYPGAVLMVSHDRD 135
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLrrlhDELGGTTVFVTHDQE 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
301-460 |
3.44e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.72 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 301 LLGPNKAGKTTFLKGM--VSRSLPGYYY--DQLSVGYFSQNF-DQLDLNQSILENVTQDSVQSMTLVRNLLAGLGFN--- 372
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLnrMNDKVSGYRYsgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHklv 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 373 ------------------IDKLDQRIST----LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG 430
Cdd:PRK14271 132 prkefrgvaqarltevglWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD 211
|
170 180 190
....*....|....*....|....*....|..
gi 1092676368 431 --TFVLVSHDQQFIKECVNRRYYIKDQQLLNE 460
Cdd:PRK14271 212 rlTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
26-63 |
3.69e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.32 E-value: 3.69e-08
10 20 30
....*....|....*....|....*....|....*...
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR 63
Cdd:COG1134 49 VERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-133 |
3.78e-08 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 54.26 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQaELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR----------------VPVD 67
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppekrdisyVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 68 YL----------------------PQIQA------------------PSPQSGGEATITAL-QPLFVWPKsLLILDEPTA 106
Cdd:cd03299 80 YAlfphmtvykniayglkkrkvdkKEIERkvleiaemlgidhllnrkPETLSGGEQQRVAIaRALVVNPK-ILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|.
gi 1092676368 107 NLDLDHKNCLIQQVKD----YPGAVLMVSHD 133
Cdd:cd03299 159 ALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
290-426 |
4.03e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLKgMVSrslpGYY--------YD-------------QLSVGYFSQNF---DQLdlnq 345
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMK-ILY----GLYqpdsgeilIDgkpvrirsprdaiALGIGMVHQHFmlvPNL---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 346 SILENVT--QDSVQSMTL--------VRNLLAGLGFNIDkLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLdl 415
Cdd:COG3845 96 TVAENIVlgLEPTKGGRLdrkaararIRELSERYGLDVD-PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL-- 172
|
170
....*....|.
gi 1092676368 416 pTLQELEAFLQ 426
Cdd:COG3845 173 -TPQEADELFE 182
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
31-106 |
4.37e-08 |
|
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: 52.27 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 31 RIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------DLRVPVDYLPQ-------------------IQAPSPQ 78
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltdderkSLRKEIGYVFQdpqlfprltvrenlrlgllLKGLSKR 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 79 ------------------------------SGGEATITALQPLFVWPKSLLILDEPTA 106
Cdd:pfam00005 93 ekdaraeealeklglgdladrpvgerpgtlSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
30-69 |
4.70e-08 |
|
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: 53.69 E-value: 4.70e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1092676368 30 DRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLRVPVDYL 69
Cdd:cd03220 49 ERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL 88
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
290-414 |
5.61e-08 |
|
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: 53.04 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLKGMVSRsLPGYY-------YDQLSVGYFSQNFDQldlnqSILENVTQDSVQSMTLV 362
Cdd:cd03233 27 SGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVsvegdihYNGIPYKEFAEKYPG-----EIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 363 RNLLAglgFNID-KLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:cd03233 101 RETLD---FALRcKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
26-155 |
6.69e-08 |
|
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: 55.05 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMG-------------MDTDYQGRIDLRVPVDYLPQ--------------------- 71
Cdd:TIGR01842 341 LQAGEALAIIGPSGSGKSTLARLIVGiwpptsgsvrldgADLKQWDRETFGKHIGYLPQdvelfpgtvaeniarfgenad 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 ----IQAP------------------------SPQSGGEATITAL-QPLFVWPKsLLILDEPTANLDLDHKNCL---IQQ 119
Cdd:TIGR01842 421 pekiIEAAklagvhelilrlpdgydtvigpggATLSGGQRQRIALaRALYGDPK-LVVLDEPNSNLDEEGEQALanaIKA 499
|
170 180 190
....*....|....*....|....*....|....*.
gi 1092676368 120 VKDYPGAVLMVSHdRDFLDQTVDWIWAIEQRRLSVY 155
Cdd:TIGR01842 500 LKARGITVVVITH-RPSLLGCVDKILVLQDGRIARF 534
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
291-428 |
7.72e-08 |
|
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: 53.04 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPGY------YYD---------QLSVGYFSQNFDQLD----------LNQ 345
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsgqiLFNgqprkpdqfQKCVAYVRQDDILLPgltvretltyTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 346 SILENVTQDSVQSMTLVRNLLAGLGfNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFL 425
Cdd:cd03234 108 LRLPRKSSDAIRKKRVEDVLLRDLA-LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTL 186
|
...
gi 1092676368 426 QEY 428
Cdd:cd03234 187 SQL 189
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-60 |
8.37e-08 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 53.55 E-value: 8.37e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 1 MAILELNHIKKTWQAE----LILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:COG1116 5 APALELRGVSKRFPTGgggvTALDdVS-LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEV 68
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
261-472 |
8.83e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.85 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 261 GHLSDPSNTLIHLQDIDVQV---DDRLLFHLQHFKLQKGDKVGLLGPNKAGKTT-------FLK--------GMVSRSL- 321
Cdd:PRK11174 338 GEKELASNDPVTIEAEDLEIlspDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSllnallgFLPyqgslkinGIELRELd 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 322 PGYYYDQLS-VGyfsQNfDQLdLNQSILENVTQDSVQ-SMTLVRNLLAGLGFN--IDKLDQRIST--------LSGGERV 389
Cdd:PRK11174 418 PESWRKHLSwVG---QN-PQL-PHGTLRDNVLLGNPDaSDEQLQQALENAWVSefLPLLPQGLDTpigdqaagLSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 390 RLSLAKVLLADHHLLFLDEPTNYLDLPTLQE-LEAFLQEYPG-TFVLVSHDQQFIKECvnrryyikDQQLLNEQ----QD 463
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLvMQALNAASRRqTTLMVTHQLEDLAQW--------DQIWVMQDgqivQQ 564
|
....*....
gi 1092676368 464 TDYSDRSQQ 472
Cdd:PRK11174 565 GDYAELSQA 573
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
273-452 |
9.18e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.17 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 273 LQDIDVQVDdrllfhlqhfklqKGDKVGLLGPNKAGKTTFLKGMvsRSLPGYYYDQLSVGYFSQN--------------- 337
Cdd:PRK09493 17 LHNIDLNID-------------QGEVVVIIGPSGSGKSTLLRCI--NKLEEITSGDLIVDGLKVNdpkvderlirqeagm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 338 -FDQLDL--NQSILENVT--------QDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFL 406
Cdd:PRK09493 82 vFQQFYLfpHLTALENVMfgplrvrgASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1092676368 407 DEPTNYLDlPTL-QELEAFLQ---EYPGTFVLVSHDQQFIKECVNRRYYI 452
Cdd:PRK09493 161 DEPTSALD-PELrHEVLKVMQdlaEEGMTMVIVTHEIGFAEKVASRLIFI 209
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
26-144 |
9.87e-08 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 54.37 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQG--RIDLrVPVD------------YLPQ-------------------- 71
Cdd:COG4618 355 LEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvRLDG-ADLSqwdreelgrhigYLPQdvelfdgtiaeniarfgdad 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 ----IQA-------------P-----------SPQSGGEATITAL-QPLFVWPKsLLILDEPTANLDLDHKNCL---IQQ 119
Cdd:COG4618 434 pekvVAAaklagvhemilrlPdgydtrigeggARLSGGQRQRIGLaRALYGDPR-LVVLDEPNSNLDDEGEAALaaaIRA 512
|
170 180
....*....|....*....|....*
gi 1092676368 120 VKDYPGAVLMVSHDRDFLdQTVDWI 144
Cdd:COG4618 513 LKARGATVVVITHRPSLL-AAVDKL 536
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
33-144 |
1.09e-07 |
|
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: 51.94 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 33 GLVGANGSGKSTLL----------RMIMGMDTDYQG---RID-LRVPVD----YLPQIQAPSPQSGGEATITAL-QPLFV 93
Cdd:cd03238 25 VVTGVSGSGKSTLVneglyasgkaRLISFLPKFSRNkliFIDqLQFLIDvglgYLTLGQKLSTLSGGELQRVKLaSELFS 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 94 WPK-SLLILDEPTANLDLDHKNCLIQQVK---DYPGAVLMVSHDRDFLdQTVDWI 144
Cdd:cd03238 105 EPPgTLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLDVL-SSADWI 158
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
376-458 |
1.16e-07 |
|
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: 53.58 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 376 LDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTF----VLVSHDQQFIKECVNRRYY 451
Cdd:TIGR02142 125 LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFgipiLYVSHSLQEVLRLADRVVV 204
|
....*..
gi 1092676368 452 IKDQQLL 458
Cdd:TIGR02142 205 LEDGRVA 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-60 |
1.16e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 53.54 E-value: 1.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092676368 1 MAILELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:COG3839 1 MASLELENVSKSYGGVEALKdID-LDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI 60
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
376-439 |
1.57e-07 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 51.87 E-value: 1.57e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 376 LDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD----LPTLQELEAFLQEYPGTFVLVSHDQ 439
Cdd:cd03301 124 LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
291-437 |
1.59e-07 |
|
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: 52.23 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSRslpgyYYDQLS--VGYFSQNFDQLDLNqSILEN---VTQDSVQ-SMTLVRN 364
Cdd:cd03253 22 FTIPAGKKVAIVGPSGSGKSTILR-LLFR-----FYDVSSgsILIDGQDIREVTLD-SLRRAigvVPQDTVLfNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 365 L-----------------LAGLGFNIDKLDQRIST--------LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQ 419
Cdd:cd03253 95 IrygrpdatdeevieaakAAQIHDKIMRFPDGYDTivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180
....*....|....*....|
gi 1092676368 420 ELEAFLQEYPG--TFVLVSH 437
Cdd:cd03253 175 EIQAALRDVSKgrTTIVIAH 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
293-485 |
1.82e-07 |
|
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: 52.50 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 293 LQKGDKVGLLGPNKAGKTTFLKGMVSRSLPGyyydQLSVGYFSQNFDQLDLNQS-----ILENVTQDSVQS----MTL-- 361
Cdd:TIGR02769 34 IEEGETVGLLGRSGCGKSTLARLLLGLEKPA----QGTVSFRGQDLYQLDRKQRrafrrDVQLVFQDSPSAvnprMTVrq 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 362 -----VRN---------------LLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDL----PT 417
Cdd:TIGR02769 110 iigepLRHltsldeseqkariaeLLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqaVI 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 418 LQELEAFLQEYPGTFVLVSHD----QQFIKECVnrryyIKDQQLLNEQQDTDYSDRSQQTLSLLqfkLQEAI 485
Cdd:TIGR02769 190 LELLRKLQQAFGTAYLFITHDlrlvQSFCQRVA-----VMDKGQIVEECDVAQLLSFKHPAGRN---LQSAV 253
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
251-448 |
1.84e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.39 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 251 KEKRYTLKALGHLSDPSNTLIH--LQDIDvqvddrllfhlqhFKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLP---GYY 325
Cdd:COG1134 18 HEPSRSLKELLLRRRRTRREEFwaLKDVS-------------FEVERGESVGIIGRNGAGKSTLLK-LIAGILEptsGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 326 YDQLSVGYFsqnfdqLDLN---QSIL---ENV-TQDSVQSMTL--VRNLL------AGLGfniDKLDQRISTLSGGERVR 390
Cdd:COG1134 84 EVNGRVSAL------LELGagfHPELtgrENIyLNGRLLGLSRkeIDEKFdeivefAELG---DFIDQPVKTYSSGMRAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 391 LSLAKVLLADHHLLFLDEPTNYLDLP----TLQELEAFLQEyPGTFVLVSHDQQFIKECVNR 448
Cdd:COG1134 155 LAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRLCDR 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-167 |
2.02e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 3 ILELNHIKKT-WQAELILEI---DRLLVQPQDRIGLVGANGSGKSTLLRMIMGMD----------------TDYQGRIDL 62
Cdd:PRK10584 6 IVEVHHLKKSvGQGEHELSIltgVELVVKRGETIALIGESGSGKSTLLAILAGLDdgssgevslvgqplhqMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 63 R-------------VP--------------------------VDYLPQI-------QAPSPQSGGEATITALQPLFVWPK 96
Cdd:PRK10584 86 RakhvgfvfqsfmlIPtlnalenvelpallrgessrqsrngaKALLEQLglgkrldHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 97 SLLILDEPTANLDLDH----KNCLIQQVKDYPGAVLMVSHDrdfldqtvDWIWAIEQRRLSVYKGnytdylKLQE 167
Cdd:PRK10584 166 DVLFADEPTGNLDRQTgdkiADLLFSLNREHGTTLILVTHD--------LQLAARCDRRLRLVNG------QLQE 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
26-133 |
2.14e-07 |
|
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: 51.74 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL------------------------------------------- 62
Cdd:cd03257 28 IKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdllklsrrlrkirrkeiqmvfqdpmsslnprmtigeqiae 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 63 ---------------RVPVDYLPQIQAPS------PQ--SGGE------ATITALQPlfvwpkSLLILDEPTANLDLDHK 113
Cdd:cd03257 108 plrihgklskkearkEAVLLLLVGVGLPEevlnryPHelSGGQrqrvaiARALALNP------KLLIADEPTSALDVSVQ 181
|
170 180
....*....|....*....|....
gi 1092676368 114 NCLIQQVKD----YPGAVLMVSHD 133
Cdd:cd03257 182 AQILDLLKKlqeeLGLTLLFITHD 205
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
281-438 |
2.84e-07 |
|
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: 50.65 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 281 DDRLLFHLQHFKlqKGDKVGLLGPNKAGKTTFLKGMVSRSLPgyyydqlsvgyfSQNFDQLDlnqsilenvtqdsvqsmt 360
Cdd:cd03222 12 VFFLLVELGVVK--EGEVIGIVGPNGTGKTTAVKILAGQLIP------------NGDNDEWD------------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 361 lvrnllaglGFNIDKLDQRIStLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD----LPTLQELEAFLQEYPGTFVLVS 436
Cdd:cd03222 60 ---------GITPVYKPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVE 129
|
..
gi 1092676368 437 HD 438
Cdd:cd03222 130 HD 131
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
267-438 |
3.61e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.71 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 267 SNTLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKgMVSRSLPGYYYDQL----------------S 330
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSEGEILldaqpleswsskafarK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 331 VGYFSQNFDQldlnqsilenvtqdsVQSMTlVRNLLA--------GLG-FNI---DKLDQRIS-------------TLSG 385
Cdd:PRK10575 87 VAYLPQQLPA---------------AEGMT-VRELVAigrypwhgALGrFGAadrEKVEEAISlvglkplahrlvdSLSG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 386 GERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQ----EYPGTFVLVSHD 438
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHrlsqERGLTVIAVLHD 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
291-437 |
3.65e-07 |
|
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: 50.12 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSrslpGYYydQLSVGyfsqnfdqldlnqSIL---ENVTQDSVQsmtlvrnlla 367
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMK-ILS----GLY--KPDSG-------------EILvdgKEVSFASPR---------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 368 glgfniDKLDQRIST---LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAF---LQEYPGTFVLVSH 437
Cdd:cd03216 71 ------DARRAGIAMvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISH 140
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
269-414 |
4.27e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.55 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 269 TLIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLK---GMVS-RSLPGYYYDQLS-------------- 330
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsGLITgDKSAGSHIELLGrtvqregrlardir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 331 -----VGYFSQNFDQLDlNQSILENV----------------------TQDSVQSMTLVRnlLAGLGFnidkldQRISTL 383
Cdd:PRK09984 83 ksranTGYIFQQFNLVN-RLSVLENVligalgstpfwrtcfswftreqKQRALQALTRVG--MVHFAH------QRVSTL 153
|
170 180 190
....*....|....*....|....*....|.
gi 1092676368 384 SGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
296-438 |
4.74e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 296 GDKVGLLGPNKAGKTTFLKGMVSRSLPGY--------------YY--------------DQLSVGYFSQNFDQL------ 341
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLgkfddppdwdeildEFrgselqnyftklleGDVKVIVKPQYVDLIpkavkg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 342 ---DLNQSILENVTQDSVQSMTLVRNLLaglgfnidklDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPtl 418
Cdd:cd03236 106 kvgELLKKKDERGKLDELVDQLELRHVL----------DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK-- 173
|
170 180
....*....|....*....|....*
gi 1092676368 419 QELEAF-----LQEYPGTFVLVSHD 438
Cdd:cd03236 174 QRLNAArlireLAEDDNYVLVVEHD 198
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
293-438 |
5.47e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 50.85 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 293 LQKGDKVGLLGPNKAGKTTFLkGMVSRSLPgyyYDQLSVgyfsqNFDQLDLNQ----------SILenvTQDSVQSMTL- 361
Cdd:COG4604 24 IPKGGITALIGPNGAGKSTLL-SMISRLLP---PDSGEV-----LVDGLDVATtpsrelakrlAIL---RQENHINSRLt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 362 VRNLLaGLG-----------------------FNIDKL-DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDL-- 415
Cdd:COG4604 92 VRELV-AFGrfpyskgrltaedreiideaiayLDLEDLaDRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkh 170
|
170 180
....*....|....*....|....*
gi 1092676368 416 --PTLQELEAFLQEYPGTFVLVSHD 438
Cdd:COG4604 171 svQMMKLLRRLADELGKTVVIVLHD 195
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-140 |
5.90e-07 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 50.32 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 3 ILELNHIKKTWQAE-LILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL-----------RVP----- 65
Cdd:TIGR02673 1 MIEFHNVSKAYPGGvAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIagedvnrlrgrQLPllrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 66 --------------------------------------------VDYLPQIQAPSPQ-SGGEATITALQPLFVWPKSLLI 100
Cdd:TIGR02673 81 igvvfqdfrllpdrtvyenvalplevrgkkereiqrrvgaalrqVGLEHKADAFPEQlSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1092676368 101 LDEPTANLDLDHKN---CLIQQVKDYPGAVLMVSHDRDFLDQT 140
Cdd:TIGR02673 161 ADEPTGNLDPDLSErilDLLKRLNKRGTTVIVATHDLSLVDRV 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
346-475 |
6.09e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.74 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 346 SILENVTQDSVQSMTLVRN--------LLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT 417
Cdd:PRK10619 108 TVLENVMEAPIQVLGLSKQeareravkYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPEL 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 418 LQELEAFLQ---EYPGTFVLVSHDQQFIKECVNRRYYIKdQQLLNEQQDTD------YSDRSQQTLS 475
Cdd:PRK10619 188 VGEVLRIMQqlaEEGKTMVVVTHEMGFARHVSSHVIFLH-QGKIEEEGAPEqlfgnpQSPRLQQFLK 253
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
291-511 |
6.47e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.89 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPgyyyDQLSVGYFSQNFDQLdlNQSILEN----VTQD---SVQSMTLVR 363
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLP----QRGRVKVMGREVNAE--NEKWVRSkvglVFQDpddQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 364 NLLAG---LGFNIDKLDQRIST-----------------LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDlP----TLQ 419
Cdd:PRK13647 100 DVAFGpvnMGLDKDEVERRVEEalkavrmwdfrdkppyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD-PrgqeTLM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 420 ELEAFLQEYPGTFVLVSHDQQFIKECVNRRYYIKDQQLLNEQQDTDYSDRSQQTLSLLQFKLQEAISN--PEVSLTEI-R 496
Cdd:PRK13647 179 EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGLRLPLVAQIFEdlPELGQSKLpL 258
|
250
....*....|....*
gi 1092676368 497 QLQDQIQDLKENIKH 511
Cdd:PRK13647 259 TVKEAVQIIRKLLTK 273
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
291-427 |
6.83e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.89 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK----------------GM----VSR-SLpgyyydQLSVGYFSQnfDQLDLNQSILE 349
Cdd:PRK13657 356 FEAKPGQTVAIVGPTGAGKSTLINllqrvfdpqsgrilidGTdirtVTRaSL------RRNIAVVFQ--DAGLFNRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 350 NV----TQDSVQSMTLVRNLLAGLGF---NIDKLD----QRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTL 418
Cdd:PRK13657 428 NIrvgrPDATDEEMRAAAERAQAHDFierKPDGYDtvvgERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
....*....
gi 1092676368 419 QELEAFLQE 427
Cdd:PRK13657 508 AKVKAALDE 516
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-148 |
7.73e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.91 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 34 LVGANGSGKSTLL----------------------RMIMGMDTDYQGRIDLRVPVD----------------YLPQ--IQ 73
Cdd:cd03240 27 IVGQNGAGKTTIIealkyaltgelppnskggahdpKLIREGEVRAQVKLAFENANGkkytitrslailenviFCHQgeSN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 74 APSPQ-----SGGEATI------TALQPLFVWPKSLLILDEPTANLDLDH-KNCLIQQVKDYPGA----VLMVSHDRDFL 137
Cdd:cd03240 107 WPLLDmrgrcSGGEKVLasliirLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQknfqLIVITHDEELV 186
|
170
....*....|.
gi 1092676368 138 DQtVDWIWAIE 148
Cdd:cd03240 187 DA-ADHIYRVE 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
32-133 |
7.87e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 50.54 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGMDTDYQGRIDL---------------RVPVdyLPQ-----------------------IQ 73
Cdd:PRK13548 31 VAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpladwspaelarRRAV--LPQhsslsfpftveevvamgraphglSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 74 APSPQ----------------------SGGE----------ATITALQPlfvwPKSLLILDEPTANLDLDHKNCLIQQVK 121
Cdd:PRK13548 109 AEDDAlvaaalaqvdlahlagrdypqlSGGEqqrvqlarvlAQLWEPDG----PPRWLLLDEPTSALDLAHQHHVLRLAR 184
|
170
....*....|....*.
gi 1092676368 122 DY----PGAVLMVSHD 133
Cdd:PRK13548 185 QLaherGLAVIVVLHD 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
273-410 |
8.72e-07 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 49.98 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 273 LQDIDVQVDdrllfhlqhfklqKGDKVGLLGPNKAGKTTFLK---GMVSRS-------------LPGYYYDQLSVGYFSQ 336
Cdd:COG0410 19 LHGVSLEVE-------------EGEIVALLGRNGAGKTTLLKaisGLLPPRsgsirfdgeditgLPPHRIARLGIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 337 N---FDQLdlnqSILENVtqdsvQSMTLVRNLLAGLGFNID-----------KLDQRISTLSGGERVRLSLAKVLLADHH 402
Cdd:COG0410 86 GrriFPSL----TVEENL-----LLGAYARRDRAEVRADLErvyelfprlkeRRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
....*...
gi 1092676368 403 LLFLDEPT 410
Cdd:COG0410 157 LLLLDEPS 164
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
33-144 |
8.95e-07 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 50.06 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 33 GLVGANGSGKSTLLRMIMGMDTDYQGRIDL------RVPVDYLPQI----QAPS--------------------PQSGGE 82
Cdd:COG1131 30 GLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvaRDPAEVRRRIgyvpQEPAlypdltvrenlrffarlyglPRKEAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 83 ATITALQPLF-VWPK--------------------------SLLILDEPTANLD-------LDhkncLIQQVKDYPGAVL 128
Cdd:COG1131 110 ERIDELLELFgLTDAadrkvgtlsggmkqrlglalallhdpELLILDEPTSGLDpearrelWE----LLRELAAEGKTVL 185
|
170
....*....|....*.
gi 1092676368 129 MVSHDRDFLDQTVDWI 144
Cdd:COG1131 186 LSTHYLEEAERLCDRV 201
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-152 |
9.24e-07 |
|
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: 49.98 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 2 AILELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------------- 60
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDgVS-LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgqditglsekelyelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 61 -------------DLRV------PVDY---------------------LPQIQA--PSPQSGGEA-------TItALQPl 91
Cdd:COG1127 83 rigmlfqggalfdSLTVfenvafPLREhtdlseaeirelvleklelvgLPGAADkmPSELSGGMRkrvalarAL-ALDP- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 92 fvwpkSLLILDEPTANLD------LDHkncLIQQVKD-YPGAVLMVSHDRDFLDQTVDWIWAIEQRRL 152
Cdd:COG1127 161 -----EILLYDEPTAGLDpitsavIDE---LIRELRDeLGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-62 |
1.10e-06 |
|
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: 49.74 E-value: 1.10e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 2 AILELNHIKKT-WQAELILEIDR---LLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL 62
Cdd:COG4181 7 PIIELRGLTKTvGTGAGELTILKgisLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL 71
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
34-152 |
1.24e-06 |
|
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: 49.33 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 34 LVGANGSGKSTLLRMIMGMDTDYQGRIDLR-VPVDYLPQIQAP----------------------------------SPQ 78
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTSGTIRVNgQDVSDLRGRAIPylrrkigvvfqdfrllpdrnvyenvafalevtgvPPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 79 --------------------------SGGEATITALQPLFVWPKSLLILDEPTANLDLDHKN---CLIQQVKDYPGAVLM 129
Cdd:cd03292 112 eirkrvpaalelvglshkhralpaelSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWeimNLLKKINKAGTTVVV 191
|
170 180
....*....|....*....|...
gi 1092676368 130 VSHDRDFLDQTVDWIWAIEQRRL 152
Cdd:cd03292 192 ATHAKELVDTTRHRVIALERGKL 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
34-139 |
1.39e-06 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 49.28 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 34 LVGANGSGKSTLLRMIMGMDTDYQGRI-----DLR----------------VPVDY--LP-------------------- 70
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEERPTSGQVlvngqDLSrlkrreipylrrrigvVFQDFrlLPdrtvyenvalplrvtgksrk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 71 QIQAPSPQ------------------SGGE--------ATITalQPlfvwpkSLLILDEPTANLDLDHKN---CLIQQVK 121
Cdd:COG2884 113 EIRRRVREvldlvglsdkakalphelSGGEqqrvaiarALVN--RP------ELLLADEPTGNLDPETSWeimELLEEIN 184
|
170
....*....|....*...
gi 1092676368 122 DYPGAVLMVSHDRDFLDQ 139
Cdd:COG2884 185 RRGTTVLIATHDLELVDR 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
291-440 |
1.96e-06 |
|
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: 49.16 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLkgmvsRSLPGYyyDQLSVG--YFS-QNFDQLDLNQSILENVTQDSV--QSMTLVRNL 365
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLL-----RLIAGF--ETPTSGeiLLDgKDITNLPPHKRPVNTVFQNYAlfPHLTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 366 LAGL---GFNIDKLDQR-----------------ISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDL---PTLQ-EL 421
Cdd:cd03300 94 AFGLrlkKLPKAEIKERvaealdlvqlegyanrkPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLklrKDMQlEL 173
|
170
....*....|....*....
gi 1092676368 422 EAFLQEYPGTFVLVSHDQQ 440
Cdd:cd03300 174 KRLQKELGITFVFVTHDQE 192
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-70 |
1.97e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 49.71 E-value: 1.97e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 1 MAILELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR-VPVDYLP 70
Cdd:COG3842 3 MPALELENVSKRYGDVTALDdVS-LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgRDVTGLP 73
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-62 |
2.12e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.84 E-value: 2.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 1 MAILELNHIKKTWQA--ELILEIDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL 62
Cdd:PRK11650 1 MAGLKLQAVRKSYDGktQVIKGID-LDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI 63
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-133 |
2.21e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.96 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 3 ILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI--DLRVPVDYLPQ--------- 71
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkrNGKLRIGYVPQklyldttlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 ------------------------------IQAPSPQ-SGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCL---I 117
Cdd:PRK09544 84 ltvnrflrlrpgtkkedilpalkrvqaghlIDAPMQKlSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydlI 163
|
170
....*....|....*..
gi 1092676368 118 QQVKDYPG-AVLMVSHD 133
Cdd:PRK09544 164 DQLRRELDcAVLMVSHD 180
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
290-445 |
2.29e-06 |
|
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: 50.13 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLKGMV--------SRSLPGYYYDQLS-------VGYFSQN---FDQldlnqSILEN- 350
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVgvwpptagSVRLDGADLSQWDreelgrhIGYLPQDvelFDG-----TIAENi 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 351 -----VTQDSV----QsmtlvrnlLAGLGFNIDKL----DQRI----STLSGGERVRLSLAKVLLADHHLLFLDEPTNYL 413
Cdd:COG4618 427 arfgdADPEKVvaaaK--------LAGVHEMILRLpdgyDTRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190
....*....|....*....|....*....|....*
gi 1092676368 414 DLPTLQELEAFLQ---EYPGTFVLVSHDQQFIKEC 445
Cdd:COG4618 499 DDEGEAALAAAIRalkARGATVVVITHRPSLLAAV 533
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
382-437 |
2.43e-06 |
|
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: 47.53 E-value: 2.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 382 TLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTFVLVSH 437
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
281-414 |
2.47e-06 |
|
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: 48.64 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 281 DDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMV-------SRSL----------PGYYYDQlsVGYFSQnfDQLDL 343
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQrfyvpenGRVLvdghdlaladPAWLRRQ--VGVVLQ--ENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 344 NQSILENVT-QDSVQSMTLVRNL--LAG---------LGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTN 411
Cdd:cd03252 89 NRSIRDNIAlADPGMSMERVIEAakLAGahdfiselpEGYD-TIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
...
gi 1092676368 412 YLD 414
Cdd:cd03252 168 ALD 170
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-60 |
2.61e-06 |
|
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: 48.37 E-value: 2.61e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI 57
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
381-438 |
2.65e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.91 E-value: 2.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 381 STLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT---LQEL-EAFLQEYPGTFVLVSHD 438
Cdd:PRK11247 132 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrieMQDLiESLWQQHGFTVLLVTHD 193
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-152 |
2.88e-06 |
|
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: 48.06 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 19 LEIDrlLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL--RVPVDYLPQIQAPSPQ------------------ 78
Cdd:cd03297 15 LKID--FDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngTVLFDSRKKINLPPQQrkiglvfqqyalfphlnv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 79 ----------------------------------------SGGEATITAL-QPLFVWPKsLLILDEPTANLDLDHKNCLI 117
Cdd:cd03297 93 renlafglkrkrnredrisvdelldllgldhllnrypaqlSGGEKQRVALaRALAAQPE-LLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092676368 118 QQV----KDYPGAVLMVSHDRDFLDQTVDWIWAIEQRRL 152
Cdd:cd03297 172 PELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-62 |
2.96e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.03 E-value: 2.96e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092676368 2 AILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL 62
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL 66
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
291-427 |
3.84e-06 |
|
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: 48.30 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK----------GMVS------RSLPGYYYDQLsVGYFSQnfDQLDLNQSILENV--- 351
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSllerfydptsGEILldgvdiRDLNLRWLRSQ-IGLVSQ--EPVLFDGTIAENIryg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 ----TQDSVQSMTLVRNL---LAGLGfniDKLD----QRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLptlqE 420
Cdd:cd03249 101 kpdaTDEEVEEAAKKANIhdfIMSLP---DGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA----E 173
|
....*..
gi 1092676368 421 LEAFLQE 427
Cdd:cd03249 174 SEKLVQE 180
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
291-446 |
4.52e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.16 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLK---GMVSRSLPGYYYDQLSV-------GYFSQNfDQLDLNQSILENVT-------Q 353
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNliaGFVPYQHGSITLDGKPVegpgaerGVVFQN-EGLLPWRNVQDNVAfglqlagV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 354 DSVQSMTLVRNLLAGLGfnIDKLDQR-ISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFL----QEY 428
Cdd:PRK11248 101 EKMQRLEIAHQMLKKVG--LEGAEKRyIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQET 178
|
170
....*....|....*...
gi 1092676368 429 PGTFVLVSHDqqfIKECV 446
Cdd:PRK11248 179 GKQVLLITHD---IEEAV 193
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-132 |
4.83e-06 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 46.92 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTW--QAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL-RVPV-DYLPQI------- 72
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdGVPVsDLEKALsslisvl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 73 -QAP------------SPQSGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCLIQQVKDY--PGAVLMVSH 132
Cdd:cd03247 81 nQRPylfdttlrnnlgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITH 155
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
290-463 |
5.01e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 47.70 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLKGM----VSRS----LPGYYYDqlsvgyFSQN----------------FDQLDL-- 343
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSSLLRVLnlleTPDSgqlnIAGHQFD------FSQKpsekairllrqkvgmvFQQYNLwp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 344 NQSILENVTQDSVQSMTLVRN--------LLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDl 415
Cdd:COG4161 96 HLTVMENLIEAPCKVLGLSKEqarekamkLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 416 P--TLQELEAF--LQEYPGTFVLVSHDQQFIKECVNRRYYIKDQQLLnEQQD 463
Cdd:COG4161 174 PeiTAQVVEIIreLSQTGITQVIVTHEVEFARKVASQVVYMEKGRII-EQGD 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-161 |
5.53e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.07 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMdTDYQGR-----IDLR--VPVDYLPQI----QAPS--------------PQSG 80
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSlkingIELRelDPESWRKHLswvgQNPQlphgtlrdnvllgnPDAS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 81 GEATITALQPLFVW-------------------------------------PKSLLILDEPTANLDLDHKNCLIQQVKDY 123
Cdd:PRK11174 452 DEQLQQALENAWVSeflpllpqgldtpigdqaaglsvgqaqrlalarallqPCQLLLLDEPTASLDAHSEQLVMQALNAA 531
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092676368 124 PGA--VLMVSHDRDFLDQtVDWIWAIEQRRLsVYKGNYTD 161
Cdd:PRK11174 532 SRRqtTLMVTHQLEDLAQ-WDQIWVMQDGQI-VQQGDYAE 569
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
330-442 |
5.61e-06 |
|
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: 47.33 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 330 SVGYFSQNfdQLDLNQSILENVTQDS---VQSMTLVRNLLAgLGFNIDKL---DQ-----RISTLSGGERVRLSLAKVLL 398
Cdd:cd03290 80 SVAYAAQK--PWLLNATVEENITFGSpfnKQRYKAVTDACS-LQPDIDLLpfgDQteigeRGINLSGGQRQRICVARALY 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1092676368 399 ADHHLLFLDEPTNYLDL----PTLQE-LEAFLQEYPGTFVLVSHDQQFI 442
Cdd:cd03290 157 QNTNIVFLDDPFSALDIhlsdHLMQEgILKFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
282-414 |
5.63e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.18 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 282 DRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMV--------SRSLPGYYYDQLSVGYFS-----QNFdqLDLNQSIL 348
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAgllppaagTIKLDGGDIDDPDVAEAChylghRNA--MKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 349 ENV--------TQDSVQSMTLVRNLLAGLgfnidkLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:PRK13539 92 ENLefwaaflgGEELDIAAALEAVGLAPL------AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
295-444 |
5.70e-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: 46.21 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 295 KGDKVGLLGPNKAGKTTFLKgMVSRSLPGYYYDQLSVgyfsqnfdqldlnqsilenvtqDSVQSMTLVRNLLAGLGFNID 374
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLAR-ALARELGPPGGGVIYI----------------------DGEDILEEVLDQLLLIIVGGK 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092676368 375 KLDqristLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD---------LPTLQELEAFLQEYPGTFVLVSHDQQFIKE 444
Cdd:smart00382 58 KAS-----GSGELRLRLALALARKLKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
291-456 |
6.24e-06 |
|
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: 47.28 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--GY---------YYDQLSVGYFSQNfDQLDLNQSILEN-VTQDSVQS 358
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdsGEvlfdgkpldIAARNRIGYLPEE-RGLYPKMKVIDQlVYLAQLKG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 359 MTL------VRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG-- 430
Cdd:cd03269 100 LKKeearrrIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARag 178
|
170 180
....*....|....*....|....*..
gi 1092676368 431 -TFVLVSHDQQFIKECVNRRYYIKDQQ 456
Cdd:cd03269 179 kTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
370-508 |
6.70e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.16 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 370 GFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQE-LEAF--LQEYPGTFVLVSHDQQFIKECV 446
Cdd:PRK13651 153 GLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEiLEIFdnLNKQGKTIILVTHDLDNVLEWT 232
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 447 NRRYYIKDQQLLNEQQ------DTDY-SDRSQQTLSLLQF--KLQE-AISNPEVslTEIRQLQDQIQDLKEN 508
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDtydilsDNKFlIENNMEPPKLLNFvnKLEKkGIDVPKV--TSIEELASEINMYLEK 302
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-150 |
7.14e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 48.65 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 16 ELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLRVPVD--YLPQ---------IQA---P-SPQSG 80
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARvlFLPQrpylplgtlREAllyPaTAEAF 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 81 GEATITA------LQPLF-------VWPKSL--------------------LILDEPTANLDLDHKNCLIQQVKD-YPGA 126
Cdd:COG4178 456 SDAELREaleavgLGHLAerldeeaDWDQVLslgeqqrlafarlllhkpdwLFLDEATSALDEENEAALYQLLREeLPGT 535
|
170 180
....*....|....*....|....*
gi 1092676368 127 -VLMVSHdRDFLDQTVDWIWAIEQR 150
Cdd:COG4178 536 tVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
380-443 |
7.89e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.83 E-value: 7.89e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 380 ISTLSGGERV------RLSLAKVLLADHHLLFLDEPTNYLDLPTLQE-----LEAFLQEYPGTFVLVSHDQQFIK 443
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
32-60 |
7.92e-06 |
|
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: 47.04 E-value: 7.92e-06
10 20
....*....|....*....|....*....
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:cd03224 29 VALLGRNGAGKTTLLKTIMGLLPPRSGSI 57
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-60 |
8.85e-06 |
|
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: 47.19 E-value: 8.85e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 3 ILELNHIKKTWQ-----AELILEIDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:cd03258 1 MIELKNVSKVFGdtggkVTALKDVS-LSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSV 62
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
373-427 |
9.61e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 9.61e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 373 IDKLDQRI-STLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQE 427
Cdd:PRK11144 118 IEPLLDRYpGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-138 |
9.82e-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: 45.44 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 28 PQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI----------DLRVPVDYLPQIQAPSPQSGGEATITALQPLFVWPKS 97
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1092676368 98 LLILDEPTANLD---------LDHKNCLIQQVKDYPGAVLMVSHDRDFLD 138
Cdd:smart00382 81 VLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
34-135 |
9.91e-06 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 46.46 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 34 LVGANGSGKSTLLRMIMGMDTDYQGRIDLR--VPVDYLPQIQAPSPQ--------------------------------- 78
Cdd:NF040873 23 VVGPNGSGKSTLLKVLAGVLRPTSGTVRRAggARVAYVPQRSEVPDSlpltvrdlvamgrwarrglwrrltrddraavdd 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 79 ------------------SGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCLIQQVKDYPG---AVLMVSHDRD 135
Cdd:NF040873 103 alervgladlagrqlgelSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
336-438 |
1.08e-05 |
|
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: 47.25 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 336 QNFDQLDlNQSILENVT--------------QDSVQSMTLVrnllaGLGfniDKLDQRISTLSGGERVRLSLAKVLLADH 401
Cdd:cd03294 109 QSFALLP-HRTVLENVAfglevqgvpraereERAAEALELV-----GLE---GWEHKYPDELSGGMQQRVGLARALAVDP 179
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1092676368 402 HLLFLDEPTNYLDlPT----LQELEAFLQ-EYPGTFVLVSHD 438
Cdd:cd03294 180 DILLMDEAFSALD-PLirreMQDELLRLQaELQKTIVFITHD 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
363-410 |
1.12e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.71 E-value: 1.12e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1092676368 363 RNLLAGLGFNIDkLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPT 410
Cdd:COG1129 122 RELLARLGLDID-PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
275-414 |
1.18e-05 |
|
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: 46.08 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 275 DIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVSR----------SLPGYYYD---QLSVGYFSQNfDQL 341
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRktagvitgeiLINGRPLDknfQRSTGYVEQQ-DVH 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 342 DLNQSILEnvtqdsvqSMTLVRNLLAglgfnidkldqristLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:cd03232 91 SPNLTVRE--------ALRFSALLRG---------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
271-497 |
1.20e-05 |
|
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: 47.87 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 271 IHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKgmVSRSLPGYYYDQLSVGYF---------------- 334
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH--VLRGMDQYEPTSGRIIYHvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 335 ------------SQNFDQLDLNQSILENVTQDSV----------QSMTLVRNLLAGL---GFNIDK-------------L 376
Cdd:TIGR03269 79 gepcpvcggtlePEEVDFWNLSDKLRRRIRKRIAimlqrtfalyGDDTVLDNVLEALeeiGYEGKEavgravdliemvqL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 377 DQRIS----TLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQ----ELEAFLQEYPGTFVLVSHDQQFIKECVNR 448
Cdd:TIGR03269 159 SHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKlvhnALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1092676368 449 RYYIKDQQLLNEQQDTDYSDRSQQTLSLLQFKLQEAISNPEVSLTEIRQ 497
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSK 287
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
272-444 |
1.30e-05 |
|
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: 45.78 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 272 HLQDIDVQVDDRLLfhlqhfklqkgdkVGLLGPNKAGKTTFL--------KGMVSRSLPGYYYDQLSVgyfsqnFDQLdl 343
Cdd:cd03238 10 NLQNLDVSIPLNVL-------------VVVTGVSGSGKSTLVneglyasgKARLISFLPKFSRNKLIF------IDQL-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 344 nQSILENvtqdsvqsmtlvrnllaGLGFNidKLDQRISTLSGGERVRLSLAKVLLAD-HHLLF-LDEPTNYLDLPTLQEL 421
Cdd:cd03238 69 -QFLIDV-----------------GLGYL--TLGQKLSTLSGGELQRVKLASELFSEpPGTLFiLDEPSTGLHQQDINQL 128
|
170 180
....*....|....*....|....*.
gi 1092676368 422 -EAF--LQEYPGTFVLVSHDQQFIKE 444
Cdd:cd03238 129 lEVIkgLIDLGNTVILIEHNLDVLSS 154
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-60 |
1.47e-05 |
|
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: 46.12 E-value: 1.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV 57
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-60 |
1.53e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 46.64 E-value: 1.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 3 ILELNHIKKTW---QA--ELILEIdrllvqPQDRI-GLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:COG4152 1 MLELKGLTKRFgdkTAvdDVSFTV------PKGEIfGLLGPNGAGKTTTIRIILGILAPDSGEV 58
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
363-458 |
1.82e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.41 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 363 RNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAF---LQEYPGTFVLVSHDQ 439
Cdd:PRK10535 126 QELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAIlhqLRDRGHTVIIVTHDP 204
|
90
....*....|....*....
gi 1092676368 440 QfIKECVNRRYYIKDQQLL 458
Cdd:PRK10535 205 Q-VAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
267-438 |
1.89e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 46.28 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 267 SNTLIHLQDIDVQVDDRLLFHLQH--FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPG----YYYDQL----------- 329
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFTLKDvsFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsgeiFYNNQAitddnfeklrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 330 SVGYFSQNFDqldlNQ---SI--------LEN--VTQDSVQSmtLVRNLLAGLGFnIDKLDQRISTLSGGERVRLSLAKV 396
Cdd:PRK13648 84 HIGIVFQNPD----NQfvgSIvkydvafgLENhaVPYDEMHR--RVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1092676368 397 LLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG----TFVLVSHD 438
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
290-437 |
1.91e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.11 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTT----------------FLKGMVSRSLPGyyyDQLSVG-YFSQN--FDQLDLNQSI--- 347
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTllnliagfltpasgslTLNGQDHTTTPP---SRRPVSmLFQENnlFSHLTVAQNIglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 348 ------LENVTQDSVQSMtlvrnllAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDlPTL-QE 420
Cdd:PRK10771 96 lnpglkLNAAQREKLHAI-------ARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD-PALrQE 167
|
170 180
....*....|....*....|.
gi 1092676368 421 ----LEAFLQEYPGTFVLVSH 437
Cdd:PRK10771 168 mltlVSQVCQERQLTLLMVSH 188
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
291-427 |
2.01e-05 |
|
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: 47.02 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKgMVSR--------------SLPGYYYDQL--SVGYFSQnfDQLDLNQSILENV--- 351
Cdd:TIGR02203 353 LVIEPGETVALVGRSGSGKSTLVN-LIPRfyepdsgqilldghDLADYTLASLrrQVALVSQ--DVVLFNDTIANNIayg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 ---------TQDSVQS---MTLVRNLLAGLGFNIDkldQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQ 419
Cdd:TIGR02203 430 rteqadraeIERALAAayaQDFVDKLPLGLDTPIG---ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
....*...
gi 1092676368 420 ELEAFLQE 427
Cdd:TIGR02203 507 LVQAALER 514
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
291-421 |
2.10e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.39 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--GYYYDQLSVGYFSQnFDQL---DLNQSILENVTQDSVQSMTLVRnl 365
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPseGKIKHSGRISFSSQ-FSWImpgTIKENIIFGVSYDEYRYKSVVK-- 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 366 LAGLGFNIDKLDQRIST--------LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQEL 421
Cdd:cd03291 135 ACQLEEDITKFPEKDNTvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
295-440 |
2.16e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 46.75 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 295 KGDKVGLLGPNKAGKTTFLkgmvsRSLPGyyydqlsvgyfsqnFDQLDLNQSILENVTQDSV-----------QS----- 358
Cdd:PRK11607 44 KGEIFALLGASGCGKSTLL-----RMLAG--------------FEQPTAGQIMLDGVDLSHVppyqrpinmmfQSyalfp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 359 -MTLVRNLLAGLgfNIDKL-----DQRIS-----------------TLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD- 414
Cdd:PRK11607 105 hMTVEQNIAFGL--KQDKLpkaeiASRVNemlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDk 182
|
170 180
....*....|....*....|....*....
gi 1092676368 415 -LPTLQELEA--FLQEYPGTFVLVSHDQQ 440
Cdd:PRK11607 183 kLRDRMQLEVvdILERVGVTCVMVTHDQE 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
377-438 |
2.23e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.13 E-value: 2.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 377 DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLP---TLQELEAFLQEYPG-TFVLVSHD 438
Cdd:PRK10253 138 DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShqiDLLELLSELNREKGyTLAAVLHD 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
272-439 |
2.36e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 46.60 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 272 HLQDIDVQVDDrllfhlqhfklqkGDKVGLLGPNKAGKTTFLK------------------------------GMVSRSl 321
Cdd:COG3839 18 ALKDIDLDIED-------------GEFLVLLGPSGCGKSTLLRmiagledptsgeiliggrdvtdlppkdrniAMVFQS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 322 pgyY--YDQLSVGyfsQNfdqldlnqsI-----LENVTQDSVQSMtlVRNLLAGLGfnIDK-LDQRISTLSGGERVRLSL 393
Cdd:COG3839 84 ---YalYPHMTVY---EN---------IafplkLRKVPKAEIDRR--VREAAELLG--LEDlLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1092676368 394 AKVLLADHHLLFLDEPTNYLDlPTL-----QELEAFLQEYPGTFVLVSHDQ 439
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLD-AKLrvemrAEIKRLHRRLGTTTIYVTHDQ 194
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
262-469 |
2.54e-05 |
|
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: 47.21 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 262 HLSD--PSNTLIHLQDIDVQV--DDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVSR-------SLPGYYYDQLS 330
Cdd:TIGR01271 1207 HAQKcwPSGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLlstegeiQIDGVSWNSVT 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 331 V------------------GYFSQNFDQLDL--NQSILENVTQDSVQSMtlVRNLLAGLGFnidKLDQRISTLSGGERVR 390
Cdd:TIGR01271 1287 LqtwrkafgvipqkvfifsGTFRKNLDPYEQwsDEEIWKVAEEVGLKSV--IEQFPDKLDF---VLVDGGYVLSNGHKQL 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 391 LSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG--TFVLVSHD-------QQF--IKECVNRRYyikD--QQL 457
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSncTVILSEHRveallecQQFlvIEGSSVKQY---DsiQKL 1438
|
250
....*....|....*.
gi 1092676368 458 LNE----QQDTDYSDR 469
Cdd:TIGR01271 1439 LNEtslfKQAMSAADR 1454
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
34-139 |
2.58e-05 |
|
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: 45.21 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 34 LVGANGSGKSTLLRMIMGmDTDY---QGRIDLR------VPVD------------YLPQIQAPSPQ----------SGGE 82
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMG-HPKYevtEGEILFKgeditdLPPEerarlgiflafqYPPEIPGVKNAdflryvnegfSGGE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 83 ------ATITALQPlfvwpkSLLILDEPTANLDLDHKNCL---IQQVKDYPGAVLMVSHDRDFLDQ 139
Cdd:cd03217 110 kkrneiLQLLLLEP------DLAILDEPDSGLDIDALRLVaevINKLREEGKSVLIITHYQRLLDY 169
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-60 |
2.91e-05 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 45.64 E-value: 2.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 4 LELNHIKKTW-QAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSV 58
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
33-60 |
3.24e-05 |
|
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: 45.36 E-value: 3.24e-05
10 20
....*....|....*....|....*...
gi 1092676368 33 GLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:COG0410 33 ALLGRNGAGKTTLLKAISGLLPPRSGSI 60
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-66 |
3.29e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 45.98 E-value: 3.29e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 1 MAIlELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRID-LRVPV 66
Cdd:PRK13536 40 VAI-DLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGVPV 105
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-133 |
3.40e-05 |
|
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: 46.58 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTW-QAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI-------------DLRVPVDYL 69
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssldqdEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 70 PQ--------------IQAP--SPQ---------------------------------SGGEATITALQPLFVWPKSLLI 100
Cdd:TIGR02868 415 AQdahlfdttvrenlrLARPdaTDEelwaalervgladwlralpdgldtvlgeggarlSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*
gi 1092676368 101 LDEPTANLDLDHKNCLIQQVKD-YPG-AVLMVSHD 133
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLAaLSGrTVVLITHH 529
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-71 |
3.78e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.95 E-value: 3.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 4 LELNHIKKTWQAELILEIdrllvQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLRVPVDYLPQ 71
Cdd:COG2401 36 VELRVVERYVLRDLNLEI-----EPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR 98
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-437 |
4.16e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.22 E-value: 4.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 374 DKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG--TFVLVSH 437
Cdd:PRK14267 141 DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
377-437 |
4.31e-05 |
|
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: 44.77 E-value: 4.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 377 DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG--TFVLVSH 437
Cdd:cd03248 145 GEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
343-410 |
5.38e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.78 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 343 LNQSILENVT---QDSVQSMTLV-----RNLLAGLgfnIDKL-------DQRISTLSGGERVRLSLAKVLLADHHLLFLD 407
Cdd:COG1129 343 LDLSIRENITlasLDRLSRGGLLdrrreRALAEEY---IKRLriktpspEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
...
gi 1092676368 408 EPT 410
Cdd:COG1129 420 EPT 422
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-437 |
5.44e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.90 E-value: 5.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 374 DKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPG--TFVLVSH 437
Cdd:PRK14247 138 DRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-60 |
5.72e-05 |
|
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: 44.17 E-value: 5.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI 57
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
290-438 |
5.96e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 44.68 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPgyyyDQLSVGYFSQNFDQLDLNQS-----ILENVTQDSVQS------ 358
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESP----SQGNVSWRGEPLAKLNRAQRkafrrDIQMVFQDSISAvnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 359 ------------MTL--------VRNLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDL--- 415
Cdd:PRK10419 108 vreiireplrhlLSLdkaerlarASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlq 187
|
170 180
....*....|....*....|....*
gi 1092676368 416 -PTLQELEAfLQEYPGT-FVLVSHD 438
Cdd:PRK10419 188 aGVIRLLKK-LQQQFGTaCLFITHD 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
286-410 |
5.99e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 44.48 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 286 FHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVS--RSLPGyyydqlsvgyfSQNFDQLDLNQSILENVTQDSV------- 356
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGdpRATSG-----------RIVFDGKDITDWQTAKIMREAVaivpegr 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 357 ---QSMTLVRNLLAGlGFNIDKLD--------------------QRISTLSGGERVRLSLAKVLLADHHLLFLDEPT 410
Cdd:PRK11614 90 rvfSRMTVEENLAMG-GFFAERDQfqerikwvyelfprlherriQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-51 |
7.41e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 44.31 E-value: 7.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 3 ILELNHIKKTWQAELILEIdRLL------VQPQDRIGLVGANGSGKSTLLRMIMG 51
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEK-RALdglnltIEEGDFVTVIGSNGAGKSTLLNAIAG 54
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
291-421 |
7.66e-05 |
|
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: 45.67 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPG----YYYDQLSvgyFSQNFDQL---DLNQSILENVTQDSVQSMTLVR 363
Cdd:TIGR01271 447 FKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSegkiKHSGRIS---FSPQTSWImpgTIKDNIIFGLSYDEYRYTSVIK 523
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 364 nlLAGLGFNIDKLDQRIS--------TLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQEL 421
Cdd:TIGR01271 524 --ACQLEEDIALFPEKDKtvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
301-440 |
9.70e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.00 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 301 LLGPNKAGKTTFLKGmVSR--------SLPGyyydqlSVGY-----FSQNFDQLDLNQSILENVTQDSVQSMTLVRNLLA 367
Cdd:PRK14239 36 LIGPSGSGKSTLLRS-INRmndlnpevTITG------SIVYnghniYSPRTDTVDLRKEIGMVFQQPNPFPMSIYENVVY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 368 GLGFN--IDK--LDQRIST---------------------LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELE 422
Cdd:PRK14239 109 GLRLKgiKDKqvLDEAVEKslkgasiwdevkdrlhdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIE 188
|
170 180
....*....|....*....|..
gi 1092676368 423 AFL----QEYpgTFVLVSHDQQ 440
Cdd:PRK14239 189 ETLlglkDDY--TMLLVTRSMQ 208
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
351-414 |
1.02e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 351 VTQDSVQSMT-LVRNLLAGLGFNIDKLD---------------QRISTLSGGER------VRLSLAKVLLADHHLLFLDE 408
Cdd:PRK01156 754 IRKSASQAMTsLTRKYLFEFNLDFDDIDvdqdfnitvsrggmvEGIDSLSGGEKtavafaLRVAVAQFLNNDKSLLIMDE 833
|
....*.
gi 1092676368 409 PTNYLD 414
Cdd:PRK01156 834 PTAFLD 839
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
357-448 |
1.06e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 44.27 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 357 QSMTLVrnllaGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDlP-----TLQELEAFLQEYPGT 431
Cdd:PRK13637 125 RAMNIV-----GLDYE-DYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD-PkgrdeILNKIKELHKEYNMT 197
|
90
....*....|....*..
gi 1092676368 432 FVLVSHDQQFIKECVNR 448
Cdd:PRK13637 198 IILVSHSMEDVAKLADR 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
291-454 |
1.10e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--------GYYYDQLS--------VGYFSQNFDQLDlNQSILENV--- 351
Cdd:PRK09700 26 LTVYPGEIHALLGENGAGKSTLMKVLSGIHEPtkgtitinNINYNKLDhklaaqlgIGIIYQELSVID-ELTVLENLyig 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 352 ----------------TQDSVQSMTLVRnllagLGFNIDkLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDL 415
Cdd:PRK09700 105 rhltkkvcgvniidwrEMRVRAAMMLLR-----VGLKVD-LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1092676368 416 PTLQELEAFLQEYPG---TFVLVSHDQQFIKECVNRRYYIKD 454
Cdd:PRK09700 179 KEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKD 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-109 |
1.17e-04 |
|
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: 43.94 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGMDTDYQGRIDLRVP-VDYLPQ-IQAPSPQ------------------------------- 78
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQyIKADYEGtvrdllssitkdfythpyfkteiakplqieq 107
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1092676368 79 ---------SGGEATITALQPLFVWPKSLLILDEPTANLD 109
Cdd:cd03237 108 ildrevpelSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
26-63 |
1.23e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 44.77 E-value: 1.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMG-MDTDyQGRI-----DLR 63
Cdd:COG1132 363 IPPGETVALVGPSGSGKSTLVNLLLRfYDPT-SGRIlidgvDIR 405
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
366-438 |
1.26e-04 |
|
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: 43.61 E-value: 1.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092676368 366 LAGLGFNIDKldqRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFL----QEYPGTFVLVSHD 438
Cdd:TIGR01184 101 LVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
290-413 |
1.31e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 290 HFKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLP--------GYYYDQLSVG-------YFSQNFDQLDLNQSILENV--- 351
Cdd:PRK15439 31 DFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPdsgtleigGNPCARLTPAkahqlgiYLVPQEPLLFPNLSVKENIlfg 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092676368 352 ---TQDSVQSMTlvrNLLAGLGFNIDkLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYL 413
Cdd:PRK15439 111 lpkRQASMQKMK---QLLAALGCQLD-LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
377-421 |
1.38e-04 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 43.70 E-value: 1.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1092676368 377 DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT---LQEL 421
Cdd:COG4525 129 RRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTreqMQEL 176
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-133 |
1.41e-04 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 43.57 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGMDTDYQGRI--------------DLR-------------------------------VPV 66
Cdd:TIGR04520 31 VAIIGHNGSGKSTLAKLLNGLLLPTSGKVtvdgldtldeenlwEIRkkvgmvfqnpdnqfvgatveddvafglenlgVPR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 67 DYLPQI---------------QAPSPQSGGE------ATITALQPlfvwpkSLLILDEPTANLDLDHKNCLIQQV----K 121
Cdd:TIGR04520 111 EEMRKRvdealklvgmedfrdREPHLLSGGQkqrvaiAGVLAMRP------DIIILDEATSMLDPKGRKEVLETIrklnK 184
|
170
....*....|..
gi 1092676368 122 DYPGAVLMVSHD 133
Cdd:TIGR04520 185 EEGITVISITHD 196
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
270-437 |
1.42e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.01 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 270 LIHLQDIDVQVDDRLLFHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPgyyyDQLSVGYFSQNFDQ-LDLNQSIL 348
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNP----EKGEILFERQSIKKdLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 349 ENVTQDS--VQSMTLVRNLLAGLGFN-----IDKL----------DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTN 411
Cdd:PRK13540 77 CFVGHRSgiNPYLTLRENCLYDIHFSpgavgITELcrlfslehliDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180
....*....|....*....|....*....
gi 1092676368 412 YLDLPTLQELEAFLQEYP---GTFVLVSH 437
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRakgGAVLLTSH 185
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
293-438 |
1.42e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 43.68 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 293 LQKGDKVGLLGPNKAGKTTFLKGM-----------------VSRSLPGYYYDQLSVGYFSQNFDQLDLNQSILENVT--- 352
Cdd:PRK13636 29 IKKGEVTAILGGNGAGKSTLFQNLngilkpssgrilfdgkpIDYSRKGLMKLRESVGMVFQDPDNQLFSASVYQDVSfga 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 353 ------QDSVQSMtlVRNLLAGLGFNIDKlDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQE----LE 422
Cdd:PRK13636 109 vnlklpEDEVRKR--VDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEimklLV 185
|
170
....*....|....*.
gi 1092676368 423 AFLQEYPGTFVLVSHD 438
Cdd:PRK13636 186 EMQKELGLTIIIATHD 201
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
301-443 |
1.50e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 301 LLGPNKAGKTTFLK------GMvsRSLPGYYYDQLSVGYFSqnfdqldlnqsilenvtqdSVQSMTLVrnllaglgfnid 374
Cdd:cd03227 26 ITGPNGSGKSTILDaiglalGG--AQSATRRRSGVKAGCIV-------------------AAVSAELI------------ 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 375 kldQRISTLSGGERVRLSLAKVL-LADHH---LLFLDEPTNYLDLPTLQELEAFLQEY---PGTFVLVSHDQQFIK 443
Cdd:cd03227 73 ---FTRLQLSGGEKELSALALILaLASLKprpLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHLPELAE 145
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-51 |
1.61e-04 |
|
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: 43.15 E-value: 1.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 1 MAILELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMG 51
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDdIS-WTVKPGEHWAILGPNGAGKSTLLSLITG 51
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
291-445 |
1.70e-04 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. 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: 213269 [Multi-domain] Cd Length: 207 Bit Score: 42.78 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPgyyyDQLSVGYFSQNFDQLDLN--QSILENVTQDSVQSMTLVRNllag 368
Cdd:cd03369 29 FKVKAGEKIGIVGRTGAGKSTLILALFRFLEA----EEGKIEIDGIDISTIPLEdlRSSLTIIPQDPTLFSGTIRS---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 369 lgfNIDKLDQ----------RIS----TLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQE--YPGTF 432
Cdd:cd03369 101 ---NLDPFDEysdeeiygalRVSegglNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTI 177
|
170
....*....|...
gi 1092676368 433 VLVSHDQQFIKEC 445
Cdd:cd03369 178 LTIAHRLRTIIDY 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-80 |
1.75e-04 |
|
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: 42.84 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAE----LILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGridlRVPVDYLPqIQAPSPQ 78
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEdIS-LSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSG----EVLVDGEP-VTGPGPD 74
|
..
gi 1092676368 79 SG 80
Cdd:cd03293 75 RG 76
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
373-414 |
1.77e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.24 E-value: 1.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1092676368 373 IDKLDQRIST--------LSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:PRK11176 463 INKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
26-52 |
1.77e-04 |
|
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: 42.88 E-value: 1.77e-04
10 20
....*....|....*....|....*..
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGM 52
Cdd:cd03263 25 VYKGEIFGLLGHNGAGKTTTLKMLTGE 51
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
381-443 |
1.88e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 1.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 381 STLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDlPTLQE-----LEAFLQEYPGTFVLVSHDQQFIK 443
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAqilalLKSLQQKHQLAYLFISHDLHVVR 490
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-152 |
1.98e-04 |
|
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: 42.87 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI----------------DLRVPV 66
Cdd:cd03261 1 IELRGLTKSFGGRTVLKgVD-LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisglseaelyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 67 DYLPQIQA----------------------------------------------PSPQSGGEA-------TItALQPlfv 93
Cdd:cd03261 80 GMLFQSGAlfdsltvfenvafplrehtrlseeeireivlekleavglrgaedlyPAELSGGMKkrvalarAL-ALDP--- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 94 wpkSLLILDEPTANLD------LDHkncLIQQVKDYPGA-VLMVSHDRDFLDQTVDWIWAIEQRRL 152
Cdd:cd03261 156 ---ELLLYDEPTAGLDpiasgvIDD---LIRSLKKELGLtSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-132 |
2.08e-04 |
|
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: 42.48 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 30 DRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL-----------RVPVDYLPQ--------------------------- 71
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIngvdvtaappaDRPVSMLFQennlfahltveqnvglglspglkltae 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 72 ------------------IQAPSPQSGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCLIQQVKDYPG----AVLM 129
Cdd:cd03298 105 drqaievalarvglagleKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAetkmTVLM 184
|
...
gi 1092676368 130 VSH 132
Cdd:cd03298 185 VTH 187
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-70 |
2.19e-04 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 42.61 E-value: 2.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR-VPVDYLP 70
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgKDITNLP 68
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
291-414 |
2.26e-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: 44.17 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSR--SLPGYYYDQLSVGYFSQN--FDQLDLNQSIL------ENVTQDSVQSMT 360
Cdd:TIGR00957 659 FSIPEGALVAVVGQVGCGKSSLLSALLAEmdKVEGHVHMKGSVAYVPQQawIQNDSLRENILfgkalnEKYYQQVLEACA 738
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 361 LVRNLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:TIGR00957 739 LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
365-512 |
2.69e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.84 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 365 LLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQE----LEAFLQEYPGTFVLVSHDQQ 440
Cdd:PRK13646 128 LLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQvmrlLKSLQTDENKTIILVSHDMN 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 441 FIKECVNRRYYIKDQQLLNEQQDTDYsdrsqqtlsllqFKLQEAISNPEVSLTEIRQLQDQIQDlKENIKHK 512
Cdd:PRK13646 208 EVARYADEVIVMKEGSIVSQTSPKEL------------FKDKKKLADWHIGLPEIVQLQYDFEQ-KYQTKLK 266
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-60 |
3.25e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 42.76 E-value: 3.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 1 MAIlELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:PRK10851 1 MSI-EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI 59
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-135 |
3.29e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.01 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 2 AILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL-------------RVPVDY 68
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFegedistlkpeiyRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 69 LPQI--------------------QAPSPQ-----------------------SGGE----ATITALQPLfvwPKSLLiL 101
Cdd:PRK10247 86 CAQTptlfgdtvydnlifpwqirnQQPDPAiflddlerfalpdtiltkniaelSGGEkqriSLIRNLQFM---PKVLL-L 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092676368 102 DEPTANLDLDHK---NCLIQQ-VKDYPGAVLMVSHDRD 135
Cdd:PRK10247 162 DEITSALDESNKhnvNEIIHRyVREQNIAVLWVTHDKD 199
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
374-440 |
3.39e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.46 E-value: 3.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092676368 374 DKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQE----YpgTFVLVSHDQQ 440
Cdd:PRK14243 143 DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHElkeqY--TIIIVTHNMQ 211
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
367-445 |
3.46e-04 |
|
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: 42.60 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 367 AGLGFNidKLDQRISTLSGGERVRLSLAKVLL--ADHHLLF-LDEPTNYLDLPTLQELEAFLQ---EYPGTFVLVSHDQQ 440
Cdd:cd03271 156 VGLGYI--KLGQPATTLSGGEAQRIKLAKELSkrSTGKTLYiLDEPTTGLHFHDVKKLLEVLQrlvDKGNTVVVIEHNLD 233
|
....*
gi 1092676368 441 FIKEC 445
Cdd:cd03271 234 VIKCA 238
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-71 |
3.46e-04 |
|
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: 43.23 E-value: 3.46e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGMDTDYQGRIDLRVPVDYLPQ 71
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ 408
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
273-437 |
3.69e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.17 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 273 LQDIDVQVDDRllfhlqHFklqkgdkVGLLGPNKAGKTTflkgmVSRSLPGYY-------------YDQLSVGYFSQNF- 338
Cdd:PRK10790 357 LQNINLSVPSR------GF-------VALVGHTGSGKST-----LASLLMGYYpltegeirldgrpLSSLSHSVLRQGVa 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 339 ----DQLDLNQSILENVTQ-------------DSVQSMTLVRNLLAGLGfniDKLDQRISTLSGGERVRLSLAKVLLADH 401
Cdd:PRK10790 419 mvqqDPVVLADTFLANVTLgrdiseeqvwqalETVQLAELARSLPDGLY---TPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190
....*....|....*....|....*....|....*...
gi 1092676368 402 HLLFLDEPTNYLDLPTLQELEAFLQEY--PGTFVLVSH 437
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH 533
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
383-444 |
3.71e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.48 E-value: 3.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 383 LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGTF----VLVSHDQQFIKE 444
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmtvIFSTHQLDLVPE 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-75 |
3.97e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 42.90 E-value: 3.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 3 ILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR-VPVDYLPQIQAP 75
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLSHVPPYQRP 92
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
291-414 |
4.75e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.09 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSRSLPGYYYDQL------------------SVGYFSQNFDqldlNQSI----- 347
Cdd:PRK13640 28 FSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKitvdgitltaktvwdireKVGIVFQNPD----NQFVgatvg 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 348 ------LENVTQDSVQSMTLVRNLLAGLGFnIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:PRK13640 104 ddvafgLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
367-414 |
4.92e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.73 E-value: 4.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1092676368 367 AGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:PRK15439 388 RALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
32-71 |
6.36e-04 |
|
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: 41.02 E-value: 6.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGMDTDYQGRI------------DLRVPVDYLPQ 71
Cdd:cd03264 28 YGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdvlkqpqKLRRRIGYLPQ 79
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-60 |
6.51e-04 |
|
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: 42.12 E-value: 6.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 3 ILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGM--DTDYQGRI 60
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEI 60
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
269-440 |
6.85e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 41.86 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 269 TLIHLQDIDVQVDDRLLfhLQHFKLQ--KGDKVGLLGPNKAGKTTFLkgmvsRSLPGyyydqlsvgyfsqnFDQLDLNQS 346
Cdd:PRK09452 13 PLVELRGISKSFDGKEV--ISNLDLTinNGEFLTLLGPSGCGKTTVL-----RLIAG--------------FETPDSGRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 347 ILENVTQDSV-----------QS------MTLVRNLLAGLGFN-----------IDKL---------DQRISTLSGGERV 389
Cdd:PRK09452 72 MLDGQDITHVpaenrhvntvfQSyalfphMTVFENVAFGLRMQktpaaeitprvMEALrmvqleefaQRKPHQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 390 RLSLAKVLLADHHLLFLDEPTNYLDLP---TLQ-ELEAfLQEYPG-TFVLVSHDQQ 440
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKlrkQMQnELKA-LQRKLGiTFVFVTHDQE 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
62-135 |
7.67e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 41.53 E-value: 7.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 62 LRVPVDYLPQiqAPSPQSGGEATITALQPLFVWPKSLLILDEPTANLD----LDHKNCLIQQVKDYPGAVLMVSHDRD 135
Cdd:PRK13645 137 VQLPEDYVKR--SPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMD 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
374-414 |
7.98e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.45 E-value: 7.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1092676368 374 DKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:PRK11701 143 ARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-154 |
1.01e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 41.03 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 1 MAILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL--------------RVPV 66
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 67 DYLPQiqapspqsggEATItaLQPLFVWPKSLLIL---DEPTANLDLDHKNCLIQQvkdypgavLMVSHDRDFLDQTVDw 143
Cdd:PRK10895 81 GYLPQ----------EASI--FRRLSVYDNLMAVLqirDDLSAEQREDRANELMEE--------FHIEHLRDSMGQSLS- 139
|
170
....*....|.
gi 1092676368 144 iwAIEQRRLSV 154
Cdd:PRK10895 140 --GGERRRVEI 148
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
281-435 |
1.01e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 281 DDRLLfHLQHFKLQKGDKVGLLGPNKAGKTTFLKGMvSRSLPgyyydQLSVGYFSQ-------NFDQLdlnQSILEN--- 350
Cdd:PRK10938 15 DTKTL-QLPSLTLNAGDSWAFVGANGSGKSALARAL-AGELP-----LLSGERQSQfshitrlSFEQL---QKLVSDewq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 351 --------------------VTQDSVQSMTLVRNLLAGLGFNiDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPT 410
Cdd:PRK10938 85 rnntdmlspgeddtgrttaeIIQDEVKDPARCEQLAQQFGIT-ALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180
....*....|....*....|....*...
gi 1092676368 411 NYLDLPTLQELEAFLQEYPG---TFVLV 435
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQsgiTLVLV 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-60 |
1.08e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.54 E-value: 1.08e-03
10 20
....*....|....*....|....*...
gi 1092676368 33 GLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEI 61
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
291-445 |
1.11e-03 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 41.63 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTT----------------FLKGMVSRSLPGYYYDQlSVGYFSQnfDQLDLNQSILENVT-- 352
Cdd:TIGR00958 502 FTLHPGEVVALVGPSGSGKSTvaallqnlyqptggqvLLDGVPLVQYDHHYLHR-QVALVGQ--EPVLFSGSVRENIAyg 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 353 -QDSVQSMTLVRNLLAGLGFNIDKLDQRIST--------LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLptlqELEA 423
Cdd:TIGR00958 579 lTDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQ 654
|
170 180
....*....|....*....|....*.
gi 1092676368 424 FLQEYPG----TFVLVSHDQQFIKEC 445
Cdd:TIGR00958 655 LLQESRSrasrTVLLIAHRLSTVERA 680
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
361-437 |
1.12e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 41.16 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 361 LVRNLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQEL-EAFL---QEYPGTFVLVS 436
Cdd:PRK13634 124 KAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMmEMFYklhKEKGLTTVLVT 203
|
.
gi 1092676368 437 H 437
Cdd:PRK13634 204 H 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-71 |
1.15e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 1.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGMDTDYQGRIDLRVPVDYLPQ 71
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ 407
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
380-440 |
1.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092676368 380 ISTLSGGERV------RLSLAKVLLADHHLLFLDEPTNYLDLPTLQEL----EAFLQEYPgTFVLVSHDQQ 440
Cdd:PRK03918 786 LTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLvdimERYLRKIP-QVIIVSHDEE 855
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
26-63 |
1.39e-03 |
|
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: 40.50 E-value: 1.39e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR 63
Cdd:cd03219 23 VRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD 60
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
380-414 |
1.60e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.02 E-value: 1.60e-03
10 20 30
....*....|....*....|....*....|....*
gi 1092676368 380 ISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-60 |
1.62e-03 |
|
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: 40.02 E-value: 1.62e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1092676368 24 LLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI 59
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
73-152 |
1.66e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 40.58 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 73 QAPSPQSGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCLIQQVKDYPGA---VLMVSHDRDFLDQTVDWIWAIEQ 149
Cdd:PRK13641 141 KSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEH 220
|
...
gi 1092676368 150 RRL 152
Cdd:PRK13641 221 GKL 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-60 |
1.78e-03 |
|
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: 40.16 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1092676368 15 AELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV 59
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-60 |
1.83e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.68 E-value: 1.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 1 MAILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGM--DTDYQGRI 60
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEI 64
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
338-438 |
1.83e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 338 FDQLDLNQSILENVTQDSVQSMTLVRNLLAGLGFNIDKLDqRISTLSGGERVRLSLAKVLladhhLLFLDepTNYLDLPT 417
Cdd:COG0419 115 YEELKERLKELEEALESALEELAELQKLKQEILAQLSGLD-PIETLSGGERLRLALADLL-----SLILD--FGSLDEER 186
|
90 100
....*....|....*....|.
gi 1092676368 418 LQELEAFLQEypgtFVLVSHD 438
Cdd:COG0419 187 LERLLDALEE----LAIITHV 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-71 |
1.96e-03 |
|
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: 39.83 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 4 LELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL------RVPVD--------YL 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdgqditKLPMHkrarlgigYL 80
|
..
gi 1092676368 70 PQ 71
Cdd:cd03218 81 PQ 82
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
365-442 |
1.99e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 365 LLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADhhlLF-----LDEPTNYL---DLPTLQELEAFLQEYPGTFVLVS 436
Cdd:PRK00635 459 ILIDLGLPYLTPERALATLSGGEQERTALAKHLGAE---LIgityiLDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVE 535
|
....*.
gi 1092676368 437 HDQQFI 442
Cdd:PRK00635 536 HDEQMI 541
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-62 |
2.01e-03 |
|
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: 39.66 E-value: 2.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092676368 3 ILELNHIKKTWQAE--LILEIDRL--LVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDL 62
Cdd:cd03266 1 MITADALTKRFRDVkkTVQAVDGVsfTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV 64
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
377-414 |
2.08e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.68 E-value: 2.08e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1092676368 377 DQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-58 |
2.43e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 40.77 E-value: 2.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 3 ILELNHIKKTWQAELILEIDRLLV--QPQDRIGLVGANGSGKSTLLRMIMGMDTDYQG 58
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDRLCVgvRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG 1994
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
360-437 |
2.44e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 39.73 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 360 TLVRNLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAF---LQEYPGTFVLVS 436
Cdd:PRK13649 123 ALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLfkkLHQSGMTIVLVT 202
|
.
gi 1092676368 437 H 437
Cdd:PRK13649 203 H 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
383-427 |
2.65e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 40.57 E-value: 2.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1092676368 383 LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQE 427
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE 539
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-142 |
3.06e-03 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 40.17 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 3 ILELNHIKKTWqaeliLEIDRLLVQPQDRI----------GLVGANGSGKSTLLRMIMGMDTDYQGRIDLRVPVDY---- 68
Cdd:TIGR03269 279 IIKVRNVSKRY-----ISVDRGVVKAVDNVslevkegeifGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWvdmt 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 69 ----------------------------------------LPQIQA-------------------------PSPQSGGEA 83
Cdd:TIGR03269 354 kpgpdgrgrakryigilhqeydlyphrtvldnlteaigleLPDELArmkavitlkmvgfdeekaeeildkyPDELSEGER 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092676368 84 TITALQPLFVWPKSLLILDEPTANLD----LDHKNCLIQQVKDYPGAVLMVSHDRDFLDQTVD 142
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCD 496
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
374-415 |
3.24e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 39.42 E-value: 3.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1092676368 374 DKLDQR-ISTLSGGERVRLSLAKVL---------LADHHLLFLDEPTNYLDL 415
Cdd:PRK13547 136 TALVGRdVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
378-458 |
3.41e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 39.61 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 378 QRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEAFLQEYPGT---FVLVSHDQQFIKECVNRRYYIKD 454
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQ 211
|
....
gi 1092676368 455 QQLL 458
Cdd:PRK13638 212 GQIL 215
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
366-445 |
3.44e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 366 LAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLA--DHHLLF-LDEPTNYLDLPTLQELEAFLQE--YPG-TFVLVSHDQ 439
Cdd:PRK00635 793 LCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLApsKKPTLYvLDEPTTGLHTHDIKALIYVLQSltHQGhTVVIIEHNM 872
|
....*.
gi 1092676368 440 QFIKEC 445
Cdd:PRK00635 873 HVVKVA 878
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
384-438 |
3.61e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 39.56 E-value: 3.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092676368 384 SGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT-LQELEAF--LQEYPGT-FVLVSHD 438
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVqAQVLNLMmdLQQELGLsYVFISHD 214
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
328-444 |
3.66e-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: 40.00 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 328 QLSVGYFSQNFDQLDLN---QSILENVTQDSVQSMTLVRNLlaGLGFNidKLDQRISTLSGGERVRLSLAKVLLADHH-- 402
Cdd:TIGR00630 435 ELSIREAHEFFNQLTLTpeeKKIAEEVLKEIRERLGFLIDV--GLDYL--SLSRAAGTLSGGEAQRIRLATQIGSGLTgv 510
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1092676368 403 LLFLDEPTNYL---DLPTLQELEAFLQEYPGTFVLVSHDQQFIKE 444
Cdd:TIGR00630 511 LYVLDEPSIGLhqrDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA 555
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
368-443 |
3.92e-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: 40.00 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 368 GLGFNidKLDQRISTLSGGERVRLSLAKVLL--ADHHLLF-LDEPTNYLDLPTLQELEAFLQEYPG---TFVLVSHDQQF 441
Cdd:TIGR00630 817 GLGYI--RLGQPATTLSGGEAQRIKLAKELSkrSTGRTLYiLDEPTTGLHFDDIKKLLEVLQRLVDkgnTVVVIEHNLDV 894
|
..
gi 1092676368 442 IK 443
Cdd:TIGR00630 895 IK 896
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
73-155 |
3.94e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 39.40 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 73 QAPSPQSGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNCLIQQVKDYPG----AVLMVSHDRDFLDQTVDWIWAIE 148
Cdd:PRK13652 133 RVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMD 212
|
....*..
gi 1092676368 149 QRRLSVY 155
Cdd:PRK13652 213 KGRIVAY 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
374-440 |
4.13e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 38.86 E-value: 4.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 374 DKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDlP--------TLQELEaflQEYpgTFVLVSHD-QQ 440
Cdd:COG1117 146 DRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD-PistakieeLILELK---KDY--TIVIVTHNmQQ 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-133 |
4.30e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 39.03 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 26 VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQG----------------RIDLR---VPVDY-----LPQIQA------- 74
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdvifngqpmsklssaaKAELRnqkLGFIYqfhhlLPDFTAlenvamp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 75 -------------------------------PSPQSGGEATITALQPLFVWPKSLLILDEPTANLDLDHKNC---LIQQV 120
Cdd:PRK11629 112 lligkkkpaeinsralemlaavglehranhrPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSifqLLGEL 191
|
170
....*....|....
gi 1092676368 121 KDYPG-AVLMVSHD 133
Cdd:PRK11629 192 NRLQGtAFLVVTHD 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
73-132 |
4.42e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 39.26 E-value: 4.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 73 QAPSPQSGGE------ATITALQPlfvwpkSLLILDEPTANLDLDHKNCLIQQVKD----YPGAVLMVSH 132
Cdd:PRK13637 140 KSPFELSGGQkrrvaiAGVVAMEP------KILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSH 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-60 |
4.45e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 39.67 E-value: 4.45e-03
10 20
....*....|....*....|....*....
gi 1092676368 32 IGLVGANGSGKSTLLRMIMGMdTDYQGRI 60
Cdd:COG4172 315 LGLVGESGSGKSTLGLALLRL-IPSEGEI 342
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-60 |
4.70e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 38.96 E-value: 4.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092676368 1 MAILELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHgID-LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI 60
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-60 |
4.82e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 38.91 E-value: 4.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092676368 5 ELNHIKKTWQAELIL-EIDrlLVQPQDRI-GLVGANGSGKSTLLRMI---MGMDtdyQGRI 60
Cdd:COG4604 3 EIKNVSKRYGGKVVLdDVS--LTIPKGGItALIGPNGAGKSTLLSMIsrlLPPD---SGEV 58
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
291-504 |
4.94e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 39.07 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 291 FKLQKGDKVGLLGPNKAGKTTFLKGMVSR-------SLPGYYYDQLSV------------------GYFSQNFDQLDL-- 343
Cdd:cd03289 25 FSISPGQRVGLLGRTGSGKSTLLSAFLRLlntegdiQIDGVSWNSVPLqkwrkafgvipqkvfifsGTFRKNLDPYGKws 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 344 NQSILEnvTQDSVQSMTLVRNLLAGLGFnidKLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPTLQELEA 423
Cdd:cd03289 105 DEEIWK--VAEEVGLKSVIEQFPGQLDF---VLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 424 FL-QEYPG-TFVLVSHDQQFIKECV--------NRRYYIKDQQLLNE----QQDTDYSDRsqqtlsLLQFKLQEAISNPE 489
Cdd:cd03289 180 TLkQAFADcTVILSEHRIEAMLECQrflvieenKVRQYDSIQKLLNEkshfKQAISPSDR------LKLFPRRNSSKSKR 253
|
250
....*....|....*
gi 1092676368 490 VSLTEIRQLQDQIQD 504
Cdd:cd03289 254 KPRPQIQALQEETEE 268
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
371-414 |
5.23e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.22 E-value: 5.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1092676368 371 FNID--KLDQRISTLSGGERVRLSLAKVLLADHHLLFLDEPTNYLD 414
Cdd:PRK10762 382 FNIKtpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
364-444 |
5.23e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.39 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 364 NLLAGLGFNIDKLDQRISTLSGGERVRLSLAKVLLADHH--LLFLDEPT-------NYLDLPTLQEleafLQEYPGTFVL 434
Cdd:cd03270 119 GFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSiglhprdNDRLIETLKR----LRDLGNTVLV 194
|
90
....*....|
gi 1092676368 435 VSHDQQFIKE 444
Cdd:cd03270 195 VEHDEDTIRA 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-60 |
5.39e-03 |
|
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: 38.28 E-value: 5.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092676368 4 LELNHIKKTWQAELILE-IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKgID-LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI 57
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
383-438 |
5.47e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.53 E-value: 5.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092676368 383 LSGGERVRLSLAKVLLADHHLLFLDEPTNYLDLPT----LQELEAFLQEYPGTFVLVSHD 438
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHD 200
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-60 |
6.34e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 39.01 E-value: 6.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1092676368 21 IDrLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:COG4615 351 ID-LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
30-61 |
6.35e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 6.35e-03
10 20 30
....*....|....*....|....*....|..
gi 1092676368 30 DRIGLVGANGSGKSTLLRMIMGMDTDYQGRID 61
Cdd:PRK13546 51 DVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-62 |
6.74e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 37.93 E-value: 6.74e-03
10 20
....*....|....*....|....*....
gi 1092676368 34 LVGANGSGKSTLLRMIMGMDTDYQGRIDL 62
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKL 61
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-60 |
7.37e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 37.86 E-value: 7.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1092676368 22 DRLL-------VQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRI 60
Cdd:PRK13538 13 ERILfsglsftLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV 58
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-67 |
7.73e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 38.14 E-value: 7.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092676368 3 ILELNHIKKTWQAELILEIDRLLVQPQDRIGLVGANGSGKSTLLRMIMGMDTDYQGRIDLR-VPVD 67
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgKPVE 66
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
368-410 |
8.16e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 8.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1092676368 368 GLGFnIdKLDQRISTLSGGE--RVRLS--LAKVllADHHLLF-LDEPT 410
Cdd:COG0178 814 GLGY-I-KLGQPATTLSGGEaqRVKLAseLSKR--STGKTLYiLDEPT 857
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
33-52 |
8.58e-03 |
|
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: 38.50 E-value: 8.58e-03
|
| |
