|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-471 |
1.39e-142 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 420.63 E-value: 1.39e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 15 DRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQC--GLLPQ--------------------- 71
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLriGYLPQeppldddltvldtvldgdael 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 ---LKRIDAIKSGGEVTQSYMN------------------------------------------------------ALFS 94
Cdd:COG0488 90 ralEAELEELEAKLAEPDEDLErlaelqeefealggweaearaeeilsglgfpeedldrpvselsggwrrrvalarALLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 95 KaPKLLLADEPTTHLDREHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKEYKGNYSDYLEQKELERRRQ 174
Cdd:COG0488 170 E-PDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRAERLEQE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 175 QSAYEQYEKKKQALERALELKKQKAERATKApkkvsrseanimgakpyfakkqkklqktaKAMETRLEKLEKVEKIKETA 254
Cdd:COG0488 249 AAAYAKQQKKIAKEEEFIRRFRAKARKAKQA-----------------------------QSRIKALEKLEREEPPRRDK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 255 PINMSLPhEDTFQDRIIIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIHR---DDG-IVISPIV 330
Cdd:COG0488 300 TVEIRFP-PPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGElepDSGtVKLGETV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 331 KIGYFSQNLDILEVEKSILENVQSTSKQ-EETLIRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDE 409
Cdd:COG0488 379 KIGYFDQHQEELDPDKTVLDELRDGAPGgTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 410 PTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFDGTYQQYEQH 471
Cdd:COG0488 459 PTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-469 |
5.97e-76 |
|
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: 249.47 E-value: 5.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 10 KHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCR--AQCGLLPQ---------------- 71
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgIKVGYLPQepqldptktvrenvee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 --------LKRIDAIK-------------------------------------------------------SGGEVTQSY 88
Cdd:TIGR03719 92 gvaeikdaLDRFNEISakyaepdadfdklaaeqaelqeiidaadawdldsqleiamdalrcppwdadvtklSGGERRRVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 89 MNALFSKAPKLLLADEPTTHLDREHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKEYKGNYSDYLEQKE 168
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 169 lERRRQQSAYEqyEKKKQALERALELKKQKAeratkapkkvsrseanimgakpyfakkqKKLQKTAKAMETRLEKLEKVE 248
Cdd:TIGR03719 252 -KRLEQEEKEE--SARQKTLKRELEWVRQSP----------------------------KGRQAKSKARLARYEELLSQE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 249 KIKETAPINMSLPHEDTFQDrIIIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIHR---DDG-I 324
Cdd:TIGR03719 301 FQKRNETAEIYIPPGPRLGD-KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeqpDSGtI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 325 VISPIVKIGYFSQNLDILEVEKSILENVqsTSKQEETLI-------RTILARLHFFRDDVYKPVEILSGGERVKVALAKL 397
Cdd:TIGR03719 380 EIGETVKLAYVDQSRDALDPNKTVWEEI--SGGLDIIKLgkreipsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKT 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 398 FVSDVNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQ-DKVIQWFDGTYQQYE 469
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYE 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
91-468 |
6.11e-75 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 246.34 E-value: 6.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 91 ALFSKaPKLLLADEPTTHLDREHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKEYKGNYSDYLEQKELE 170
Cdd:PRK15064 169 ALFSN-PDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 171 RRRQQSAYEqyeKKKqalERALELKKqkaeratkapkKVSRSEANimgakpyfAKKQKklQKTAKAmeTRLEKLeKVEKI 250
Cdd:PRK15064 248 RERLLADNA---KKK---AQIAELQS-----------FVSRFSAN--------ASKAK--QATSRA--KQIDKI-KLEEV 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 251 KETAPINMSLPHEdtfQD----RIIIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIHR---DDG 323
Cdd:PRK15064 298 KPSSRQNPFIRFE---QDkklhRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGElepDSG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 324 IV-ISPIVKIGYFSQ-NLDILEVEKSILE--NVQSTSKQEETLIRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFV 399
Cdd:PRK15064 375 TVkWSENANIGYYAQdHAYDFENDLTLFDwmSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890659908 400 SDVNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFDGTYQQY 468
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-469 |
5.02e-70 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 233.86 E-value: 5.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 32 IGLVGKNGSGKTTLLNILAKKISPEQGSVlcRAQ----CGLLPQ------------------------LKRIDAIK---- 79
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEA--RPApgikVGYLPQepqldpektvrenveegvaevkaaLDRFNEIYaaya 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 80 ---------------------------------------------------SGGEVTQSYMNALFSKAPKLLLADEPTTH 108
Cdd:PRK11819 114 epdadfdalaaeqgelqeiidaadawdldsqleiamdalrcppwdakvtklSGGERRRVALCRLLLEKPDMLLLDEPTNH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 109 LDREHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKEYKGNYSDYLEQKElERRRQQSAYEqyEKKKQAL 188
Cdd:PRK11819 194 LDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKA-KRLAQEEKQE--AARQKAL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 189 ERALELKKQKAeratKApkkvsrseanimgakpyfakKQKKlqktAKAMETRLEKL--EKVEKIKETAPINMSLPhedtf 266
Cdd:PRK11819 271 KRELEWVRQSP----KA--------------------RQAK----SKARLARYEELlsEEYQKRNETNEIFIPPG----- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 267 qDR---IIIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMI----HRDDG-IVISPIVKIGYFSQN 338
Cdd:PRK11819 318 -PRlgdKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFK-MItgqeQPDSGtIKIGETVKLAYVDQS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 339 LDILEVEKSILENVqstSKQEETLI--------RTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEP 410
Cdd:PRK11819 396 RDALDPNKTVWEEI---SGGLDIIKvgnreipsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 411 TNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQ-DKVIQWFDGTYQQYE 469
Cdd:PRK11819 473 TNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEYE 532
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-526 |
1.60e-66 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 226.76 E-value: 1.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKIS---------------------P--EQGSV-------------------- 60
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLlddgriiyeqdlivarlqqdpPrnVEGTVydfvaegieeqaeylkryhd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 61 ----------------LCRAQCGL---------------LPQLKrIDAIK-----SGGEVTQSYM-NALFSkAPKLLLAD 103
Cdd:PRK11147 104 ishlvetdpseknlneLAKLQEQLdhhnlwqlenrinevLAQLG-LDPDAalsslSGGWLRKAALgRALVS-NPDVLLLD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 104 EPTTHLDREHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKEYKGNYSDYLEQKELERRRQQSAYEQYEK 183
Cdd:PRK11147 182 EPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVEELQNAEFDR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 184 KkQALERALELKKQKAERatkapkkvSRSEANImgakpyfakkqkklqKTAKAMetRLEKLEKVEkIKETAPINMSlphE 263
Cdd:PRK11147 262 K-LAQEEVWIRQGIKARR--------TRNEGRV---------------RALKAL--RRERSERRE-VMGTAKMQVE---E 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 264 DTFQDRIIIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIHR---DDGIV-ISPIVKIGYFSQNL 339
Cdd:PRK11147 312 ASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQlqaDSGRIhCGTKLEVAYFDQHR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 340 DILEVEKSILENVqSTSKQEETL---IRTILARLHFF-----RddVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPT 411
Cdd:PRK11147 392 AELDPEKTVMDNL-AEGKQEVMVngrPRHVLGYLQDFlfhpkR--AMTPVKALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 412 NFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQ-DKVIQWFDGTYQQYEQHVRQKDRHADTQADQRLLLE 490
Cdd:PRK11147 469 NDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAA 548
|
570 580 590
....*....|....*....|....*....|....*.
gi 1890659908 491 TKMSEVLSRLSMEPSEELEKEFQLLLEKKRKLDKGI 526
Cdd:PRK11147 549 APKAETVKRSSKKLSYKLQRELEQLPQLLEDLEAEI 584
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
274-486 |
3.66e-51 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 182.57 E-value: 3.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 274 VEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDG-IVISPIVKIGYFSQNLDILEvEKSIL 349
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKilaGELEPDSGeVSIPKGLRIGYLPQEPPLDD-DLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 350 ENV------------------QSTSKQEETL---------------------IRTILARLHFFRDDVYKPVEILSGGERV 390
Cdd:COG0488 80 DTVldgdaelraleaeleeleAKLAEPDEDLerlaelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 391 KVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFDGTYQQYEQ 470
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
250
....*....|....*.
gi 1890659908 471 HvRQKDRHADTQADQR 486
Cdd:COG0488 240 Q-RAERLEQEAAAYAK 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-152 |
1.66e-48 |
|
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: 164.16 E-value: 1.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQC--GLLPQLkridaikSG 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVkiGYFEQL-------SG 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890659908 82 GEVTQSYMNALFSKAPKLLLADEPTTHLDREHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGK 152
Cdd:cd03221 74 GEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-485 |
1.97e-48 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 177.28 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 1 MILLEALNVKHYVkdRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQCGL-----------L 69
Cdd:PRK10636 1 MIVFSSLQIRRGV--RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLawvnqetpalpQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 70 PQLK---------------------------------RIDAIK-----------------------------SGG-EVTQ 86
Cdd:PRK10636 79 PALEyvidgdreyrqleaqlhdanerndghaiatihgKLDAIDawtirsraasllhglgfsneqlerpvsdfSGGwRMRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 87 SYMNALFSKApKLLLADEPTTHLDREHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKEYKGNYSDYLEQ 166
Cdd:PRK10636 159 NLAQALICRS-DLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 167 KELERRRQQSAYEQYEKKKQALERALELKKQKAERATKApkkvsrseanimgakpyfakkqkklqktakamETRLEKLEK 246
Cdd:PRK10636 238 RATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQA--------------------------------QSRIKMLER 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 247 VEKIketAPINMSLPHEDTFQD-----RIIIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK----KM 317
Cdd:PRK10636 286 MELI---APAHVDNPFHFSFRApeslpNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKllagEL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 318 IHRDDGIVISPIVKIGYFSQN-LDILEVEKSILENVQSTSKQE-ETLIRTILARLHFFRDDVYKPVEILSGGERVKVALA 395
Cdd:PRK10636 363 APVSGEIGLAKGIKLGYFAQHqLEFLRADESPLQHLARLAPQElEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 396 KLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFDGTYQQYEQHV--- 472
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLsdv 522
|
570
....*....|....
gi 1890659908 473 -RQKDRHADTQADQ 485
Cdd:PRK10636 523 qKQENQTDEAPKEN 536
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
272-456 |
3.78e-47 |
|
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: 160.69 E-value: 3.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIHR---DDGIVI-SPIVKIGYFSQnldileveks 347
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGElepDEGIVTwGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 348 ilenvqstskqeetlirtilarlhffrddvykpveiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQ 427
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180
....*....|....*....|....*....
gi 1890659908 428 EYKGTVIFASHDRRFIENVATKMLVIQDK 456
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
71-473 |
6.05e-41 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 156.94 E-value: 6.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 71 QLKRIDAIKSGGEVTQSYMNALFSKaPKLLLADEPTTHLDREHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDE 150
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIE-PDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 151 GKIKEYKGNYSDYLEQKELERRRQQSAYEQYEKKKQALERALELKKQKAERATKapkkvsrseanimgakpyfakkqkkL 230
Cdd:PLN03073 417 QKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASL-------------------------V 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 231 QKTAKAmetrLEKLEKVEKIKETAPINMSLPHEDTFQDRIIIRVEEVT-GVIGQRVLWEKTSFHVRGGDKLAVIGPNGSG 309
Cdd:PLN03073 472 QSRIKA----LDRLGHVDAVVNDPDYKFEFPTPDDRPGPPIISFSDASfGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIG 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 310 KTTLLKKM---IHRDDGIVI-SPIVKIGYFSQN-LDILEVEKS-ILENVQSTSKQEETLIRTILARLHFFRDDVYKPVEI 383
Cdd:PLN03073 548 KSTILKLIsgeLQPSSGTVFrSAKVRMAVFSQHhVDGLDLSSNpLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYT 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 384 LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFDG 463
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHG 707
|
410
....*....|
gi 1890659908 464 TYQQYEQHVR 473
Cdd:PLN03073 708 TFHDYKKTLQ 717
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-166 |
2.51e-37 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 144.44 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 2 ILLEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSV--------------------- 60
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgetvkigyfdqhqeeldpd 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 61 ------LCRA-------------QCGLLP---QLKRIDAIkSGGEVTQSYMNALFSKAPKLLLADEPTTHLDREHIEWLE 118
Cdd:COG0488 394 ktvldeLRDGapggteqevrgylGRFLFSgddAFKPVGVL-SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1890659908 119 KKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKEYKGNYSDYLEQ 166
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
272-448 |
4.31e-28 |
|
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: 111.03 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVI---SPIVK--------IGYFSQ 337
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILaglLPPSAGEVLwngEPIRDaredyrrrLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 338 NLDILEvEKSILENVQSTSK-----QEETLIRTILAR--LHFFRDdvyKPVEILSGGERVKVALAKLFVSDVNTLILDEP 410
Cdd:COG4133 83 ADGLKP-ELTVRENLRFWAAlyglrADREAIDEALEAvgLAGLAD---LPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1890659908 411 TNFLDIEAARALESLLQEYK---GTVIFASHDRRFIENVAT 448
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAARV 199
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
271-460 |
1.07e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 111.33 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM----------IHRDDGIVISPIVKIGYFSQNLD 340
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlgllpptsgtVRLFGKPPRRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 341 I--------LEV-------EKSILenvQSTSKQEETLIRTILARLHF--FRDdvyKPVEILSGGERVKVALAKLFVSDVN 403
Cdd:COG1121 86 VdwdfpitvRDVvlmgrygRRGLF---RRPSRADREAVDEALERVGLedLAD---RPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 404 TLILDEPTNFLDIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQDKVIQW 460
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
272-476 |
7.62e-27 |
|
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: 108.79 E-value: 7.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK-----------KMIHRDDGIVISPIV---KIGYFSQ 337
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRmlagllkpdsgSILIDGEDVRKEPREarrQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 338 NlDILEVEKSILENVQSTSKQEETLIRTILAR----LHFFRDDVY--KPVEILSGGERVKVALAKLFVSDVNTLILDEPT 411
Cdd:COG4555 82 E-RGLYDRLTVRENIRYFAELYGLFDEELKKRieelIELLGLEEFldRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 412 NFLDIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQDKVIQwFDGTYQQYEQHVRQKD 476
Cdd:COG4555 161 NGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKVV-AQGSLDELREEIGEEN 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-152 |
3.51e-26 |
|
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: 104.25 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 8 NVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL-------------CRAQCGLLPQLkr 74
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILidgkdiaklpleeLRRRIGYVPQL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 75 idaikSGGEVTQSYMNALFSKAPKLLLADEPTTHLDREHIEWLE---KKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEG 151
Cdd:cd00267 82 -----SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLellRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
.
gi 1890659908 152 K 152
Cdd:cd00267 157 K 157
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-170 |
1.67e-25 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 109.98 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC--RAQCGLLPQ---------- 71
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWseNANIGYYAQdhaydfendl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 ----------------------LKRI----DAIK------SGGEvtQSYMnaLFSK----APKLLLADEPTTHLDREHIE 115
Cdd:PRK15064 400 tlfdwmsqwrqegddeqavrgtLGRLlfsqDDIKksvkvlSGGE--KGRM--LFGKlmmqKPNVLVMDEPTNHMDMESIE 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 116 WLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKEYKGNYSDYLEQKELE 170
Cdd:PRK15064 476 SLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGIE 530
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
297-447 |
9.96e-25 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 107.90 E-value: 9.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 297 GDKLAVIGPNGSGKTTLLKKMIHRDDGI----VISPIVKIGYFSQNLDiLEVEKSILENVqstskqEETL--IRTILARL 370
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFegeaRPAPGIKVGYLPQEPQ-LDPEKTVRENV------EEGVaeVKAALDRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 371 hffrDDVY-------------------------------------------------KPVEILSGGERVKVALAKLFVSD 401
Cdd:PRK11819 106 ----NEIYaayaepdadfdalaaeqgelqeiidaadawdldsqleiamdalrcppwdAKVTKLSGGERRRVALCRLLLEK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1890659908 402 VNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVA 447
Cdd:PRK11819 182 PDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVA 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
273-455 |
8.61e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 97.70 E-value: 8.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 273 RVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIhrddGIVISPIVKIgyfsqnldileveksILENV 352
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA----GLLKPTSGEI---------------LIDGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 QSTSKQEETLIRTILARLHffrddvykpveiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKG- 431
Cdd:cd00267 62 DIAKLPLEELRRRIGYVPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEe 129
|
170 180
....*....|....*....|....*.
gi 1890659908 432 --TVIFASHDRRFIENVATKMLVIQD 455
Cdd:cd00267 130 grTVIIVTHDPELAELAADRVIVLKD 155
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-265 |
1.06e-23 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 105.03 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 2 ILLEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC------------RA----- 64
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtklevayfdqhRAeldpe 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 65 ---------------------------QCGLLPQLKRIDAIK--SGGEVTQSYMNALFSKAPKLLLADEPTTHLDREHIE 115
Cdd:PRK11147 398 ktvmdnlaegkqevmvngrprhvlgylQDFLFHPKRAMTPVKalSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 116 WLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMD-EGKIKEYKGNYSDyleqkeleRRRQQSAYeqYEKKKQALERALEL 194
Cdd:PRK11147 478 LLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYVGGYHD--------ARQQQAQY--LALKQPAVKKKEEA 547
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 195 KKQKAERATKAPKKVSrseanimgakpYfakkqkKLQKTAKAMETRLEKLE-KVEKIKET--APINMSLPHEDT 265
Cdd:PRK11147 548 AAPKAETVKRSSKKLS-----------Y------KLQRELEQLPQLLEDLEaEIEALQAQvaDADFFSQPHEQT 604
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
291-455 |
2.03e-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: 98.31 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM----------IHRDDGIVISPIV-----KIGYFSQNLD--ILE--VEKSI--- 348
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLngllgptsgeVLVDGKDLTKLSLkelrrKVGLVFQNPDdqFFGptVEEEVafg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 LENVQSTSKQEETLIRTILARLHF--FRDdvyKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLL 426
Cdd:cd03225 101 LENLGLPEEEIEERVEEALELVGLegLRD---RSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELL 177
|
170 180 190
....*....|....*....|....*....|..
gi 1890659908 427 QEYKG---TVIFASHDRRFIENVATKMLVIQD 455
Cdd:cd03225 178 KKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
271-439 |
2.09e-23 |
|
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: 99.35 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIV---------ISPIV---KIGYF 335
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRalaGLLKPSSGEVlldgrdlasLSRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 336 SQNLDI---LEVEKSIL-------ENVQSTSKQEETLIRTILARLH--FFRDdvyKPVEILSGGERVKVALAKLFVSDVN 403
Cdd:COG1120 81 PQEPPApfgLTVRELVAlgryphlGLFGRPSAEDREAVEEALERTGleHLAD---RPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1890659908 404 TLILDEPTNFLDI----EAARALESLLQEYKGTVIFASHD 439
Cdd:COG1120 158 LLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
272-455 |
2.56e-23 |
|
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: 96.70 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVI---SPIVK--------IGYFSQ 337
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlglLKPDSGEIKvlgKDIKKepeevkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 338 NLDILEvEKSILENVQstskqeetlirtilarlhffrddvykpveiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIE 417
Cdd:cd03230 81 EPSLYE-NLTVRENLK------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1890659908 418 AARALESLLQEYK---GTVIFASHDRRFIENVATKMLVIQD 455
Cdd:cd03230 130 SRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNN 170
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
286-468 |
3.61e-23 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 103.49 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 286 LWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDG-IVISPIVKIGYFSQN----------------------- 338
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKilnGEVLLDDGrIIYEQDLIVARLQQDpprnvegtvydfvaegieeqaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 339 -------LDILEVEKS-----ILENVQSTSK-----QEETLIRTILARLHFfrdDVYKPVEILSGGERVKVALAKLFVSD 401
Cdd:PRK11147 98 lkryhdiSHLVETDPSeknlnELAKLQEQLDhhnlwQLENRINEVLAQLGL---DPDAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890659908 402 VNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKmlvIQD----KVIQWfDGTYQQY 468
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATR---IVDldrgKLVSY-PGNYDQY 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
272-464 |
3.93e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 98.21 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMI----HRDDGIVI---------SPIVK--IGYFS 336
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIR-MLlgllRPTSGEVRvlgedvardPAEVRrrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 337 QNLDILEvEKSILENVQSTS-------KQEETLIRTILARLHFfRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDE 409
Cdd:COG1131 80 QEPALYP-DLTVRENLRFFArlyglprKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1890659908 410 PTNFLDIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQD-KVIqwFDGT 464
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKgRIV--ADGT 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
272-464 |
7.05e-23 |
|
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: 97.02 E-value: 7.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVT-GVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVI---SPIV---------KIGY- 334
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLnglLKPTSGEVLvdgKDITkknlrelrrKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 335 FsQNLDILEVEKSILENV------QSTSKQE-ETLIRTILARLHF--FRDdvyKPVEILSGGERVKVALAKLFVSDVNTL 405
Cdd:COG1122 81 F-QNPDDQLFAPTVEEDVafgpenLGLPREEiRERVEEALELVGLehLAD---RPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 406 ILDEPTNFLDIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQD-KVIqwFDGT 464
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDgRIV--ADGT 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
273-460 |
7.06e-23 |
|
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: 96.83 E-value: 7.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 273 RVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVI---SPIVK----IGYFSQNLDIL 342
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlglLKPTSGSIRvfgKPLEKerkrIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 343 -EVEKSILENV-----------QSTSKQEETLIRTILAR--LHFFRDdvyKPVEILSGGERVKVALAKLFVSDVNTLILD 408
Cdd:cd03235 81 rDFPISVRDVVlmglyghkglfRRLSKADKAKVDEALERvgLSELAD---RQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 409 EPTNFLDIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQDKVIQW 460
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
273-458 |
3.41e-21 |
|
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: 90.96 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 273 RVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIV---------ISPIV---KIGYFSQ 337
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKtlaGLLKPSSGEIlldgkdlasLSPKElarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 338 NLDILEVEKsilenvqstskqeetlirtilarlhfFRDdvyKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIE 417
Cdd:cd03214 81 ALELLGLAH--------------------------LAD---RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1890659908 418 AARALESLLQEYKG----TVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:cd03214 132 HQIELLELLRRLARergkTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
272-455 |
5.09e-21 |
|
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: 90.32 E-value: 5.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMIhrdDGIVISPIVKIGYFSQNLDILEVEKSILEN 351
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLR-CI---AGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 VQSTSKQEETLirtilarlhFFRDDVYKPVEI-LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLL---- 426
Cdd:cd03229 77 RIGMVFQDFAL---------FPHLTVLENIALgLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLkslq 147
|
170 180
....*....|....*....|....*....
gi 1890659908 427 QEYKGTVIFASHDRRFIENVATKMLVIQD 455
Cdd:cd03229 148 AQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
272-460 |
1.61e-20 |
|
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: 89.97 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVispIVKIGYFSQNLDILEVEKSI 348
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIlglIKPDSGEI---TFDGKSYQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 L------------ENVQSTSKQ---EETLIRTILARLHfFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNF 413
Cdd:cd03268 78 IeapgfypnltarENLRLLARLlgiRKKRIDEVLDVVG-LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1890659908 414 LD---IEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQW 460
Cdd:cd03268 157 LDpdgIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
272-458 |
7.44e-20 |
|
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: 86.89 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIG--QRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIH---------RDDGIVISPI------VKIGY 334
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGllrptsgrvRLDGADISQWdpnelgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 335 FSQnlDILEVEKSILENvqstskqeetlirtilarlhffrddvykpveILSGGERVKVALAKLFVSDVNTLILDEPTNFL 414
Cdd:cd03246 81 LPQ--DDELFSGSIAEN-------------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1890659908 415 DIEAARALESLLQEYK---GTVIFASHDRRFIEnVATKMLVIQDKVI 458
Cdd:cd03246 128 DVEGERALNQAIAALKaagATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-455 |
1.26e-19 |
|
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: 91.89 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPE---QGSV-------------LCRAQCGLLPQ--LKRIDAIKSGGEVT 85
Cdd:COG1123 27 LTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVlldgrdllelseaLRGRRIGMVFQdpMTQLNPVTVGDQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 86 QSYMNALFSKA-------------------------------------------PKLLLADEPTTHLD---REHIEWLEK 119
Cdd:COG1123 107 EALENLGLSRAeararvlelleavglerrldryphqlsggqrqrvaiamalaldPDLLIADEPTTALDvttQAEILDLLR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 120 KLSQWKG-AFVIVSHDRAFLDALCTTIWEMDEGKIKEykgnysdyleqkelerrrqQSAYEQYEKKKQALEralelkkqk 198
Cdd:COG1123 187 ELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVE-------------------DGPPEEILAAPQALA--------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 199 aeratkapkkvsrseanimgAKPYFAKKQKKLQKTAKAMETRLEkLEKVEKiketapinmslphedTFQDRIIIRVEEVT 278
Cdd:COG1123 239 --------------------AVPRLGAARGRAAPAAAAAEPLLE-VRNLSK---------------RYPVRGKGGVRAVD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 279 GVigqrvlwektSFHVRGGDKLAVIGPNGSGKTTLLKKMIH---------RDDGIVISPIV---------KIGYFSQN-- 338
Cdd:COG1123 283 DV----------SLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsiLFDGKDLTKLSrrslrelrrRVQMVFQDpy 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 339 --LD-ILEVEKSI---LENVQSTSKQE-ETLIRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPT 411
Cdd:COG1123 353 ssLNpRMTVGDIIaepLRLHGLLSRAErRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPT 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1890659908 412 NFLDIeAARA-----LESLLQEYKGTVIFASHDRRFIENVATKMLVIQD 455
Cdd:COG1123 433 SALDV-SVQAqilnlLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
241-467 |
5.17e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 90.66 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 241 LEKLEKVEKIKETAPINMSLPHEDTFQDRIiiRVEEVT---GVIGQRVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLK-- 315
Cdd:COG2274 445 LERLDDILDLPPEREEGRSKLSLPRLKGDI--ELENVSfryPGDSPPVL-DNISLTIKPGERVAIVGRSGSGKSTLLKll 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 316 -KMIHRDDGIV---------ISPIV---KIGYFSQNLDILevEKSILENVQSTSKQ--EETLIRTI-LARLHffrDDVYK 379
Cdd:COG2274 522 lGLYEPTSGRIlidgidlrqIDPASlrrQIGVVLQDVFLF--SGTIRENITLGDPDatDEEIIEAArLAGLH---DFIEA 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 380 -------PV----EILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKG--TVIFASHDRRFIENv 446
Cdd:COG2274 597 lpmgydtVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL- 675
|
250 260
....*....|....*....|..
gi 1890659908 447 ATKMLVIQD-KVIQwfDGTYQQ 467
Cdd:COG2274 676 ADRIIVLDKgRIVE--DGTHEE 695
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-173 |
7.53e-19 |
|
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: 89.61 E-value: 7.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 2 ILLEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGS---------------------- 59
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTieigetvklayvdqsrdaldpn 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 60 --------------------VLCRAQCGLL-----PQLKRIDAIkSGGEVTQSYMNALFSKAPKLLLADEPTTHLDREHI 114
Cdd:TIGR03719 401 ktvweeisggldiiklgkreIPSRAYVGRFnfkgsDQQKKVGQL-SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890659908 115 EWLEKKLSQWKGAFVIVSHDRAFLDALCTTI--WEmDEGKIKEYKGNYSDYLEQKeleRRR 173
Cdd:TIGR03719 480 RALEEALLNFAGCAVVISHDRWFLDRIATHIlaFE-GDSHVEWFEGNFSEYEEDK---KRR 536
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
291-412 |
2.27e-18 |
|
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: 81.93 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM----------IHRDDGIVISPIVK-----IGYFSQNlDILEVEKSILENV--- 352
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIagllsptegtILLDGQDLTDDERKslrkeIGYVFQD-PQLFPRLTVRENLrlg 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890659908 353 ------QSTSKQEEtlIRTILARL--HFFRDD-VYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTN 412
Cdd:pfam00005 84 lllkglSKREKDAR--AEEALEKLglGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
291-455 |
2.49e-18 |
|
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: 82.43 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHRD----------DGIVISPIV------KIGYFSQNLDILEveKSILENvqs 354
Cdd:cd03228 22 SLTIKPGEKVAIVGPSGSGKSTLLK-LLLRLydptsgeiliDGVDLRDLDleslrkNIAYVPQDPFLFS--GTIREN--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 355 tskqeetlirtilarlhffrddvykpveILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKG--T 432
Cdd:cd03228 96 ----------------------------ILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkT 147
|
170 180
....*....|....*....|...
gi 1890659908 433 VIFASHDRRFIENvATKMLVIQD 455
Cdd:cd03228 148 VIVIAHRLSTIRD-ADRIIVLDD 169
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
282-438 |
2.74e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.31 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 282 GQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVI---SPIVKIG--YFSQNLDI-----LEVEKSI 348
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRilaGLARPDAGEVLwqgEPIRRQRdeYHQDLLYLghqpgIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 LENVQSTSK----QEETLIRTILAR--LHFFrDDVykPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARAL 422
Cdd:PRK13538 92 LENLRFYQRlhgpGDDEALWEALAQvgLAGF-EDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
170
....*....|....*....
gi 1890659908 423 ESLLQEY---KGTVIFASH 438
Cdd:PRK13538 169 EALLAQHaeqGGMVILTTH 187
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-241 |
2.88e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 87.92 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 15 DRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSV-----------------LCRAQCGLLPQLKRI-- 75
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgyfaqhqleFLRADESPLQHLARLap 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 76 ------------------DAIK------SGGEVTQSYMNALFSKAPKLLLADEPTTHLDREHIEWLEKKLSQWKGAFVIV 131
Cdd:PRK10636 404 qeleqklrdylggfgfqgDKVTeetrrfSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVV 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 132 SHDRAFLDALCTTIWEMDEGKIKEYKGNYSDYlEQKELERRRQQSAYEQYEKKKQALErALELKKQK---AE-RATKAP- 206
Cdd:PRK10636 484 SHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY-QQWLSDVQKQENQTDEAPKENNANS-AQARKDQKrreAElRTQTQPl 561
|
250 260 270
....*....|....*....|....*....|....*.
gi 1890659908 207 -KKVSRSEanimgakpyfaKKQKKLQKTAKAMETRL 241
Cdd:PRK10636 562 rKEIARLE-----------KEMEKLNAQLAQAEEKL 586
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
291-458 |
3.26e-18 |
|
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: 83.31 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIH----------RDDGIVISPIV----------KIGYFSQNLDILEvEKSILE 350
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLN-ILGgldrptsgevRVDGTDISKLSekelaafrrrHIGFVFQSFNLLP-DLTALE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 351 NV-------QSTSKQEETLIRTILARLHFfRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALE 423
Cdd:cd03255 102 NVelplllaGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVM 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1890659908 424 SLLQE----YKGTVIFASHDRRfIENVATKMLVIQDKVI 458
Cdd:cd03255 181 ELLRElnkeAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
267-467 |
3.76e-18 |
|
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: 83.88 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 267 QDRIIIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMI---HRDDGIVIspivkigYFSQNL---- 339
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIgllRPDSGEIL-------VDGQDItgls 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 340 --DILEVEK---------------SILENV-----QSTSKQEETLIRTILARLHFF--RDDVYK-PVEiLSGGERVKVAL 394
Cdd:COG1127 74 ekELYELRRrigmlfqggalfdslTVFENVafplrEHTDLSEAEIRELVLEKLELVglPGAADKmPSE-LSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890659908 395 AKLFVSDVNTLILDEPTNFLDIEAARALESLL----QEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWfDGTYQQ 467
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA-EGTPEE 228
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
282-508 |
5.08e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 87.15 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 282 GQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLL---KKMIHRDDGIVISPIV-KIGYFSQNLDILEVekSILENV----- 352
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLallKNEISADGGSYTFPGNwQLAWVNQETPALPQ--PALEYVidgdr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 ----------QSTSKQEETLIRTI-------------------LARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVN 403
Cdd:PRK10636 90 eyrqleaqlhDANERNDGHAIATIhgkldaidawtirsraaslLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 404 TLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFDGTYQQYE-------------- 469
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEvqratrlaqqqamy 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 1890659908 470 QHVRQKDRHADTQADQRLLLETKMSEVLSRLSMEPSEEL 508
Cdd:PRK10636 250 ESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL 288
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
291-445 |
5.63e-18 |
|
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: 86.96 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIH---------RDDGIVISPIV------KIGYFSQNLDIleVEKSILENVQ-S 354
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGfvdptegsiAVNGVPLADADadswrdQIAWVPQHPFL--FAGTIAENIRlA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 355 TSKQEETLIRTILAR--LHFFRDDVYKPVEI--------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIE-AARALE 423
Cdd:TIGR02857 420 RPDASDAEIREALERagLDEFVAALPQGLDTpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAEtEAEVLE 499
|
170 180
....*....|....*....|...
gi 1890659908 424 SLLQEYKG-TVIFASHDRRFIEN 445
Cdd:TIGR02857 500 ALRALAQGrTVLLVTHRLALAAL 522
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
24-153 |
1.25e-17 |
|
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: 80.56 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL------------CRAQ-CGLLPQ-LKRIDAIK---------S 80
Cdd:cd03214 20 LSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlaslspkELARkIAYVPQaLELLGLAHladrpfnelS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 81 GGEvTQSymnALFSKA----PKLLLADEPTTHLDREH-IEWLE--KKLSQWKGAFVI-VSHD--RAFLdaLCTTIWEMDE 150
Cdd:cd03214 100 GGE-RQR---VLLARAlaqePPILLLDEPTSHLDIAHqIELLEllRRLARERGKTVVmVLHDlnLAAR--YADRVILLKD 173
|
...
gi 1890659908 151 GKI 153
Cdd:cd03214 174 GRI 176
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
291-455 |
1.38e-17 |
|
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: 81.48 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIH---------RDDGIVIS---PIV---KIGYFSQnlDILEVEKSILENVQS- 354
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGlykptsgsvLLDGTDIRqldPADlrrNIGYVPQ--DVTLFYGTLRDNITLg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 355 -TSKQEETLIRTI-LARLHFFRDDVYKPVEI--------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALES 424
Cdd:cd03245 102 aPLADDERILRAAeLAGVTDFVNKHPNGLDLqigergrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKE 181
|
170 180 190
....*....|....*....|....*....|...
gi 1890659908 425 LLQEYKG--TVIFASHDRRFIEnVATKMLVIQD 455
Cdd:cd03245 182 RLRQLLGdkTLIIITHRPSLLD-LVDRIIVMDS 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
272-462 |
1.50e-17 |
|
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: 81.41 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLkKMIHR----DDG-IVIS-------PIVK--IGYFSQ 337
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLL-RLIAGlerpDSGeILIDgrdvtgvPPERrnIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 338 NlDILEVEKSILENVQ-------STSKQEETLIRTILARLHfFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEP 410
Cdd:cd03259 80 D-YALFPHLTVAENIAfglklrgVPKAEIRARVRELLELVG-LEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1890659908 411 TNFLDIEAARALESLLQEY----KGTVIFASHDRRFIENVATKMLVIQDKVIQWFD 462
Cdd:cd03259 158 LSALDAKLREELREELKELqrelGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
274-438 |
1.55e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.87 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 274 VEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVI-----------SPIVKIGYFSqNL 339
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRilaGLLRPDSGEVRwngtplaeqrdEPHENILYLG-HL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 340 DILEVEKSILENVQ---STSKQEETLIRTILARLHfFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDI 416
Cdd:TIGR01189 82 PGLKPELSALENLHfwaAIHGGAQRTIEDALAAVG-LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*
gi 1890659908 417 EAARALESLLQEY---KGTVIFASH 438
Cdd:TIGR01189 161 AGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
274-438 |
1.99e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 274 VEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK-----------KMIHRDDGI----VISPIVKIGYfsqn 338
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRliagllppaagTIKLDGGDIddpdVAEACHYLGH---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 339 LDILEVEKSILENVQSTSK---QEETLIRTILARLHFfrDDV-YKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFL 414
Cdd:PRK13539 81 RNAMKPALTVAENLEFWAAflgGEELDIAAALEAVGL--APLaHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 1890659908 415 DIEAARALESLLQEYK---GTVIFASH 438
Cdd:PRK13539 159 DAAAVALFAELIRAHLaqgGIVIAATH 185
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
272-474 |
2.14e-17 |
|
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: 81.39 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVI---------SPI------VKIG 333
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIvglLRPDSGEVLidgedisglSEAelyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 334 Y-FSQN--LDILevekSILENV-----QSTSKQEETLIRTILARLHFF--RDDVYK-PVEiLSGGERVKVALAKLFVSDV 402
Cdd:cd03261 81 MlFQSGalFDSL----TVFENVafplrEHTRLSEEEIREIVLEKLEAVglRGAEDLyPAE-LSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 403 NTLILDEPTNFLDIEAARALESLL----QEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFdGTYQQYEQH----VRQ 474
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE-GTPEELRASddplVRQ 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
291-458 |
2.19e-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: 80.76 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVIS---------PIVKIGYFSQNLDILEVEKSILENVQSTSKQ 358
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKilaGLIKESSGSILLngkpikakeRRKSIGYVMQDVDYQLFTDSVREELLLGLKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 359 ---EETLIRTILARLhffrdDVYKPVE----ILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESL---LQE 428
Cdd:cd03226 100 ldaGNEQAETVLKDL-----DLYALKErhplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELireLAA 174
|
170 180 190
....*....|....*....|....*....|
gi 1890659908 429 YKGTVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:cd03226 175 QGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
271-455 |
2.63e-17 |
|
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: 81.01 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVIGQRVLWEKT----SFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVI---SPIVK--------- 331
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARailGLLKPTSGSIIfdgKDLLKlsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 332 ---IGYFSQN----LD-ILEVEKSILE---NVQSTSKQEETLIRTILARLHFFRDDVY---KPVEiLSGGERVKVALAKL 397
Cdd:cd03257 81 rkeIQMVFQDpmssLNpRMTIGEQIAEplrIHGKLSKKEARKEAVLLLLVGVGLPEEVlnrYPHE-LSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 398 FVSDVNTLILDEPTNFLDIEAARALESLL----QEYKGTVIFASHDRRFIENVATKMLVIQD 455
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLkklqEELGLTLLFITHDLGVVAKIADRVAVMYA 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-153 |
3.21e-17 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 79.36 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNV-KHYVKDRLLFEIErLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL------------CRAQCGLLP 70
Cdd:cd03230 1 IEVRNLsKRYGKKTALDDIS-LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdikkepeeVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 71 Q-------LKRIDAIK-SGGevtqsyMN-------ALFSKaPKLLLADEPTTHLDREHIEWLE---KKLSQWKGAFVIVS 132
Cdd:cd03230 80 EepslyenLTVRENLKlSGG------MKqrlalaqALLHD-PELLILDEPTSGLDPESRREFWellRELKKEGKTILLSS 152
|
170 180
....*....|....*....|.
gi 1890659908 133 HDRAFLDALCTTIWEMDEGKI 153
Cdd:cd03230 153 HILEEAERLCDRVAILNNGRI 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
291-485 |
4.22e-17 |
|
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: 84.43 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHRD----------DGIVISPIV------KIGYFSQNLDILEveKSILENV-- 352
Cdd:COG4987 355 SLTLPPGERVAIVGPSGSGKSTLLA-LLLRFldpqsgsitlGGVDLRDLDeddlrrRIAVVPQRPHLFD--TTLRENLrl 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 ---QSTskqEETLIRTI-LARLHFFRDDVYK----PV----EILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR 420
Cdd:COG4987 432 arpDAT---DEELWAALeRVGLGDWLAALPDgldtWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQ 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890659908 421 A-LESLLQEYKG-TVIFASHDRRFIENVatkmlviqDKVIQWFDGtyqqyeqHVRQKDRHADTQADQ 485
Cdd:COG4987 509 AlLADLLEALAGrTVLLITHRLAGLERM--------DRILVLEDG-------RIVEQGTHEELLAQN 560
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
272-482 |
4.83e-17 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 84.53 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM-IHRDDGIvispivkigyfSQNLDILEVEKSIL- 349
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMaMHAIDGI-----------PKNCQILHVEQEVVg 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 350 ---------------------ENVQSTSKQEETLIRT------------------------------------------- 365
Cdd:PLN03073 247 ddttalqcvlntdiertqlleEEAQLVAQQRELEFETetgkgkgankdgvdkdavsqrleeiykrlelidaytaearaas 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 366 ILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIEN 445
Cdd:PLN03073 327 ILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNT 406
|
250 260 270
....*....|....*....|....*....|....*..
gi 1890659908 446 VATKMLVIQDKVIQWFDGTYQQYEqhvRQKDRHADTQ 482
Cdd:PLN03073 407 VVTDILHLHGQKLVTYKGDYDTFE---RTREEQLKNQ 440
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
274-438 |
9.41e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.69 E-value: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 274 VEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM-----------------IHRDDGIVISPIVKIGYfs 336
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILaglspplagrvllnggpLDFQRDSIARGLLYLGH-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 337 qnLDILEVEKSILENVQ------STSKQEETLIRTILARLhffrDDVykPVEILSGGERVKVALAKLFVSDVNTLILDEP 410
Cdd:cd03231 81 --APGIKTTLSVLENLRfwhadhSDEQVEEALARVGLNGF----EDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|.
gi 1890659908 411 TNFLDIEAARALESLLQEY---KGTVIFASH 438
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-152 |
1.01e-16 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 79.05 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC-------------RAQCGLLP 70
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdgkdltklslkelRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 71 Q-----------------------LKRIDAIK----------------------SGGE---VTQSYMNALfskAPKLLLA 102
Cdd:cd03225 82 QnpddqffgptveeevafglenlgLPEEEIEErveealelvgleglrdrspftlSGGQkqrVAIAGVLAM---DPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 103 DEPTTHLDREHIEWLEKKLSQWKGA---FVIVSHDRAFLDALCTTIWEMDEGK 152
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
291-458 |
1.14e-16 |
|
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: 78.95 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVI--------SPI---VKIGYFSQNLDILEvEKSILENVQ--- 353
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTTLRmlaGLLEPDAGFATvdgfdvvkEPAearRRLGFVSDSTGLYD-RLTARENLEyfa 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 ---STSKQEETLIRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYK 430
Cdd:cd03266 104 glyGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLR 183
|
170 180 190
....*....|....*....|....*....|.
gi 1890659908 431 G---TVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:cd03266 184 AlgkCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
294-463 |
1.56e-16 |
|
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: 79.37 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVISPIVKIGYFSQNLdileveksilenvqsTSKQEET---LIRTIL 367
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLagvLKPDEGDIEIELDTVSYKPQYI---------------KADYEGTvrdLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 368 ARLH---FFRDDVYKPVEI----------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIE----AARALESLLQEYK 430
Cdd:cd03237 87 KDFYthpYFKTEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRFAENNE 166
|
170 180 190
....*....|....*....|....*....|...
gi 1890659908 431 GTVIFASHDRRFIENVATKMLViqdkviqwFDG 463
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIV--------FEG 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
272-439 |
2.03e-16 |
|
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: 78.38 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVISPIVKIG---YFSQNLDILEV- 344
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRllnRLNDLIPGAPDEGEVLLDgkdIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 345 -------------EKSILENV--------QSTSKQEETLIRTILARLHFFrDDVYKPVEI--LSGGERVKVALAKLFVSD 401
Cdd:cd03260 81 rrvgmvfqkpnpfPGSIYDNVayglrlhgIKLKEELDERVEEALRKAALW-DEVKDRLHAlgLSGGQQQRLCLARALANE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1890659908 402 VNTLILDEPTNFLDIEAARALESLLQEYKG--TVIFASHD 439
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
271-438 |
3.13e-16 |
|
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: 78.20 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLkKMIHRDD----------------GIVISPIVK-IG 333
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLL-SLITGDLpptygndvrlfgerrgGEDVWELRKrIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 334 YFSQNL-DILEVEKSILENV-----------QSTSKQEETLIRTILARLHF--FRDdvyKPVEILSGGERVKVALAKLFV 399
Cdd:COG1119 82 LVSPALqLRFPRDETVLDVVlsgffdsiglyREPTDEQRERARELLELLGLahLAD---RPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1890659908 400 SDVNTLILDEPTNFLDIEAA----RALESLLQEYKGTVIFASH 438
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARelllALLDKLAAEGAPTLVLVTH 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-153 |
3.17e-16 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 77.55 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC-------------RAQCGLLP 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdgkplsampppewRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 71 Q------------LKRIDAIK------------------------------SGGEvTQ--SYMNALfSKAPKLLLADEPT 106
Cdd:COG4619 81 QepalwggtvrdnLPFPFQLRerkfdreralellerlglppdildkpverlSGGE-RQrlALIRAL-LLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1890659908 107 THLDREHIEWLEKKLSQWK----GAFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:COG4619 159 SALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
291-455 |
4.99e-16 |
|
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: 77.47 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHR-------------DDGIV----ISP--IVK-----IGYFSQNLDI----- 341
Cdd:COG4778 31 SFSVAAGECVALTGPSGAGKSTLLK-CIYGnylpdsgsilvrhDGGWVdlaqASPreILAlrrrtIGYVSQFLRViprvs 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 342 -LE-VEKSILEnvQSTSKQE-ETLIRTILARLH------------FfrddvykpveilSGGERVKVALAKLFVSDVNTLI 406
Cdd:COG4778 110 aLDvVAEPLLE--RGVDREEaRARARELLARLNlperlwdlppatF------------SGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 407 LDEPTNFLDIEAARALESLLQEYK--GTVIFA-SHDRRFIENVATKMLVIQD 455
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAKarGTAIIGiFHDEEVREAVADRVVDVTP 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-152 |
7.02e-16 |
|
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: 75.69 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 2 ILLEALnVKHYVKDRLLFEIErLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCR------------------ 63
Cdd:cd03229 1 LELKNV-SKRYGQKTVLNDVS-LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdledelpplrrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 64 ----AQCGLLPQLKRIDAIK---SGGEvTQ--SYMNALFSKaPKLLLADEPTTHLD---REHIEWLEKKLSQWKG-AFVI 130
Cdd:cd03229 79 gmvfQDFALFPHLTVLENIAlglSGGQ-QQrvALARALAMD-PDVLLLDEPTSALDpitRREVRALLKSLQAQLGiTVVL 156
|
170 180
....*....|....*....|..
gi 1890659908 131 VSHDRAFLDALCTTIWEMDEGK 152
Cdd:cd03229 157 VTHDLDEAARLADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
272-440 |
1.36e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 78.26 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMI----HRDDG-IVISPIV----------KIGYFS 336
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLR-IIagleTPDSGrIVLNGRDlftnlpprerRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 337 QN------LdilevekSILENV------QSTSKQEetlIRTILARL-------HFfrDDVYkPVEiLSGGERVKVALAKL 397
Cdd:COG1118 82 QHyalfphM-------TVAENIafglrvRPPSKAE---IRARVEELlelvqleGL--ADRY-PSQ-LSGGQRQRVALARA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1890659908 398 FVSDVNTLILDEPtnF--LDIEAARALES----LLQEYKGTVIFASHDR 440
Cdd:COG1118 148 LAVEPEVLLLDEP--FgaLDAKVRKELRRwlrrLHDELGGTTVFVTHDQ 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
291-474 |
2.36e-15 |
|
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: 78.41 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIH------------RDDGIVISPI------VKIGYFSQN----LDILEVEKSI 348
Cdd:COG1123 26 SLTIAPGETVALVGESGSGKSTLALALMGllphggrisgevLLDGRDLLELsealrgRRIGMVFQDpmtqLNPVTVGDQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 ---LENVQSTSKQEETLIRTILARLHFFRDDVYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAARA 421
Cdd:COG1123 106 aeaLENLGLSRAEARARVLELLEAVGLERRLDRYPHQ-LSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 422 LESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWfDGTYQQYEQHVRQ 474
Cdd:COG1123 185 LRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE-DGPPEEILAAPQA 236
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
272-455 |
5.37e-15 |
|
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: 73.85 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMIHR----DDGIV--------ISPIVKIGYFS--- 336
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIR-MILGiilpDSGEVlfdgkpldIAARNRIGYLPeer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 337 ---QNLDILEVEKSI--LENVQSTSKQEEtlIRTILARLHFfRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPT 411
Cdd:cd03269 80 glyPKMKVIDQLVYLaqLKGLKKEEARRR--IDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1890659908 412 NFLDIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQD 455
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNK 203
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
291-471 |
6.95e-15 |
|
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: 77.11 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDG-IVISPIV-----------KIGYFSQNLDILEveKSILENVQ-- 353
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNlllGFLPPYSGsILINGVDlsdldpaswrrQIAWVPQNPYLFA--GTIRENLRlg 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 --STSKQEetlIRTILARLHFfrDDVYK--P----VEI------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAA 419
Cdd:COG4988 435 rpDASDEE---LEAALEAAGL--DEFVAalPdgldTPLgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 420 RALESLLQEYKG--TVIFASHDRRFIENvATKMLVIQD-KVIQwfDGTYQQYEQH 471
Cdd:COG4988 510 AEILQALRRLAKgrTVILITHRLALLAQ-ADRILVLDDgRIVE--QGTHEELLAK 561
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
291-459 |
7.05e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.93 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHRD----------DGIVISPIV---------KIGYFSQNLDILEvEKSILEN 351
Cdd:COG2884 22 SLEIEKGEFVFLTGPSGAGKSTLLK-LLYGEerptsgqvlvNGQDLSRLKrreipylrrRIGVVFQDFRLLP-DRTVYEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 V------QSTSKQE-ETLIRTILAR---LHffRDDVYkPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARA 421
Cdd:COG2884 100 ValplrvTGKSRKEiRRRVREVLDLvglSD--KAKAL-PHE-LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1890659908 422 LESLLQEY--KG-TVIFASHDRRFIENVATKMLVIQDKVIQ 459
Cdd:COG2884 176 IMELLEEInrRGtTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
291-464 |
7.56e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.02 E-value: 7.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMI----HRDDGIVIspivkIGyfSQNLDILEVEK---SIL-------------E 350
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLN-LIagflPPDSGRIL-----WN--GQDLTALPPAErpvSMLfqennlfphltvaQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 351 NVQ-------STSKQEETLIRTILAR--LHFFRDdvYKPvEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIeAARA 421
Cdd:COG3840 91 NIGlglrpglKLTAEQRAQVEQALERvgLAGLLD--RLP-GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP-ALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1890659908 422 -----LESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFDGT 464
Cdd:COG3840 167 emldlVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
291-446 |
8.95e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 72.35 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHRDdgivispivkigYFSQNLDILEVEKsileNVQSTSKQEETLIRTILARL 370
Cdd:cd03247 22 SLELKQGEKIALLGRSGSGKSTLLQ-LLTGD------------LKPQQGEITLDGV----PVSDLEKALSSLISVLNQRP 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890659908 371 HFFRDDVYKPVEI-LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARA-LESLLQEYKG-TVIFASHDRRFIENV 446
Cdd:cd03247 85 YLFDTTLRNNLGRrFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQlLSLIFEVLKDkTLIWITHHLTGIEHM 163
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
15-140 |
1.01e-14 |
|
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: 72.90 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 15 DRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC------------RAQCGLLPQLkriDAIKS-- 80
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepirdaredyRRRLAYLGHA---DGLKPel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 81 -------------GGEVT-------------QSYMN------------------ALFSKAPkLLLADEPTTHLDREHIEW 116
Cdd:COG4133 91 tvrenlrfwaalyGLRADreaidealeavglAGLADlpvrqlsagqkrrvalarLLLSPAP-LWLLDEPFTALDAAGVAL 169
|
170 180
....*....|....*....|....*..
gi 1890659908 117 LEKKLSQWK---GAFVIVSHDRAFLDA 140
Cdd:COG4133 170 LAELIAAHLargGAVLLTTHQPLELAA 196
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
24-169 |
1.26e-14 |
|
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: 73.14 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL-------------CRAQCGLLPQ------------------- 71
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkditkknlreLRRKVGLVFQnpddqlfaptveedvafgp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 ----------LKRID-AIK---------------SGGE----------VTQsymnalfskaPKLLLADEPTTHLDREHIE 115
Cdd:COG1122 102 enlglpreeiRERVEeALElvglehladrpphelSGGQkqrvaiagvlAME----------PEVLVLDEPTAGLDPRGRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1890659908 116 WLE---KKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKeYKGNYSDYLEQKEL 169
Cdd:COG1122 172 ELLellKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV-ADGTPREVFSDYEL 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
294-464 |
1.49e-14 |
|
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: 76.36 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTT---LLKKMIHRDDGIVISPiVKIGYFSQNLDI---LEVEkSILENVqSTSKQEETLIRTIL 367
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTfakILAGVLKPDEGEVDED-LKISYKPQYISPdydGTVE-EFLRSA-NTDDFGSSYYKTEI 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 368 AR---LHFFRDdvyKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIE----AARALESLLQEYKGTVIFASHDR 440
Cdd:COG1245 440 IKplgLEKLLD---KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRFAENRGKTAMVVDHDI 516
|
170 180
....*....|....*....|....
gi 1890659908 441 RFIENVATKMLViqdkviqwFDGT 464
Cdd:COG1245 517 YLIDYISDRLMV--------FEGE 532
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-173 |
1.64e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNVKHYVKDRLLFE-----IERLAIyendrIGLVGKNGSGKTTLLNILAKKISPEQGSVL----------------- 61
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDdlsfsLPPGGI-----VGIIGPNGAGKSTLFKMITGQEQPDSGTIKigetvklayvdqsrdal 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 62 -------------------------CRAQCGLL-----PQLKRIDAIkSGGEVTQSYMNALFSKAPKLLLADEPTTHLDR 111
Cdd:PRK11819 400 dpnktvweeisggldiikvgnreipSRAYVGRFnfkggDQQKKVGVL-SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 112 EHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTI--WEmDEGKIKEYKGNYSDYLEQKeleRRR 173
Cdd:PRK11819 479 ETLRALEEALLEFPGCAVVISHDRWFLDRIATHIlaFE-GDSQVEWFEGNFQEYEEDK---KRR 538
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
272-439 |
2.93e-14 |
|
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: 72.12 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVT-----GVIGQRVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM----------IHRDDGIVISPIVKIGYFS 336
Cdd:cd03293 1 LEVRNVSktyggGGGAVTAL-EDISLSVEEGEFVALVGPSGCGKSTLLRIIaglerptsgeVLVDGEPVTGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 337 QNlDILEVEKSILENV------QSTSKQE-ETLIRTILARLHF--FRDdvYKPVEiLSGGERVKVALAKLFVSDVNTLIL 407
Cdd:cd03293 80 QQ-DALLPWLTVLDNValglelQGVPKAEaRERAEELLELVGLsgFEN--AYPHQ-LSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1890659908 408 DEPTNFLDIEAARALESLL----QEYKGTVIFASHD 439
Cdd:cd03293 156 DEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-154 |
3.06e-14 |
|
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: 71.52 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNVKHYVKDRLLfEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL------CRAQ----CGLLPQ-- 71
Cdd:cd03226 2 IENISFSYKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngkpiKAKErrksIGYVMQdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 -------------LKRIDAIKSGGEVTQSYMN---------------------------ALFSKaPKLLLADEPTTHLDR 111
Cdd:cd03226 81 dyqlftdsvreelLLGLKELDAGNEQAETVLKdldlyalkerhplslsggqkqrlaiaaALLSG-KDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1890659908 112 EHIEWLE---KKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIK 154
Cdd:cd03226 160 KNMERVGeliRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
271-458 |
3.31e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.00 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVT-----GVIGQRVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLkKMI----HRDDGIVI---SPIV-------- 330
Cdd:COG1136 4 LLELRNLTksygtGEGEVTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLL-NILggldRPTSGEVLidgQDISslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 331 -----KIGYFSQNLDILEvEKSILENV------QSTSKQE-ETLIRTILARL---HffRDDvYKPVEiLSGGERVKVALA 395
Cdd:COG1136 82 rlrrrHIGFVFQFFNLLP-ELTALENValplllAGVSRKErRERARELLERVglgD--RLD-HRPSQ-LSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 396 KLFVSDvNTLIL-DEPTNFLDIEAARA----LESLLQEYKGTVIFASHDRRfIENVATKMLVIQDKVI 458
Cdd:COG1136 157 RALVNR-PKLILaDEPTGNLDSKTGEEvlelLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRI 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
271-455 |
4.47e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKK---MIHRDDGIVI---SPI--------VKIGYFS 336
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMllgLTHPDAGSISlcgEPVpsrarharQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 337 QnLDILEVEKSILENVQS-------TSKQEETLIRTIL--ARLHFFRDdvyKPVEILSGGERVKVALAKLFVSDVNTLIL 407
Cdd:PRK13537 87 Q-FDNLDPDFTVRENLLVfgryfglSAAAARALVPPLLefAKLENKAD---AKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 408 DEPTNFLDIEAA----RALESLLQEYKgTVIFASHDRRFIENVATKMLVIQD 455
Cdd:PRK13537 163 DEPTTGLDPQARhlmwERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEE 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
282-439 |
5.63e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 282 GQRVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMihrdDGiVISP----IVKIGYFSQNLDILEVEKSILENVQSTSK 357
Cdd:PRK09536 15 DTTVL-DGVDLSVREGSLVGLVGPNGAGKTTLLRAI----NG-TLTPtagtVLVAGDDVEALSARAASRRVASVPQDTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 358 QEETLIRTI--------LARLHFFRDD-----------------VYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTN 412
Cdd:PRK09536 89 SFEFDVRQVvemgrtphRSRFDTWTETdraaveramertgvaqfADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190
....*....|....*....|....*....|
gi 1890659908 413 FLDI-EAARALESL--LQEYKGTVIFASHD 439
Cdd:PRK09536 169 SLDInHQVRTLELVrrLVDDGKTAVAAIHD 198
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-153 |
5.98e-14 |
|
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: 71.61 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 1 MILLEALNVKHyvKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC------------RAQ-CG 67
Cdd:COG1120 1 MLEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlaslsrreLARrIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 68 LLPQ-------------------------------------------------LKRIDAIkSGGE---VtqsymnaLFSK 95
Cdd:COG1120 79 YVPQeppapfgltvrelvalgryphlglfgrpsaedreaveealertglehlaDRPVDEL-SGGErqrV-------LIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890659908 96 A----PKLLLADEPTTHLDREH-IEWLE--KKLSQWKG-AFVIVSHDrafLD---ALCTTIWEMDEGKI 153
Cdd:COG1120 151 AlaqePPLLLLDEPTSHLDLAHqLEVLEllRRLARERGrTVVMVLHD---LNlaaRYADRLVLLKDGRI 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
272-464 |
6.38e-14 |
|
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: 71.45 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQ--RVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDG-IVISPIV--------------K 331
Cdd:cd03256 1 IEVENLSKTYPNgkKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRclnGLVEPTSGsVLIDGTDinklkgkalrqlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 332 IGYFSQNLDILEvEKSILENV---------------QSTSKQEETLIRTILARLHfFRDDVYKPVEILSGGERVKVALAK 396
Cdd:cd03256 80 IGMIFQQFNLIE-RLSVLENVlsgrlgrrstwrslfGLFPKEEKQRALAALERVG-LLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 397 LFVSDVNTLILDEPTNFLDIEAARALESLL----QEYKGTVIFASHDRRFIENVATKMLVIQD-KVIqwFDGT 464
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLkrinREEGITVIVSLHQVDLAREYADRIVGLKDgRIV--FDGP 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
289-463 |
9.26e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 70.82 E-value: 9.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 289 KTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIV-----------ISPIVKIGY-FSQN---------LDILEV 344
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILsglLQPTSGEVrvaglvpwkrrKKFLRRIGVvFGQKtqlwwdlpvIDSFYL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 345 EKSI--LENVQSTSKQEEtlirtiLARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARAL 422
Cdd:cd03267 119 LAAIydLPPARFKKRLDE------LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1890659908 423 ESLLQEY----KGTVIFASHDRRFIENVATKMLVIQDKVIQwFDG 463
Cdd:cd03267 193 RNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRLL-YDG 236
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
272-461 |
9.80e-14 |
|
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: 73.63 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVI--GQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIH---------RDDGIVISPIVK------IGY 334
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGvwpptagsvRLDGADLSQWDReelgrhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 335 FSQNLDILevEKSILENVqstskqeetlirtilARlhfFRD-DVYKPVE---------------------------ILSG 386
Cdd:COG4618 411 LPQDVELF--DGTIAENI---------------AR---FGDaDPEKVVAaaklagvhemilrlpdgydtrigeggaRLSG 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 387 GERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYK---GTVIFASHDRRFIeNVATKMLVIQDKVIQWF 461
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLL-AAVDKLLVLRDGRVQAF 547
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-167 |
1.28e-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: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 2 ILLEALNVKHYVKDRLL----FEIERlaiyeNDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC-------------RA 64
Cdd:COG4988 337 IELEDVSFSYPGGRPALdglsLTIPP-----GERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngvdlsdldpaswRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 65 QCGLLPQ--------------LKRIDA-----------------IK-----------------SGGE-----VTQsymnA 91
Cdd:COG4988 412 QIAWVPQnpylfagtirenlrLGRPDAsdeeleaaleaagldefVAalpdgldtplgeggrglSGGQaqrlaLAR----A 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 92 LFSKAPkLLLADEPTTHLDREHIEWLEKKLSQW-KGAFVI-VSHDRAFLdALCTTIWEMDEGKIKEyKGNYSDYLEQK 167
Cdd:COG4988 488 LLRDAP-LLLLDEPTAHLDAETEAEILQALRRLaKGRTVIlITHRLALL-AQADRILVLDDGRIVE-QGTHEELLAKN 562
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
272-461 |
1.52e-13 |
|
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: 69.53 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGdKLAVIGPNGSGKTTLLKKMIH---------RDDGIVISPIV-----KIGYFSQ 337
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATltppssgtiRIDGQDVLKQPqklrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 338 N------------LDILEVEKSIlenvqsTSKQEETLIRTILARLHFFrDDVYKPVEILSGGERVKVALAKLFVSDVNTL 405
Cdd:cd03264 80 EfgvypnftvrefLDYIAWLKGI------PSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 406 ILDEPTNFLDIEAARALESLLQEYKG--TVIFASHDRRFIENVATKMLVIQDKVIQWF 461
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEdrIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
294-464 |
1.68e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.92 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTT---LLKKMIHRDDGiVISPIVKIGYFSQNLdileveksilenvqsTSKQEET---LIRTIL 367
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTfakLLAGVLKPDEG-EVDPELKISYKPQYI---------------KPDYDGTvedLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 368 ARLH--FFRDDVYKPVEI----------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIE----AARALESLLQEYKG 431
Cdd:PRK13409 426 DDLGssYYKSEIIKPLQLerlldknvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREA 505
|
170 180 190
....*....|....*....|....*....|...
gi 1890659908 432 TVIFASHDRRFIENVATKMLViqdkviqwFDGT 464
Cdd:PRK13409 506 TALVVDHDIYMIDYISDRLMV--------FEGE 530
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
301-444 |
1.71e-13 |
|
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: 69.56 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 301 AVIGPNGSGKTTLL--------------KKMIHRDDGIV----ISPIVKIGYFSQNLDILEVEKS--ILENVqSTSKQEE 360
Cdd:cd03240 26 LIVGQNGAGKTTIIealkyaltgelppnSKGGAHDPKLIregeVRAQVKLAFENANGKKYTITRSlaILENV-IFCHQGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 361 tlIRTILARlhffrddvykPVEILSGGERVKV------ALAKLFVSDVNTLILDEPTNFLDIE-AARALESLLQEYKGTV 433
Cdd:cd03240 105 --SNWPLLD----------MRGRCSGGEKVLAsliirlALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQK 172
|
170
....*....|....*
gi 1890659908 434 IF----ASHDRRFIE 444
Cdd:cd03240 173 NFqlivITHDEELVD 187
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
291-467 |
1.78e-13 |
|
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: 69.84 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMI---HRDDG--IVISPI----------VKIGYFSQNlDILEVEKSILENV--- 352
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLK-MLtgeLRPTSgtAYINGYsirtdrkaarQSLGYCPQF-DALFDELTVREHLrfy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 ---QSTSKQEETLIRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEY 429
Cdd:cd03263 100 arlKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1890659908 430 KG--TVIFASHDRRFIENVATKMLVIQDKVIqWFDGTYQQ 467
Cdd:cd03263 180 RKgrSIILTTHSMDEAEALCDRIAIMSDGKL-RCIGSPQE 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
271-439 |
2.00e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVI-SPIVKIGYFSQNLDI----- 341
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRvvlGLVAPDEGVIKrNGKLRIGYVPQKLYLdttlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 342 LEVEKSILenVQSTSKQEE---TLIRTILARLHFFrddvykPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEA 418
Cdd:PRK09544 84 LTVNRFLR--LRPGTKKEDilpALKRVQAGHLIDA------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*
gi 1890659908 419 ARALESLL----QEYKGTVIFASHD 439
Cdd:PRK09544 156 QVALYDLIdqlrRELDCAVLMVSHD 180
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
146-255 |
2.65e-13 |
|
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: 65.29 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 146 WEMDEGKIKEYKGNYSDYLEQKELERRRQQSAYEQYEKKKQALERALELKKQKAERATKapkkvsrseanimgakpyfak 225
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQ--------------------- 59
|
90 100 110
....*....|....*....|....*....|
gi 1890659908 226 kqkklqktAKAMETRLEKLEKVEKIKETAP 255
Cdd:pfam12848 60 --------AQSRIKALEKMERIEKPERDKP 81
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
24-172 |
3.04e-13 |
|
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: 72.11 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC-------------RAQCGLLPQ------------------- 71
Cdd:COG4987 356 LTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdlrdldeddlRRRIAVVPQrphlfdttlrenlrlarpd 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 ---------LKR------IDAIK--------------SGGE-----VTQsymnALFSKAPKLLLaDEPTTHLDR--EHiE 115
Cdd:COG4987 436 atdeelwaaLERvglgdwLAALPdgldtwlgeggrrlSGGErrrlaLAR----ALLRDAPILLL-DEPTEGLDAatEQ-A 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 116 WLEKKLSQWKG-AFVIVSHDRAFLDAlCTTIWEMDEGKIKEyKGNYSDYLEQKELERR 172
Cdd:COG4987 510 LLADLLEALAGrTVLLITHRLAGLER-MDRILVLEDGRIVE-QGTHEELLAQNGRYRQ 565
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
272-456 |
3.23e-13 |
|
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: 67.56 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQ-RVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkmihrddgiVIS---PivkigYFSQNLDILEVEKS 347
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFR---------ALAglwP-----WGSGRIGMPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 348 ILenvqstskqeetlirtiLARLHFF-----RDDVYKP-VEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARA 421
Cdd:cd03223 67 LF-----------------LPQRPYLplgtlREQLIYPwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180 190
....*....|....*....|....*....|....*
gi 1890659908 422 LESLLQEYKGTVIFASHdRRFIENVATKMLVIQDK 456
Cdd:cd03223 130 LYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
297-459 |
3.37e-13 |
|
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: 68.86 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 297 GDKLAVIGPNGSGKTTLLKKM--IHRDDG--IVISPIV---------------KIGYFSQNLDI---LEVEKSILENVQS 354
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIagLEKPDGgtIVLNGTVlfdsrkkinlppqqrKIGLVFQQYALfphLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 355 TSKQEET-LIRTILARLHFfRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAA----RALESLLQEY 429
Cdd:cd03297 103 KRNREDRiSVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRlqllPELKQIKKNL 181
|
170 180 190
....*....|....*....|....*....|
gi 1890659908 430 KGTVIFASHDRRFIENVATKMLVIQDKVIQ 459
Cdd:cd03297 182 NIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-155 |
4.28e-13 |
|
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: 69.06 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL---------------CRAQ----------------------- 65
Cdd:COG1124 26 LEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrrrrkafrRRVQmvfqdpyaslhprhtvdrilaep 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 66 ---CGLLPQLKRIDAIKSGGEVTQSYMN------------------ALFSKaPKLLLADEPTTHLD---REHIEWLEKKL 121
Cdd:COG1124 106 lriHGLPDREERIAELLEQVGLPPSFLDryphqlsggqrqrvaiarALILE-PELLLLDEPTSALDvsvQAEILNLLKDL 184
|
170 180 190
....*....|....*....|....*....|....*
gi 1890659908 122 SQWKG-AFVIVSHDRAFLDALCTTIWEMDEGKIKE 155
Cdd:COG1124 185 REERGlTYLFVSHDLAVVAHLCDRVAVMQNGRIVE 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
290-439 |
4.30e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 290 TSFHVRGGDKLAVIGPNGSGKTTLLKKM---------IHRDDGIVIS-PIVKI----GYFSQN---LDILEVEK--SILE 350
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMagllpgsgsIQFAGQPLEAwSAAELarhrAYLSQQqtpPFAMPVFQylTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 351 NVQSTSKQEETLIRTILARLHFfRDDVYKPVEILSGGE--RVKVALAKLFV-SDVNT----LILDEPTNFLDIEAARALE 423
Cdd:PRK03695 95 PDKTRTEAVASALNEVAEALGL-DDKLGRSVNQLSGGEwqRVRLAAVVLQVwPDINPagqlLLLDEPMNSLDVAQQAALD 173
|
170
....*....|....*....
gi 1890659908 424 SLLQEY---KGTVIFASHD 439
Cdd:PRK03695 174 RLLSELcqqGIAVVMSSHD 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
387-488 |
4.34e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.46 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 387 GERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFDGTYQ 466
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYD 238
|
90 100
....*....|....*....|..
gi 1890659908 467 QYEQhvrqkdrhADTQADQRLL 488
Cdd:PRK15064 239 EYMT--------AATQARERLL 252
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
24-152 |
4.45e-13 |
|
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: 67.41 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL-------------CRAQCGLLPQ--------LKriDAIKSGG 82
Cdd:cd03228 23 LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdldlesLRKNIAYVPQdpflfsgtIR--ENILSGG 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 83 E---VtqsymnAL---FSKAPKLLLADEPTTHLDREHIEWLEKKLSQWKG--AFVIVSHDRAfLDALCTTIWEMDEGK 152
Cdd:cd03228 101 QrqrI------AIaraLLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-171 |
4.47e-13 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 68.96 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSV--------LCRAQCGLLPQLKRID------------------- 76
Cdd:COG1121 27 LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpprRARRRIGYVPQRAEVDwdfpitvrdvvlmgrygrr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 77 ----------------AIK---------------SGGE-----VTQsymnALFSKaPKLLLADEPTTHLDREHIEWLEKK 120
Cdd:COG1121 107 glfrrpsradreavdeALErvgledladrpigelSGGQqqrvlLAR----ALAQD-PDLLLLDEPFAGVDAATEEALYEL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 121 LSQWKG---AFVIVSHDRAFLDALCTTIWEMDEGKIKEykGNYSDYLEQKELER 171
Cdd:COG1121 182 LRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLVAH--GPPEEVLTPENLSR 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
267-439 |
5.04e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 68.96 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 267 QDRIIIRVEEVT----GVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLkKMI-----------HRDDGIVISPIVK 331
Cdd:COG1116 3 AAAPALELRGVSkrfpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLL-RLIaglekptsgevLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 332 IGYFSQNLDILEvEKSILENV------QSTSKQE-ETLIRTILAR--LHFFRDdvYKPVEiLSGGERVKVALAKLFVSDV 402
Cdd:COG1116 82 RGVVFQEPALLP-WLTVLDNValglelRGVPKAErRERARELLELvgLAGFED--AYPHQ-LSGGMRQRVAIARALANDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1890659908 403 NTLILDEPtnF--LDiEAARA-----LESLLQEYKGTVIFASHD 439
Cdd:COG1116 158 EVLLMDEP--FgaLD-ALTRErlqdeLLRLWQETGKTVLFVTHD 198
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
291-467 |
5.15e-13 |
|
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: 68.41 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTT----LLKKMIHRD-----DGIVISPIV------KIGYFSQnlDILEVEKSILENVQ-- 353
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTlinlLMRFYDPQKgqiliDGIDIRDISrkslrsMIGVVLQ--DTFLFSGTIMENIRlg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 -STSKQEETLIRTILARLHFFRDDVYKPVE--------ILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALES 424
Cdd:cd03254 101 rPNATDEEVIEAAKEAGAHDFIMKLPNGYDtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1890659908 425 LLQE-YKG-TVIFASHDRRFIENvATKMLVIQD-KVIQwfDGTYQQ 467
Cdd:cd03254 181 ALEKlMKGrTSIIIAHRLSTIKN-ADKILVLDDgKIIE--EGTHDE 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
272-459 |
6.43e-13 |
|
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: 68.05 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMI----HRDDG-IVISPIV---------KIGYFSQ 337
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLR-MIagleEPTSGrIYIGGRDvtdlppkdrDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 338 NLdILEVEKSILENVQSTSKQEETLIRTILARLHffrdDVYKPVEI----------LSGGERVKVALAKLFVSDVNTLIL 407
Cdd:cd03301 80 NY-ALYPHMTVYDNIAFGLKLRKVPKDEIDERVR----EVAELLQIehlldrkpkqLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1890659908 408 DEPTNFLDI---EAARA-LESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQ 459
Cdd:cd03301 155 DEPLSNLDAklrVQMRAeLKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-171 |
8.51e-13 |
|
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: 67.96 E-value: 8.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 1 MILLEALnVKHYVKDRLL----FEIERLAIYendriGLVGKNGSGKTTLLNILAKKISPEQGSVL------------CRA 64
Cdd:COG4555 1 MIEVENL-SKKYGKVPALkdvsFTAKDGEIT-----GLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepreARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 65 QCGLLPQ----------------------------LKRIDAIK----------------SGGEVTQSYMNALFSKAPKLL 100
Cdd:COG4555 75 QIGVLPDerglydrltvreniryfaelyglfdeelKKRIEELIellgleefldrrvgelSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 101 LADEPTTHLDREHIEWLEKKLSQWKG---AFVIVSHDRAFLDALCTTIWEMDEGKIKeYKGNYSDYLEQKELER 171
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKVV-AQGSLDELREEIGEEN 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
291-459 |
1.00e-12 |
|
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: 67.75 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVI---------SPIVK-IGYFSQNLDI---LEVEKSI---LEN 351
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIagfIKPDSGKILlngkditnlPPEKRdISYVPQNYALfphMTVYKNIaygLKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 VQSTSKQEETLIRTILARLHFFRDDVYKPvEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLL----Q 427
Cdd:cd03299 99 RKVDKKEIERKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELkkirK 177
|
170 180 190
....*....|....*....|....*....|...
gi 1890659908 428 EYKGTVIFASHDRRFIENVATKMLVIQD-KVIQ 459
Cdd:cd03299 178 EFGVTVLHVTHDFEEAWALADKVAIMLNgKLIQ 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
282-439 |
1.10e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.87 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 282 GQRVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM--IHRDDG--IVISPIVKIGYFSQnldILEVEKSILENVQST-- 355
Cdd:NF040873 4 GRPVL-HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLagVLRPTSgtVRRAGGARVAYVPQ---RSEVPDSLPLTVRDLva 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 356 -------------SKQEETLIRTILARLHFfRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARAL 422
Cdd:NF040873 80 mgrwarrglwrrlTRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|
gi 1890659908 423 ESLLQEYKG---TVIFASHD 439
Cdd:NF040873 159 IALLAEEHArgaTVVVVTHD 178
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
289-462 |
1.15e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 67.56 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 289 KTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIV-----ISPIVKIGYFSQNldilevEKSILENV------QS 354
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRllaGIYPPDSGTVtvrgrVSSLLGLGGGFNP------ELTGRENIylngrlLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 355 TSKQEetlIRTILARLHFFR---DDVYKPVEILSGGERVKVALAklfVS---DVNTLILDEPT-----NFLDiEAARALE 423
Cdd:cd03220 114 LSRKE---IDEKIDEIIEFSelgDFIDLPVKTYSSGMKARLAFA---IAtalEPDILLIDEVLavgdaAFQE-KCQRRLR 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 1890659908 424 SLLQEYKgTVIFASHDRRFIENVATKMLVIQDKVIQWFD 462
Cdd:cd03220 187 ELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
291-467 |
1.25e-12 |
|
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: 67.46 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVI---------SP--IVKIGY---FsQNLDILEvEKSILENVQ 353
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNlisGFLRPTSGSVLfdgeditglPPheIARLGIgrtF-QIPRLFP-ELTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 --------------STSKQEETLIRTILARLHFFR--DDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIE 417
Cdd:cd03219 98 vaaqartgsglllaRARREEREARERAEELLERVGlaDLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 418 AARALESLLQEYKG---TVIFASHDRRFIENVATKMLVI-QDKVIqwFDGTYQQ 467
Cdd:cd03219 178 ETEELAELIRELRErgiTVLLVEHDMDVVMSLADRVTVLdQGRVI--AEGTPDE 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
290-429 |
1.67e-12 |
|
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: 66.91 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 290 TSFHVRGGDKLAVIGPNGSGKTTLLKKMIHRDDG-------IVI--SPIVK------IGYFSQ---NLDILEVEKSILEN 351
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqILFngQPRKPdqfqkcVAYVRQddiLLPGLTVRETLTYT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 VQ------STSKQEETLIRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESL 425
Cdd:cd03234 106 AIlrlprkSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVST 185
|
....
gi 1890659908 426 LQEY 429
Cdd:cd03234 186 LSQL 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
270-454 |
1.83e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 270 IIIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRDDG---IVISPI--------VKIGYF 335
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTiarMILGMTSPDAGkitVLGVPVpararlarARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 336 SQnLDILEVEKSILENV-------QSTSKQEETLIRTIL--ARLHFFRDdvyKPVEILSGGERVKVALAKLFVSDVNTLI 406
Cdd:PRK13536 120 PQ-FDNLDLEFTVRENLlvfgryfGMSTREIEAVIPSLLefARLESKAD---ARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 407 LDEPTNFLDIEAA----RALESLLQEYKgTVIFASHDRRFIENVATKMLVIQ 454
Cdd:PRK13536 196 LDEPTTGLDPHARhliwERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLE 246
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
282-439 |
2.03e-12 |
|
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: 69.31 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 282 GQRVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM-----------------IHRDDGIVISPIVkiGYFSQNLDILEV 344
Cdd:TIGR02868 347 APPVL-DGVSLDLPPGERVAILGPSGSGKSTLLATLaglldplqgevtldgvpVSSLDQDEVRRRV--SVCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 345 ekSILENVQ----STSKQE--ETLIRTILARLHFFRDDVYKPV-----EILSGGERVKVALAKLFVSDVNTLILDEPTNF 413
Cdd:TIGR02868 424 --TVRENLRlarpDATDEElwAALERVGLADWLRALPDGLDTVlgeggARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180
....*....|....*....|....*...
gi 1890659908 414 LDIEAARA-LESLLQEYKG-TVIFASHD 439
Cdd:TIGR02868 502 LDAETADElLEDLLAALSGrTVVLITHH 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
32-153 |
2.29e-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: 65.32 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 32 IGLVGKNGSGKTTLLNILAKKISPEQGSVLC-------------RAQCGLLPQLKR------IDAIKSGGEVTQSYM-NA 91
Cdd:cd03246 31 LAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdpnelGDHVGYLPQDDElfsgsiAENILSGGQRQRLGLaRA 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 92 LFsKAPKLLLADEPTTHLDREHIEWLEKKLSQWKGAF---VIVSHDRAFLdALCTTIWEMDEGKI 153
Cdd:cd03246 111 LY-GNPRILVLDEPNSHLDVEGERALNQAIAALKAAGatrIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
291-467 |
3.57e-12 |
|
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: 66.10 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHR--D--------DGIVISPIV------KIGYFSQnlDILEVEKSILENVqS 354
Cdd:cd03251 22 SLDIPAGETVALVGPSGSGKSTLVN-LIPRfyDvdsgriliDGHDVRDYTlaslrrQIGLVSQ--DVFLFNDTVAENI-A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 355 TSKQEETLIRTI----LARLHFFRDDVYKPVEI--------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARAL 422
Cdd:cd03251 98 YGRPGATREEVEeaarAANAHEFIMELPEGYDTvigergvkLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1890659908 423 ESLLQE-YKG-TVIFASHDRRFIENvATKMLVIQD-KVIQwfDGTYQQ 467
Cdd:cd03251 178 QAALERlMKNrTTFVIAHRLSTIEN-ADRIVVLEDgKIVE--RGTHEE 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
284-455 |
4.39e-12 |
|
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: 65.45 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 284 RVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIHRD---------DGIVISPIV--KIGYF-SQNLDI------LEVE 345
Cdd:TIGR02211 19 RVL-KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDnptsgevlfNGQSLSKLSsnERAKLrNKKLGFiyqfhhLLPD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 346 KSILENVQ------STSKQE-ETLIRTILARLHFFRDDVYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEA 418
Cdd:TIGR02211 98 FTALENVAmplligKKSVKEaKERAYEMLEKVGLEHRINHRPSE-LSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1890659908 419 ARALESLLQE----YKGTVIFASHDRRFIENvATKMLVIQD 455
Cdd:TIGR02211 177 AKIIFDLMLElnreLNTSFLVVTHDLELAKK-LDRVLEMKD 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
291-458 |
4.39e-12 |
|
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: 68.59 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRDDG-IVISPIVKIGYFSQNL---------DILEVEKSILENVQ---- 353
Cdd:TIGR02203 352 SLVIEPGETVALVGRSGSGKSTlvnLIPRFYEPDSGqILLDGHDLADYTLASLrrqvalvsqDVVLFNDTIANNIAygrt 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 STSKQEETLIRTILARLHFFRDDVYKPVE--------ILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR----A 421
Cdd:TIGR02203 432 EQADRAEIERALAAAYAQDFVDKLPLGLDtpigengvLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERlvqaA 511
|
170 180 190
....*....|....*....|....*....|....*..
gi 1890659908 422 LESLLQEYKGTVIfaSHDRRFIENvATKMLVIQDKVI 458
Cdd:TIGR02203 512 LERLMQGRTTLVI--AHRLSTIEK-ADRIVVMDDGRI 545
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
24-175 |
6.34e-12 |
|
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: 68.32 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC-------------RAQCGLLPQ------------------- 71
Cdd:COG2274 496 LTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidpaslRRQIGVVLQdvflfsgtirenitlgdpd 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 --LKRI----------DAIK-----------------SGGEVtQSYM--NALFSKaPKLLLADEPTTHLDREhiewLEKK 120
Cdd:COG2274 576 atDEEIieaarlaglhDFIEalpmgydtvvgeggsnlSGGQR-QRLAiaRALLRN-PRILILDEATSALDAE----TEAI 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 121 ----LSQWKG--AFVIVSHDRAFLdALCTTIWEMDEGKIKEyKGNYSDYLEQKELERR--RQQ 175
Cdd:COG2274 650 ilenLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRIVE-DGTHEELLARKGLYAElvQQQ 710
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-153 |
6.46e-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: 64.92 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 23 RLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL-------------CRAQCGLLPQ--------LK-------- 73
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdirqldpadLRRNIGYVPQdvtlfygtLRdnitlgap 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 74 -----RI-DAIK--------------------------SGGEvTQSYMNA-LFSKAPKLLLADEPTTHLDREHIEWLEKK 120
Cdd:cd03245 104 laddeRIlRAAElagvtdfvnkhpngldlqigergrglSGGQ-RQAVALArALLNDPPILLLDEPTSAMDMNSEERLKER 182
|
170 180 190
....*....|....*....|....*....|....*
gi 1890659908 121 LSQWKG--AFVIVSHDRAFLDaLCTTIWEMDEGKI 153
Cdd:cd03245 183 LRQLLGdkTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
291-439 |
6.66e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.63 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM--IHRDDGIVI---SPIVKI---------GYFSQNLD---ILEVEKSI---LE 350
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMagLLPGQGEILlngRPLSDWsaaelarhrAYLSQQQSppfAMPVFQYLalhQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 351 NVQSTSKQEeTLIRTILARLHFfrDDVY-KPVEILSGGERVKVALAKLFV---SDVNT----LILDEPTNFLDIEAARAL 422
Cdd:COG4138 96 AGASSEAVE-QLLAQLAEALGL--EDKLsRPLTQLSGGEWQRVRLAAVLLqvwPTINPegqlLLLDEPMNSLDVAQQAAL 172
|
170 180
....*....|....*....|
gi 1890659908 423 ESLLQEYK---GTVIFASHD 439
Cdd:COG4138 173 DRLLRELCqqgITVVMSSHD 192
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
291-467 |
6.85e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.88 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHR--D--------DGIVISPIV------KIGYFSQNLDILEveKSILENV-- 352
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVN-LLLRfyDptsgriliDGVDIRDLTleslrrQIGVVPQDTFLFS--GTIRENIry 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 ---QSTskqEETLIRTI-LARLHFFrddvykpveI-----------------LSGGERVKVALAKLFVSDVNTLILDEPT 411
Cdd:COG1132 437 grpDAT---DEEVEEAAkAAQAHEF---------IealpdgydtvvgergvnLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890659908 412 NFLDIEAARAL-ESLLQEYKG-TVIFASHdrRF--IENvATKMLVIQD-KVIQwfDGTYQQ 467
Cdd:COG1132 505 SALDTETEALIqEALERLMKGrTTIVIAH--RLstIRN-ADRILVLDDgRIVE--QGTHEE 560
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
294-460 |
7.68e-12 |
|
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: 64.82 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTTLL------------KKMIHRDDGIVISPI---VKIGYFSQNL-DILEVEKSI----LENVQ 353
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLnliagfetpqsgRVLINGVDVTAAPPAdrpVSMLFQENNLfAHLTVEQNVglglSPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 STSKQEETlIRTILARLHFFRDDVYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDiEAARA-----LESLLQE 428
Cdd:cd03298 101 LTAEDRQA-IEVALARVGLAGLEKRLPGE-LSGGERQRVALARVLVRDKPVLLLDEPFAALD-PALRAemldlVLDLHAE 177
|
170 180 190
....*....|....*....|....*....|..
gi 1890659908 429 YKGTVIFASHDRRFIENVATKMLVIQDKVIQW 460
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
272-459 |
9.73e-12 |
|
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: 65.05 E-value: 9.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVI--------SPIVK--IGYFSQN 338
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRliaGLERPDSGTILfggedatdVPVQErnVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 339 LDILEvEKSILENV--------QSTSKQEETLIRTILARLHFFRDDVYK---PVEiLSGGERVKVALAKLFVSDVNTLIL 407
Cdd:cd03296 83 YALFR-HMTVFDNVafglrvkpRSERPPEAEIRAKVHELLKLVQLDWLAdryPAQ-LSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1890659908 408 DEPTNFLDIEAARALESLLQEYKG----TVIFASHDRRFIENVATKMLVI-QDKVIQ 459
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVVMnKGRIEQ 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
272-439 |
1.76e-11 |
|
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: 64.24 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVI-GQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLkKMIHR----DDGIV---------ISPIV---KIGY 334
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTM-KMINRliepTSGEIfidgedireQDPVElrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 335 FSQNLDILEvEKSILEN---VQSTSKQEETLIRT----ILARLHF----FRDDvYkPVEiLSGGERVKVALAKLFVSDVN 403
Cdd:cd03295 80 VIQQIGLFP-HMTVEENialVPKLLKWPKEKIREradeLLALVGLdpaeFADR-Y-PHE-LSGGQQQRVGVARALAADPP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1890659908 404 TLILDEPTNFLDIEAARALES----LLQEYKGTVIFASHD 439
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEefkrLQQELGKTIVFVTHD 195
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
291-476 |
1.92e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.33 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIV-----ISPIVKIG-------------YFSQNL------DILE 343
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKliaGILEPTSGRVevngrVSALLELGagfhpeltgreniYLNGRLlglsrkEIDE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 344 VEKSILEnvqstskqeetlirtiLARLHFFRDdvyKPVEILSGGERVKVALAklfVS-----DVntLILDEPTNFLDIE- 417
Cdd:COG1134 126 KFDEIVE----------------FAELGDFID---QPVKTYSSGMRARLAFA---VAtavdpDI--LLVDEVLAVGDAAf 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 418 ---AARALESLLQEyKGTVIFASHDRRFIENVATKMLVIQDKVIQWFDGT---YQQYEQHVRQKD 476
Cdd:COG1134 182 qkkCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPeevIAAYEALLAGRE 245
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
277-460 |
2.04e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 277 VTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIHRDDGIVISPIVKIgyfsqNLDILEVEKSILENV---Q 353
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDV-----PDNQFGREASLIDAIgrkG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 STSKQEETLIRTILARLHFFRddvyKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAARALESLLQEY 429
Cdd:COG2401 111 DFKDAVELLNAVGLSDAVLWL----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRA 186
|
170 180 190
....*....|....*....|....*....|.
gi 1890659908 430 KGTVIFASHDRRFIENVATKMLVIQDKVIQW 460
Cdd:COG2401 187 GITLVVATHHYDVIDDLQPDLLIFVGYGGVP 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
291-441 |
2.07e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 63.99 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLkkMI-----HRDDGIV------ISPI----------VKIGYFSQN---LDILevek 346
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLL--GLlagldRPTSGTVrlagqdLFALdedararlraRHVGFVFQSfqlLPTL---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 347 SILENV----------QSTSKQEETLIRTILA-RLHFFrddvykPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLD 415
Cdd:COG4181 106 TALENVmlplelagrrDARARARALLERVGLGhRLDHY------PAQ-LSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
170 180 190
....*....|....*....|....*....|
gi 1890659908 416 IEAARALESLL----QEYKGTVIFASHDRR 441
Cdd:COG4181 179 AATGEQIIDLLfelnRERGTTLVLVTHDPA 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
291-458 |
2.43e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 63.32 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIH---------RDDGIVISP--------IVKIGYFSQNLDILEvEKSILEN-- 351
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKSTLLRCINLleepdsgtiIIDGLKLTDdkkninelRQKVGMVFQQFNLFP-HLTVLENit 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 -----VQSTSKQE-ETLIRTILARLHFF-RDDVYkPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR-ALE 423
Cdd:cd03262 99 lapikVKGMSKAEaEERALELLEKVGLAdKADAY-PAQ-LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGeVLD 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1890659908 424 SLLQ--EYKGTVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:cd03262 177 VMKDlaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
270-439 |
2.55e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.02 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 270 IIIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGivispivKIGYFSQNLDILEVEK 346
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgeLSPDSG-------EVRLNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 347 ------------------SILENV-------QSTSKQEETLIRTILAR--LHFFRDDVYKPveiLSGGERVKVALAKLFV 399
Cdd:PRK13548 74 larrravlpqhsslsfpfTVEEVVamgraphGLSRAEDDALVAAALAQvdLAHLAGRDYPQ---LSGGEQQRVQLARVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1890659908 400 ------SDVNTLILDEPTNFLDI----EAARALESLLQEYKGTVIFASHD 439
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD 200
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
282-458 |
2.80e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 282 GQRVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM---------------IHRDDGIVISP---IVK-----IGYFSQN 338
Cdd:PRK11264 15 GQTVL-HGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirvgdITIDTARSLSQqkgLIRqlrqhVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 339 LDILEvEKSILEN-------VQSTSKQE-ETLIRTILARLHFF-RDDVYKpvEILSGGERVKVALAKLFVSDVNTLILDE 409
Cdd:PRK11264 94 FNLFP-HRTVLENiiegpviVKGEPKEEaTARARELLAKVGLAgKETSYP--RRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 410 PTNFLDIE-AARALESL--LQEYKGTVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:PRK11264 171 PTSALDPElVGEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
291-455 |
4.81e-11 |
|
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: 63.02 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHR--D--------DGIVISPIV------KIGYFSQnlDILEVEKSILENVQ- 353
Cdd:cd03253 21 SFTIPAGKKVAIVGPSGSGKSTILR-LLFRfyDvssgsiliDGQDIREVTldslrrAIGVVPQ--DTVLFNDTIGYNIRy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 -STSKQEETLIRT-ILARLHFF---RDDVYKPV--E---ILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARAL- 422
Cdd:cd03253 98 gRPDATDEEVIEAaKAAQIHDKimrFPDGYDTIvgErglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIq 177
|
170 180 190
....*....|....*....|....*....|....
gi 1890659908 423 ESLLQEYKG-TVIFASHDRRFIENvATKMLVIQD 455
Cdd:cd03253 178 AALRDVSKGrTTIVIAHRLSTIVN-ADKIIVLKD 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-156 |
7.26e-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: 62.14 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 3 LLEALNV-KHYVKDRLLFEIER---LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSV----------------LC 62
Cdd:cd03257 1 LLEVKNLsVSFPTGGGSVKALDdvsFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrrlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 63 RAQCGLLPQ--------------------------------LKRIDAIKSGGEVTQSYMN------------------AL 92
Cdd:cd03257 81 RKEIQMVFQdpmsslnprmtigeqiaeplrihgklskkearKEAVLLLLVGVGLPEEVLNryphelsggqrqrvaiarAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 93 FSKaPKLLLADEPTTHLD---REHIEWLEKKLSQWKG-AFVIVSHDRAFLDALCTTIWEMDEGKIKEY 156
Cdd:cd03257 161 ALN-PKLLIADEPTSALDvsvQAQILDLLKKLQEELGlTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
291-455 |
8.49e-11 |
|
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: 61.65 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIHRD---------DGIVIS-------PIV--KIGYFSQNLDILeVEKSILENV 352
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEElptsgtirvNGQDVSdlrgraiPYLrrKIGVVFQDFRLL-PDRNVYENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 -------QSTSKQEETLIRTILARLHFFRDDVYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESL 425
Cdd:cd03292 100 afalevtGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNL 178
|
170 180 190
....*....|....*....|....*....|...
gi 1890659908 426 LQEYK---GTVIFASHDRRFIENVATKMLVIQD 455
Cdd:cd03292 179 LKKINkagTTVVVATHAKELVDTTRHRVIALER 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
271-469 |
1.68e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.57 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRD----------------DGIVISPIVK 331
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglITGDksagshiellgrtvqrEGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 332 ----IGYFSQNLDILEvEKSILENV------------------QSTSKQEETLIRTILARLHFfrddVYKPVEILSGGER 389
Cdd:PRK09984 84 sranTGYIFQQFNLVN-RLSVLENVligalgstpfwrtcfswfTREQKQRALQALTRVGMVHF----AHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 390 VKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKG----TVIFASHDRRFIENVATKMLVIQDKVIqWFDGTY 465
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQGHV-FYDGSS 237
|
....
gi 1890659908 466 QQYE 469
Cdd:PRK09984 238 QQFD 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
271-455 |
2.41e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.66 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVT-GVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM--IHRDD-------GIVIS-------PIVK-- 331
Cdd:PRK10908 1 MIRFEHVSkAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIcgIERPSagkiwfsGHDITrlknrevPFLRrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 332 IGYFSQNLDILeVEKSILENVQS----TSKQEETLIRTILARLhffrDDV-------YKPVEiLSGGERVKVALAKLFVS 400
Cdd:PRK10908 81 IGMIFQDHHLL-MDRTVYDNVAIpliiAGASGDDIRRRVSAAL----DKVglldkakNFPIQ-LSGGEQQRVGIARAVVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 401 DVNTLILDEPTNFLDIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQD 455
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-155 |
2.43e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 60.44 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 3 LLEALNVKHYVKD-----RLLFEIErLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC--------------- 62
Cdd:COG1136 4 LLELRNLTKSYGTgegevTALRGVS-LSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdgqdisslserelar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 63 --RAQCG-------LLPQL---------------------KRIDAI------------K----SGGE----------VTQ 86
Cdd:COG1136 83 lrRRHIGfvfqffnLLPELtalenvalplllagvsrkerrERARELlervglgdrldhRpsqlSGGQqqrvaiaralVNR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 87 symnalfskaPKLLLADEPTTHLDR---EHIewLE--KKLSQWKG-AFVIVSHDRAfLDALCTTIWEMDEGKIKE 155
Cdd:COG1136 163 ----------PKLILADEPTGNLDSktgEEV--LEllRELNRELGtTIVMVTHDPE-LAARADRVIRLRDGRIVS 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-156 |
3.12e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQC--------GLLPQL---------------------KR 74
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsallelgaGFHPELtgreniylngrllglsrkeidEK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 75 IDAIK-----------------SGgevtqsyMNA--LFSKA----PKLLLADeptthldrehiEWL-----------EKK 120
Cdd:COG1134 127 FDEIVefaelgdfidqpvktysSG-------MRArlAFAVAtavdPDILLVD-----------EVLavgdaafqkkcLAR 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1890659908 121 LSQWK---GAFVIVSHDRAFLDALCT-TIWeMDEGKIKEY 156
Cdd:COG1134 189 IRELResgRTVIFVSHSMGAVRRLCDrAIW-LEKGRLVMD 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
291-463 |
4.37e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.98 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM------------IHRDDGIVISPI---VKIGYFSQNL-DILEVEKSI---LE- 350
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIagfltpasgsltLNGQDHTTTPPSrrpVSMLFQENNLfSHLTVAQNIglgLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 351 NVQSTSKQEETL--------IRTILARLhffrddvykPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEA 418
Cdd:PRK10771 99 GLKLNAAQREKLhaiarqmgIEDLLARL---------PGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1890659908 419 ARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWfDG 463
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAW-DG 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
271-453 |
4.67e-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: 59.90 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVIGQR----VLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMIH----------RDDGIVISPIV------ 330
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINglerptsgsvLVDGTDLTLLSgkelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 331 ---KIGYFSQNLDILEvEKSILENVQ------STSKQEetLIRTILARLHFF----RDDVYkPVEiLSGGERVKVALAKL 397
Cdd:cd03258 80 arrRIGMIFQHFNLLS-SRTVFENVAlpleiaGVPKAE--IEERVLELLELVgledKADAY-PAQ-LSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 398 FVSDVNTLILDEPTNFLDIEAARALESLL----QEYKGTVIFASHDRRFIENVATKMLVI 453
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLrdinRELGLTIVLITHEMEVVKRICDRVAVM 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
291-427 |
4.79e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHR--D--------DGIVISPIVK------IGYFSQnlDILEVEKSILENVQ- 353
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLIN-LLQRvfDpqsgriliDGTDIRTVTRaslrrnIAVVFQ--DAGLFNRSIEDNIRv 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 --STSKQEETLIRTILARLHFF---RDDVYKPV-----EILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR--- 420
Cdd:PRK13657 432 grPDATDEEMRAAAERAQAHDFierKPDGYDTVvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAkvk 511
|
....*...
gi 1890659908 421 -ALESLLQ 427
Cdd:PRK13657 512 aALDELMK 519
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
294-441 |
5.45e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.79 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTTLLKKMIHRDDG------IVISPIVK-------------IGYFSQNLdILEVEKSILENVQ- 353
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGssgevsLVGQPLHQmdeearaklrakhVGFVFQSF-MLIPTLNALENVEl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 ------STSKQEETLIRTILARLHFFRDDVYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEA----ARALE 423
Cdd:PRK10584 112 pallrgESSRQSRNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLF 190
|
170
....*....|....*...
gi 1890659908 424 SLLQEYKGTVIFASHDRR 441
Cdd:PRK10584 191 SLNREHGTTLILVTHDLQ 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
271-439 |
5.92e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVIS---PIVKIG--YFSQNLDIL 342
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKcfaRLLTPQSGTVFLgdkPISMLSsrQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 343 EVEKSILENVQ-----------------STSKQEETLIRTILARLHF--FRDdvyKPVEILSGGERVKVALAKLFVSDVN 403
Cdd:PRK11231 82 PQHHLTPEGITvrelvaygrspwlslwgRLSAEDNARVNQAMEQTRInhLAD---RRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1890659908 404 TLILDEPTNFLDIEAARALESLLQEYKG---TVIFASHD 439
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHD 197
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
271-455 |
7.49e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.75 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVI--GQRVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM--IH-------RDDGIVISPIV------KIG 333
Cdd:PRK13647 4 IIEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLngIYlpqrgrvKVMGREVNAENekwvrsKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 334 YFSQNLDILEVEKSILENV------QSTSKQE-ETLIRTILA--RLHFFRDdvyKPVEILSGGERVKVALAKLFVSDVNT 404
Cdd:PRK13647 83 LVFQDPDDQVFSSTVWDDVafgpvnMGLDKDEvERRVEEALKavRMWDFRD---KPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 405 LILDEPTNFLDIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQD 455
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKE 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
291-467 |
8.37e-10 |
|
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: 59.28 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVI---------SP--IVKIGY---FsQNLDILEvEKSILENVQ 353
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNlitGFYRPTSGRILfdgrditglPPhrIARLGIartF-QNPRLFP-ELTVLENVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 -------------------STSKQEETLIRTILARLHFFR--DDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPT- 411
Cdd:COG0411 102 vaaharlgrgllaallrlpRARREEREARERAEELLERVGlaDRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAa 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 412 --NFLDIEA-ARALESLLQEYKGTVIFASHDRRFIENVATKMLVI-QDKVIqwFDGTYQQ 467
Cdd:COG0411 182 glNPEETEElAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLdFGRVI--AEGTPAE 239
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
289-455 |
9.31e-10 |
|
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: 60.51 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 289 KTSFHVRGGDKLAVIGPNGSGKTTLLKKM----------IHRDD--------GIVISP-IVKIGYFSQNLDI---LEVEK 346
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIagltrpdegeIVLNGrtlfdsrkGIFLPPeKRRIGYVFQEARLfphLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 347 SIL-----ENVQSTSKQEETLIRtILARLHFFRddvyKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARA 421
Cdd:TIGR02142 95 NLRygmkrARPSERRISFERVIE-LLGIGHLLG----RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1890659908 422 ----LESLLQEYKGTVIFASHDRRFIENVATKMLVIQD 455
Cdd:TIGR02142 170 ilpyLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED 207
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
297-443 |
1.05e-09 |
|
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: 57.00 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 297 GDKLAVIGPNGSGKTTLLKKMIHRddgivispivkigYFSQNLDILEVEKSILENVQSTSKQEETLIRTILArlhffrdd 376
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARE-------------LGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS-------- 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890659908 377 vykpveiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAA---------RALESLLQEYKGTVIFASHDRRFI 443
Cdd:smart00382 61 -------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllleelRLLLLLKSEKNLTVILTTNDEKDL 129
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
291-440 |
1.07e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.11 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLkKMI----HRD------DGIVISPIV----KIGYFSQNLDI---LevekSILENV- 352
Cdd:COG3842 25 SLSIEPGEFVALLGPSGCGKTTLL-RMIagfeTPDsgrillDGRDVTGLPpekrNVGMVFQDYALfphL----TVAENVa 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 -----QSTSKQE-ETLIRTILARLHF--FRDDvyKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAAR 420
Cdd:COG3842 100 fglrmRGVPKAEiRARVAELLELVGLegLADR--YPHQ-LSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMRE 176
|
170 180
....*....|....*....|
gi 1890659908 421 ALESLLQEYKGTVIFASHDR 440
Cdd:COG3842 177 ELRRLQRELGITFIYVTHDQ 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-455 |
1.22e-09 |
|
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: 60.59 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNIL--AKKISPEQGSVLCRAqcGLLPQLKRIDAIKSG 81
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHV--ALCEKCGYVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 82 GEVTQSYMNALFSKAPKLLLADEPTTHLDREHIE-WLEKKLSQWKGAFVIVSHDRAFLDAlcttiwemdegkikEYKGNY 160
Cdd:TIGR03269 79 GEPCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAiMLQRTFALYGDDTVLDNVLEALEEI--------------GYEGKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 161 S-----DYLEQKELERRRQQSAYEQY--EKKKQALERAL--------------ELKKQKAERATKAPKKVSRSEANIMGA 219
Cdd:TIGR03269 145 AvgravDLIEMVQLSHRITHIARDLSggEKQRVVLARQLakepflfladeptgTLDPQTAKLVHNALEEAVKASGISMVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 220 KPYFAKKQKKLQKTAKAMETRL-----EKLEKVEKIKETAPinMSLPHEDTFQDRIIIRVEEVT--------GVIgQRVl 286
Cdd:TIGR03269 225 TSHWPEVIEDLSDKAIWLENGEikeegTPDEVVAVFMEGVS--EVEKECEVEVGEPIIKVRNVSkryisvdrGVV-KAV- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 287 wEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIHrddgiVISPI-----VKIG---------------YFSQNLDILEVE- 345
Cdd:TIGR03269 301 -DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG-----VLEPTsgevnVRVGdewvdmtkpgpdgrgRAKRYIGILHQEy 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 346 -----KSILENVQSTSKQE---ETLIRTILARLHFFRDDVYKPVEIL-------SGGERVKVALAKLFVSDVNTLILDEP 410
Cdd:TIGR03269 375 dlyphRTVLDNLTEAIGLElpdELARMKAVITLKMVGFDEEKAEEILdkypdelSEGERHRVALAQVLIKEPRIVILDEP 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1890659908 411 TNFLD-IEAARALESLL---QEYKGTVIFASHDRRFIENVATKMLVIQD 455
Cdd:TIGR03269 455 TGTMDpITKVDVTHSILkarEEMEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
271-453 |
1.34e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.57 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 271 IIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK-----KMIHRDDGIV-----ISPIVKI-------G 333
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinklEEITSGDLIVdglkvNDPKVDErlirqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 334 YFSQNLDILEvEKSILENV-------QSTSKQE-ETLIRTILARLHFF-RDDVYkPVEiLSGGERVKVALAKLFVSDVNT 404
Cdd:PRK09493 81 MVFQQFYLFP-HLTALENVmfgplrvRGASKEEaEKQARELLAKVGLAeRAHHY-PSE-LSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 405 LILDEPTNFLDI----EAARALESLLQEykG-TVIFASHDRRFIENVATKMLVI 453
Cdd:PRK09493 158 MLFDEPTSALDPelrhEVLKVMQDLAEE--GmTMVIVTHEIGFAEKVASRLIFI 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
284-455 |
1.36e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 284 RVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM----------IHRDDGIVI-----SPIVKIGyfsqnldilevekSI 348
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsgrIARPAGARVlflpqRPYLPLG-------------TL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 LENV---QSTSKQEETLIRTIL--ARLHFFRDDVYKPV---EILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR 420
Cdd:COG4178 443 REALlypATAEAFSDAELREALeaVGLGHLAERLDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522
|
170 180 190
....*....|....*....|....*....|....*..
gi 1890659908 421 ALESLLQE--YKGTVIFASHdRRFIENVATKMLVIQD 455
Cdd:COG4178 523 ALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTG 558
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
26-156 |
1.97e-09 |
|
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: 57.93 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 26 IYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSV--------LCRAQCGLLPQL---------------------KRID 76
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvrgrvssLLGLGGGFNPELtgreniylngrllglsrkeidEKID 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 77 AIKSGGEVTQSY----------MNA--LFSKA----PKLLLADEPTTHLDREHIEWLEKKLSQWK---GAFVIVSHDRAF 137
Cdd:cd03220 125 EIIEFSELGDFIdlpvktyssgMKArlAFAIAtalePDILLIDEVLAVGDAAFQEKCQRRLRELLkqgKTVILVSHDPSS 204
|
170
....*....|....*....
gi 1890659908 138 LDALCTTIWEMDEGKIKEY 156
Cdd:cd03220 205 IKRLCDRALVLEKGKIRFD 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
291-455 |
1.97e-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: 56.67 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVIspivkigyfsqnldILEVEKSILenvqSTSKQEETLIRTil 367
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILsglYKPDSGEIL--------------VDGKEVSFA----SPRDARRAGIAM-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 368 arlhffrddVYKpveiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKG---TVIFASHDRRFIE 444
Cdd:cd03216 80 ---------VYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVF 146
|
170
....*....|.
gi 1890659908 445 NVATKMLVIQD 455
Cdd:cd03216 147 EIADRVTVLRD 157
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-133 |
2.13e-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: 56.28 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQcgLLPQLKRIDAIKSGGE------VTQSYMNAL---FS 94
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--EVSFASPRDARRAGIAmvyqlsVGERQMVEIaraLA 98
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1890659908 95 KAPKLLLADEPTTHLDREHIEWLE---KKLSQWKGAFVIVSH 133
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFkviRRLRAQGVAVIFISH 140
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
299-454 |
2.27e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.28 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 299 KLAVIGPNGSGKTTLLKK---MIHRDDGIVI---SPIVK---------IGYFSQNLD--ILE--VEKSILENVQSTSKQE 359
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHfngILKPTSGSVLirgEPITKenirevrkfVGLVFQNPDdqIFSptVEQDIAFGPINLGLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 360 ETLIRTILARLHF-----FRDDVykpVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARAL----ESLLQEYK 430
Cdd:PRK13652 112 ETVAHRVSSALHMlgleeLRDRV---PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELidflNDLPETYG 188
|
170 180
....*....|....*....|....
gi 1890659908 431 GTVIFASHDRRFIENVATKMLVIQ 454
Cdd:PRK13652 189 MTVIFSTHQLDLVPEMADYIYVMD 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
227-467 |
2.35e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 60.14 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 227 QKKLQkTAKAMETRLEKLEKV--EKIKETAPINMSLPHEDTFQDRIiirveEVTGVIGQRVLwEKTSFHVRGGDKLAVIG 304
Cdd:TIGR01193 435 QPKLQ-AARVANNRLNEVYLVdsEFINKKKRTELNNLNGDIVINDV-----SYSYGYGSNIL-SDISLTIKMNSKTTIVG 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 305 PNGSGKTTLLKKMIHRDD---------GIVISPIVK------IGYFSQNLDILEveKSILENVQSTSKqEETLIRTILAR 369
Cdd:TIGR01193 508 MSGSGKSTLAKLLVGFFQarsgeillnGFSLKDIDRhtlrqfINYLPQEPYIFS--GSILENLLLGAK-ENVSQDEIWAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 370 LHF--FRDDVYK-----PVEI------LSGGERVKVALAKLFVSDVNTLILDEPTNFLD-IEAARALESLLQEYKGTVIF 435
Cdd:TIGR01193 585 CEIaeIKDDIENmplgyQTELseegssISGGQKQRIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIF 664
|
250 260 270
....*....|....*....|....*....|...
gi 1890659908 436 ASHdRRFIENVATKMLVIQD-KVIQwfDGTYQQ 467
Cdd:TIGR01193 665 VAH-RLSVAKQSDKIIVLDHgKIIE--QGSHDE 694
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
291-458 |
2.48e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.65 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRDDGIVIspivkigyfsqnLDILEVE----KSILENVQSTSKQEETLI 363
Cdd:PRK11176 363 NFKIPAGKTVALVGRSGSGKSTianLLTRFYDIDEGEIL------------LDGHDLRdytlASLRNQVALVSQNVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 364 RTILARLHFFRDDVYKPVEI------------------------------LSGGERVKVALAKLFVSDVNTLILDEPTNF 413
Cdd:PRK11176 431 DTIANNIAYARTEQYSREQIeeaarmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1890659908 414 LDIEAARALESLLQEYKG--TVIFASHDRRFIENvATKMLVIQDKVI 458
Cdd:PRK11176 511 LDTESERAIQAALDELQKnrTSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
265-437 |
2.94e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 265 TFQDRIIIrvEEVTGVIGQrvlwektsfhvrgGDKLAVIGPNGSGKTTLLKKMIHR------------DDGIVISPIVK- 331
Cdd:PLN03211 77 QIQERTIL--NGVTGMASP-------------GEILAVLGPSGSGKSTLLNALAGRiqgnnftgtilaNNRKPTKQILKr 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 332 IGYFSQNlDILEVEKSILENV---------QSTSKQEETLI-RTILARL------------HFFRDdvykpveiLSGGER 389
Cdd:PLN03211 142 TGFVTQD-DILYPHLTVRETLvfcsllrlpKSLTKQEKILVaESVISELgltkcentiignSFIRG--------ISGGER 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1890659908 390 VKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQE--YKGTVIFAS 437
Cdd:PLN03211 213 KRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSlaQKGKTIVTS 262
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
284-440 |
3.38e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 284 RVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIhrddGIVISPIVKIGYFSQNLD---------------------IL 342
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIA----GLLNPEKGEILFERQSIKkdlctyqkqlcfvghrsginpYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 343 EVEKSILENVQSTSKQEETlirTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARAL 422
Cdd:PRK13540 90 TLRENCLYDIHFSPGAVGI---TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|.
gi 1890659908 423 ESLLQEYK---GTVIFASHDR 440
Cdd:PRK13540 167 ITKIQEHRakgGAVLLTSHQD 187
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
291-438 |
3.83e-09 |
|
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: 56.41 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIHRDDGIVISPIVKIGYFSQNLDILeveKSILENVQstskQEETLIRTILAR- 369
Cdd:cd03213 29 SGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRSF---RKIIGYVP----QDDILHPTLTVRe 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 370 -LHFfrddvykPVEI--LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEY-KG--TVIFASH 438
Cdd:cd03213 102 tLMF-------AAKLrgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTgrTIICSIH 169
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
291-467 |
4.77e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.97 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRDDGIVI---SPIVKIG--YFSQNLDILEVE-----KSILENVQ---S 354
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPTGGQVLldgVPLVQYDhhYLHRQVALVGQEpvlfsGSVRENIAyglT 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 355 TSKQEETLIRTILARLHFF--------RDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLL 426
Cdd:TIGR00958 581 DTPDEEIMAAAKAANAHDFimefpngyDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESR 660
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1890659908 427 QEYKGTVIFASHDRRFIENvATKMLVI-QDKVIQWfdGTYQQ 467
Cdd:TIGR00958 661 SRASRTVLLIAHRLSTVER-ADQILVLkKGSVVEM--GTHKQ 699
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
32-153 |
5.04e-09 |
|
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: 56.34 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 32 IGLVGKNGSGKTTLLNILAKKISPEQGSV-----------------LCRAQCG-------LLPQL--------------- 72
Cdd:cd03255 33 VAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklsekelaaFRRRHIGfvfqsfnLLPDLtalenvelplllagv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 73 ----KRIDAIK------------------SGGE-----VTQSYMNAlfskaPKLLLADEPTTHLDREH---IEWLEKKLS 122
Cdd:cd03255 113 pkkeRRERAEEllervglgdrlnhypselSGGQqqrvaIARALAND-----PKIILADEPTGNLDSETgkeVMELLRELN 187
|
170 180 190
....*....|....*....|....*....|..
gi 1890659908 123 QWKG-AFVIVSHDRaFLDALCTTIWEMDEGKI 153
Cdd:cd03255 188 KEAGtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
291-439 |
5.25e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.43 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMI----HRDDGIVI--------SPIVKIGYfsqnldiLEVEKSILENVqstsKQ 358
Cdd:COG4152 21 SFTVPKGEIFGLLGPNGAGKTTTIR-IIlgilAPDSGEVLwdgepldpEDRRRIGY-------LPEERGLYPKM----KV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 359 EETLIRtiLARLH--------------FFRDDV----YKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR 420
Cdd:COG4152 89 GEQLVY--LARLKglskaeakrradewLERLGLgdraNKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVE 166
|
170 180
....*....|....*....|..
gi 1890659908 421 ALESLLQEYK--G-TVIFASHD 439
Cdd:COG4152 167 LLKDVIRELAakGtTVIFSSHQ 188
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
24-145 |
5.30e-09 |
|
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: 56.39 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSV--------LCRAQCGLLPQLKRID------------------- 76
Cdd:cd03235 20 FEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrvfgkpleKERKRIGYVPQRRSIDrdfpisvrdvvlmglyghk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 77 ----------------AIK---------------SGGEvTQsymNALFSKA----PKLLLADEPTTHLDREHIEWLEKKL 121
Cdd:cd03235 100 glfrrlskadkakvdeALErvglseladrqigelSGGQ-QQ---RVLLARAlvqdPDLLLLDEPFAGVDPKTQEDIYELL 175
|
170 180
....*....|....*....|....*..
gi 1890659908 122 SQWKG---AFVIVSHDRAFLDALCTTI 145
Cdd:cd03235 176 RELRRegmTILVVTHDLGLVLEYFDRV 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-107 |
6.18e-09 |
|
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: 54.96 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC-------------RAQCGLLPQ------------------- 71
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkslRKEIGYVFQdpqlfprltvrenlrlgll 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890659908 72 LKRIDAIKSGGEVTQ----------------------SY--------MNALFSKaPKLLLADEPTT 107
Cdd:pfam00005 86 LKGLSKREKDARAEEaleklglgdladrpvgerpgtlSGgqrqrvaiARALLTK-PKLLLLDEPTA 150
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
272-470 |
7.28e-09 |
|
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: 56.48 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLkKMI----HRDDG-IVIS--PIVKIGYFSQNLDI--- 341
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLL-RLIagfeTPTSGeILLDgkDITNLPPHKRPVNTvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 342 ---LEVEKSILENV------QSTSKQEetLIRTILARLHFFRDDVY---KPVEiLSGGERVKVALAKLFVSDVNTLILDE 409
Cdd:cd03300 80 nyaLFPHLTVFENIafglrlKKLPKAE--IKERVAEALDLVQLEGYanrKPSQ-LSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 410 PTNFLDI----EAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFDGTYQQYEQ 470
Cdd:cd03300 157 PLGALDLklrkDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
284-454 |
9.60e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 55.96 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 284 RVLWEKTSFHVRGGDKLAVIGPNGSGKTTLlKKMIHR----DDGIVISPIV------------KIGYFSQnlDILEVEKS 347
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTL-TKLIQRfyvpENGRVLVDGHdlaladpawlrrQVGVVLQ--ENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 348 ILENVQSTSK---QEETLIRTILARLHFFRDDVYKPVEI--------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDI 416
Cdd:cd03252 92 IRDNIALADPgmsMERVIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1890659908 417 EAARALESLLQEY-KG-TVIFASHDRRFIENvATKMLVIQ 454
Cdd:cd03252 172 ESEHAIMRNMHDIcAGrTVIIIAHRLSTVKN-ADRIIVME 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
272-467 |
1.03e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.02 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMI----HRDDGIV------ISPI----VKIGYFSQ 337
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLR-IIagleHQTSGHIrfhgtdVSRLhardRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 338 NLDILEvEKSILENVqstskqeeTLIRTILAR-----LHFFRDDVYKPVEI-------------LSGGERVKVALAKLFV 399
Cdd:PRK10851 82 HYALFR-HMTVFDNI--------AFGLTVLPRrerpnAAAIKAKVTQLLEMvqlahladrypaqLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 400 SDVNTLILDEPTNFLDI----EAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVIQWFdGTYQQ 467
Cdd:PRK10851 153 VEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQA-GTPDQ 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
297-445 |
1.04e-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: 54.67 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 297 GDKLAVIGPNGSGKTTLLKKmihrddgivispivkIGY-FSQNLDILEVEKSILENVQSTskqeetlirTILARLHFFRD 375
Cdd:cd03227 21 GSLTIITGPNGSGKSTILDA---------------IGLaLGGAQSATRRRSGVKAGCIVA---------AVSAELIFTRL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890659908 376 DvykpveiLSGGERVKVALAKLF----VSDVNTLILDEPTNFLDIEAARALESLLQEY---KGTVIFASHDRRFIEN 445
Cdd:cd03227 77 Q-------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHLPELAEL 146
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
291-438 |
1.09e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.34 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM--IHRDDG--IVI--------SPI----VKIGYFSQNLDILEvEKSILENV-- 352
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILsgVYQPDSgeILLdgepvrfrSPRdaqaAGIAIIHQELNLVP-NLSVAENIfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 --QSTS------KQEETLIRTILARLHFfRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALES 424
Cdd:COG1129 103 grEPRRgglidwRAMRRRARELLARLGL-DIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFR 181
|
170
....*....|....*..
gi 1890659908 425 LLQEYKG---TVIFASH 438
Cdd:COG1129 182 IIRRLKAqgvAIIYISH 198
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
291-410 |
1.15e-08 |
|
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: 55.74 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRDDGIV--------ISPI-----VKIGYFSQNLDI---LEVE---KSI 348
Cdd:TIGR04406 21 SLSVKSGEIVGLLGPNGAGKTTsfyMIVGLVRPDAGKIlidgqditHLPMherarLGIGYLPQEASIfrkLTVEeniMAV 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 349 LENVQSTSKQE-ETLIRTILARLHF--FRDdvyKPVEILSGGERVKVALAKLFVSDVNTLILDEP 410
Cdd:TIGR04406 101 LEIRKDLDRAErEERLEALLEEFQIshLRD---NKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-148 |
1.28e-08 |
|
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: 57.30 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 31 RIGLVGKNGSGKTTLLNILAKKISPEQGSVLC-------------RAQCGLLPQ--------------LKRIDA----IK 79
Cdd:TIGR02857 350 RVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladadadswRDQIAWVPQhpflfagtiaenirLARPDAsdaeIR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 80 ------------------------------SGGEVTQSYMNALFSKAPKLLLADEPTTHLDREHIEWLEKKLSQW-KGAF 128
Cdd:TIGR02857 430 ealeragldefvaalpqgldtpigeggaglSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGRT 509
|
170 180
....*....|....*....|.
gi 1890659908 129 V-IVSHDRAFLdALCTTIWEM 148
Cdd:TIGR02857 510 VlLVTHRLALA-ALADRIVVL 529
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
272-458 |
1.36e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.15 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVISPIVKIGYFSQNldilEVEKSI 348
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRtlsRLMTPAHGHVWLDGEHIQHYASK----EVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 LENVQSTSKQEETLIRTILARLHFFRDDVY-------------------------KPVEILSGGERVKVALAKLFVSDVN 403
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGRYPHQPLFtrwrkedeeavtkamqatgithladQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1890659908 404 TLILDEPTNFLDIEAARALESLLQEY---KGTVIFAS-HDRRFIENVATKMLVIQDKVI 458
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELnreKGYTLAAVlHDLNQACRYASHLIALREGKI 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-155 |
1.45e-08 |
|
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: 57.22 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC----------------RAQCGLLPQ--------LKRIDAI- 78
Cdd:COG1123 286 LTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdgkdltklsrrslrelRRRVQMVFQdpysslnpRMTVGDIi 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 79 ---------KSGGEVTQ-------------SYMNAL---FSK--------------APKLLLADEPTTHLD---REHIew 116
Cdd:COG1123 366 aeplrlhglLSRAERRErvaellervglppDLADRYpheLSGgqrqrvaiaralalEPKLLILDEPTSALDvsvQAQI-- 443
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1890659908 117 LE--KKLSQWKG-AFVIVSHDRAFLDALCTTIWEMDEGKIKE 155
Cdd:COG1123 444 LNllRDLQRELGlTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
291-464 |
1.48e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.25 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIV----ISPI-------VKIGY-FSQN---------LDILEVEK 346
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLtgiLVPTSGEVrvlgYVPFkrrkefaRRIGVvFGQRsqlwwdlpaIDSFRLLK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 347 SILEnvqsTSKQEetlirtILARLHFFRD--DV----YKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR 420
Cdd:COG4586 122 AIYR----IPDAE------YKKRLDELVEllDLgellDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1890659908 421 ALESLL----QEYKGTVIFASHDRRFIENVATKMLVI-QDKVIqwFDGT 464
Cdd:COG4586 192 AIREFLkeynRERGTTILLTSHDMDDIEALCDRVIVIdHGRII--YDGS 238
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-141 |
1.54e-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: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 9 VKHYVKDRLLFEIErlAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSV-LCRAQCGLLPQLKRIdaikSGGEVTQS 87
Cdd:cd03222 7 VKRYGVFFLLVELG--VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDeWDGITPVYKPQYIDL----SGGELQRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1890659908 88 YMNALFSKAPKLLLADEPTTHLD---REHIEWLEKKLSQ--WKGAFViVSHDRAFLDAL 141
Cdd:cd03222 81 AIAAALLRNATFYLFDEPSAYLDieqRLNAARAIRRLSEegKKTALV-VEHDLAVLDYL 138
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
272-464 |
1.57e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.82 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKT-----SFHVRGGDKLAVIGPNGSGKTTL---LKKMIHRDDGIVIspIVKIGYFSQNLDILE 343
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKaldnvNIEIEDGEFVGLIGHTGSGKSTLiqhLNGLLKPTSGKII--IDGVDITDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 344 VEKSILENVQSTSKQ--EETLIRTI---LARLHFFRDDVYKPV----EI---------------LSGGERVKVALAKLFV 399
Cdd:PRK13637 81 IRKKVGLVFQYPEYQlfEETIEKDIafgPINLGLSEEEIENRVkramNIvgldyedykdkspfeLSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 400 SDVNTLILDEPTNFLDI----EAARALESLLQEYKGTVIFASHDRRFIENVATKMLVI-QDKVIqwFDGT 464
Cdd:PRK13637 161 MEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMnKGKCE--LQGT 228
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
292-454 |
1.58e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 292 FHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDG---IVISPIVK------IGYFSqNLDILEVEKSILENVQ------ 353
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRvlaGLLHVESGqiqIDGKTATRgdrsrfMAYLG-HLPGLKADLSTLENLHflcglh 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 -STSKQEETLIRTILArLHFFRDDVykpVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEY--- 429
Cdd:PRK13543 111 gRRAKQMPGSALAIVG-LAGYEDTL---VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrg 186
|
170 180
....*....|....*....|....*
gi 1890659908 430 KGTVIFASHDRRFIENVATKMLVIQ 454
Cdd:PRK13543 187 GGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
294-454 |
1.68e-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: 54.12 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTTLLKKMIhrddGIVISpivkigyfsqnldileveksilenvqSTSKQEETLIRTilarlhff 373
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILA----GQLIP--------------------------NGDNDEWDGITP-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 374 rddVYKPVEI-LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIE----AARALESLLQEYKGTVIFASHDRRFIENVAT 448
Cdd:cd03222 64 ---VYKPQYIdLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLSD 140
|
....*.
gi 1890659908 449 KMLVIQ 454
Cdd:cd03222 141 RIHVFE 146
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
291-458 |
1.78e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.85 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTL---LKKMIHRDDGIVI---SPI-----------VKIGYFSQNLDILEVEKSILENVQ 353
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLflhFNGILKPTSGEVLikgEPIkydkksllevrKTVGIVFQNPDDQLFAPTVEEDVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 ------STSKQE-ETLIRTILARLHF--FRDdvyKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALES 424
Cdd:PRK13639 102 fgplnlGLSKEEvEKRVKEALKAVGMegFEN---KPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 1890659908 425 LLQEY--KG-TVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:PRK13639 179 LLYDLnkEGiTIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-158 |
1.95e-08 |
|
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: 54.51 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 9 VKHYVKDRLLFEIErlAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL------------CRAQCGLLPQ----- 71
Cdd:cd03264 7 TKRYGKKRALDGVS--LTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkqpqkLRRRIGYLPQefgvy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 --------------LKRIDAIK-------------------------SGGEVTQSYMNALFSKAPKLLLADEPTTHLD-- 110
Cdd:cd03264 85 pnftvrefldyiawLKGIPSKEvkarvdevlelvnlgdrakkkigslSGGMRRRVGIAQALVGDPSILIVDEPTAGLDpe 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1890659908 111 -REHIEWLEKKLSqwKGAFVIVS-HDRAFLDALCTTIWEMDEGKIKeYKG 158
Cdd:cd03264 165 eRIRFRNLLSELG--EDRIVILStHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
291-438 |
2.00e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.98 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIHRD-DGIVISPIVKigyfsqnLDILEVEKSILENVQSTSKQEETLIRTILAR 369
Cdd:TIGR00955 45 SGVAKPGELLAVMGSSGAGKTTLMNALAFRSpKGVKGSGSVL-------LNGMPIDAKEMRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 370 LHF-----FR--DDVYK----------------------------PVEILSGGERVKVALAKLFVSDVNTLILDEPTNFL 414
Cdd:TIGR00955 118 EHLmfqahLRmpRRVTKkekrervdevlqalglrkcantrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180
....*....|....*....|....*....
gi 1890659908 415 DIEAA----RALESLLQeyKG-TVIFASH 438
Cdd:TIGR00955 198 DSFMAysvvQVLKGLAQ--KGkTIICTIH 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-153 |
2.14e-08 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 55.07 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNV-KHYVKDRLL----FEIERLAIYendriGLVGKNGSGKTTLLNILAKKISPEQGSVL------------CRAQC 66
Cdd:COG1131 1 IEVRGLtKRYGDKTALdgvsLTVEPGEIF-----GLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardpaeVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 67 GLLPQ-------------LKRIDAIK--SGGEVTQSYMNAL---------------FSK--------------APKLLLA 102
Cdd:COG1131 76 GYVPQepalypdltvrenLRFFARLYglPRKEARERIDELLelfgltdaadrkvgtLSGgmkqrlglalallhDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 103 DEPTTHLD-------REHIewleKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:COG1131 156 DEPTSGLDpearrelWELL----RELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
291-447 |
2.55e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 55.41 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIH---------RDDGIVISPIV------KIGYFSQNLDILEVEKSI------- 348
Cdd:PRK13635 27 SFSVYEGEWVAIVGHNGSGKSTLAKLLNGlllpeagtiTVGGMVLSEETvwdvrrQVGMVFQNPDNQFVGATVqddvafg 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 LENVQSTSKQEETLIRTILARLHF--FRDdvYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAARAL 422
Cdd:PRK13635 107 LENIGVPREEMVERVDQALRQVGMedFLN--REPHR-LSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETV 183
|
170 180
....*....|....*....|....*
gi 1890659908 423 ESLLQEYKGTVIFASHDrrfIENVA 447
Cdd:PRK13635 184 RQLKEQKGITVLSITHD---LDEAA 205
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-145 |
2.80e-08 |
|
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: 53.15 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 29 NDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL--------CRAQCGLLPQLKRIDAIKSGGEVTQSYMNAL-FSKAPKL 99
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedilEEVLDQLLLIIVGGKKASGSGELRLRLALALaRKLKPDV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 100 LLADEPTTHLDRE---------HIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTI 145
Cdd:smart00382 82 LILDEITSLLDAEqeallllleELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
291-439 |
4.14e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.05 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIHRD---DGIVI---SPIVK-------------IGYFSQNLDILEvEKSILEN 351
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDtptSGDVIfngQPMSKlssaakaelrnqkLGFIYQFHHLLP-DFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 V-------QSTSKQEETLIRTILARLHFFRDDVYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALES 424
Cdd:PRK11629 108 VamplligKKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170
....*....|....*....
gi 1890659908 425 LLQEY---KGTV-IFASHD 439
Cdd:PRK11629 187 LLGELnrlQGTAfLVVTHD 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
272-458 |
4.22e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 53.30 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMIHRDDGIVISPIVKIgyfsQNLDILEVEKsilen 351
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILF----KGEDITDLPP----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 vqstskqEETlirtilARLHFFRDDVYkPVEI---------------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDI 416
Cdd:cd03217 72 -------EER------ARLGIFLAFQY-PPEIpgvknadflryvnegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1890659908 417 EA----ARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:cd03217 138 DAlrlvAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRI 183
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
245-438 |
5.11e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.53 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 245 EKVEKIKETAPINMSLPHEDTFQDRI-IIRVEEVTGVI--GQrVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK------ 315
Cdd:TIGR00954 424 EEIESGREGGRNSNLVPGRGIVEYQDnGIKFENIPLVTpnGD-VLIESLSFEVPSGNNLLICGPNGCGKSSLFRilgelw 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 316 -------------KMIH------------RDDgiVISPIVKIGYFSQNLDILEVEKsILENVQSTSkqeetlirtILARL 370
Cdd:TIGR00954 503 pvyggrltkpakgKLFYvpqrpymtlgtlRDQ--IIYPDSSEDMKRRGLSDKDLEQ-ILDNVQLTH---------ILERE 570
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 371 HFFrDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASH 438
Cdd:TIGR00954 571 GGW-SAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-155 |
6.30e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 53.59 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 3 LLEALNVKHYVKDR-----LLFEIErLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSV----------------- 60
Cdd:COG4181 8 IIELRGLTKTVGTGageltILKGIS-LEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVrlagqdlfaldedarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 61 LCRAQCG-------LLPQL--------------------------------KRIDAIK---SGGE---VtqsymnAL--- 92
Cdd:COG4181 87 LRARHVGfvfqsfqLLPTLtalenvmlplelagrrdarararallervglgHRLDHYPaqlSGGEqqrV------ALara 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890659908 93 FSKAPKLLLADEPTTHLDR---EHIEWLEKKLSQWKGA-FVIVSHDRAfLDALCTTIWEMDEGKIKE 155
Cdd:COG4181 161 FATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGTtLVLVTHDPA-LAARCDRVLRLRAGRLVE 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
291-464 |
7.29e-08 |
|
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: 52.86 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMI---HRDDGIVISPiVKIGYFSQNLDILevEKSILENVQSTSKQEETLIRTIL 367
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLgelEKLSGSVSVP-GSIAYVSQEPWIQ--NGTIRENILFGKPFDEERYEKVI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 368 ARLHFFRDdvykpVEI---------------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARAL-ESLLQEY-- 429
Cdd:cd03250 102 KACALEPD-----LEIlpdgdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLll 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1890659908 430 -KGTVIFASHDRRFIENVatkmlviqDKVIQWFDGT 464
Cdd:cd03250 177 nNKTRILVTHQLQLLPHA--------DQIVVLDNGR 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
272-458 |
8.01e-08 |
|
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: 53.14 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDG--------IVISPI---VKIGYFSQ 337
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKmltTLLKPTSGratvaghdVVREPRevrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 338 NLdILEVEKSILENVQSTSK----QEETLIRTILARLHF-----FRDdvyKPVEILSGGERVKVALAKLFVSDVNTLILD 408
Cdd:cd03265 81 DL-SVDDELTGWENLYIHARlygvPGAERRERIDELLDFvglleAAD---RLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 409 EPTNFLDIEAARAL----ESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:cd03265 157 EPTIGLDPQTRAHVweyiEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
24-154 |
8.28e-08 |
|
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: 52.89 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC--------RAQC----GLLPQ-------------------L 72
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngysirtdRKAArqslGYCPQfdalfdeltvrehlrfyarL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 73 KRI--DAIKSGGEVTQSYMNaLFSKA------------------------PKLLLADEPTTHLD---REHIeW-LEKKLS 122
Cdd:cd03263 103 KGLpkSEIKEEVELLLRVLG-LTDKAnkrartlsggmkrklslaialiggPSVLLLDEPTSGLDpasRRAI-WdLILEVR 180
|
170 180 190
....*....|....*....|....*....|..
gi 1890659908 123 QWKgAFVIVSHDRAFLDALCTTIWEMDEGKIK 154
Cdd:cd03263 181 KGR-SIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
297-457 |
9.14e-08 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 52.66 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 297 GDKLAVI-GPNGSGKTTLLKKMI------------HRDDGIVISPIVKIG----YFSQNLDILEVEKSILENvqstskqE 359
Cdd:cd03279 27 NNGLFLIcGPTGAGKSTILDAITyalygktprygrQENLRSVFAPGEDTAevsfTFQLGGKKYRVERSRGLD-------Y 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 360 ETLIRTILARLHFFRDDVYKPVEILSGGERVKVALA-KLFVSDV---------NTLILDEPTNFLDIEAARALESLLQEY 429
Cdd:cd03279 100 DQFTRIVLLPQGEFDRFLARPVSTLSGGETFLASLSlALALSEVlqnrggarlEALFIDEGFGTLDPEALEAVATALELI 179
|
170 180 190
....*....|....*....|....*....|.
gi 1890659908 430 KGT---VIFASHDRRFIENVATKMLVIQDKV 457
Cdd:cd03279 180 RTEnrmVGVISHVEELKERIPQRLEVIKTPG 210
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
33-153 |
9.68e-08 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 53.28 E-value: 9.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 33 GLVGKNGSGKTTLLNILAKKISPEQGSVL------------CRA-QCGLLPQ---------------LKRI--------- 75
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrrARArRVALVEQdsdtavpltvrdvvaLGRIphrslwagd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 76 ----DAIK--------------------SGGEVTQSYMNALFSKAPKLLLADEPTTHLD-REHIEWLE--KKLSQWKGAF 128
Cdd:TIGR03873 111 sphdAAVVdralartelshladrdmstlSGGERQRVHVARALAQEPKLLLLDEPTNHLDvRAQLETLAlvRELAATGVTV 190
|
170 180
....*....|....*....|....*
gi 1890659908 129 VIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:TIGR03873 191 VAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
24-134 |
1.03e-07 |
|
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: 52.86 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL--------CRAQCGLLPQ-------------------LKRID 76
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgPGPDRGYVFQqdallpwltvldnvalgleLQGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 77 AiKSGGEVTQSYMNAL----FSKA----------------------PKLLLADEPTTHLD---REHI-EWLEKKLSQWKG 126
Cdd:cd03293 105 K-AEARERAEELLELVglsgFENAyphqlsggmrqrvalaralavdPDVLLLDEPFSALDaltREQLqEELLDIWRETGK 183
|
....*...
gi 1890659908 127 AFVIVSHD 134
Cdd:cd03293 184 TVLLVTHD 191
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
294-439 |
1.10e-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: 53.14 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTTLLK----KMI-----HRD----DGIV-------------------ISPIVKigyfSQNLDI 341
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKilagKLKpnlgkFDDppdwDEILdefrgselqnyftkllegdVKVIVK----PQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 342 L--EVEKS---ILENVQSTSKQEETLIRTILARLhffrddVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDI 416
Cdd:cd03236 99 IpkAVKGKvgeLLKKKDERGKLDELVDQLELRHV------LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*..
gi 1890659908 417 ----EAARALESLLQEYKgTVIFASHD 439
Cdd:cd03236 173 kqrlNAARLIRELAEDDN-YVLVVEHD 198
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
291-439 |
1.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRDDG-IVISPIV-----------KIGYFSQNLDI----LEVEKSI--- 348
Cdd:PRK13650 27 SFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAESGqIIIDGDLlteenvwdirhKIGMVFQNPDNqfvgATVEDDVafg 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 LENvQSTSKQEetLIRTILARLHFFRDDVYKPVEI--LSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAARAL 422
Cdd:PRK13650 107 LEN-KGIPHEE--MKERVNEALELVGMQDFKEREParLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTI 183
|
170
....*....|....*..
gi 1890659908 423 ESLLQEYKGTVIFASHD 439
Cdd:PRK13650 184 KGIRDDYQMTVISITHD 200
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
282-441 |
1.29e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.59 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 282 GQRVLwEKTSFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRDDG--------IVISPIVK-----IGYFSQNLDILEvE 345
Cdd:PRK10895 15 GRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGniiiddedISLLPLHArarrgIGYLPQEASIFR-R 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 346 KSILENVQS--------TSKQEETLIRTILARLHF--FRDDVYKPveiLSGGERVKVALAKLFVSDVNTLILDEPTNFLD 415
Cdd:PRK10895 93 LSVYDNLMAvlqirddlSAEQREDRANELMEEFHIehLRDSMGQS---LSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190
....*....|....*....|....*....|
gi 1890659908 416 ----IEAARALESlLQEYKGTVIFASHDRR 441
Cdd:PRK10895 170 pisvIDIKRIIEH-LRDSGLGVLITDHNVR 198
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
272-411 |
1.30e-07 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 52.44 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQ-RVLWEkTSFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDGIVI---------SP--IVK--IGY 334
Cdd:cd03224 1 LEVENLNAGYGKsQILFG-VSLTVPEGEIVALLGRNGAGKTTLLKtimGLLPPRSGSIRfdgrditglPPheRARagIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 335 FSQNLDI---LEVEKSIL--ENVQSTSKQEETLIRtILA---RLHFFRDdvyKPVEILSGGERVKVALAKLFVSDVNTLI 406
Cdd:cd03224 80 VPEGRRIfpeLTVEENLLlgAYARRRAKRKARLER-VYElfpRLKERRK---QLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
....*
gi 1890659908 407 LDEPT 411
Cdd:cd03224 156 LDEPS 160
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
291-438 |
1.59e-07 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 52.11 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTL---LKKMIHRDDG-IVIS--PIVKIG----------------YFS----QNLDILEv 344
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLllaLFRLVELSSGsILIDgvDISKIGlhdlrsrisiipqdpvLFSgtirSNLDPFG- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 345 EKS------ILENVQstskqeetLIRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEA 418
Cdd:cd03244 103 EYSdeelwqALERVG--------LKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180
....*....|....*....|..
gi 1890659908 419 ARALESLLQEY-KG-TVIFASH 438
Cdd:cd03244 175 DALIQKTIREAfKDcTVLTIAH 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
272-458 |
1.72e-07 |
|
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: 53.65 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK-----KMIHRDDGIVISPIV---KIGYF-------- 335
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHvlrgmDQYEPTSGRIIYHVAlceKCGYVerpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 336 ----------SQNLDILEVEKSILENV--------QSTSK--QEETLIRTILARLHFF----RDDVYKPVEI-------- 383
Cdd:TIGR03269 81 pcpvcggtlePEEVDFWNLSDKLRRRIrkriaimlQRTFAlyGDDTVLDNVLEALEEIgyegKEAVGRAVDLiemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 384 --------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR----ALESLLQEYKGTVIFASHDRRFIENVATKML 451
Cdd:TIGR03269 161 rithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKlvhnALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
....*..
gi 1890659908 452 VIQDKVI 458
Cdd:TIGR03269 241 WLENGEI 247
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
272-410 |
1.77e-07 |
|
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: 52.16 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVI--------SPIVK-----IGYF 335
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIvglVKPDSGKILldgqditkLPMHKrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 336 SQNLDI---LEVE---KSILENVQSTSKQEETLIRTILARLHF--FRDdvyKPVEILSGGERVKVALAKLFVSDVNTLIL 407
Cdd:cd03218 81 PQEASIfrkLTVEeniLAVLEIRGLSKKEREEKLEELLEEFHIthLRK---SKASSLSGGERRRVEIARALATNPKFLLL 157
|
...
gi 1890659908 408 DEP 410
Cdd:cd03218 158 DEP 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
291-438 |
1.94e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLK---KMIHRDDG-IVI--------SPIV----KIG----YFS--QNLdilevekSI 348
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKilyGLYQPDSGeILIdgkpvrirSPRDaialGIGmvhqHFMlvPNL-------TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 LENV----------QSTSKQEETLIRTILARLHFfRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEA 418
Cdd:COG3845 98 AENIvlgleptkggRLDRKAARARIRELSERYGL-DVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQE 176
|
170 180
....*....|....*....|...
gi 1890659908 419 ARALESLLQEYKG---TVIFASH 438
Cdd:COG3845 177 ADELFEILRRLAAegkSIIFITH 199
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
291-454 |
1.99e-07 |
|
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: 52.09 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRDDGIVI---SPI--VKIGYFSQNLDILEVE-----KSILENVQ---S 354
Cdd:cd03248 34 SFTLHPGEVTALVGPSGSGKSTvvaLLENFYQPQGGQVLldgKPIsqYEHKYLHSKVSLVGQEpvlfaRSLQDNIAyglQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 355 TSKQEETLIRTILARLHFF--------RDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLL 426
Cdd:cd03248 114 SCSFECVKEAAQKAHAHSFiselasgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
|
170 180 190
....*....|....*....|....*....|
gi 1890659908 427 QEY--KGTVIFASHDRRFIENvATKMLVIQ 454
Cdd:cd03248 194 YDWpeRRTVLVIAHRLSTVER-ADQILVLD 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
32-110 |
2.23e-07 |
|
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: 51.40 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 32 IGLVGKNGSGKTTLLNILAKKISPEQ--GSVLC----------RAQCGLLPQ-------------------LKRIdaikS 80
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLIngrpldkrsfRKIIGYVPQddilhptltvretlmfaakLRGL----S 113
|
90 100 110
....*....|....*....|....*....|.
gi 1890659908 81 GGEVTQ-SYMNALFSKaPKLLLADEPTTHLD 110
Cdd:cd03213 114 GGERKRvSIALELVSN-PSLLFLDEPTSGLD 143
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
291-439 |
2.36e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.06 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIhrddGIVISPIVKIGYFSQ---NLDILEVEKSI------------------- 348
Cdd:PRK13648 29 SFNIPKGQWTSIVGHNGSGKSTIAKLMI----GIEKVKSGEIFYNNQaitDDNFEKLRKHIgivfqnpdnqfvgsivkyd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 ----LENVQSTSKQEETLIRTILARLHFFRDDVYKPvEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALES 424
Cdd:PRK13648 105 vafgLENHAVPYDEMHRRVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170
....*....|....*....
gi 1890659908 425 LLQEYKG----TVIFASHD 439
Cdd:PRK13648 184 LVRKVKSehniTIISITHD 202
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-155 |
2.69e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 51.59 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 1 MILLEalNV-KHYVKDRLL-----FEIERlaiyendriG----LVGKNGSGKTTLLNILAKKISPEQGSV---------L 61
Cdd:COG2884 1 MIRFE--NVsKRYPGGREAlsdvsLEIEK---------GefvfLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 62 CRAQ--------------CGLLPQL---------------------KRIDAI--------K--------SGGEvtQ---S 87
Cdd:COG2884 70 KRREipylrrrigvvfqdFRLLPDRtvyenvalplrvtgksrkeirRRVREVldlvglsdKakalphelSGGE--QqrvA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890659908 88 YMNALFSKaPKLLLADEPTTHLDREH-IEWLE--KKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKE 155
Cdd:COG2884 148 IARALVNR-PELLLADEPTGNLDPETsWEIMEllEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
281-447 |
2.94e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.97 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 281 IGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMIHRDDGIVISPIV---KIGYFSQNL---DILEVEK-------- 346
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLK-VLNRLIEIYDSKIKvdgKVLYFGKDIfqiDAIKLRKevgmvfqq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 347 -------SILENV----QSTSKQEETLIRTI----LARLHFFR---DDVYKPVEILSGGERVKVALAKLFVSDVNTLILD 408
Cdd:PRK14246 99 pnpfphlSIYDNIayplKSHGIKEKREIKKIveecLRKVGLWKevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1890659908 409 EPTNFLDIEAARALESLLQEYKG--TVIFASHDRRFIENVA 447
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVA 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-153 |
3.24e-07 |
|
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: 50.99 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNVKHYVKDRllfEIER---LAIYENDRIGLVGKNGSGKTTLLNILAKKISPE--QGSVLC------------RAQC 66
Cdd:cd03217 1 LEIKDLHVSVGGK---EILKgvnLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFkgeditdlppeeRARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 67 GL---------LPQLKRIDAIK------SGGEVTQSYMNALFSKAPKLLLADEPTTHLDREHIEWLEKKLSQWKG---AF 128
Cdd:cd03217 78 GIflafqyppeIPGVKNADFLRyvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSV 157
|
170 180
....*....|....*....|....*.
gi 1890659908 129 VIVSHDRAFLDAL-CTTIWEMDEGKI 153
Cdd:cd03217 158 LIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
261-439 |
3.45e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.71 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 261 PHEDTfqdriIIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMIHR----DDGIVI---SPIV--- 330
Cdd:PRK10575 6 NHSDT-----TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRhqppSEGEILldaQPLEsws 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 331 ------KIGYFSQNLDILEvEKSILENV----------------QSTSKQEETLIRTILARLhffrddVYKPVEILSGGE 388
Cdd:PRK10575 80 skafarKVAYLPQQLPAAE-GMTVRELVaigrypwhgalgrfgaADREKVEEAISLVGLKPL------AHRLVDSLSGGE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 389 RVKVALAKLFVSDVNTLILDEPTNFLDI----EAARALESLLQEYKGTVIFASHD 439
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
384-458 |
3.50e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 3.50e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890659908 384 LSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
291-510 |
3.66e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRDDG----IVISPIV-----------KIGYFSQNLDILEVEKSI---- 348
Cdd:PRK13640 27 SFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNpnskITVDGITltaktvwdireKVGIVFQNPDNQFVGATVgddv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 ---LENVQSTSKQEETLIRTILARLHFFRDDVYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESL 425
Cdd:PRK13640 107 afgLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPAN-LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 426 ---LQEYKG-TVIFASHDrrfIE--NVATKMLVIQDKVIQWFDGTYQQYEQHVRQKDRHADTQADQRLLLETKMSEVLSR 499
Cdd:PRK13640 186 irkLKKKNNlTVISITHD---IDeaNMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDIPFVYKLKNKLKEKGISVP 262
|
250
....*....|.
gi 1890659908 500 LSMEPSEELEK 510
Cdd:PRK13640 263 QEINTEEKLVQ 273
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
291-467 |
4.18e-07 |
|
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: 51.00 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHR--D--------DGIVISPIV------KIGYFSQNLDILEVekSILENV-- 352
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVS-LLERfyDptsgeillDGVDIRDLNlrwlrsQIGLVSQEPVLFDG--TIAENIry 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 ---QSTSKQEETLIRtiLARLHFFRD---DVYKPV-----EILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARA 421
Cdd:cd03249 100 gkpDATDEEVEEAAK--KANIHDFIMslpDGYDTLvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1890659908 422 LESLLQEYKG--TVIFASHDRRFIENvATKMLVIQD-KVIQwfDGTYQQ 467
Cdd:cd03249 178 VQEALDRAMKgrTTIVIAHRLSTIRN-ADLIAVLQNgQVVE--QGTHDE 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
291-459 |
5.06e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 51.61 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMI----HRDDGIVIspivkIGyfsqNLDILEVE------------------KSI 348
Cdd:COG3839 23 DLDIEDGEFLVLLGPSGCGKSTLLR-MIagleDPTSGEIL-----IG----GRDVTDLPpkdrniamvfqsyalyphMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 LENVQS------TSKQE---------ETL-IRTILARlhffrddvyKPVEiLSGGERVKVALAKLFVSDVNTLILDEP-T 411
Cdd:COG3839 93 YENIAFplklrkVPKAEidrrvreaaELLgLEDLLDR---------KPKQ-LSGGQRQRVALGRALVREPKVFLLDEPlS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 412 NfLDI---EAARA-LESLLQEYKGTVIFASHDRrfIE--NVATKMLVIQDKVIQ 459
Cdd:COG3839 163 N-LDAklrVEMRAeIKRLHRRLGTTTIYVTHDQ--VEamTLADRIAVMNDGRIQ 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
291-436 |
6.47e-07 |
|
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: 49.95 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHRDDGIVISPIVKIGYfsQNLDILEVEKS----ILENVQSTSKQEE-TLIRT 365
Cdd:cd03233 27 SGVVKPGEMVLVLGRPGSGCSTLLK-ALANRTEGNVSVEGDIHY--NGIPYKEFAEKypgeIIYVSEEDVHFPTlTVRET 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 366 ILARLHFFRDDVykpVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAARALESLLQEYKGTVIFA 436
Cdd:cd03233 104 LDFALRCKGNEF---VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDsstaLEILKCIRTMADVLKTTTFVS 175
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
282-439 |
6.84e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.85 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 282 GQRVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLKKM----------IHRDDGIVISPIVKIGYFSQNlDILEVEKSILEN 351
Cdd:PRK11248 13 GKPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIagfvpyqhgsITLDGKPVEGPGAERGVVFQN-EGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 V------QSTSK-QEETLIRTILARLHFFRDDvYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALES 424
Cdd:PRK11248 91 VafglqlAGVEKmQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170
....*....|....*....
gi 1890659908 425 LL----QEYKGTVIFASHD 439
Cdd:PRK11248 170 LLlklwQETGKQVLLITHD 188
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
290-439 |
6.86e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.04 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 290 TSFHVRGGDKLAVIGPNGSGKTTLLKKMI------HRDDGIVISPIVK------IGYFSQNLDILEVEKSILENV----- 352
Cdd:PRK15056 26 ASFTVPGGSIAALVGVNGSGKSTLFKALMgfvrlaSGKISILGQPTRQalqknlVAYVPQSEEVDWSFPVLVEDVvmmgr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 -------QSTSKQEETLIRTILARLHFFrDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESL 425
Cdd:PRK15056 106 yghmgwlRRAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISL 184
|
170
....*....|....*..
gi 1890659908 426 LQEYKG---TVIFASHD 439
Cdd:PRK15056 185 LRELRDegkTMLVSTHN 201
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-141 |
8.26e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.96 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 1 MILLEALNV-----KHYVKDRLLFEIErlaiyENDRIGLVGKNGSGKTTLLNILAKKIS--PEQGSV-LCRAQCGllPQL 72
Cdd:COG2401 28 AIVLEAFGVelrvvERYVLRDLNLEIE-----PGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVdVPDNQFG--REA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 73 KRIDAIKSGGEVTQS--YMNA----------------------------LFSKAPKLLLADEPTTHLDREHIEWLEKKLS 122
Cdd:COG2401 101 SLIDAIGRKGDFKDAveLLNAvglsdavlwlrrfkelstgqkfrfrlalLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170 180
....*....|....*....|...
gi 1890659908 123 ----QWKGAFVIVSHDRAFLDAL 141
Cdd:COG2401 181 klarRAGITLVVATHHYDVIDDL 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
291-438 |
8.37e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 51.75 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkMIHR----DDG-IVIS--PIVK---------IGYFSQNLDILEveKSILENVQ- 353
Cdd:PRK11160 360 SLQIKAGEKVALLGRTGCGKSTLLQ-LLTRawdpQQGeILLNgqPIADyseaalrqaISVVSQRVHLFS--ATLRDNLLl 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 -STSKQEETLIrTILAR--LHFFRDDvYKPVEI--------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARAL 422
Cdd:PRK11160 437 aAPNASDEALI-EVLQQvgLEKLLED-DKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQI 514
|
170
....*....|....*...
gi 1890659908 423 ESLLQEY-KG-TVIFASH 438
Cdd:PRK11160 515 LELLAEHaQNkTVLMITH 532
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-155 |
8.70e-07 |
|
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: 49.23 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC------------RAQCGLLPQ---------LKRIDAIKSGG 82
Cdd:cd03247 23 LELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgvpvsdlekalSSLISVLNQrpylfdttlRNNLGRRFSGG 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890659908 83 EVTQ-SYMNALFSKAPKLLLaDEPTTHLDRE-HIEWLEKKLSQWKGAFVI-VSHDRAFLDALcTTIWEMDEGKIKE 155
Cdd:cd03247 103 ERQRlALARILLQDAPIVLL-DEPTVGLDPItERQLLSLIFEVLKDKTLIwITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
379-439 |
8.74e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 8.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 379 KPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDI----EAARALESLLQEYKgTVIFASHD 439
Cdd:COG1245 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrlNVARLIRELAEEGK-YVLVVEHD 271
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
8-134 |
8.82e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.56 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 8 NVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQ-------------CGLLPQ--- 71
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQqlp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 ---------------------LKRI---------DAIK---------------SGGEVTQSYMNALFSKAPKLLLADEPT 106
Cdd:PRK10575 96 aaegmtvrelvaigrypwhgaLGRFgaadrekveEAISlvglkplahrlvdslSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190
....*....|....*....|....*....|..
gi 1890659908 107 THLDREH---IEWLEKKLSQWKGAFVI-VSHD 134
Cdd:PRK10575 176 SALDIAHqvdVLALVHRLSQERGLTVIaVLHD 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
302-458 |
1.24e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.39 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 302 VIGPNGSGKTTllkkMIHRDDGIVIS----PIVKIGYFSQNLDILEVEKSILENV----QSTSKQ--EETLIRTI-LARL 370
Cdd:PRK13645 42 VIGTTGSGKST----MIQLTNGLIISetgqTIVGDYAIPANLKKIKEVKRLRKEIglvfQFPEYQlfQETIEKDIaFGPV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 371 HFFRD--DVYK-------------------PVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR----ALESL 425
Cdd:PRK13645 118 NLGENkqEAYKkvpellklvqlpedyvkrsPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERL 196
|
170 180 190
....*....|....*....|....*....|....
gi 1890659908 426 LQEYKGTVIFASHDRRFIENVATKMLVIQD-KVI 458
Cdd:PRK13645 197 NKEYKKRIIMVTHNMDQVLRIADEVIVMHEgKVI 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
291-452 |
1.25e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTL--LKKMIH--------------------------RDDGIV-------ISPIVKIGyf 335
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLarLLTMIEtptggelyyqgqdllkadpeaqkllrQKIQIVfqnpygsLNPRKKVG-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 336 sqnlDILEveKSILENVQSTSKQEETLIRTILARL-----HFFRddvYkPvEILSGGERVKVALAKLFVSDVNTLILDEP 410
Cdd:PRK11308 113 ----QILE--EPLLINTSLSAAERREKALAMMAKVglrpeHYDR---Y-P-HMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1890659908 411 TNFLDIeAARA-----LESLLQEYKGTVIFASHDRRFIENVATKMLV 452
Cdd:PRK11308 182 VSALDV-SVQAqvlnlMMDLQQELGLSYVFISHDLSVVEHIADEVMV 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
291-458 |
1.35e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 49.61 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLkKMIHR----DDG-IVISPiVKIGYFSQNLDILEVE-------------KSILEN- 351
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLL-RCINLleepDSGtITVDG-EDLTDSKKDINKLRRKvgmvfqqfnlfphLTVLENv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 ------VQSTSKQE-ETLIRTILAR---LHffRDDVYkPVEiLSGGE--RVKVA--LA---KLfvsdvntLILDEPTNFL 414
Cdd:COG1126 99 tlapikVKKMSKAEaEERAMELLERvglAD--KADAY-PAQ-LSGGQqqRVAIAraLAmepKV-------MLFDEPTSAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1890659908 415 DIEAAR----ALESLLQEykG-TVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:COG1126 168 DPELVGevldVMRDLAKE--GmTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
282-439 |
1.37e-06 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 49.95 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 282 GQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMIHR----------DDGIVISPIV----------KIGYFSQNLDI 341
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLR-CINRlieptsgkvlIDGQDIAAMSrkelrelrrkKISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 342 LEvEKSILEN------VQSTSKQE--ETLIRTI-LARLHFFRDdvYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTN 412
Cdd:cd03294 114 LP-HRTVLENvafgleVQGVPRAEreERAAEALeLVGLEGWEH--KYPDE-LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190
....*....|....*....|....*....|.
gi 1890659908 413 FLD----IEAARALESLLQEYKGTVIFASHD 439
Cdd:cd03294 190 ALDplirREMQDELLRLQAELQKTIVFITHD 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-153 |
1.41e-06 |
|
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: 49.36 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC------------RAQCG---------LLPQLKRIDAIKSGG 82
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdgeditglppheIARLGigrtfqiprLFPELTVLENVMVAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 83 EVTQSYMNALFSKA-----------------------------------------------PKLLLADEPT---THLDRE 112
Cdd:cd03219 101 QARTGSGLLLARARreereareraeellervgladladrpagelsygqqrrleiaralatdPKLLLLDEPAaglNPEETE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1890659908 113 HIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:cd03219 181 ELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
294-454 |
1.41e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.99 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTTL---LKKMIHRDDGIVISPIVKIGYFSQNLDILEVEKSILENVQStskqeETLIRTILARL 370
Cdd:PRK13644 25 IKKGEYIGIIGKNGSGKSTLalhLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPET-----QFVGRTVEEDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 371 HFFRDDV-YKPVEI-----------------------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARA-LESL 425
Cdd:PRK13644 100 AFGPENLcLPPIEIrkrvdralaeiglekyrhrspktLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAvLERI 179
|
170 180 190
....*....|....*....|....*....|.
gi 1890659908 426 --LQEYKGTVIFASHDRRFIEnVATKMLVIQ 454
Cdd:PRK13644 180 kkLHEKGKTIVYITHNLEELH-DADRIIVMD 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
272-439 |
1.47e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 49.70 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLkKMIHR----DDGIVIspivkigyfsqnLDILEVEK- 346
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISRllppDSGEVL------------VDGLDVATt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 347 ---------SIL--ENVQST--------------------SKQEETLIRTILARLHF--FRDdvyKPVEILSGGERVKVA 393
Cdd:COG4604 69 psrelakrlAILrqENHINSrltvrelvafgrfpyskgrlTAEDREIIDEAIAYLDLedLAD---RYLDELSGGQRQRAF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1890659908 394 LAKLFVSDVNTLILDEPTNFLDIEAARALESLLQ----EYKGTVIFASHD 439
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRrladELGKTVVIVLHD 195
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-153 |
1.47e-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: 49.54 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQ--CGLLPQLKRIdaiksgGEVTQSYmnALF-------- 93
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdiTNLPPHKRPV------NTVFQNY--ALFphltvfen 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 94 ----------SKA-------------------------------------------PKLLLADEPTTHLD---REHIEWL 117
Cdd:cd03300 93 iafglrlkklPKAeikervaealdlvqlegyanrkpsqlsggqqqrvaiaralvnePKVLLLDEPLGALDlklRKDMQLE 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1890659908 118 EKKLSQWKG-AFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:cd03300 173 LKRLQKELGiTFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
294-439 |
1.49e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.85 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTTLLKKMihrdDGIVISPIVKIGYFSQNLD-----ILEVEKSI-------------------- 348
Cdd:PRK13636 29 IKKGEVTAILGGNGAGKSTLFQNL----NGILKPSSGRILFDGKPIDysrkgLMKLRESVgmvfqdpdnqlfsasvyqdv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 ---LENVQSTSKQEETLIRTILAR--LHFFRDdvyKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAA 419
Cdd:PRK13636 105 sfgAVNLKLPEDEVRKRVDNALKRtgIEHLKD---KPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIM 181
|
170 180
....*....|....*....|
gi 1890659908 420 RALESLLQEYKGTVIFASHD 439
Cdd:PRK13636 182 KLLVEMQKELGLTIIIATHD 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
294-439 |
1.49e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTTLLK--------------------KMIHRDDGIV------------ISPIVKIGYFSQnldI 341
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKilsgelipnlgdyeeepswdEVLKRFRGTElqnyfkklyngeIKVVHKPQYVDL---I 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 342 LEVEK----SILENVQSTSKQEETL----IRTILARlhffrddvykPVEILSGGERVKVALAKLFVSDVNTLILDEPTNF 413
Cdd:PRK13409 173 PKVFKgkvrELLKKVDERGKLDEVVerlgLENILDR----------DISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|
gi 1890659908 414 LDI----EAARALESLLQeyKGTVIFASHD 439
Cdd:PRK13409 243 LDIrqrlNVARLIRELAE--GKYVLVVEHD 270
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-141 |
1.51e-06 |
|
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: 49.71 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 20 EIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC-RAQCGLLPQ-------------LKRIDAIK------ 79
Cdd:cd03237 16 EVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIeLDTVSYKPQyikadyegtvrdlLSSITKDFythpyf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 80 ---------------------SGGEVTQSYMNALFSKAPKLLLADEPTTHLDREHIEWLEKKLSQW-----KGAFViVSH 133
Cdd:cd03237 96 kteiakplqieqildrevpelSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaenneKTAFV-VEH 174
|
....*...
gi 1890659908 134 DRAFLDAL 141
Cdd:cd03237 175 DIIMIDYL 182
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
291-439 |
1.60e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.60 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIH---------RDDGIVISPIV------KIGYFSQNLDI----LEVEKSI--- 348
Cdd:PRK13632 29 SFEINEGEYVAILGHNGSGKSTISKILTGllkpqsgeiKIDGITISKENlkeirkKIGIIFQNPDNqfigATVEDDIafg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 349 LENVQSTSKQEETLIrtilarlhffrDDVYKPVEI----------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEA 418
Cdd:PRK13632 109 LENKKVPPKKMKDII-----------DDLAKKVGMedyldkepqnLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKG 177
|
170 180
....*....|....*....|....*
gi 1890659908 419 ARALESLL----QEYKGTVIFASHD 439
Cdd:PRK13632 178 KREIKKIMvdlrKTRKKTLISITHD 202
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-153 |
2.44e-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: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 10 KHYVKDRLLFEIErLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQG-------------SVLCRAQC-----GLLPQ 71
Cdd:cd03268 8 KTYGKKRVLDDIS-LHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGeitfdgksyqkniEALRRIGAlieapGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 L-----------------KRIDAI-------KSGGEVTQSY---MN-------ALFSKaPKLLLADEPTTHLDREHIEWL 117
Cdd:cd03268 87 LtarenlrllarllgirkKRIDEVldvvglkDSAKKKVKGFslgMKqrlgialALLGN-PDLLILDEPTNGLDPDGIKEL 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1890659908 118 EKKLSQWK---GAFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:cd03268 166 RELILSLRdqgITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-72 |
2.70e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.77 E-value: 2.70e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 3 LLEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQCGLLPQL 72
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDL 75
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
291-467 |
2.86e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.84 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIH--------RDDGIVISPIV------KIGYFSQNLDILEVekSILENV---- 352
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslKINGIELRELDpeswrkHLSWVGQNPQLPHG--TLRDNVllgn 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 -QSTSKQEETLIRtiLARLHFFRDDVYKPV--EI------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARA-L 422
Cdd:PRK11174 448 pDASDEQLQQALE--NAWVSEFLPLLPQGLdtPIgdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLvM 525
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1890659908 423 ESLLQEYKG-TVIFASHDRRFIENVaTKMLVIQD-KVIQwfDGTYQQ 467
Cdd:PRK11174 526 QALNAASRRqTTLMVTHQLEDLAQW-DQIWVMQDgQIVQ--QGDYAE 569
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
261-418 |
3.52e-06 |
|
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: 49.44 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 261 PHEDTFQDRIIIRVEEVTG--VIG---QRVlwEKTSFHVRGGDKLAVIGPNGSGKTTLLK-------------------- 315
Cdd:TIGR02633 247 PHEPHEIGDVILEARNLTCwdVINphrKRV--DDVSFSLRRGEILGVAGLVGAGRTELVQalfgaypgkfegnvfingkp 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 316 --------------KMIHRD---DGIVisPIVKIGyfsQNLdILEVEKSILENVQSTSKQEETLIRTILARLHFFRDDVY 378
Cdd:TIGR02633 325 vdirnpaqairagiAMVPEDrkrHGIV--PILGVG---KNI-TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF 398
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1890659908 379 KPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEA 418
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-153 |
3.59e-06 |
|
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: 47.90 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNV-KHYVKDRLLFEIeRLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL--------------------- 61
Cdd:cd03259 1 LELKGLsKTYGSVRALDDL-SLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtgvpperrnigmvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 62 ---------------------------CRAQC-------GLLPQLKRIDAIKSGGEvtQ---SYMNALfSKAPKLLLADE 104
Cdd:cd03259 80 dyalfphltvaeniafglklrgvpkaeIRARVrellelvGLEGLLNRYPHELSGGQ--QqrvALARAL-AREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 105 PTTHLD---REHIEWLEKKLSQWKGA-FVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:cd03259 157 PLSALDaklREELREELKELQRELGItTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-153 |
4.49e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 48.99 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNV-KHYVKDRLLFEIErLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL------------CRAQCGLLP 70
Cdd:COG1118 3 IEVRNIsKRFGSFTLLDDVS-LEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlftnlppRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 71 Q-----------------LKRI----DAIK-----------------------SGGE---VtqsymnALfskA------P 97
Cdd:COG1118 82 QhyalfphmtvaeniafgLRVRppskAEIRarveellelvqlegladrypsqlSGGQrqrV------AL---AralaveP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 98 KLLLADEPTTHLD---REHIE-WLEKKLSQWKGAFVIVSHDRafLDAL--CTTIWEMDEGKI 153
Cdd:COG1118 153 EVLLLDEPFGALDakvRKELRrWLRRLHDELGGTTVFVTHDQ--EEALelADRVVVMNQGRI 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-155 |
4.94e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.14 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 1 MILLEALNV-KHYVKDRLLFEIER--------LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQCglLPQ 71
Cdd:PRK10419 1 MTLLNVSGLsHHYAHGGLSGKHQHqtvlnnvsLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEP--LAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 LKRI--------------DAIK----------------------------------------------------SGGEVT 85
Cdd:PRK10419 79 LNRAqrkafrrdiqmvfqDSISavnprktvreiireplrhllsldkaerlarasemlravdlddsvldkrppqlSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 86 QSYMNALFSKAPKLLLADEPTTHLDR----EHIEWLeKKLSQWKG-AFVIVSHDRAFLDALCTTIWEMDEGKIKE 155
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLL-KKLQQQFGtACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
291-462 |
5.20e-06 |
|
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: 47.41 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIHRDDgiVISPIVKIgyfsQNLDILEVEKSILENVQSTSKQEETL----IRTI 366
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLE--AEEGKIEI----DGIDISTIPLEDLRSSLTIIPQDPTLfsgtIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 367 LARLHFFRD-DVYKPVEI------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEA-ARALESLLQEYKG-TVIFAS 437
Cdd:cd03369 102 LDPFDEYSDeEIYGALRVsegglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATdALIQKTIREEFTNsTILTIA 181
|
170 180
....*....|....*....|....*
gi 1890659908 438 HDRRFIENVAtKMLVIQDKVIQWFD 462
Cdd:cd03369 182 HRLRTIIDYD-KILVMDAGEVKEYD 205
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-167 |
6.41e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 48.67 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC-------------RAQCGLLPQ------------------- 71
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLngqpiadyseaalRQAISVVSQrvhlfsatlrdnlllaapn 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 72 ---------LKRIDAIK-------------------SGGEvtQSYM---NALFSKAPKLLLaDEPTTHLDRE---HIEWL 117
Cdd:PRK11160 441 asdealievLQQVGLEKlleddkglnawlgeggrqlSGGE--QRRLgiaRALLHDAPLLLL-DEPTEGLDAEterQILEL 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 118 EKKLSQWKgAFVIVSHdRAF----LDALCTtiweMDEGKIKEYkGNYSDYLEQK 167
Cdd:PRK11160 518 LAEHAQNK-TVLMITH-RLTgleqFDRICV----MDNGQIIEQ-GTHQELLAQQ 564
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
291-410 |
7.50e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 47.33 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRD------DGIVIS--PIVK-----IGYFSQNLDI---LEVE---KSI 348
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTtfyMIVGLVKPDsgriflDGEDIThlPMHKrarlgIGYLPQEASIfrkLTVEdniLAV 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 349 LENVQSTSKQEETLIRTILARLHF--FRDdvyKPVEILSGGERVKVALAKLFVSDVNTLILDEP 410
Cdd:COG1137 103 LELRKLSKKEREERLEELLEEFGIthLRK---SKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
301-438 |
9.86e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.21 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 301 AVIGPNGSGKTTLLKKMihrDDGIVISPIVKI-------GYFSQNLDILEVEK---------------SILENVQ----- 353
Cdd:PRK14247 33 ALMGPSGSGKSTLLRVF---NRLIELYPEARVsgevyldGQDIFKMDVIELRRrvqmvfqipnpipnlSIFENVAlglkl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 ---STSKQE-ETLIRTILARLHFF---RDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLL 426
Cdd:PRK14247 110 nrlVKSKKElQERVRWALEKAQLWdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLF 189
|
170
....*....|....
gi 1890659908 427 QEYKG--TVIFASH 438
Cdd:PRK14247 190 LELKKdmTIVLVTH 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
291-454 |
1.03e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.52 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLlkkMIHRDDGIVISP--IVKIGYF------SQNLDILEVEKSILENVQSTSKQEETL 362
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTL---MQHFNALLKPSSgtITIAGYHitpetgNKNLKKLRKKVSLVFQFPEAQLFENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 363 IRTI-LARLHF-FRDDVYK--------------------PVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR 420
Cdd:PRK13641 104 LKDVeFGPKNFgFSEDEAKekalkwlkkvglsedlisksPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1890659908 421 ALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQ 454
Cdd:PRK13641 183 EMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLE 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
282-459 |
1.11e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.89 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 282 GQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK--------------------KMIHRDDG-IVISPIVKIGYFSQNLD 340
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRcinflekpsegsivvngqtiNLVRDKDGqLKVADKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 341 I------LEVEKSILENVQSTSKQEETLIRTIL-ARLHFFRDDV--------YKPVEiLSGGERVKVALAKLFVSDVNTL 405
Cdd:PRK10619 96 MvfqhfnLWSHMTVLENVMEAPIQVLGLSKQEArERAVKYLAKVgideraqgKYPVH-LSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 406 ILDEPTNFLDI----EAARALESLLQEYKgTVIFASHDRRFIENVATKMLVIQDKVIQ 459
Cdd:PRK10619 175 LFDEPTSALDPelvgEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
20-139 |
1.31e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 20 EIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQCGLLPQLKRID----------AIK---------- 79
Cdd:PRK13409 356 EVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKPDydgtvedllrSITddlgssyyks 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 80 -------------------SGGEVTQSYMNALFSKAPKLLLADEPTTHLD-----------REHIEwlEKKlsqwKGAFV 129
Cdd:PRK13409 436 eiikplqlerlldknvkdlSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavakaiRRIAE--ERE----ATALV 509
|
170
....*....|
gi 1890659908 130 iVSHDRAFLD 139
Cdd:PRK13409 510 -VDHDIYMID 518
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
261-437 |
1.34e-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: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 261 PHEDTFQDRIIIRVEEVTGviGQRVlwEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMI----HRDDGIVI---------S 327
Cdd:COG1129 246 PKRAAAPGEVVLEVEGLSV--GGVV--RDVSFSVRAGEILGIAGLVGAGRTELAR-ALfgadPADSGEIRldgkpvrirS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 328 PIV----KIGYFSQN-------LDileveKSILENVQSTS------------KQEETLIRTILARLHFFRDDVYKPVEIL 384
Cdd:COG1129 321 PRDairaGIAYVPEDrkgeglvLD-----LSIRENITLASldrlsrgglldrRRERALAEEYIKRLRIKTPSPEQPVGNL 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1890659908 385 SGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEY--KGT-VIFAS 437
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaaEGKaVIVIS 451
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
280-459 |
1.41e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 280 VIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTL---LKKMIHRDDGIVI--SPIVKIGYfSQNLDI------------- 341
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTglaLLRLINSQGEIWFdgQPLHNLNR-RQLLPVrhriqvvfqdpns 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 342 -----LEVEKSILENVQS-----TSKQEETLIRTILARLHFFRDDVYK-PVEiLSGGERVKVALAKLFVSDVNTLILDEP 410
Cdd:PRK15134 374 slnprLNVLQIIEEGLRVhqptlSAAQREQQVIAVMEEVGLDPETRHRyPAE-FSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 411 TNFLD--IEAA--RALESLLQEYKGTVIFASHDRRFIENVATKMLVI-QDKVIQ 459
Cdd:PRK15134 453 TSSLDktVQAQilALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLrQGEVVE 506
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
291-455 |
1.63e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKkmihrddgiVISPIVKIGYFSQNLdILEVEKSILENVQSTSK-------QEETLI 363
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMK---------VLSGVYPHGTYEGEI-IFEGEELQASNIRDTERagiaiihQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 364 R------------------------------TILARLHFFRDdVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNF 413
Cdd:PRK13549 95 KelsvleniflgneitpggimdydamylraqKLLAQLKLDIN-PATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1890659908 414 LDIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQD 455
Cdd:PRK13549 174 LTESETAVLLDIIRDLKAhgiACIYISHKLNEVKAISDTICVIRD 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
291-458 |
1.63e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.70 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLK------------------KMIHRDDGIVISPIVK-IGYFSQ--NLDILE--VEKS 347
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQninallkpttgtvtvddiTITHKTKDKYIRPVRKrIGMVFQfpESQLFEdtVERE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 348 IL---ENVQSTSKQEETLIRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALES 424
Cdd:PRK13646 107 IIfgpKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMR 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1890659908 425 LLQEYK----GTVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:PRK13646 187 LLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
383-455 |
1.89e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 45.50 E-value: 1.89e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890659908 383 ILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYK---GTVIFASHDRRFIENVATKMLVIQD 455
Cdd:cd03215 104 LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRILVMYE 179
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
376-458 |
2.03e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 376 DVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIeAARA-----LESLLQEyKGTVIFASHDRRFIENVATKM 450
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV-SARNdiyqlIRSIAAQ-NVAVLFISSDLEEIEQMADRV 473
|
....*...
gi 1890659908 451 LVIQDKVI 458
Cdd:PRK15439 474 LVMHQGEI 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
301-438 |
2.29e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 301 AVIGPNGSGKTTLLKKMIhrddGIV--ISPIVKIGY--FSQNLDI-----------------LEVEKSILENVQSTSKQE 359
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILT----GLLppTSGTVLVGGkdIETNLDAvrqslgmcpqhnilfhhLTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 360 ETLIRTILARL-----HFFRDDvykPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKG--T 432
Cdd:TIGR01257 1036 EEAQLEMEAMLedtglHHKRNE---EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSgrT 1112
|
....*.
gi 1890659908 433 VIFASH 438
Cdd:TIGR01257 1113 IIMSTH 1118
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-61 |
2.50e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 45.52 E-value: 2.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890659908 1 MILLEALNVKHyvkDRLLFEIErLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:COG3840 1 MLRLDDLTYRY---GDFPLRFD-LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL 57
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-155 |
2.74e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.54 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 32 IGLVGKNGSGKTTLLNILA-----------------KKISPEQGSVLcRA------------------------------ 64
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAglddgssgevslvgqplHQMDEEARAKL-RAkhvgfvfqsfmliptlnalenvelpallrg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 65 ---------------QCGLLPQLKRIDAIKSGGEVTQSYMNALFSKAPKLLLADEPTTHLDR---EHIEWLEKKLSQWKG 126
Cdd:PRK10584 118 essrqsrngakalleQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRqtgDKIADLLFSLNREHG 197
|
170 180 190
....*....|....*....|....*....|
gi 1890659908 127 -AFVIVSHDRAfLDALCTTIWEMDEGKIKE 155
Cdd:PRK10584 198 tTLILVTHDLQ-LAARCDRRLRLVNGQLQE 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
80-151 |
2.77e-05 |
|
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: 45.50 E-value: 2.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890659908 80 SGGEvtQSYMN-AL-FSKAPKLLLADEPTTHLD---REH-IEWLEKKLSQwkGAFVI-VSHDRAFLDALCTTIWEMDEG 151
Cdd:COG4778 154 SGGE--QQRVNiARgFIADPPLLLLDEPTASLDaanRAVvVELIEEAKAR--GTAIIgIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-66 |
2.87e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.18 E-value: 2.87e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 3 LLEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQC 66
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP 64
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
301-444 |
2.98e-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: 44.62 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 301 AVIGPNGSGKTTLLKKmihrddgivispivkIGYFSQNLDILEVEKSILENVQSTSKQEETLIRTILARLHFFRddvykP 380
Cdd:cd03238 25 VVTGVSGSGKSTLVNE---------------GLYASGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGYLTLGQ-----K 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 381 VEILSGGERVKVALAK-LFVSDVNTL-ILDEPTNFLDieaARALESLLQEYKG------TVIFASHDRRFIE 444
Cdd:cd03238 85 LSTLSGGELQRVKLASeLFSEPPGTLfILDEPSTGLH---QQDINQLLEVIKGlidlgnTVILIEHNLDVLS 153
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
297-428 |
3.06e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 297 GDKLAVIGPNGSGKTT---LLKKMIHRDDGIVISPIVKIGYFSQNLDILEVEK----------------SILENVQ---- 353
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTimqLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKkvglvfqfpesqlfeeTVLKDVAfgpq 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 --STSKQE-ETLIRTILArLHFFRDDVYK--PVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQE 428
Cdd:PRK13649 113 nfGVSQEEaEALAREKLA-LVGISESLFEknPFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK 190
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
359-418 |
3.06e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 3.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 359 EETLIRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEA 418
Cdd:PRK13549 381 ELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGA 440
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
225-438 |
3.07e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 225 KKQKKLQKTAKAMETRLEKLEKVeKIKETA--PINMSLPHEdtfQDRIIIRveevTGVI--GQRVLWEKTSFHVRGGDKL 300
Cdd:PRK10938 218 EREEILQQALVAQLAHSEQLEGV-QLPEPDepSARHALPAN---EPRIVLN----NGVVsyNDRPILHNLSWQVNPGEHW 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 301 AVIGPNGSGKTTLLKkMI---H--------------RDDGIVISPIVK-IGYFSQNLDI-LEVEKSILeNV--------- 352
Cdd:PRK10938 290 QIVGPNGAGKSTLLS-LItgdHpqgysndltlfgrrRGSGETIWDIKKhIGYVSSSLHLdYRVSTSVR-NVilsgffdsi 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 ---QSTSKQEETLIRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAARALESL 425
Cdd:PRK10938 368 giyQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnrQLVRRFVDVL 447
|
250
....*....|...
gi 1890659908 426 LQEYKGTVIFASH 438
Cdd:PRK10938 448 ISEGETQLLFVSH 460
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-61 |
3.09e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 45.85 E-value: 3.09e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:COG1101 27 LTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
304-445 |
3.29e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 304 GPNGSGKTTLLKkMIhrdDGIV-------------ISPIVK--IGYFSQNLDiLEVEKSILENVQSTSKQEETlIRTILA 368
Cdd:PRK13541 33 GANGCGKSSLLR-MI---AGIMqpssgniyykncnINNIAKpyCTYIGHNLG-LKLEMTVFENLKFWSEIYNS-AETLYA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 369 RLHFFR--DDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLL---QEYKGTVIFASHDRRFI 443
Cdd:PRK13541 107 AIHYFKlhDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIvmkANSGGIVLLSSHLESSI 186
|
..
gi 1890659908 444 EN 445
Cdd:PRK13541 187 KS 188
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-186 |
3.34e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 5 EALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSV-------LCRAQCGLLPQLKRIDA 77
Cdd:PRK13546 26 DALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdrngevsVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 78 I-----------KSGGEVT-----------------QSYMNALFSKA---------PKLLLADEPTTHLDREHIEWLEKK 120
Cdd:PRK13546 106 IefkmlcmgfkrKEIKAMTpkiiefselgefiyqpvKKYSSGMRAKLgfsinitvnPDILVIDEALSVGDQTFAQKCLDK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890659908 121 LSQWKGA---FVIVSHDRAFLDALCTTIWEMDEGKIKEYkGNYSDYLEQKE--LERRRQQSAYEQYEKKKQ 186
Cdd:PRK13546 186 IYEFKEQnktIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDVLPKYEafLNDFKKKSKAEQKEFRNK 255
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
291-455 |
3.43e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.36 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMI----HRD-DGIVI---SPIVK----------IGYFSQNLDILEvEKSILENV 352
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSgvypHGTwDGEIYwsgSPLKAsnirdteragIVIIHQELTLVP-ELSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 ----------QSTSKQEETL-IRTILARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARA 421
Cdd:TIGR02633 100 flgneitlpgGRMAYNAMYLrAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEI 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 1890659908 422 LESLLQEYKG---TVIFASHDRRFIENVATKMLVIQD 455
Cdd:TIGR02633 180 LLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRD 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
291-464 |
3.48e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.85 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVI---------SPIVKI----GYFSQNLD--ILE--VEKSIL- 349
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMnalLIPSEGKVYvdgldtsdeENLWDIrnkaGMVFQNPDnqIVAtiVEEDVAf 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 350 --ENVQSTSKQEETLIRTILARLHFFRDDVYKPvEILSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAARALE 423
Cdd:PRK13633 110 gpENLGIPPEEIRERVDESLKKVGMYEYRRHAP-HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1890659908 424 SLLQEYKGTVIFASHdrrFIENV--ATKMLVIQD-KVIqwFDGT 464
Cdd:PRK13633 189 ELNKKYGITIILITH---YMEEAveADRIIVMDSgKVV--MEGT 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
24-153 |
3.89e-05 |
|
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: 45.19 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQCglLPQLKRIDAIKSG---GEVTQSymNALFS------ 94
Cdd:cd03261 21 LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGED--ISGLSEAELYRLRrrmGMLFQS--GALFDsltvfe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 95 ----------------------------------------------------KA----PKLLLADEPTTHLD---REHIE 115
Cdd:cd03261 97 nvafplrehtrlseeeireivlekleavglrgaedlypaelsggmkkrvalaRAlaldPELLLYDEPTAGLDpiaSGVID 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1890659908 116 WLEKKLSQWKGA-FVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:cd03261 177 DLIRSLKKELGLtSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
272-439 |
4.03e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.46 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 272 IRVEEVTGVIGQRVLWE-----KTSFHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIVI------SPIVKIGYFSQ 337
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLnalLLPDTGTIEwifkdeKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 338 NLDILEVEKSI---LENVQSTSKQ-------------EETLIRTI--------------LARLHFFRDDVYKPVEIL--- 384
Cdd:PRK13651 83 VLEKLVIQKTRfkkIKKIKEIRRRvgvvfqfaeyqlfEQTIEKDIifgpvsmgvskeeaKKRAAKYIELVGLDESYLqrs 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 385 ----SGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAARALESLLQEYKgTVIFASHD 439
Cdd:PRK13651 163 pfelSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNLNKQGK-TIILVTHD 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
24-153 |
4.10e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 45.86 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQC--GLLPQLKRIdaiksgGEVTQSYmnALF-------- 93
Cdd:COG3842 26 LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtGLPPEKRNV------GMVFQDY--ALFphltvaen 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 94 ----------SKA-------------------------------------------PKLLLADEPTTHLD---REHIEWL 117
Cdd:COG3842 98 vafglrmrgvPKAeirarvaellelvglegladryphqlsggqqqrvalaralapePRVLLLDEPLSALDaklREEMREE 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1890659908 118 EKKLSQWKGA-FVIVSHDR--AFldALCTTIWEMDEGKI 153
Cdd:COG3842 178 LRRLQRELGItFIYVTHDQeeAL--ALADRIAVMNDGRI 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
291-459 |
4.12e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 45.00 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM----IHRDDGIVISpivkiGY---FSQNLDILEVEK----------------- 346
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSSLLRVLnlleTPDSGQLNIA-----GHqfdFSQKPSEKAIRLlrqkvgmvfqqynlwph 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 347 -SILEN-------VQSTSKQEeTLIRT--ILARLHF--FRDDVykPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFL 414
Cdd:COG4161 97 lTVMENlieapckVLGLSKEQ-AREKAmkLLARLRLtdKADRF--PLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1890659908 415 DIEAARALESLLQEYKGTVI---FASHDRRFIENVATKMLVIQD-KVIQ 459
Cdd:COG4161 173 DPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEKgRIIE 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
276-430 |
4.24e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 276 EVTGVIGQRVlwEKTSFHVRGGDKLAVIGPNGSGKTTLLKkMIH----------RDDGIVISPIVK-------IGYFSQN 338
Cdd:PRK10762 259 KVDNLSGPGV--NDVSFTLRKGEILGVSGLMGAGRTELMK-VLYgalprtsgyvTLDGHEVVTRSPqdglangIVYISED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 339 L--DILEVEKSILENVQSTS------------KQEETLIRTILARLhfF------RDdvyKPVEILSGGERVKVALAKLF 398
Cdd:PRK10762 336 RkrDGLVLGMSVKENMSLTAlryfsraggslkHADEQQAVSDFIRL--FniktpsME---QAIGLLSGGNQQKVAIARGL 410
|
170 180 190
....*....|....*....|....*....|..
gi 1890659908 399 VSDVNTLILDEPTNFLDIEAARALESLLQEYK 430
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFK 442
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
297-439 |
4.43e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 297 GDKLAVI-GPNGSGKTTLL--------------KKM--------------------------IHRDDG------------ 323
Cdd:COG0419 22 DDGLNLIvGPNGAGKSTILeairyalygkarsrSKLrsdlinvgseeasvelefehggkryrIERRQGefaefleakpse 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 324 --IVISPIVKIGYFSQNLDILEVEKSILENVQSTSKQEETLIRTILARLHffrddVYKPVEILSGGERVKVALAKLFvsd 401
Cdd:COG0419 102 rkEALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLS-----GLDPIETLSGGERLRLALADLL--- 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1890659908 402 vnTLILDepTNFLDIEaarALESLLQEYKGTVIFaSHD 439
Cdd:COG0419 174 --SLILD--FGSLDEE---RLERLLDALEELAII-THV 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
292-438 |
4.76e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 45.49 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 292 FHVRGGDKLAVIGPNGSGKTTLLKKM---IHRDDGIV---------------ISPI-VKIGYFSQNLDILEVEKSILENV 352
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLnglLQPTEGKVtvgdivvsstskqkeIKPVrKKVGVVFQFPESQLFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 Q------STSKQEETLIRTILARLHFFRDDVYK--PVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAAR 420
Cdd:PRK13643 107 AfgpqnfGIPKEKAEKIAAEKLEMVGLADEFWEksPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQ 185
|
170
....*....|....*...
gi 1890659908 421 ALESLLQEYKgTVIFASH 438
Cdd:PRK13643 186 LFESIHQSGQ-TVVLVTH 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
24-61 |
5.12e-05 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 45.08 E-value: 5.12e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:COG1116 32 LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVL 69
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
301-481 |
5.36e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.09 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 301 AVIGPNGSGKTTLLKKMIHRDD---GIVISPIVKIGYFS--QNLDILEVEK--------------SILENVQSTSKQEET 361
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDkvsGYRYSGDVLLGGRSifNYRDVLEFRRrvgmlfqrpnpfpmSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 362 LIRTIL-----ARL------HFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEY- 429
Cdd:PRK14271 131 VPRKEFrgvaqARLtevglwDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLa 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 430 -KGTVIFASHdrrfieNVAtKMLVIQDKVIQWFDGTYQQY--EQHVRQKDRHADT 481
Cdd:PRK14271 211 dRLTVIIVTH------NLA-QAARISDRAALFFDGRLVEEgpTEQLFSSPKHAET 258
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-141 |
6.13e-05 |
|
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: 43.68 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 15 DRLLFEIErLAIYENDRIGLVGKNGSGKTTLLNILA--------KKISPEQGSVLCRAQCGLLPQ--LKRI-----DAIK 79
Cdd:cd03223 14 RVLLKDLS-FEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLFLPQRPYLPLgtLREQliypwDDVL 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890659908 80 SGGEvtQ---SYMNALFSKaPKLLLADEPTTHLDREHIEWLEKKLSQWKGAFVIVSHdRAFLDAL 141
Cdd:cd03223 93 SGGE--QqrlAFARLLLHK-PKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKF 153
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
271-315 |
6.14e-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: 44.59 E-value: 6.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1890659908 271 IIRVEEVTGVIGQ-RVLWEkTSFHVRGGDKLAVIGPNGSGKTTLLK 315
Cdd:COG0410 3 MLEVENLHAGYGGiHVLHG-VSLEVEEGEIVALLGRNGAGKTTLLK 47
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-157 |
6.55e-05 |
|
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: 44.21 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 30 DRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQC-----------------GLLPQ-----------------LKR- 74
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQqyalfphlnvrenlafgLKRk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 75 -----------------IDAIK-------SGGEVTQ-SYMNALFSKaPKLLLADEPTTHLDREHIEWLEKKLSQWKGAF- 128
Cdd:cd03297 104 rnredrisvdelldllgLDHLLnrypaqlSGGEKQRvALARALAAQ-PELLLLDEPFSALDRALRLQLLPELKQIKKNLn 182
|
170 180 190
....*....|....*....|....*....|..
gi 1890659908 129 ---VIVSHDRAFLDALCTTIWEMDEGKIKEYK 157
Cdd:cd03297 183 ipvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
99-141 |
7.31e-05 |
|
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: 44.14 E-value: 7.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1890659908 99 LLLADEPTTHLDREHIEW-----LEKKLSQWKGAFVIVSHDRAFLDAL 141
Cdd:cd03240 142 ILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
291-439 |
7.73e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 44.70 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTT---LLKKMIHRDDGIV------------ISPIVKIGYFSQNLDI----LEVEKSILEN 351
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTtarLIDGLFEEFEGKVkidgelltaenvWNLRRKIGMVFQNPDNqfvgATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 VQSTSKQEETLIRTI---LARLHFFRDDVYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLD----IEAARALES 424
Cdd:PRK13642 107 MENQGIPREEMIKRVdeaLLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHE 185
|
170
....*....|....*
gi 1890659908 425 LLQEYKGTVIFASHD 439
Cdd:PRK13642 186 IKEKYQLTVLSITHD 200
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
302-454 |
7.89e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 44.61 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 302 VIGPNGSGKTTL---LKKMIHRDDGIVISPIVKIGYFSQNLDIL------------------EVEKSILENVQSTSKQEE 360
Cdd:PRK13638 32 LVGANGCGKSTLfmnLSGLLRPQKGAVLWQGKPLDYSKRGLLALrqqvatvfqdpeqqifytDIDSDIAFSLRNLGVPEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 361 TLIRTI-----LARLHFFRddvYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKGT--- 432
Cdd:PRK13638 112 EITRRVdealtLVDAQHFR---HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnh 188
|
170 180
....*....|....*....|..
gi 1890659908 433 VIFASHDRRFIENVATKMLVIQ 454
Cdd:PRK13638 189 VIISSHDIDLIYEISDAVYVLR 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
34-153 |
8.44e-05 |
|
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: 43.94 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 34 LVGKNGSGKTTLLNILAKKISPEQGSVLCRAQ--CGL----LPQLKR--------------------------------- 74
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvSDLrgraIPYLRRkigvvfqdfrllpdrnvyenvafalevtgvppr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 75 ------------------IDAIK---SGGEVTQSYMNALFSKAPKLLLADEPTTHLDREH---IEWLEKKLSQWKGAFVI 130
Cdd:cd03292 112 eirkrvpaalelvglshkHRALPaelSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTtweIMNLLKKINKAGTTVVV 191
|
170 180
....*....|....*....|...
gi 1890659908 131 VSHDRAFLDALCTTIWEMDEGKI 153
Cdd:cd03292 192 ATHAKELVDTTRHRVIALERGKL 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-145 |
8.80e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.16 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 20 EIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQCGLLPQLKRID-----------AIK--------- 79
Cdd:COG1245 357 EVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISPDydgtveeflrsANTddfgssyyk 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 80 --------------------SGGEVTQSYMNALFSKAPKLLLADEPTTHLD-----------REHIEwlEKKlsqwKGAF 128
Cdd:COG1245 437 teiikplgleklldknvkdlSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavakaiRRFAE--NRG----KTAM 510
|
170
....*....|....*..
gi 1890659908 129 ViVSHDRAFLDALCTTI 145
Cdd:COG1245 511 V-VDHDIYLIDYISDRL 526
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
294-467 |
9.56e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 44.55 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 294 VRGGDKLAVIGPNGSGKTTLLKkMI----HRDDG-IVISpivkigyfSQNLDILEVEK----------------SILENV 352
Cdd:PRK09452 37 INNGEFLTLLGPSGCGKTTVLR-LIagfeTPDSGrIMLD--------GQDITHVPAENrhvntvfqsyalfphmTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 353 ------QSTSKQE-ETLIRTILA--RLHFFRDdvYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALE 423
Cdd:PRK09452 108 afglrmQKTPAAEiTPRVMEALRmvQLEEFAQ--RKPHQ-LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQ 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1890659908 424 S---LLQEYKG-TVIFASHDRRfienvatKMLVIQDKVIQWFDGTYQQ 467
Cdd:PRK09452 185 NelkALQRKLGiTFVFVTHDQE-------EALTMSDRIVVMRDGRIEQ 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-153 |
9.69e-05 |
|
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: 43.90 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 1 MILLEAL-----NVKHYVK--DRLLFEIERLAIYendriGLVGKNGSGKTTLLNILAKKISPEQGSVL------------ 61
Cdd:cd03266 1 MITADALtkrfrDVKKTVQavDGVSFTVKPGEVT-----GLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkepae 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 62 CRAQCGLLPQLKRIDAIKSGGEVTQSY-----------------------MNAL-------FSK--------------AP 97
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLTARENLEYFaglyglkgdeltarleeladrlgMEELldrrvggFSTgmrqkvaiaralvhDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 98 KLLLADEPTTHLD----REHIEWLEKKLSQWKgAFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:cd03266 156 PVLLLDEPTTGLDvmatRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
291-455 |
1.03e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM------------IHRDD--------------GIVIspivkigyFSQNLdILEV 344
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLsgvyphgsyegeILFDGevcrfkdirdsealGIVI--------IHQEL-ALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 345 EKSILENV-----QSTSK---QEETLIRT--ILARLHFfRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFL 414
Cdd:NF040905 92 YLSIAENIflgneRAKRGvidWNETNRRAreLLAKVGL-DESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1890659908 415 DIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVIQD 455
Cdd:NF040905 171 NEEDSAALLDLLLELKAqgiTSIIISHKLNEIRRVADSITVLRD 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
297-470 |
1.13e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.85 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 297 GDKLAVIGPNGSGKTTLLKKM----IHRDDGIVISpivkiGY---FSQNLD---ILEVEK---------------SILEN 351
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLnlleMPRSGTLNIA-----GNhfdFSKTPSdkaIRELRRnvgmvfqqynlwphlTVQQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 -------VQSTSKQE-ETLIRTILARLHF--FRDDVykPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARA 421
Cdd:PRK11124 103 lieapcrVLGLSKDQaLARAEKLLERLRLkpYADRF--PLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 422 LESLLQEYKGTVI---FASHDRRFIENVATKMLVI-QDKVIQwfDGTYQQYEQ 470
Cdd:PRK11124 180 IVSIIRELAETGItqvIVTHEVEVARKTASRVVYMeNGHIVE--QGDASCFTQ 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
384-458 |
1.58e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 43.94 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 384 LSGGERVKVALAKLFVSDVNTLILDEPTNFLDiEAARA-----LESLLQEYKGTVIFASHDRRFIENVATKMLVIQD-KV 457
Cdd:COG4148 134 LSGGERQRVAIGRALLSSPRLLLMDEPLAALD-LARKAeilpyLERLRDELDIPILYVSHSLDEVARLADHVVLLEQgRV 212
|
.
gi 1890659908 458 I 458
Cdd:COG4148 213 V 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-61 |
2.09e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 44.00 E-value: 2.09e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-155 |
2.20e-04 |
|
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: 43.26 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 3 LLEALNVKHYVKDRLLFEIER---------LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQ-------- 65
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAKQrapvltnvsLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyqldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 66 -------------------------------------------------------CGLLPQ-LKRIDAIKSGGEVTQSYM 89
Cdd:TIGR02769 82 qrrafrrdvqlvfqdspsavnprmtvrqiigeplrhltsldeseqkariaelldmVGLRSEdADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 90 NALFSKAPKLLLADEPTTHLDR----EHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKE 155
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-134 |
2.38e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.08 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 1 MILLEALNVKhYVKDRLLFEIErLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSV--------------LCRaQC 66
Cdd:PRK11231 2 TLRTENLTVG-YGTKRILNDLS-LSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdkpismlssrqLAR-RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 67 GLLPQL-------------------------------------------------KRIDAIkSGGEVTQSYMNALFSKAP 97
Cdd:PRK11231 79 ALLPQHhltpegitvrelvaygrspwlslwgrlsaednarvnqameqtrinhladRRLTDL-SGGQRQRAFLAMVLAQDT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1890659908 98 KLLLADEPTTHLDREH-IEW--LEKKLSQwKGAFVI-VSHD 134
Cdd:PRK11231 158 PVVLLDEPTTYLDINHqVELmrLMRELNT-QGKTVVtVLHD 197
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
34-134 |
2.78e-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: 41.58 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 34 LVGKNGSGKTTLLN----ILAKKISPEQGSVLCRAQC----------GLLPQLkridaikSGGEVTQSYMNALFSKAPK- 98
Cdd:cd03227 26 ITGPNGSGKSTILDaiglALGGAQSATRRRSGVKAGCivaavsaeliFTRLQL-------SGGEKELSALALILALASLk 98
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1890659908 99 ---LLLADEPTTHLDREH---IEWLEKKLSQwKGAFVIV-SHD 134
Cdd:cd03227 99 prpLYILDEIDRGLDPRDgqaLAEAILEHLV-KGAQVIViTHL 140
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
384-447 |
2.86e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.54 E-value: 2.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 384 LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKG----TVIFASHD----RRFIENVA 447
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNlsivRKLADRVA 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
24-153 |
2.92e-04 |
|
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: 42.13 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL---------------CRAQCG-------LLPQLKRIDAI--- 78
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltddkknineLRQKVGmvfqqfnLFPHLTVLENItla 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 79 ------KSGGEVTQSYMNAL-----FSKA------------------------PKLLLADEPTTHLDREHI-EWLE--KK 120
Cdd:cd03262 101 pikvkgMSKAEAEERALELLekvglADKAdaypaqlsggqqqrvaiaralamnPKVMLFDEPTSALDPELVgEVLDvmKD 180
|
170 180 190
....*....|....*....|....*....|...
gi 1890659908 121 LSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:cd03262 181 LAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
384-454 |
3.07e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.09 E-value: 3.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890659908 384 LSGGERVKVALAKLFVSDVNTLILDEPTNFLD--------IEAARalesLLQEYKGTVIFASHDRRFIENVATKMLVIQ 454
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIEISR----LHKRLGRTMIYVTHDQVEAMTLADKIVVLD 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-155 |
3.35e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 42.87 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNV-KHY----VKDRLLFEIERLAIYendriGLVGKNGSGKTTLLNILAKKISPEQGSV-LC-----------RAQC 66
Cdd:PRK13537 8 IDFRNVeKRYgdklVVDGLSFHVQRGECF-----GLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCgepvpsrarhaRQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 67 GLLPQLKRID---AIKSGGEVTQSY--MNA---------------LFSKA------------------------PKLLLA 102
Cdd:PRK13537 83 GVVPQFDNLDpdfTVRENLLVFGRYfgLSAaaaralvppllefakLENKAdakvgelsggmkrrltlaralvndPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 103 DEPTTHLDRE--HIEW--LEKKLSQWKgAFVIVSHDRAFLDALCTTIWEMDEG-KIKE 155
Cdd:PRK13537 163 DEPTTGLDPQarHLMWerLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGrKIAE 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
24-153 |
4.72e-04 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 42.52 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL----------CRA------------------------QCGLL 69
Cdd:PRK09536 24 LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsARAasrrvasvpqdtslsfefdvrqvvEMGRT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 70 PQLKRID------------AIK---------------SGGEvTQSYM--NALFSKAPKLLLaDEPTTHLDREH-IEWLE- 118
Cdd:PRK09536 104 PHRSRFDtwtetdraaverAMErtgvaqfadrpvtslSGGE-RQRVLlaRALAQATPVLLL-DEPTASLDINHqVRTLEl 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 1890659908 119 -KKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:PRK09536 182 vRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
295-419 |
4.85e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 295 RGGDKLAVIGPNGSGKTTLLKKMIHRDDGIVISPIVKIGYFSQNLDILE-----VEKSILENVQSTSKqeETLIRTILAR 369
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFArisgyCEQNDIHSPQVTVR--ESLIYSAFLR 981
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 370 L---------HFFRDDVYKPVEI---------------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAA 419
Cdd:PLN03140 982 LpkevskeekMMFVDEVMELVELdnlkdaivglpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-153 |
5.83e-04 |
|
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: 42.48 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRA---------------------------QCGLLP------ 70
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVgdewvdmtkpgpdgrgrakryigilhqEYDLYPhrtvld 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 71 ------------QLKRIDAIK-----------------------SGGEVTQSYMNALFSKAPKLLLADEPTTHLD----- 110
Cdd:TIGR03269 385 nlteaiglelpdELARMKAVItlkmvgfdeekaeeildkypdelSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkv 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1890659908 111 --REHIEWLEKKLSQwkgAFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:TIGR03269 465 dvTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
300-438 |
6.03e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.75 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 300 LAVIGPNGSGKTTLLK---KMIHRDDGIVISPIVKI---GYFSQNLDILEVEK---------------SILENVQ----- 353
Cdd:PRK14267 33 FALMGPSGCGKSTLLRtfnRLLELNEEARVEGEVRLfgrNIYSPDVDPIEVRRevgmvfqypnpfphlTIYDNVAigvkl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 ---STSKQE-ETLIRTILARLHFF---RDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLL 426
Cdd:PRK14267 113 nglVKSKKElDERVEWALKKAALWdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELL 192
|
170
....*....|....
gi 1890659908 427 QEYKG--TVIFASH 438
Cdd:PRK14267 193 FELKKeyTIVLVTH 206
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
384-464 |
6.21e-04 |
|
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: 41.55 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 384 LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAralESLLQEykGTVIFASHDRRFIENVATKM--LVIQDKVIQWF 461
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS---DHLMQE--GILKFLQDDKRTLVLVTHKLqyLPHADWIIAMK 215
|
...
gi 1890659908 462 DGT 464
Cdd:cd03290 216 DGS 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-60 |
6.47e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 41.01 E-value: 6.47e-04
10 20
....*....|....*....|....*..
gi 1890659908 34 LVGKNGSGKTTLLNILAKKISPEQGSV 60
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTI 59
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
291-426 |
7.94e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTL---LKKMIHRDDGIVISPIVKIGYFS--------------QNLDILEVE-----KSI 348
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALaraLAGELPLLSGERQSQFSHITRLSfeqlqklvsdewqrNNTDMLSPGeddtgRTT 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 349 LENVQSTSKQEETLIRtiLARLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLL 426
Cdd:PRK10938 103 AEIIQDEVKDPARCEQ--LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
24-153 |
8.65e-04 |
|
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: 41.12 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC----------------RAQCGLL------------------ 69
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdgqditglsekelyelRRRIGMLfqggalfdsltvfenvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 70 ----------PQLKRI-----------DAIK------SGGevtqsyMN---ALfskA------PKLLLADEPTTHLD--- 110
Cdd:COG1127 106 plrehtdlseAEIRELvleklelvglpGAADkmpselSGG------MRkrvAL---AralaldPEILLYDEPTAGLDpit 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1890659908 111 REHIEWLEKKLSQWKGA-FVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:COG1127 177 SAVIDELIRELRDELGLtSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-61 |
9.07e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 41.25 E-value: 9.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 4 LEALNV------KHYVKDrLLFEIERLAIYendriGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:COG4152 2 LELKGLtkrfgdKTAVDD-VSFTVPKGEIF-----GLLGPNGAGKTTTIRIILGILAPDSGEVL 59
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
32-61 |
9.54e-04 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 40.91 E-value: 9.54e-04
10 20 30
....*....|....*....|....*....|
gi 1890659908 32 IGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:PRK13548 31 VAILGPNGAGKSTLLRALSGELSPDSGEVR 60
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
384-453 |
9.99e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.76 E-value: 9.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 384 LSGGERVKVALAKLFVSDVNTLILDEPTNFLDI----EAARALESLLQEYKGTVIFASHDRRFIENVATKMLVI 453
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
291-420 |
1.01e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 42.24 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIHRDDGIVISPIVK--IGYFSQNLDILEveKSILENVQSTSKQEETLIRTILA 368
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKgsVAYVPQQAWIQN--DSLRENILFGKALNEKYYQQVLE 735
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 369 RLHFFRDDVYKP----VEI------LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAAR 420
Cdd:TIGR00957 736 ACALLPDLEILPsgdrTEIgekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
291-486 |
1.19e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTlLKKMIhrddGIVISPIVkiGYFSQNLDI--------LEVEKSILENVQ-------ST 355
Cdd:PRK13546 44 SLKAYEGDVIGLVGINGSGKST-LSNII----GGSLSPTV--GKVDRNGEVsviaisagLSGQLTGIENIEfkmlcmgFK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 356 SKQEETLIRTILaRLHFFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYK---GT 432
Cdd:PRK13546 117 RKEIKAMTPKII-EFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKeqnKT 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1890659908 433 VIFASHDRRFIENVATKMLVIQDKVIQWF---DGTYQQYEQHVrqKDRHADTQADQR 486
Cdd:PRK13546 196 IFFVSHNLGQVRQFCTKIAWIEGGKLKDYgelDDVLPKYEAFL--NDFKKKSKAEQK 250
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-61 |
1.20e-03 |
|
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: 40.50 E-value: 1.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 4 LEALNVkHYVKDRLLFEIeRLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:cd03224 3 VENLNA-GYGKSQILFGV-SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIR 58
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
80-156 |
1.22e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 41.25 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 80 SGGeVTQSYM--NALFSKaPKLLLADEPTTHLD---REHIEWLEKKL-SQWKGAFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:PRK09473 163 SGG-MRQRVMiaMALLCR-PKLLIADEPTTALDvtvQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
...
gi 1890659908 154 KEY 156
Cdd:PRK09473 241 MEY 243
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
283-458 |
1.37e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 40.83 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 283 QRVLwEKTSFHVRGGDKLAVIGPNGSGKTTLLKKMI---HRDDGIVI---SPIVK--------------------IGYFS 336
Cdd:PRK10419 25 QTVL-NNVSLSLKSGETVALLGRSGCGKSTLARLLVgleSPSQGNVSwrgEPLAKlnraqrkafrrdiqmvfqdsISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 337 QNLDILEVEKSILENVQSTSKQEEtlirtiLARLHFFRDDVYKPVEI-------LSGGERVKVALAKLFVSDVNTLILDE 409
Cdd:PRK10419 104 PRKTVREIIREPLRHLLSLDKAER------LARASEMLRAVDLDDSVldkrppqLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 410 PTNFLDI----EAARALESLLQEYKGTVIFASHDRRFIENVATKMLVIQDKVI 458
Cdd:PRK10419 178 AVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
376-418 |
1.62e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 1.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1890659908 376 DVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEA 418
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGA 439
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
301-520 |
1.62e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 301 AVIGPNGSGKTTLLK--KMIHRDDGIVISPIVKIGYFSQNLDILEVEKSILENVQSTSKQEETLIRTILARLhFFRDDVY 378
Cdd:pfam13304 3 VLIGPNGSGKSNLLEalRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRY-GLDLERE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 379 KPVEILSGGERV---------KVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKGTVIFASHDRRFIENvATK 449
Cdd:pfam13304 82 DVEEKLSSKPTLlekrlllreDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLL-DEG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890659908 450 MLVIQDKVIQWFDGTYQQYEqhvRQKDRHADTQADQRLLLETKMSEVLSRLSMEPSEELEKEFQLLLEKKR 520
Cdd:pfam13304 161 LLLEDWAVLDLAADLALFPD---LKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGG 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-71 |
1.63e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 41.54 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 3 LLEALNVKHYVKdrlLFE------IERLAI--YENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL------------C 62
Cdd:TIGR01257 925 LVPGVCVKNLVK---IFEpsgrpaVDRLNItfYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLvggkdietnldaV 1001
|
....*....
gi 1890659908 63 RAQCGLLPQ 71
Cdd:TIGR01257 1002 RQSLGMCPQ 1010
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
80-155 |
1.67e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.45 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 80 SGGeVTQSYM--NALFSKAPkLLLADEPTTHLD---REHIEWLEKKLSQWKG-AFVIVSHDRAFLDALCTTIWEMDEGKI 153
Cdd:PRK10418 142 SGG-MLQRMMiaLALLCEAP-FIIADEPTTDLDvvaQARILDLLESIVQKRAlGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
..
gi 1890659908 154 KE 155
Cdd:PRK10418 220 VE 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
31-110 |
1.84e-03 |
|
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: 40.81 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 31 RIGLVGKNGSGKTTLLNILAKKISPEQGSVL-------------CRAQCGLLPQ--------------LKRIDAIK---- 79
Cdd:TIGR02868 363 RVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvssldqdeVRRRVSVCAQdahlfdttvrenlrLARPDATDeelw 442
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890659908 80 ------------------------------SGGEVTQ-SYMNALFSKAPKLLLaDEPTTHLD 110
Cdd:TIGR02868 443 aalervgladwlralpdgldtvlgeggarlSGGERQRlALARALLADAPILLL-DEPTEHLD 503
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
291-453 |
1.89e-03 |
|
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: 40.17 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLK----------------------------KMIHRDDGIVISPivKIGYFSQNLDIL 342
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARlllglekpaqgtvsfrgqdlyqldrkqrRAFRRDVQLVFQD--SPSAVNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 343 EVEKSILENVQSTSKQEETLIRTILARLHFFRDDVYK--PVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDI---- 416
Cdd:TIGR02769 109 QIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADklPRQ-LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqa 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 1890659908 417 EAARALESLLQEYKGTVIFASHDRRFIENVATKMLVI 453
Cdd:TIGR02769 188 VILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-61 |
1.90e-03 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 39.78 E-value: 1.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1890659908 16 RLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL 58
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
291-458 |
1.97e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 40.86 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKM---------IHRDDGIVISPI----------VKIGYFSQNLDILEvEKSILEN 351
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILgcldkptsgTYRVAGQDVATLdadalaqlrrEHFGFIFQRYHLLS-HLTAAQN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 352 VQ-------STSKQEETLIRTILARLHFFRDDVYKPVEiLSGGERVKVALAKLFVSDVNTLILDEPTNFLDI---EAARA 421
Cdd:PRK10535 107 VEvpavyagLERKQRLLRAQELLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARALMNGGQVILADEPTGALDShsgEEVMA 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 1890659908 422 LESLLQEYKGTVIFASHDRRfIENVATKMLVIQDKVI 458
Cdd:PRK10535 186 ILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEI 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-71 |
2.03e-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: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 4 LEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLC------------RAQCGL--L 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdgqditklpmhkRARLGIgyL 80
|
..
gi 1890659908 70 PQ 71
Cdd:cd03218 81 PQ 82
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-154 |
2.11e-03 |
|
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: 40.48 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 29 NDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQC------------------------------------------ 66
Cdd:TIGR02142 23 QGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrrigyvfqearlfphlsvrgnlrygmkr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 67 -----------------GLLPQLKRIDAIKSGGEVTQSYM-NALFSKaPKLLLADEPTTHLD----REHIEWLEKKLSQW 124
Cdd:TIGR02142 103 arpserrisferviellGIGHLLGRLPGRLSGGEKQRVAIgRALLSS-PRLLLMDEPLAALDdprkYEILPYLERLHAEF 181
|
170 180 190
....*....|....*....|....*....|
gi 1890659908 125 KGAFVIVSHDRAFLDALCTTIWEMDEGKIK 154
Cdd:TIGR02142 182 GIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-60 |
2.13e-03 |
|
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: 40.01 E-value: 2.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1890659908 19 FEIERLAIyendrIGLVGKNGSGKTTLLNILAKKISPEQGSV 60
Cdd:cd03267 42 FTIEKGEI-----VGFIGPNGAGKTTTLKILSGLLQPTSGEV 78
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
373-427 |
2.18e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890659908 373 FRDDVYKPVEILSGGER------VKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQ 427
Cdd:PRK01156 791 SRGGMVEGIDSLSGGEKtavafaLRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIE 851
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
34-61 |
2.31e-03 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 39.26 E-value: 2.31e-03
10 20
....*....|....*....|....*...
gi 1890659908 34 LVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:TIGR01189 31 VTGPNGIGKTTLLRILAGLLRPDSGEVR 58
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
149-252 |
2.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 149 DEGKIKEYKGNYSDYLEQKELERRRQQSAYEQYEKKKQALE---------RALELKKQKAERATKAPKKVSRSEANIMGA 219
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaeeakKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
90 100 110
....*....|....*....|....*....|....
gi 1890659908 220 KPYFAKKQKKLQKTAKAMETR-LEKLEKVEKIKE 252
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKkADEAKKAEEKKK 1547
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-174 |
2.36e-03 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 39.69 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 3 LLEALNV-KHYVKDRLLFEIErLAIYENDRIGLVGKNGSGKTTLL---NIL---------------------AKKISPEQ 57
Cdd:PRK09493 1 MIEFKNVsKHFGPTQVLHNID-LNIDQGEVVVIIGPSGSGKSTLLrciNKLeeitsgdlivdglkvndpkvdERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 58 GSVLcrAQCGLLPQL----------------KRIDAIK----------------------SGGEVTQ-SYMNALFSKaPK 98
Cdd:PRK09493 80 GMVF--QQFYLFPHLtalenvmfgplrvrgaSKEEAEKqarellakvglaerahhypselSGGQQQRvAIARALAVK-PK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 99 LLLADEPTTHLDRE--HiEWLE--KKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIKEyKGNYSDYLEQKELERRRQ 174
Cdd:PRK09493 157 LMLFDEPTSALDPElrH-EVLKvmQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAE-DGDPQVLIKNPPSQRLQE 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
384-453 |
2.40e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.22 E-value: 2.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 384 LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARALESLLQEYKG---TVIFASHDRRFIENVATKMLVI 453
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVM 249
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-176 |
2.66e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 40.60 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 26 IYENDRIGLVGKNGSGKTTLLNILAKKIsPEQGSVLC-------------RAQCG------LLPQ--------LKRIDAi 78
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKIngielreldpeswRKHLSwvgqnpQLPHgtlrdnvlLGNPDA- 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 79 kSGGEVTQSYMNALFS------------------------------------KAPKLLLADEPTTHLDREHiewlEKKLS 122
Cdd:PRK11174 451 -SDEQLQQALENAWVSeflpllpqgldtpigdqaaglsvgqaqrlalarallQPCQLLLLDEPTASLDAHS----EQLVM 525
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890659908 123 Q-----WKGAFVI-VSHDRAFLDAlCTTIWEMDEGKIKEyKGNYSDYLEQ----KELERRRQQS 176
Cdd:PRK11174 526 QalnaaSRRQTTLmVTHQLEDLAQ-WDQIWVMQDGQIVQ-QGDYAELSQAgglfATLLAHRQEE 587
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
165-254 |
2.75e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 165 EQKELERRRQQsAYEQYEKKKQALERALELKKQKAERATKAPKKvsrseanimgAKPYFAKKQKKLQKTAKAMETRLEKL 244
Cdd:PRK09510 102 RLKQLEKERLA-AQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA----------AKAKAEAEAKRAAAAAKKAAAEAKKK 170
|
90
....*....|
gi 1890659908 245 EKVEKIKETA 254
Cdd:PRK09510 171 AEAEAAKKAA 180
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
291-452 |
2.87e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 39.71 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 291 SFHVRGGDKLAVIGPNGSGKTTLLKKMIHR---DDGIVI-----------SPIVKIGY---FsQNLDILEvEKSILENVQ 353
Cdd:COG4674 30 SLYVDPGELRVIIGPNGAGKTTLMDVITGKtrpDSGSVLfggtdltgldeHEIARLGIgrkF-QKPTVFE-ELTVFENLE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 354 STSKQEETLIRTILARLH--------------FFRDDVYKPVEILSGGERVKVALAKLFVSDVNTLILDEPTNFL-DIEA 418
Cdd:COG4674 108 LALKGDRGVFASLFARLTaeerdrieevletiGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMtDAET 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 1890659908 419 ARALEsLLQEYKG--TVIFASHDRRFIENVATKMLV 452
Cdd:COG4674 188 ERTAE-LLKSLAGkhSVVVVEHDMEFVRQIARKVTV 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-61 |
4.70e-03 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 38.42 E-value: 4.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 4 LEALNVKHYVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL 58
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-61 |
4.74e-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: 39.78 E-value: 4.74e-03
10 20 30
....*....|....*....|....*....|
gi 1890659908 32 IGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:COG4615 361 VFIVGGNGSGKSTLAKLLTGLYRPESGEIL 390
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
24-153 |
5.19e-03 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 38.70 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL----------------CRAQCGLLPQ----LKRIDAIKS--G 81
Cdd:cd03256 22 LSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklkgkalrqLRRQIGMIFQqfnlIERLSVLENvlS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 82 GEVtqSYMNA------LFSKA------------------------------------------PKLLLADEPTTHLD--- 110
Cdd:cd03256 102 GRL--GRRSTwrslfgLFPKEekqralaalervglldkayqradqlsggqqqrvaiaralmqqPKLILADEPVASLDpas 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1890659908 111 -REHIEWLeKKLSQWKGAFVIVS-HDRAFLDALCTTIWEMDEGKI 153
Cdd:cd03256 180 sRQVMDLL-KRINREEGITVIVSlHQVDLAREYADRIVGLKDGRI 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
80-155 |
5.70e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 38.95 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 80 SGGeVTQSYMNAL-FSKAPKLLLADEPTTHLD----REHIEWLEKKLSQWKGAFVIVSHDRAFLDALCTTIWEMDEGKIK 154
Cdd:PRK11022 155 SGG-MSQRVMIAMaIACRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
.
gi 1890659908 155 E 155
Cdd:PRK11022 234 E 234
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
384-458 |
5.70e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.09 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 384 LSGGERVKVALAKLFVSDVNTLILDEPTNFLDIEAARA----LESLLQEYKGTVIFASHDRRFIENVATKMLVI-QDKVI 458
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREllpyLERLAREINIPILYVSHSLDEILRLADRVVVLeQGKVK 208
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
271-315 |
7.04e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 38.37 E-value: 7.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1890659908 271 IIRVEEVTGVIGQRVLWEKTSFHVRGGDKLAVIGPNGSGKTTLLK 315
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLN 50
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-61 |
7.21e-03 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 38.28 E-value: 7.21e-03
10 20 30
....*....|....*....|....*....|.
gi 1890659908 31 RIGLVGKNGSGKTTLLNILAkKISPEQGSVL 61
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMA-GLLPGQGEIL 53
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-61 |
7.23e-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: 38.09 E-value: 7.23e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1890659908 24 LAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVL 61
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIL 60
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-65 |
7.34e-03 |
|
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: 38.32 E-value: 7.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890659908 4 LEALNVKHYVKDR-LLFEIErLAIYENDRIGLVGKNGSGKTTLLNILAK-----KISPEQGSVLCRAQ 65
Cdd:cd03260 1 IELRDLNVYYGDKhALKDIS-LDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGK 67
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
149-254 |
7.44e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 149 DEGKIKEYKGNYSDYLEQKELERRRQQSAYEQYEKKKQALE--------RALELKKQKAERATKAPKKVSRSEAnimgak 220
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEakkkaeeaKKAEEAKKKAEEAKKADEAKKKAEE------ 1481
|
90 100 110
....*....|....*....|....*....|....
gi 1890659908 221 pyfAKKQKKLQKTAKAMETRLEKLEKVEKIKETA 254
Cdd:PTZ00121 1482 ---AKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
164-281 |
7.56e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 164 LEQK----ELERRRQQSAYEQYEKKKQALERALELKKQKAERATKAPKKVSRSEANIMGAKPYFAKKQKKLQKTAKAMET 239
Cdd:PRK00409 532 LEQKaeeaEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIE 611
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1890659908 240 RLEKLEKVEKIKETAPINMSLPhEDTFQ--DRIIIRVEEVTGVI 281
Cdd:PRK00409 612 ARKRLNKANEKKEKKKKKQKEK-QEELKvgDEVKYLSLGQKGEV 654
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-172 |
8.32e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 38.25 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 1 MILLEALNVKH-YVKDRLLFEIERLAIYENDRIGLVGKNGSGKTTLLNILAKKISPEQGSVLCRAQ-------------C 66
Cdd:PRK13652 1 MHLIETRDLCYsYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890659908 67 GLLPQ---------------------------------------------LKRIDAIKSGGEVTQSYMNALFSKAPKLLL 101
Cdd:PRK13652 81 GLVFQnpddqifsptveqdiafgpinlgldeetvahrvssalhmlgleelRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890659908 102 ADEPTTHLD----REHIEWLeKKLSQWKGAFVIVS-HDRAFLDALCTTIWEMDEGKIKEYkGNYSDYLEQKELERR 172
Cdd:PRK13652 161 LDEPTAGLDpqgvKELIDFL-NDLPETYGMTVIFStHQLDLVPEMADYIYVMDKGRIVAY-GTVEEIFLQPDLLAR 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
97-155 |
9.47e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 38.53 E-value: 9.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890659908 97 PKLLLADEPTTHLDR---EHIEWLEKKLSQ-WKGAFVIVSHDRAFLDALCTTIWEMDEGKIKE 155
Cdd:PRK15134 444 PSLIILDEPTSSLDKtvqAQILALLKSLQQkHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| |
