|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-456 |
0e+00 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 900.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKLSSFPGDYENYLLEKEEALRVEEMQNAEFDKK 80
Cdd:PRK11147 183 PTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVEELQNAEFDRK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 81 LAQEEVWIRQGIKARRTRNEGRVRALKKLREERINRREVQGKAVIQIDDGQRSGKIVFEAENLNFGFEGKEIVKDFSFNI 160
Cdd:PRK11147 263 LAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQV 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 161 MRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREILDPEKSVIDNLADGKQEVTVGGRERHALS 240
Cdd:PRK11147 343 QRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEVMVNGRPRHVLG 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 241 YLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSHDRQFVDN 320
Cdd:PRK11147 423 YLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDN 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 321 TVMTSWIFEGNGVVEEFVGGYHDAQQQRKQAIEYRQvekPSKPEKVVEETPKTAPVKAKAKKLSYKLQRELEALPLRLEE 400
Cdd:PRK11147 503 TVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQ---PAVKKKEEAAAPKAETVKRSSKKLSYKLQRELEQLPQLLED 579
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2793968422 401 LETQIETLQEEVNDPSFFSKSVEQTQPVLDKLSAAEQELEVAFERWEELEALQQES 456
Cdd:PRK11147 580 LEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALKNGG 635
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-347 |
4.75e-165 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 475.32 E-value: 4.75e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKLSSFPGDYENYLLEKEEALRVEEMQNAEFDKK 80
Cdd:COG0488 179 PTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRAERLEQEAAAYAKQQKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 81 LAQEEVWIRQ-GIKARR-TRNEGRVRALKKLREERINRREvqGKAVIQIDDGQRSGKIVFEAENLNFGFEGKEIVKDFSF 158
Cdd:COG0488 259 IAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVLELEGLSKSYGDKTLLDDLSL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 159 NIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREILDPEKSVIDNLADGKQevtvGGRERHA 238
Cdd:COG0488 337 RIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTVLDELRDGAP----GGTEQEV 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 239 LSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSHDRQFV 318
Cdd:COG0488 413 RGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFL 492
|
330 340
....*....|....*....|....*....
gi 2793968422 319 DNTVMTSWIFEgNGVVEEFVGGYHDAQQQ 347
Cdd:COG0488 493 DRVATRILEFE-DGGVREYPGGYDDYLEK 520
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-349 |
6.52e-92 |
|
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: 288.76 E-value: 6.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKLSSFPGDYENYLLEKEEALRVEEMQNAEFDKK 80
Cdd:TIGR03719 188 PTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKT 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 81 LAQEEVWIRQGIKARRTRNEGRVRALKKLREERINRREvqGKAVIQIDDGQRSGKIVFEAENLNFGFEGKEIVKDFSFNI 160
Cdd:TIGR03719 268 LKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 161 MRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREILDPEKSVIDNLADGKQEVTVGGRERHALS 240
Cdd:TIGR03719 346 PPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRA 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 241 YLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSHDRQFVDN 320
Cdd:TIGR03719 426 YVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDR 505
|
330 340
....*....|....*....|....*....
gi 2793968422 321 TVMTSWIFEGNGVVEEFVGGYHDAQQQRK 349
Cdd:TIGR03719 506 IATHILAFEGDSHVEWFEGNFSEYEEDKK 534
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-350 |
6.09e-88 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 278.54 E-value: 6.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKLSSFPGDYENYLLEKEEALRVEEMQNAEFDKK 80
Cdd:PRK11819 190 PTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKA 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 81 LAQEEVWIRQGIKARRTRNEGRVRALKKLREERINRREvqGKAVIQIDDGQRSGKIVFEAENLNFGFEGKEIVKDFSFNI 160
Cdd:PRK11819 270 LKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRN--ETNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 161 MRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREILDPEKSVIDNLADGKQEVTVGGRERHALS 240
Cdd:PRK11819 348 PPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKVGNREIPSRA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 241 YLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSHDRQFVDN 320
Cdd:PRK11819 428 YVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDR 507
|
330 340 350
....*....|....*....|....*....|
gi 2793968422 321 TVMTSWIFEGNGVVEEFVGGYHDAQQQRKQ 350
Cdd:PRK11819 508 IATHILAFEGDSQVEWFEGNFQEYEEDKKR 537
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-343 |
8.84e-63 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 212.06 E-value: 8.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKLSSFPGDYENYLlekEEALRVEEMQNAEFDKK 80
Cdd:PRK15064 182 PTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYM---TAATQARERLLADNAKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 81 LAQ-EEVwirQGIKARRTRNEGRVR-ALKKLRE-ERINRREVqgKA------VIQIDDGQRSGKIVFEAENLNFGFEGKE 151
Cdd:PRK15064 259 KAQiAEL---QSFVSRFSANASKAKqATSRAKQiDKIKLEEV--KPssrqnpFIRFEQDKKLHRNALEVENLTKGFDNGP 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 152 IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQ-YREILDPEKSVIDNLADGKQEvt 230
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDFENDLTLFDWMSQWRQE-- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 231 vGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLL 310
Cdd:PRK15064 412 -GDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIF 490
|
330 340 350
....*....|....*....|....*....|....
gi 2793968422 311 VSHDRQFVdNTVMTSWI-FEGNGVVeEFVGGYHD 343
Cdd:PRK15064 491 VSHDREFV-SSLATRIIeITPDGVV-DFSGTYEE 522
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
139-332 |
1.22e-51 |
|
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: 171.09 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQyreildpeksv 218
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 idnladgkqevtvggrerhalsylqdflfspkrartpvkaLSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLE 298
Cdd:cd03221 71 ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....
gi 2793968422 299 DLLANYQGTLLLVSHDRQFVDNTVMTSWIFEGNG 332
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
140-358 |
5.44e-48 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 172.17 E-value: 5.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 140 AENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREiLDPEKSVI 219
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPP-LDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 220 DNLADGKQEVTVGGRERHALSY--------------LQDFL--------------------FSPKRARTPVKALSGGEKN 265
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAklaepdedlerlaeLQEEFealggweaearaeeilsglgFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 266 RLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSHDRQFVDNTVmtSWIFE-GNGVVEEFVGGYHDA 344
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVA--TRILElDRGKLTLYPGNYSAY 237
|
250
....*....|....
gi 2793968422 345 QQQRKQAIEYRQVE 358
Cdd:COG0488 238 LEQRAERLEQEAAA 251
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-455 |
7.77e-47 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 171.12 E-value: 7.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKLSSFPGDYENYllEKEEALRVEEmQNAEFD-- 78
Cdd:PRK10636 176 PTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF--EVQRATRLAQ-QQAMYEsq 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 79 -KKLAQEEVWI-RQGIKARRTRN-EGRVRALKklREERINRREVQGKAVIQIDDGQRSGKIVFEAENLNFGFEGKEIVKD 155
Cdd:PRK10636 253 qERVAHLQSYIdRFRAKATKAKQaQSRIKMLE--RMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSAGYGDRIILDS 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 156 FSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYR-EILDPEKSVIDNLADGKQEVTvggr 234
Cdd:PRK10636 331 IKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQlEFLRADESPLQHLARLAPQEL---- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 235 ERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSHD 314
Cdd:PRK10636 407 EQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHD 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 315 RQFVDNTVMTSWIFEgNGVVEEFVGGYHDAQQ----QRKQaiEYRQVEKPSKPEKVVEETPKTAPVK-AKAKKLSYKLQR 389
Cdd:PRK10636 487 RHLLRSTTDDLYLVH-DGKVEPFDGDLEDYQQwlsdVQKQ--ENQTDEAPKENNANSAQARKDQKRReAELRTQTQPLRK 563
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2793968422 390 ELEALPLRLEELETQIETLQEEVNDPSFF--SKSVEQTQpVLDKLSAAEQELEVAFERW----EELEALQQE 455
Cdd:PRK10636 564 EIARLEKEMEKLNAQLAQAEEKLGDSELYdqSRKAELTA-CLQQQASAKSGLEECEMAWleaqEQLEQMLLE 634
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-343 |
5.34e-39 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 149.63 E-value: 5.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKLSSFPGDYENYLLEKEEALRVEEMQNAEFDKK 80
Cdd:PLN03073 371 PTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERS 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 81 LAQEEVWI---RQGIKaRRTRNEGRVRALKKLR--EERINRREVQGKAVIQIDdgqRSGKIVFEAENLNFGFEGKEIV-K 154
Cdd:PLN03073 451 RSHMQAFIdkfRYNAK-RASLVQSRIKALDRLGhvDAVVNDPDYKFEFPTPDD---RPGPPIISFSDASFGYPGGPLLfK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 155 DFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYR-EILDPEKSVIDNLAdgkqEVTVGG 233
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHvDGLDLSSNPLLYMM----RCFPGV 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 234 RERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSH 313
Cdd:PLN03073 603 PEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSH 682
|
330 340 350
....*....|....*....|....*....|
gi 2793968422 314 DRQFVDNTVMTSWIFEgNGVVEEFVGGYHD 343
Cdd:PLN03073 683 DEHLISGSVDELWVVS-EGKVTPFHGTFHD 711
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
138-316 |
7.90e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.69 E-value: 7.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKL-----------EVAYFD 206
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 QyreilDP---EKSVIDNLADGKQEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILD 283
Cdd:COG4619 81 Q-----EPalwGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 2793968422 284 EPTNDLDIETLELLEDLLANY----QGTLLLVSHDRQ 316
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPE 192
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
153-287 |
3.19e-29 |
|
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: 111.59 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG-----------TKLEVAYFDQYREiLDPEKSVIDN 221
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQ-LFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 222 LADGKQEVTVGGRER-----HALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTN 287
Cdd:pfam00005 80 LRLGLLLKGLSKREKdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
137-323 |
6.18e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.03 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLE-----VAYFDQYRE 210
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlFGKPPRrarrrIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 211 I---------------LDPEKSVIDNL-ADGKQEVtvggreRHALSY--LQDFlfspkrARTPVKALSGGEKNRLLLARI 272
Cdd:COG1121 86 VdwdfpitvrdvvlmgRYGRRGLFRRPsRADREAV------DEALERvgLEDL------ADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2793968422 273 FLKSNNLLILDEPTNDLDIETLELLE---DLLANYQGTLLLVSHD----RQFVDNTVM 323
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYellRELRREGKTILVVTHDlgavREYFDRVLL 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
139-323 |
2.58e-28 |
|
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: 111.09 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLE-----VAYFDQYREI- 211
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvFGKPLEkerkrIGYVPQRRSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 --------------LDPEKSVIDNL-ADGKQEVtvggreRHALSYLQDFLFspkrARTPVKALSGGEKNRLLLARIFLKS 276
Cdd:cd03235 81 rdfpisvrdvvlmgLYGHKGLFRRLsKADKAKV------DEALERVGLSEL----ADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2793968422 277 NNLLILDEPTNDLDIETLELLEDLLANYQG---TLLLVSHDRQ----FVDNTVM 323
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGlvleYFDRVLL 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
139-291 |
4.71e-27 |
|
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: 106.75 E-value: 4.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLE----------VAYFDQ 207
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILlDGKDLAslspkelarkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 208 YREILDpeksvIDNLADgkqevtvggRerhalsylqdflfspkrartPVKALSGGEKNRLLLARIFLKSNNLLILDEPTN 287
Cdd:cd03214 81 ALELLG-----LAHLAD---------R--------------------PFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
....
gi 2793968422 288 DLDI 291
Cdd:cd03214 127 HLDI 130
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
139-291 |
1.14e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 107.46 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLEVAYFDQYREI------ 211
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVARDPAEVRRRIgyvpqe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 --LDPEKSVIDNLA--------DGKQevtvggRERHALSYLQDF-LfsPKRARTPVKALSGGEKNRLLLARIFLKSNNLL 280
Cdd:COG1131 82 paLYPDLTVRENLRffarlyglPRKE------ARERIDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170
....*....|.
gi 2793968422 281 ILDEPTNDLDI 291
Cdd:COG1131 154 ILDEPTSGLDP 164
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
139-291 |
8.67e-26 |
|
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: 102.86 E-value: 8.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGrlhcgtklEVAYFDqyreildpeKSV 218
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG--------EIKVLG---------KDI 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2793968422 219 IDNLADGKQEVtvggrerhalSYL-QDFLFSPK-RARTPVKaLSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:cd03230 65 KKEPEEVKRRI----------GYLpEEPSLYENlTVRENLK-LSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
139-347 |
1.46e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 109.46 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGF-EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLE----------VAYFD 206
Cdd:COG4988 338 ELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILiNGVDLSdldpaswrrqIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 QyreilDP---EKSVIDNLADGKQEVTvggRE--RHAL--SYLQDFLFS-PKRARTPV----KALSGGEKNRLLLARIFL 274
Cdd:COG4988 418 Q-----NPylfAGTIRENLRLGRPDAS---DEelEAALeaAGLDEFVAAlPDGLDTPLgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2793968422 275 KSNNLLILDEPTNDLDIETLELLEDLLANY-QG-TLLLVSHDRQFVDNtvMTSWIFEGNGVVEEfVGGYHDAQQQ 347
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTVILITHRLALLAQ--ADRILVLDDGRIVE-QGTHEELLAK 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
112-319 |
3.97e-25 |
|
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: 108.31 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 112 ERINRREVQGKAVIQIDDG-QRSGKIVFEAENLNFGFEG--KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLK 188
Cdd:COG4987 307 RRLNELLDAPPAVTEPAEPaPAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 189 PDSGRLHC-GTKLE----------VAYFDQYREILDpeKSVIDNLADGKQEVTvggRE--RHALS--YLQDFLFS-PKRA 252
Cdd:COG4987 387 PQSGSITLgGVDLRdldeddlrrrIAVVPQRPHLFD--TTLRENLRLARPDAT---DEelWAALErvGLGDWLAAlPDGL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2793968422 253 RTPV----KALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD-IETLELLEDLLANYQG-TLLLVSHDRQFVD 319
Cdd:COG4987 462 DTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDaATEQALLADLLEALAGrTVLLITHRLAGLE 534
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
137-321 |
6.10e-25 |
|
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: 101.79 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLEVAYFDQYREI---- 211
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwNGEPIRDAREDYRRRLaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 ----LDPEKSVIDNL---ADGKQEVTVGGRERHALSYLQdfLfsPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDE 284
Cdd:COG4133 82 hadgLKPELTVRENLrfwAALYGLRADREAIDEALEAVG--L--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2793968422 285 PTNDLD---IETLELLEDLLANYQGTLLLVSHDRQFVDNT 321
Cdd:COG4133 158 PFTALDaagVALLAELIAAHLARGGAVLLTTHQPLELAAA 197
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
139-313 |
6.50e-25 |
|
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: 100.54 E-value: 6.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEG--KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhcgtklevaYFDQYreildpek 216
Cdd:cd03228 2 EFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI---------LIDGV-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 svidNLADGKQEVTvggreRHALSYL-QD-FLFSpkrarTPVKA--LSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIE 292
Cdd:cd03228 65 ----DLRDLDLESL-----RKNIAYVpQDpFLFS-----GTIREniLSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180
....*....|....*....|...
gi 2793968422 293 TLELLEDLLANYQG--TLLLVSH 313
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAH 153
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
139-320 |
6.82e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 100.01 E-value: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGrlhcgtklevayfdqyreildpeksv 218
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 idnladgkqEVTVGGRERHALsylqdflfSPKRARTP---VKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLE 295
Cdd:cd00267 55 ---------EILIDGKDIAKL--------PLEELRRRigyVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180
....*....|....*....|....*...
gi 2793968422 296 LLEDLLANYQG---TLLLVSHDRQFVDN 320
Cdd:cd00267 118 RLLELLRELAEegrTVIIVTHDPELAEL 145
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-290 |
7.97e-25 |
|
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: 106.91 E-value: 7.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 1 PTNHLDVAT----IEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKLssfpgdyenyllekeealrVEEMQNAE 76
Cdd:COG1123 169 PTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI-------------------VEDGPPEE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 77 FdkklaqeevwirqgikarrTRNEGRVRALKKLREERINRREVQgkaviqiddgqRSGKIVFEAENLNFGFEGKE----- 151
Cdd:COG1123 230 I-------------------LAAPQALAAVPRLGAARGRAAPAA-----------AAAEPLLEVRNLSKRYPVRGkggvr 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 152 IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG-----TKLEVAYFDQYREI----------LDPEK 216
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkdltKLSRRSLRELRRRVqmvfqdpyssLNPRM 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2793968422 217 SVIDNLADG---KQEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:COG1123 360 TVGDIIAEPlrlHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD 436
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
137-291 |
9.10e-25 |
|
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: 102.43 E-value: 9.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLE----------VAYF 205
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLlDGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 206 DQYREILDPeKSVIDnladgkqevTVG-GRERHalsylQDFLFSPKR------------------ARTPVKALSGGEKNR 266
Cdd:COG1120 81 PQEPPAPFG-LTVRE---------LVAlGRYPH-----LGLFGRPSAedreaveealertglehlADRPVDELSGGERQR 145
|
170 180
....*....|....*....|....*
gi 2793968422 267 LLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDL 170
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
149-409 |
3.45e-24 |
|
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: 105.40 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 149 GKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSG--RLHCGTKleVAYFDQYREiLDPEKSVIDNLADGK 226
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGeaRPQPGIK--VGYLPQEPQ-LDPTKTVRENVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 227 QEVtvggreRHALSYLQ-------------DFLFSpKRAR------------------------------TPVKALSGGE 263
Cdd:TIGR03719 94 AEI------KDALDRFNeisakyaepdadfDKLAA-EQAElqeiidaadawdldsqleiamdalrcppwdADVTKLSGGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 264 KNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSHDRQFVDNtvMTSWIFE---GNGVVEEfvGG 340
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDN--VAGWILEldrGRGIPWE--GN 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2793968422 341 YHD--AQQQRKQAIEYRQVEKPSKPEKV----VEETPKTAPVKAKAKKLSYKlqrELEAlplrlEELETQIETLQ 409
Cdd:TIGR03719 243 YSSwlEQKQKRLEQEEKEESARQKTLKRelewVRQSPKGRQAKSKARLARYE---ELLS-----QEFQKRNETAE 309
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
133-290 |
5.30e-24 |
|
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: 105.30 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 133 SGKIVFEaeNLNFGFEG--KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhcgtklevaYFDQY-- 208
Cdd:COG2274 471 KGDIELE--NVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI---------LIDGIdl 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 REIlDPEK-----------------SVIDNLADGKQEVTvggRER--HA--LSYLQDFLFS-PKRARTPV----KALSGG 262
Cdd:COG2274 540 RQI-DPASlrrqigvvlqdvflfsgTIRENITLGDPDAT---DEEiiEAarLAGLHDFIEAlPMGYDTVVgeggSNLSGG 615
|
170 180
....*....|....*....|....*...
gi 2793968422 263 EKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALD 643
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
139-291 |
5.34e-23 |
|
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: 97.24 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCG---------TKLEVAYFDQY 208
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSiLIDGedvrkepreARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 REiLDPEKSVIDNL---ADGKQevtVGGRERHAL--SYLQDFLFSPKRARtPVKALSGGEKNRLLLARIFLKSNNLLILD 283
Cdd:COG4555 83 RG-LYDRLTVRENIryfAELYG---LFDEELKKRieELIELLGLEEFLDR-RVGELSTGMKKKVALARALVHDPKVLLLD 157
|
....*...
gi 2793968422 284 EPTNDLDI 291
Cdd:COG4555 158 EPTNGLDV 165
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
139-319 |
7.71e-23 |
|
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: 96.80 E-value: 7.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGF----EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAY--------- 204
Cdd:COG1124 3 EVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVTRRRrkafrrrvq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 205 --FDQYREILDPEKSVIDNLADGKQEVTVGGRERHALSYLQ------DFLFspkraRTPvKALSGGEKNRLLLARIFLKS 276
Cdd:COG1124 83 mvFQDPYASLHPRHTVDRILAEPLRIHGLPDREERIAELLEqvglppSFLD-----RYP-HQLSGGQRQRVAIARALILE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2793968422 277 NNLLILDEPTNDLDIETLELL----EDLLANYQGTLLLVSHDRQFVD 319
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEIlnllKDLREERGLTYLFVSHDLAVVA 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
163-382 |
1.37e-22 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 100.63 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 163 GDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREILDpeKSVIDNLADGKQE-------------- 228
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALP--QPALEYVIDGDREyrqleaqlhdaner 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 229 ------VTVGGR---------ERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIET 293
Cdd:PRK10636 105 ndghaiATIHGKldaidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 294 LELLEDLLANYQGTLLLVSHDRQFVDnTVMTSWIFEGNGVVEEFVGGYHDAQQQRKQAIEYRQVEKPSKPEKVVEETPKT 373
Cdd:PRK10636 185 VIWLEKWLKSYQGTLILISHDRDFLD-PIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYI 263
|
....*....
gi 2793968422 374 APVKAKAKK 382
Cdd:PRK10636 264 DRFRAKATK 272
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
139-315 |
2.88e-22 |
|
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: 99.28 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGK-EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKL----------EVAYFD 206
Cdd:TIGR02857 323 EFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLadadadswrdQIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 QYREILdpEKSVIDNLADGKQEVTVGGRERHA-LSYLQDFLFS-PKRARTPV----KALSGGEKNRLLLARIFLKSNNLL 280
Cdd:TIGR02857 403 QHPFLF--AGTIAENIRLARPDASDAEIREALeRAGLDEFVAAlPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190
....*....|....*....|....*....|....*..
gi 2793968422 281 ILDEPTNDLDIETLELLEDLLANY-QG-TLLLVSHDR 315
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALaQGrTVLLVTHRL 517
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
138-290 |
5.03e-22 |
|
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: 92.76 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGFEGKE--IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhcgtklevayfdqyreildpe 215
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI--------------------- 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2793968422 216 ksvidnLADGKQEVTVGGRERHALSYLQD--FLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:cd03247 60 ------TLDGVPVSDLEKALSSLISVLNQrpYLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
139-322 |
8.26e-22 |
|
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: 92.92 E-value: 8.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKE--IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAYFDQYREIL--- 212
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 --DPE-----KSVIDNLADG-------KQEVtvggRERhALSYLQDFLFSPKRARtPVKALSGGEKNRLLLARIFLKSNN 278
Cdd:cd03225 81 fqNPDdqffgPTVEEEVAFGlenlglpEEEI----EER-VEEALELVGLEGLRDR-SPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2793968422 279 LLILDEPTNDLDIETLELLEDLLANYQG---TLLLVSHDRQFVDNTV 322
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELA 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
138-318 |
1.70e-21 |
|
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: 92.78 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGF-EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLEVAYFDQYRE---IL 212
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvDGKDITKKNLRELRRkvgLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 --DPE-----KSVIDNLADG-------KQEVtvggRER--HALSY--LQDFlfspkrARTPVKALSGGEKNRLLLARIFL 274
Cdd:COG1122 81 fqNPDdqlfaPTVEEDVAFGpenlglpREEI----RERveEALELvgLEHL------ADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2793968422 275 KSNNLLILDEPTNDLDIETLELLEDLLANYQG---TLLLVSHDRQFV 318
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLV 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
139-317 |
1.78e-21 |
|
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: 91.93 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGF-EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-------LHCGTKLEVAYF---DQ 207
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSillngkpIKAKERRKSIGYvmqDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 208 YREILdpEKSVIDNLADGKQEvtVGGRERHALSYLQDFLFSPKRARTPvKALSGGEKNRLLLARIFLKSNNLLILDEPTN 287
Cdd:cd03226 81 DYQLF--TDSVREELLLGLKE--LDAGNEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190
....*....|....*....|....*....|...
gi 2793968422 288 DLD---IETLELLEDLLANYQGTLLLVSHDRQF 317
Cdd:cd03226 156 GLDyknMERVGELIRELAAQGKAVIVITHDYEF 188
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
149-405 |
3.22e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 96.34 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 149 GKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDqlKPDSG--RLHCGTKleVAYFDQYREiLDPEKSVIDNLAD 224
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagVD--KEFEGeaRPAPGIK--VGYLPQEPQ-LDPEKTVRENVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 225 GKQEVTVGGRERHALSY------------------LQ-------------------DFLFSPKrARTPVKALSGGEKNRL 267
Cdd:PRK11819 94 GVAEVKAALDRFNEIYAayaepdadfdalaaeqgeLQeiidaadawdldsqleiamDALRCPP-WDAKVTKLSGGERRRV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 268 LLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSHDRQFVDNtvMTSWIFE---GNGVVEEfvGGYHD- 343
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDN--VAGWILEldrGRGIPWE--GNYSSw 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 344 -AQQQRKQAIEYRQVEKPSKPEKV----VEETPKTAPVKAKAkklsyKLQR--EL--EALPLRLEELETQI 405
Cdd:PRK11819 249 lEQKAKRLAQEEKQEAARQKALKRelewVRQSPKARQAKSKA-----RLARyeELlsEEYQKRNETNEIFI 314
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
138-318 |
4.28e-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: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlevayfdqyreildpeks 217
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 218 vidNLADGKQEVtvgGRERHALSYL-QDF-LFSPKRARTPVK-ALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETL 294
Cdd:cd03229 63 ---DLTDLEDEL---PPLRRRIGMVfQDFaLFPHLTVLENIAlGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180
....*....|....*....|....*...
gi 2793968422 295 ELLEDL----LANYQGTLLLVSHDRQFV 318
Cdd:cd03229 137 REVRALlkslQAQLGITVVLVTHDLDEA 164
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
139-290 |
1.02e-20 |
|
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: 90.22 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGK----EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH------CGTKLEVAY-FDQ 207
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYvFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 208 YReiLDPEKSVIDNLADGKQEVTVGGRER--HALSYLQDFLFSPKRARTPvKALSGGEKNRLLLARIFLKSNNLLILDEP 285
Cdd:cd03293 82 DA--LLPWLTVLDNVALGLELQGVPKAEAreRAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
....*
gi 2793968422 286 TNDLD 290
Cdd:cd03293 159 FSALD 163
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
139-315 |
1.74e-20 |
|
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: 89.50 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKL---------EVAY-FDQY 208
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperrNIGMvFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 reILDPEKSVIDNLADG--KQEVTVGGRERHALSYLQDFLFSPKRARTPvKALSGGEKNRLLLARIFLKSNNLLILDEPT 286
Cdd:cd03259 82 --ALFPHLTVAENIAFGlkLRGVPKAEIRARVRELLELVGLEGLLNRYP-HELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|...
gi 2793968422 287 NDLDIETLELLEDLLANYQG----TLLLVSHDR 315
Cdd:cd03259 159 SALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
147-290 |
2.46e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.82 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 147 FEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhcgTKLEVAYFDQYR------------EILDP 214
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---TVLGVPVPARARlararigvvpqfDNLDL 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2793968422 215 EKSVIDNLADGKQEVTVGGRERHA-LSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK13536 128 EFTVRENLLVFGRYFGMSTREIEAvIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
139-323 |
6.45e-20 |
|
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: 88.33 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGK----EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGTKL------------- 200
Cdd:cd03257 3 EVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSiIFDGKDLlklsrrlrkirrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 201 EVAY-FDQYREILDPEKSVIDNLADGKQEVTVGG----RERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLK 275
Cdd:cd03257 83 EIQMvFQDPMSSLNPRMTIGEQIAEPLRIHGKLSkkeaRKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2793968422 276 SNNLLILDEPTNDLDIETLELL----EDLLANYQGTLLLVSHD----RQFVDNT-VM 323
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQIldllKKLQEELGLTLLFITHDlgvvAKIADRVaVM 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
134-313 |
1.18e-19 |
|
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: 87.26 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEaeNLNFGFEGKEI--VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhcgtklevaYFD--QYR 209
Cdd:cd03245 1 GRIEFR--NVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV---------LLDgtDIR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 210 EIlDPEK-----------------SVIDNLADGKQEVTVGGRERHA-LSYLQDFL-FSPKRARTPV----KALSGGEKNR 266
Cdd:cd03245 70 QL-DPADlrrnigyvpqdvtlfygTLRDNITLGAPLADDERILRAAeLAGVTDFVnKHPNGLDLQIgergRGLSGGQRQA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2793968422 267 LLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQG--TLLLVSH 313
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH 197
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
139-319 |
1.36e-19 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 87.16 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNF----GFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKL------------- 200
Cdd:cd03255 2 ELKNLSKtyggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvDGTDIsklsekelaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 201 -EVAY-FDQYReiLDPEKSVIDNLADGKQEVTVGGRERHA-LSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSN 277
Cdd:cd03255 82 rHIGFvFQSFN--LLPDLTALENVELPLLLAGVPKKERRErAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2793968422 278 NLLILDEPTNDLDIETLELL----EDLLANYQGTLLLVSHDRQFVD 319
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVmellRELNKEAGTTIVVVTHDPELAE 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
139-285 |
1.38e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.84 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGK----EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC------GTKLEVAY-FDQ 207
Cdd:COG1116 9 ELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVvFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 208 YReiLDPEKSVIDNLADGKQEVTVGGRERH--ALSYLQDFLFSPKRARTPvKALSGGEKNRLLLARIFLKSNNLLILDEP 285
Cdd:COG1116 89 PA--LLPWLTVLDNVALGLELRGVPKAERRerARELLELVGLAGFEDAYP-HQLSGGMRQRVAIARALANDPEVLLMDEP 165
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
139-290 |
1.65e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.71 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CG---------TKLEVAYFDQY 208
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlCGepvpsrarhARQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 rEILDPEKSVIDNL-ADGKQEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTN 287
Cdd:PRK13537 89 -DNLDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
...
gi 2793968422 288 DLD 290
Cdd:PRK13537 168 GLD 170
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
138-313 |
2.45e-19 |
|
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: 84.96 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGFEGKE--IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAYFDQYREIldp 214
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELGDH--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 215 eksvidnladgkqevtVGgrerhalsYL-QDF-LFSPKRARTpvkALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIE 292
Cdd:cd03246 78 ----------------VG--------YLpQDDeLFSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180
....*....|....*....|....
gi 2793968422 293 TLELLEDLLANYQ---GTLLLVSH 313
Cdd:cd03246 131 GERALNQAIAALKaagATRIVIAH 154
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
137-291 |
3.10e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 86.68 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLldqlkpdSGRLHCGTKLEVAYFDQYR------E 210
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLI-------TGDLPPTYGNDVRLFGERRggedvwE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 211 I--------------LDPEKSVIDNLADGK-------QEVTVGGRERhALSYLQDFLFSPKRARtPVKALSGGEKNRLLL 269
Cdd:COG1119 76 LrkriglvspalqlrFPRDETVLDVVLSGFfdsiglyREPTDEQRER-ARELLELLGLAHLADR-PFGTLSQGEQRRVLI 153
|
170 180
....*....|....*....|..
gi 2793968422 270 ARIFLKSNNLLILDEPTNDLDI 291
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDL 175
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
133-290 |
4.09e-19 |
|
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: 89.73 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 133 SGKIVFEAENLNFGFEGKEIV-KDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL-----------HCGTKL 200
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssldQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 201 EVAYFDQYREILDpeKSVIDNLADGKQEVTvgGRE-RHALSY--LQDFLFS-PKRARTPV----KALSGGEKNRLLLARI 272
Cdd:TIGR02868 410 RVSVCAQDAHLFD--TTVRENLRLARPDAT--DEElWAALERvgLADWLRAlPDGLDTVLgeggARLSGGERQRLALARA 485
|
170
....*....|....*...
gi 2793968422 273 FLKSNNLLILDEPTNDLD 290
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLD 503
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
133-290 |
4.11e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.84 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 133 SGKIVFEaeNLNFGF-EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGTKL-EVAYfDQYR 209
Cdd:COG1132 337 RGEIEFE--NVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRiLIDGVDIrDLTL-ESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 210 EIL-----DP---EKSVIDNLADGKQEVTvggRE--RHAL--SYLQDFLFS-PKRARTPV----KALSGGEKNRLLLARI 272
Cdd:COG1132 414 RQIgvvpqDTflfSGTIRENIRYGRPDAT---DEevEEAAkaAQAHEFIEAlPDGYDTVVgergVNLSGGQRQRIAIARA 490
|
170
....*....|....*...
gi 2793968422 273 FLKSNNLLILDEPTNDLD 290
Cdd:COG1132 491 LLKDPPILILDEATSALD 508
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
382-451 |
7.77e-19 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 80.20 E-value: 7.77e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 382 KLSYKLQRELEALPLRLEELETQIETLQEEVNDPSFFSKSvEQTQPVLDKLSAAEQELEVAFERWEELEA 451
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSDY-EKLQELSAELEELEAELEELYERWEELEE 69
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
141-290 |
1.20e-18 |
|
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: 84.59 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKE--IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhCGTKLEVAYF--DQYREIL---- 212
Cdd:cd03251 4 KNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI-LIDGHDVRDYtlASLRRQIglvs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 -DP---EKSVIDNLADGKQEVTVGGRERHA-LSYLQDFLFS-PKRARTPVK----ALSGGEKNRLLLARIFLKSNNLLIL 282
Cdd:cd03251 83 qDVflfNDTVAENIAYGRPGATREEVEEAArAANAHEFIMElPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILIL 162
|
....*...
gi 2793968422 283 DEPTNDLD 290
Cdd:cd03251 163 DEATSALD 170
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
139-291 |
1.23e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFD-QY-REI----- 211
Cdd:PRK11231 4 RTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLaRRLallpq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 --LDPEK-SVIDNLADGKQE-VTVGGR-----ERHALSYLQDFLFSpKRARTPVKALSGGEKNRLLLARIFLKSNNLLIL 282
Cdd:PRK11231 84 hhLTPEGiTVRELVAYGRSPwLSLWGRlsaedNARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
....*....
gi 2793968422 283 DEPTNDLDI 291
Cdd:PRK11231 163 DEPTTYLDI 171
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1-48 |
1.34e-18 |
|
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: 82.11 E-value: 1.34e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGK 48
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
139-290 |
1.35e-18 |
|
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: 84.34 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHcgtkleVAYFDQYRE-------- 210
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT------VAGHDVVREprevrrri 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 211 -------ILDPEKSVIDNLADGKQEVTVGGRE-RHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLIL 282
Cdd:cd03265 76 givfqdlSVDDELTGWENLYIHARLYGVPGAErRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
....*...
gi 2793968422 283 DEPTNDLD 290
Cdd:cd03265 156 DEPTIGLD 163
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
125-290 |
1.65e-18 |
|
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: 87.85 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 125 IQIDDGQRS-----GKIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGT 198
Cdd:TIGR02203 315 PEKDTGTRAierarGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQiLLDGH 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 199 KLE----------VAYFDQYREILDpeKSVIDNLADGKQEVTVGGRERHAL--SYLQDFL-FSPKRARTPVKA----LSG 261
Cdd:TIGR02203 395 DLAdytlaslrrqVALVSQDVVLFN--DTIANNIAYGRTEQADRAEIERALaaAYAQDFVdKLPLGLDTPIGEngvlLSG 472
|
170 180
....*....|....*....|....*....
gi 2793968422 262 GEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
139-290 |
1.95e-18 |
|
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: 83.71 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLN--FGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG----------TKLEVAYFD 206
Cdd:cd03263 2 QIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirtdrkaARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 QYReILDPEKSVIDNL-----ADGkqeVTVGGRERHALSYLQDFLFSPKRARtPVKALSGGEKNRLLLARIFLKSNNLLI 281
Cdd:cd03263 82 QFD-ALFDELTVREHLrfyarLKG---LPKSEIKEEVELLLRVLGLTDKANK-RARTLSGGMKRKLSLAIALIGGPSVLL 156
|
....*....
gi 2793968422 282 LDEPTNDLD 290
Cdd:cd03263 157 LDEPTSGLD 165
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
139-313 |
3.28e-18 |
|
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: 82.65 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhcgTKLEVAYFDQY---------- 208
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSYQKNIealrrigali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 -REILDPEKSVIDNLadgKQEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTN 287
Cdd:cd03268 79 eAPGFYPNLTARENL---RLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180
....*....|....*....|....*....
gi 2793968422 288 DLD---IETLELLEDLLANYQGTLLLVSH 313
Cdd:cd03268 156 GLDpdgIKELRELILSLRDQGITVLISSH 184
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
146-314 |
1.17e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.74 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 146 GFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREILD--PeKSVIDNLA 223
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDslP-LTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 224 DGK-QEVTVGGRER--------HALSY--LQDFlfspkrARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD-- 290
Cdd:NF040873 80 MGRwARRGLWRRLTrddraavdDALERvgLADL------AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDae 153
|
170 180
....*....|....*....|....*
gi 2793968422 291 -IETLELLEDLLANYQGTLLLVSHD 314
Cdd:NF040873 154 sRERIIALLAEEHARGATVVVVTHD 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
138-316 |
1.32e-17 |
|
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: 81.46 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL-----LDQLKPDSGRLHCGTKlevayfDQYREIL 212
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGK------DIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 DPE-----------------KSVIDNLADGKQevTVGGRERHALSYL-QDFLfspKRA--------RTPVKALSGGEKNR 266
Cdd:cd03260 75 DVLelrrrvgmvfqkpnpfpGSIYDNVAYGLR--LHGIKLKEELDERvEEAL---RKAalwdevkdRLHALGLSGGQQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2793968422 267 LLLARIFLKSNNLLILDEPTNDLDIETLEL--LEDLLANYQGTLLLVSHDRQ 316
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKieELIAELKKEYTIVIVTHNMQ 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
139-318 |
1.59e-17 |
|
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: 81.33 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTklEVAYFDQYR-------- 209
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGE--DITGLPPHEiarlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 210 -----EILdPEKSVIDNLAdgkqevtVGGRERHALSYLQDFLFSPKR------------------ARTPVKALSGGEKNR 266
Cdd:cd03219 80 tfqipRLF-PELTVLENVM-------VAAQARTGSGLLLARARREEReareraeellervgladlADRPAGELSYGQQRR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2793968422 267 LLLARIFLKSNNLLILDEPT---NDLDIETLELLEDLLANYQGTLLLVSHDRQFV 318
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVV 206
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
141-318 |
2.06e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.70 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQyREILDPeksvid 220
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDT------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 221 nladgKQEVTVGGRER-HALSYLQDFLFSPKRART------PVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIET 293
Cdd:PRK09544 81 -----TLPLTVNRFLRlRPGTKKEDILPALKRVQAghlidaPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*....
gi 2793968422 294 LELLEDLLANYQGTL----LLVSHDRQFV 318
Cdd:PRK09544 156 QVALYDLIDQLRRELdcavLMVSHDLHLV 184
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
139-314 |
3.67e-17 |
|
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: 79.99 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG----TKLEVA------YFDQY 208
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvTDLPPKdrdiamVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 reILDPEKSVIDNLADG-------KQEVTVGGRERHALSYLQDFLfspkrARTPvKALSGGEKNRLLLARIFLKSNNLLI 281
Cdd:cd03301 82 --ALYPHMTVYDNIAFGlklrkvpKDEIDERVREVAELLQIEHLL-----DRKP-KQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 2793968422 282 LDEPTNDLD----IETLELLEDLLANYQGTLLLVSHD 314
Cdd:cd03301 154 MDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
134-290 |
9.39e-17 |
|
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: 79.19 E-value: 9.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEaeNLNFGFEGKEIV-KDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGTKLEVAYFDQYREI 211
Cdd:cd03254 1 GEIEFE--NVNFSYDEKKPVlKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQiLIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 L-----DP---EKSVIDNLADGKQ-----EVTVGGRERHALSYLQdflFSPKRARTPV----KALSGGEKNRLLLARIFL 274
Cdd:cd03254 79 IgvvlqDTflfSGTIMENIRLGRPnatdeEVIEAAKEAGAHDFIM---KLPNGYDTVLgengGNLSQGERQLLAIARAML 155
|
170
....*....|....*.
gi 2793968422 275 KSNNLLILDEPTNDLD 290
Cdd:cd03254 156 RDPKILILDEATSNID 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
136-290 |
1.31e-16 |
|
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: 78.81 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 136 IVFEaeNLNFGFE-GKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAYFDQYREILD 213
Cdd:cd03253 1 IEFE--NVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 214 --PEKSVI------DNLADGKQEVTVGGRERHA-LSYLQDFLFS-PKRARTPVKA----LSGGEKNRLLLARIFLKSNNL 279
Cdd:cd03253 79 vvPQDTVLfndtigYNIRYGRPDATDEEVIEAAkAAQIHDKIMRfPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPI 158
|
170
....*....|.
gi 2793968422 280 LILDEPTNDLD 290
Cdd:cd03253 159 LLLDEATSALD 169
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
134-318 |
1.33e-16 |
|
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: 79.31 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEAENL--NFGfeGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHcgtklevayFDQyREI 211
Cdd:COG0411 1 SDPLLEVRGLtkRFG--GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL---------FDG-RDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 --LDPEK-------------------SVIDNLAdgkqevtVGGRERHALSYLQDFLFSPK-------------------- 250
Cdd:COG0411 69 tgLPPHRiarlgiartfqnprlfpelTVLENVL-------VAAHARLGRGLLAALLRLPRarreereareraeellervg 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2793968422 251 ---RARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPT---NDLDIETLELLEDLLANYQG-TLLLVSHDRQFV 318
Cdd:COG0411 142 ladRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLV 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
131-290 |
1.57e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 131 QRSGKIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCgTKLEVAYFDQY-R 209
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPPYqR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 210 EI--------LDPEKSVIDNLADG-------KQEVTVGGRERHALSYLQDFlfspkRARTPvKALSGGEKNRLLLARIFL 274
Cdd:PRK11607 92 PInmmfqsyaLFPHMTVEQNIAFGlkqdklpKAEIASRVNEMLGLVHMQEF-----AKRKP-HQLSGGQRQRVALARSLA 165
|
170
....*....|....*.
gi 2793968422 275 KSNNLLILDEPTNDLD 290
Cdd:PRK11607 166 KRPKLLLLDEPMGALD 181
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
147-314 |
1.71e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.95 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 147 FEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREI-----LDPEKSVIDN 221
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMfqdarLLPWKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 222 LADGKQevtvGGRERHALSYLQDFLFSPKRARTPVkALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD----IETLELL 297
Cdd:PRK11247 102 VGLGLK----GQWRDAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLI 176
|
170
....*....|....*..
gi 2793968422 298 EDLLANYQGTLLLVSHD 314
Cdd:PRK11247 177 ESLWQQHGFTVLLVTHD 193
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-60 |
1.90e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 81.48 E-value: 1.90e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKLSSFPGDYENYL 60
Cdd:PRK15064 465 PTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYL 524
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
147-314 |
3.00e-16 |
|
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: 77.76 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 147 FEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRlhcgtkLEVAYFDQY----------------RE 210
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE------VRVAGLVPWkrrkkflrrigvvfgqKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 211 ILDPEKSVIDNLADGKQEVTVG-GRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDL 289
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDLPpARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180
....*....|....*....|....*....
gi 2793968422 290 DIETLEL----LEDLLANYQGTLLLVSHD 314
Cdd:cd03267 185 DVVAQENirnfLKEYNRERGTTVLLTSHY 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
151-290 |
3.82e-16 |
|
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: 77.58 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 151 EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG----TKLEVAYfdqYREIL-----DP---EKSV 218
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDgvdiRDLNLRW---LRSQIglvsqEPvlfDGTI 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2793968422 219 IDNLADGKQEVTVGGRERHA-LSYLQDFLFS-PKRARTPVKA----LSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAkKANIHDFIMSlPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
136-291 |
4.36e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.89 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 136 IVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKL------EVAyfdQY 208
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlNGRPLadwspaELA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 REILdPEKSVIdNLADGKQEVTVGGRERHALSYLQD-FLFSPKRART--------PVKALSGGEKNRLLLARIFL----- 274
Cdd:PRK13548 78 RAVL-PQHSSL-SFPFTVEEVVAMGRAPHGLSRAEDdALVAAALAQVdlahlagrDYPQLSGGEQQRVQLARVLAqlwep 155
|
170
....*....|....*...
gi 2793968422 275 -KSNNLLILDEPTNDLDI 291
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDL 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
139-290 |
4.44e-16 |
|
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: 77.33 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRlhcgtkleVAYFDQYREILDPEK-- 216
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE--------ILVDGQDITGLSEKEly 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 -------------------SVIDNLAdgkqevtVGGRERHALsylqdflfSPKRARTPVKA-----------------LS 260
Cdd:COG1127 79 elrrrigmlfqggalfdslTVFENVA-------FPLREHTDL--------SEAEIRELVLEklelvglpgaadkmpseLS 143
|
170 180 190
....*....|....*....|....*....|.
gi 2793968422 261 GGEKNRLLLAR-IFLKSnNLLILDEPTNDLD 290
Cdd:COG1127 144 GGMRKRVALARaLALDP-EILLYDEPTAGLD 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
139-291 |
5.91e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.46 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG-------TKLEVAyfdQYREI 211
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawSPWELA---RRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 LdPEKSVIdNLADGKQEVtVG-GRERHALSYLQDflfsPKRART-------------PVKALSGGEKNRLLLARIFL--- 274
Cdd:COG4559 80 L-PQHSSL-AFPFTVEEV-VAlGRAPHGSSAAQD----RQIVREalalvglahlagrSYQTLSGGEQQRVQLARVLAqlw 152
|
170 180
....*....|....*....|.
gi 2793968422 275 ----KSNNLLILDEPTNDLDI 291
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDL 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
135-290 |
7.01e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 76.62 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 135 KIVFEAENLNF----GFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDqlKPDSGRLH-CGTKL------E 201
Cdd:COG1136 2 SPLLELRNLTKsygtGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggLD--RPTSGEVLiDGQDIsslserE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 202 VAyfdQYR--EI--------LDPEKSVIDNLA-----DGkqeVTVGGRERHALSYLQDF-LfsPKRARTPVKALSGGEKN 265
Cdd:COG1136 80 LA---RLRrrHIgfvfqffnLLPELTALENVAlplllAG---VSRKERRERARELLERVgL--GDRLDHRPSQLSGGQQQ 151
|
170 180
....*....|....*....|....*
gi 2793968422 266 RLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLD 176
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
142-314 |
7.51e-16 |
|
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: 76.18 E-value: 7.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 142 NLNFGFEGKeiVKDFSFNI---MRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGtklEVAYFD---------QYR 209
Cdd:cd03297 1 MLCVDIEKR--LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN---GTVLFDsrkkinlppQQR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 210 EI--------LDPEKSVIDNLADG-----KQEVTVGGRERHALSYLQDFLFSPkrartpVKALSGGEKNRLLLARIFLKS 276
Cdd:cd03297 76 KIglvfqqyaLFPHLNVRENLAFGlkrkrNREDRISVDELLDLLGLDHLLNRY------PAQLSGGEKQRVALARALAAQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2793968422 277 NNLLILDEPTNDLDIETLELLEDL----LANYQGTLLLVSHD 314
Cdd:cd03297 150 PELLLLDEPFSALDRALRLQLLPElkqiKKNLNIPVIFVTHD 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
138-290 |
1.05e-15 |
|
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: 76.45 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGF-EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH---------CGTKL-----EV 202
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklKGKALrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 203 AY-FDQYREIldPEKSVIDNLADGK-----------QEVTVGGRERhALSYLQDFLFSPKrARTPVKALSGGEKNRLLLA 270
Cdd:cd03256 81 GMiFQQFNLI--ERLSVLENVLSGRlgrrstwrslfGLFPKEEKQR-ALAALERVGLLDK-AYQRADQLSGGQQQRVAIA 156
|
170 180
....*....|....*....|
gi 2793968422 271 RIFLKSNNLLILDEPTNDLD 290
Cdd:cd03256 157 RALMQQPKLILADEPVASLD 176
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
158-326 |
1.13e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.22 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 158 FNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQyreilDPEK----SVIDNLADGKQEVTVGG 233
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQ-----DPPRnvegTVYDFVAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 234 RERHALSY----------------LQDFL-------FSPK----------RARTPVKALSGGEKNRLLLARIFLKSNNLL 280
Cdd:PRK11147 99 KRYHDISHlvetdpseknlnelakLQEQLdhhnlwqLENRinevlaqlglDPDAALSSLSGGWLRKAALGRALVSNPDVL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2793968422 281 ILDEPTNDLDIETLELLEDLLANYQGTLLLVSHDRQFV----------DNTVMTSW 326
Cdd:PRK11147 179 LLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIrnmatrivdlDRGKLVSY 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
137-314 |
1.20e-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: 79.18 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEG--KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLdQLKPDSGRLH-----CGTKL--------- 200
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALM-GLLPHGGRISgevllDGRDLlelsealrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 201 -EVAYFDQyreilDPEKS-----VIDNLADGKQEVTVGGRERHALSY-LQDFLFSPKRARTPVKALSGGEKNRLLLARIF 273
Cdd:COG1123 83 rRIGMVFQ-----DPMTQlnpvtVGDQIAEALENLGLSRAEARARVLeLLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2793968422 274 LKSNNLLILDEPTNDLD----IETLELLEDLLANYQGTLLLVSHD 314
Cdd:COG1123 158 ALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHD 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
134-319 |
1.65e-15 |
|
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: 75.59 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEaeNLNFGFEGK---EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL----HCGTKLEVAYFD 206
Cdd:cd03248 10 GIVKFQ--NVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 QYREILDPE-----KSVIDNLADGKQ-----EVTVGGRERHALSYLQDFlfsPKRARTPV----KALSGGEKNRLLLARI 272
Cdd:cd03248 88 SKVSLVGQEpvlfaRSLQDNIAYGLQscsfeCVKEAAQKAHAHSFISEL---ASGYDTEVgekgSQLSGGQKQRVAIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 273 FLKSNNLLILDEPTNDLDIetLELLEDLLANYQG----TLLLVSHDRQFVD 319
Cdd:cd03248 165 LIRNPQVLILDEATSALDA--ESEQQVQQALYDWperrTVLVIAHRLSTVE 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
150-356 |
2.32e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.61 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL-----------HCGTKLEVAYFDQyrEILDPEKSV 218
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvqydHHYLHRQVALVGQ--EPVLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 IDNLADG-----KQEVTVGGRERHALSYLQDFlfsPKRARTPVKA----LSGGEKNRLLLARIFLKSNNLLILDEPTNDL 289
Cdd:TIGR00958 572 RENIAYGltdtpDEEIMAAAKAANAHDFIMEF---PNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2793968422 290 DIETLELLEDLLANYQGTLLLVSHDRQFVDNTvmTSWIFEGNGVVEEfvGGYHDaqQQRKQAIEYRQ 356
Cdd:TIGR00958 649 DAECEQLLQESRSRASRTVLLIAHRLSTVERA--DQILVLKKGSVVE--MGTHK--QLMEDQGCYKH 709
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
155-321 |
2.37e-15 |
|
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: 74.75 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 155 DFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKL------EVAY--------FDQYReiLDPEKSVI 219
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYlrrkigvvFQDFR--LLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 220 DNLADGKQEVTVGGRE-RHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLE 298
Cdd:cd03292 97 ENVAFALEVTGVPPREiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180
....*....|....*....|....*.
gi 2793968422 299 D--LLANYQGTLLLVS-HDRQFVDNT 321
Cdd:cd03292 177 NllKKINKAGTTVVVAtHAKELVDTT 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
139-290 |
3.26e-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: 74.24 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-------CGTKLEVAYFDQYREi 211
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEERG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 LDPEKSVIDNLADGKQEVTVGGRE--RHALSYLQDFLFSPKRARtPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDL 289
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEarRRIDEWLERLELSEYANK-RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
.
gi 2793968422 290 D 290
Cdd:cd03269 160 D 160
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
138-317 |
3.57e-15 |
|
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: 74.10 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKL------------EVAY 204
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 205 -FDQYReiLDPEKSVIDNLADGkqEVTVGGR-----ERHALSYLQDFLFSPKRARTPVKaLSGGEKNRLLLARIFLKSNN 278
Cdd:cd03262 81 vFQQFN--LFPHLTVLENITLA--PIKVKGMskaeaEERALELLEKVGLADKADAYPAQ-LSGGQQQRVAIARALAMNPK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2793968422 279 LLILDEPTNDLD---IETLELLEDLLANYQGTLLLVSHDRQF 317
Cdd:cd03262 156 VMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGF 197
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
141-417 |
3.84e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 77.98 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLK----------------LLLDQ--LKPDSGRLHC------ 196
Cdd:PLN03073 181 ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqiLHVEQevVGDDTTALQCvlntdi 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 197 -GTKL---EVAYFDQYREILDPEKSVIDNLA--DGKQEVTVGGR----------------ERHALSYLQDFLFSPKRART 254
Cdd:PLN03073 261 eRTQLleeEAQLVAQQRELEFETETGKGKGAnkDGVDKDAVSQRleeiykrlelidaytaEARAASILAGLSFTPEMQVK 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 255 PVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSHDRQFVdNTVMTSWIFEGNGVV 334
Cdd:PLN03073 341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFL-NTVVTDILHLHGQKL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 335 EEFVGGYHDAQQQRKQAIEYRQvekpskpeKVVEETPKT-APVKAKAKKLSYKLQRElEALPLRLEELEtQIETLQEEVN 413
Cdd:PLN03073 420 VTYKGDYDTFERTREEQLKNQQ--------KAFESNERSrSHMQAFIDKFRYNAKRA-SLVQSRIKALD-RLGHVDAVVN 489
|
....
gi 2793968422 414 DPSF 417
Cdd:PLN03073 490 DPDY 493
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
148-290 |
5.25e-15 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 73.23 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 148 EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlEVAY----FDQYRE-----ILDPEKSV 218
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE-PLDYsrkgLLERRQrvglvFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 ID------------NLADGKQEVTVGGRERHALSYLQDFlfspkrARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPT 286
Cdd:TIGR01166 82 FAadvdqdvafgplNLGLSEAEVERRVREALTAVGASGL------RERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
....
gi 2793968422 287 NDLD 290
Cdd:TIGR01166 156 AGLD 159
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
137-291 |
5.69e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL-HCGtklEVAYFDQYREI---- 211
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkLDG---GDIDDPDVAEAchyl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 -----LDPEKSVIDNL---ADgkqevTVGGRERHALSYLQDFLFSPKrARTPVKALSGGEKNRLLLARIFLKSNNLLILD 283
Cdd:PRK13539 79 ghrnaMKPALTVAENLefwAA-----FLGGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
....*...
gi 2793968422 284 EPTNDLDI 291
Cdd:PRK13539 153 EPTAALDA 160
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
120-313 |
5.93e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 120 QGKAVIQIDDGqrsgkIVFEAENLN-FGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLkPDSGRLHC-G 197
Cdd:PRK11174 337 QGEKELASNDP-----VTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKInG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 198 TKLEVAYFDQYREILD--------PEKSVIDNLADGKQEVTvGGRERHAL--SYLQDFLFS-PKRARTPVK----ALSGG 262
Cdd:PRK11174 411 IELRELDPESWRKHLSwvgqnpqlPHGTLRDNVLLGNPDAS-DEQLQQALenAWVSEFLPLlPQGLDTPIGdqaaGLSVG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2793968422 263 EKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLED--LLANYQGTLLLVSH 313
Cdd:PRK11174 490 QAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQalNAASRRQTTLMVTH 542
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
139-290 |
7.37e-15 |
|
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: 72.78 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREILdpekSV 218
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENI----LY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 IDNLADGKQEVTVggreRHALSYLQDFLFSPKR--------------ARTPVKALSGGEKNRLLLARIFLKSNNLLILDE 284
Cdd:TIGR01189 78 LGHLPGLKPELSA----LENLHFWAAIHGGAQRtiedalaavgltgfEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
....*.
gi 2793968422 285 PTNDLD 290
Cdd:TIGR01189 154 PTTALD 159
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
139-286 |
1.03e-14 |
|
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: 72.85 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGT-----------KLEVAYFD 206
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRditglppheraRAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 QYREILdPEKSVIDNLadgkqEVTVGGRERHALSYLQDFLFS--PK---RARTPVKALSGGEKNRLLLARIFLKSNNLLI 281
Cdd:cd03224 82 EGRRIF-PELTVEENL-----LLGAYARRRAKRKARLERVYElfPRlkeRRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
....*
gi 2793968422 282 LDEPT 286
Cdd:cd03224 156 LDEPS 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
141-290 |
1.24e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.72 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDqlKPDSGRLHCG----TKLE-----VAY-FDQY 208
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagLE--DPTSGEILIGgrdvTDLPpkdrnIAMvFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 reILDPEKSVIDNLADG-------KQEVtvggRER--HALSYLQ--DFLfspkrARTPvKALSGGEKNRLLLARIFLKSN 277
Cdd:COG3839 85 --ALYPHMTVYENIAFPlklrkvpKAEI----DRRvrEAAELLGleDLL-----DRKP-KQLSGGQRQRVALGRALVREP 152
|
170
....*....|...
gi 2793968422 278 NLLILDEPTNDLD 290
Cdd:COG3839 153 KVFLLDEPLSNLD 165
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
127-284 |
1.46e-14 |
|
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: 72.57 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 127 IDDGQRSGKIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL--HCGTK--LEV 202
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvRGRVSslLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 203 AYFdqyreiLDPEKSVIDN-----LADGKQEVTVGGRER--HALSYLQDFLfspkraRTPVKALSGGEKNRLLLARIFLK 275
Cdd:cd03220 92 GGG------FNPELTGRENiylngRLLGLSRKEIDEKIDeiIEFSELGDFI------DLPVKTYSSGMKARLAFAIATAL 159
|
....*....
gi 2793968422 276 SNNLLILDE 284
Cdd:cd03220 160 EPDILLIDE 168
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
128-290 |
1.48e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 75.63 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 128 DDGQRSGKIVFEAENLNFGFEGKE--IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLevay 204
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLnGQPI---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 205 fDQYRE-ILDPEKSVI------------DNLADGKQEVT----------VGgrerhaLSYLqdfLFSPKRARTPV----K 257
Cdd:PRK11160 405 -ADYSEaALRQAISVVsqrvhlfsatlrDNLLLAAPNASdealievlqqVG------LEKL---LEDDKGLNAWLgeggR 474
|
170 180 190
....*....|....*....|....*....|...
gi 2793968422 258 ALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
137-285 |
2.41e-14 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 72.31 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR------------LHCGTKLEVAY 204
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKilidgqdithlpMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 205 FDQYREILDpEKSVIDNLA---DGKQEVTVGGRERHALSYLQDFLFSPKRaRTPVKALSGGEKNRLLLARIFLKSNNLLI 281
Cdd:TIGR04406 81 LPQEASIFR-KLTVEENIMavlEIRKDLDRAEREERLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARALATNPKFIL 158
|
....
gi 2793968422 282 LDEP 285
Cdd:TIGR04406 159 LDEP 162
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
141-314 |
2.69e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.09 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKEivKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG----TKLEVAYfdqyREI----- 211
Cdd:COG3840 5 DDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdlTALPPAE----RPVsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 ---LDPEKSVIDNLADG-----------KQEVtvggreRHALSY--LQDFLfspkrARTPvKALSGGEKNRLLLARIFLK 275
Cdd:COG3840 79 ennLFPHLTVAQNIGLGlrpglkltaeqRAQV------EQALERvgLAGLL-----DRLP-GQLSGGQRQRVALARCLVR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2793968422 276 SNNLLILDEPTNDLDIETLEL----LEDLLANYQGTLLLVSHD 314
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEmldlVDELCRERGLTVLMVTHD 189
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
127-290 |
3.34e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.61 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 127 IDDGQRSGKIVFEaeNLNFGFEGK-EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEvay 204
Cdd:PRK13657 326 IDLGRVKGAVEFD--DVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIR--- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 205 fDQYREIL---------DP---EKSVIDNLADGKQEVTvGGRERHALSYLQ--DFLF-SPKRARTPV----KALSGGEKN 265
Cdd:PRK13657 401 -TVTRASLrrniavvfqDAglfNRSIEDNIRVGRPDAT-DEEMRAAAERAQahDFIErKPDGYDTVVgergRQLSGGERQ 478
|
170 180
....*....|....*....|....*
gi 2793968422 266 RLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALD 503
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
144-290 |
3.56e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 144 NFGFEG----KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLK--PDSGRlhcgtklevayFDQYREILDPEKS 217
Cdd:COG2401 33 AFGVELrvveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGC-----------VDVPDNQFGREAS 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2793968422 218 VIDNLADgKQEVTVGGRERHALSYLQDFLFspkraRTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:COG2401 102 LIDAIGR-KGDFKDAVELLNAVGLSDAVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
138-290 |
3.64e-14 |
|
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: 70.15 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGrlhcgtklevayfdqyreildpeks 217
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG------------------------- 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2793968422 218 vidnladgkqEVTVGGRERHALsylqdflfSPKRAR----TPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:cd03216 56 ----------EILVDGKEVSFA--------SPRDARragiAMVYQLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
156-291 |
3.65e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.80 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 156 FSFNIMRGDRIALIGPNGCGKSTVLKLLLDqLKPDSGRLHC-GTKLEV----------AYFDQyREILDPEKSVIDNLAD 224
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLnGRPLSDwsaaelarhrAYLSQ-QQSPPFAMPVFQYLAL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2793968422 225 GKQEVTVGGRERHALSYL-QDFLFSPKRARtPVKALSGGEKNRLLLARIFLK---SNN----LLILDEPTNDLDI 291
Cdd:COG4138 93 HQPAGASSEAVEQLLAQLaEALGLEDKLSR-PLTQLSGGEWQRVRLAAVLLQvwpTINpegqLLLLDEPMNSLDV 166
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
139-290 |
3.72e-14 |
|
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: 71.76 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAYFDQYREI------ 211
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDISGLSEAELYRLrrrmgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 ------LDPEKSVIDNLADGKQEVTVGGRE---RHALSYLQDFLFSPKRARTPVKaLSGGEKNRLLLAR-IFLKSnNLLI 281
Cdd:cd03261 82 lfqsgaLFDSLTVFENVAFPLREHTRLSEEeirEIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARaLALDP-ELLL 159
|
....*....
gi 2793968422 282 LDEPTNDLD 290
Cdd:cd03261 160 YDEPTAGLD 168
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
131-290 |
4.92e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.44 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 131 QRSGKIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH----CGTKLEV---- 202
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqDITHVPAenrh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 203 --AYFDQYreILDPEKSVIDNLADG-------KQEVTVGGRERHALSYLQDFlfspkrARTPVKALSGGEKNRLLLARIF 273
Cdd:PRK09452 88 vnTVFQSY--ALFPHMTVFENVAFGlrmqktpAAEITPRVMEALRMVQLEEF------AQRKPHQLSGGQQQRVAIARAV 159
|
170
....*....|....*..
gi 2793968422 274 LKSNNLLILDEPTNDLD 290
Cdd:PRK09452 160 VNKPKVLLLDESLSALD 176
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
139-291 |
9.43e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlEVAYFDQY---REILD-P 214
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD-DVEALSARaasRRVASvP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 215 EKSVIDNLADGKQEVTVG-----GR-------ERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLIL 282
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMGrtphrSRfdtwtetDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
....*....
gi 2793968422 283 DEPTNDLDI 291
Cdd:PRK09536 164 DEPTASLDI 172
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
156-291 |
1.28e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 156 FSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLkPDSGRLHC-GTKLEV----------AYFDQ------------YREIL 212
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFaGQPLEAwsaaelarhrAYLSQqqtppfampvfqYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 DPEKSVIDNLadgkqevtvggreRHALSYLQDFL-FSPKRARtPVKALSGGEKNRLLLARIFLK---SNN----LLILDE 284
Cdd:PRK03695 94 QPDKTRTEAV-------------ASALNEVAEALgLDDKLGR-SVNQLSGGEWQRVRLAAVVLQvwpDINpagqLLLLDE 159
|
....*..
gi 2793968422 285 PTNDLDI 291
Cdd:PRK03695 160 PMNSLDV 166
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
153-314 |
1.35e-13 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 70.06 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GT--------KLEVAYFDQyREILDPEKSVIDNLA 223
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKditnlppeKRDISYVPQ-NYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 224 DGKQEVTVGGRERHA----------LSYLQDflfspkraRTPvKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIET 293
Cdd:cd03299 94 YGLKKRKVDKKEIERkvleiaemlgIDHLLN--------RKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180
....*....|....*....|....*
gi 2793968422 294 LELLEDLLA----NYQGTLLLVSHD 314
Cdd:cd03299 165 KEKLREELKkirkEFGVTVLHVTHD 189
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
139-286 |
2.69e-13 |
|
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: 69.24 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG----TKLE--------VAYFD 206
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgediTGLPphriarlgIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 QYREILdPEKSVIDNLADGKQEVTVGGRERHALSYLQDfLFsPK---RARTPVKALSGGEKNRLLLARIFLKSNNLLILD 283
Cdd:COG0410 85 EGRRIF-PSLTVEENLLLGAYARRDRAEVRADLERVYE-LF-PRlkeRRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
...
gi 2793968422 284 EPT 286
Cdd:COG0410 162 EPS 164
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
140-290 |
2.84e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 140 AENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR------------LHCGTKLEVAYFDQ 207
Cdd:PRK10895 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 208 YREILDpEKSVIDNLA---DGKQEVTVGGRERHALSYLQDFLFSPKRARTPvKALSGGEKNRLLLARIFLKSNNLLILDE 284
Cdd:PRK10895 86 EASIFR-RLSVYDNLMavlQIRDDLSAEQREDRANELMEEFHIEHLRDSMG-QSLSGGERRRVEIARALAANPKFILLDE 163
|
....*.
gi 2793968422 285 PTNDLD 290
Cdd:PRK10895 164 PFAGVD 169
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
139-290 |
2.87e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 70.90 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDQlkPDSGRLHCG----TKLEVayfdQYREI- 211
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagFET--PDSGRILLDgrdvTGLPP----EKRNVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 -------LDPEKSVIDNLADG-------KQEVtvggRER--HALSY--LQDFlfspkrARTPVKALSGGEKNRLLLARIF 273
Cdd:COG3842 81 mvfqdyaLFPHLTVAENVAFGlrmrgvpKAEI----RARvaELLELvgLEGL------ADRYPHQLSGGQQQRVALARAL 150
|
170
....*....|....*..
gi 2793968422 274 LKSNNLLILDEPTNDLD 290
Cdd:COG3842 151 APEPRVLLLDEPLSALD 167
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
139-290 |
3.99e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 68.87 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKlLLDQL-KPDSGRLH-CGTKLEV--AYFDQYR-EI-- 211
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLR-CINLLeEPDSGTITvDGEDLTDskKDINKLRrKVgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 ------LDPEKSVIDNLADGKqeVTVGGR-----ERHALSYLQDFLFSPKRARTPVKaLSGGEKNRLLLARIFLKSNNLL 280
Cdd:COG1126 82 vfqqfnLFPHLTVLENVTLAP--IKVKKMskaeaEERAMELLERVGLADKADAYPAQ-LSGGQQQRVAIARALAMEPKVM 158
|
170
....*....|
gi 2793968422 281 ILDEPTNDLD 290
Cdd:COG1126 159 LFDEPTSALD 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
160-291 |
6.73e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 160 IMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhcGTKLEVAYFDQYREIlDPEKSVIDNLAdgKQEVTVGGrerhal 239
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKP-DYDGTVEDLLR--SITDDLGS------ 430
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2793968422 240 SYLQDFLFSP----KRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK13409 431 SYYKSEIIKPlqleRLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
148-290 |
8.24e-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: 66.02 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 148 EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDqLKP-DSGRLHCGTKLEVAYFdqyreildPEKSVIdnladgk 226
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRIGMPEGEDLLFL--------PQRPYL------- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2793968422 227 qevtVGGRERHALSYLQDflfspkrartpvKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:cd03223 76 ----PLGTLREQLIYPWD------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
134-290 |
8.72e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 70.23 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEaeNLNFGFEGK-EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLevayfdqyREI 211
Cdd:COG5265 356 GEVRFE--NVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDI--------RDV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 ----------LDPEKSVI------DNLADGKQEVTvggRE--RHA--LSYLQDFLFS-PKRARTPV-----KaLSGGEKN 265
Cdd:COG5265 426 tqaslraaigIVPQDTVLfndtiaYNIAYGRPDAS---EEevEAAarAAQIHDFIESlPDGYDTRVgerglK-LSGGEKQ 501
|
170 180
....*....|....*....|....*
gi 2793968422 266 RLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALD 526
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
149-290 |
1.02e-12 |
|
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: 67.46 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 149 GKEI--VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL---HCGTKLEVAYFDQyREILD---------- 213
Cdd:COG4778 21 GKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrHDGGWVDLAQASP-REILAlrrrtigyvs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 214 ------PEKSVIDN-----LADGKQEVTVGGRERHALSYLQdflfSPKR-ARTPVKALSGGEKNRLLLARIFLKSNNLLI 281
Cdd:COG4778 100 qflrviPRVSALDVvaeplLERGVDREEARARARELLARLN----LPERlWDLPPATFSGGEQQRVNIARGFIADPPLLL 175
|
....*....
gi 2793968422 282 LDEPTNDLD 290
Cdd:COG4778 176 LDEPTASLD 184
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
135-290 |
1.22e-12 |
|
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: 66.42 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 135 KIVFEAENLNF------GFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLldqlkpdSGRLH-CGTKLEVA---- 203
Cdd:cd03213 1 GVTLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------AGRRTgLGVSGEVLingr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 204 --YFDQYREIL---DPEKSVIDNLadgkqevTVggreRHALsylqdfLFSPKrartpVKALSGGEKNRLLLARIFLKSNN 278
Cdd:cd03213 74 plDKRSFRKIIgyvPQDDILHPTL-------TV----RETL------MFAAK-----LRGLSGGERKRVSIALELVSNPS 131
|
170
....*....|..
gi 2793968422 279 LLILDEPTNDLD 290
Cdd:cd03213 132 LLFLDEPTSGLD 143
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
141-291 |
1.60e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHcgtkLEVAYFDQYreildPEKSV-- 218
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW----LDGEHIQHY-----ASKEVar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 -IDNLADGK--------QEVTVGGRERHALSYL------QDFLFSPKR-------ARTPVKALSGGEKNRLLLARIFLKS 276
Cdd:PRK10253 82 rIGLLAQNAttpgditvQELVARGRYPHQPLFTrwrkedEEAVTKAMQatgithlADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170
....*....|....*
gi 2793968422 277 NNLLILDEPTNDLDI 291
Cdd:PRK10253 162 TAIMLLDEPTTWLDI 176
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
139-290 |
1.60e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 66.45 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGdRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLeVAYFDQYREIL----- 212
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRiDGQDV-LKQPQKLRRRIgylpq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 ----DPEKSVIDNLA---------DGKQEVTVggreRHALSYLQdfLFspKRARTPVKALSGGEKNRLLLARIFLKSNNL 279
Cdd:cd03264 80 efgvYPNFTVREFLDyiawlkgipSKEVKARV----DEVLELVN--LG--DRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170
....*....|.
gi 2793968422 280 LILDEPTNDLD 290
Cdd:cd03264 152 LIVDEPTAGLD 162
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
156-313 |
1.64e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.91 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 156 FSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL------HCGT---KLEVAYFDQYREiLDPEKSVIDNLA--- 223
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdHTTTppsRRPVSMLFQENN-LFSHLTVAQNIGlgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 224 ------DGKQEVTVggRERHALSYLQDFLfspkrARTPvKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD----IET 293
Cdd:PRK10771 97 npglklNAAQREKL--HAIARQMGIEDLL-----ARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEM 168
|
170 180
....*....|....*....|
gi 2793968422 294 LELLEDLLANYQGTLLLVSH 313
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSH 188
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
147-316 |
1.68e-12 |
|
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: 66.88 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 147 FEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlEVAYFDQY-REI--------LDPEKS 217
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPPHkRPVntvfqnyaLFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 218 VIDNLADG-------KQEVTVGGRERHALSYLQDFlfspkRARTPvKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:cd03300 89 VFENIAFGlrlkklpKAEIKERVAEALDLVQLEGY-----ANRKP-SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190
....*....|....*....|....*....|
gi 2793968422 291 IETLELLEDLLANYQG----TLLLVSHDRQ 316
Cdd:cd03300 163 LKLRKDMQLELKRLQKelgiTFVFVTHDQE 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
160-330 |
2.44e-12 |
|
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: 68.66 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 160 IMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHcgTKLEVAYFDQYREIlDPEKSVIDNLADGKQEvTVGGrerhal 239
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQYISP-DYDGTVEEFLRSANTD-DFGS------ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 240 SYLQDFLFSP----KRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD----IETLELLEDLLANYQGTLLLV 311
Cdd:COG1245 433 SYYKTEIIKPlgleKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVV 512
|
170 180
....*....|....*....|..
gi 2793968422 312 SHDRQFVD---NTVMtswIFEG 330
Cdd:COG1245 513 DHDIYLIDyisDRLM---VFEG 531
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
138-285 |
2.68e-12 |
|
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: 66.03 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR------------LHCGTKLEVAYF 205
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqditklpMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 206 DQ----YREIldpekSVIDNLADGKQEVTVGGRERHAL--SYLQDFLFSPKRaRTPVKALSGGEKNRLLLARIFLKSNNL 279
Cdd:cd03218 81 PQeasiFRKL-----TVEENILAVLEIRGLSKKEREEKleELLEEFHITHLR-KSKASSLSGGERRRVEIARALATNPKF 154
|
....*.
gi 2793968422 280 LILDEP 285
Cdd:cd03218 155 LLLDEP 160
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
139-336 |
3.18e-12 |
|
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: 68.29 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDQLKPDSGRL---------------------- 194
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 195 --HCGTKLE--------------------VAYFDQYREILDPEKSVIDNLADGKQEVTVGGRE--RHALSYLQDFLFSpK 250
Cdd:TIGR03269 82 cpVCGGTLEpeevdfwnlsdklrrrirkrIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEavGRAVDLIEMVQLS-H 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 251 RARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETL----ELLEDLLANYQGTLLLVSHDRQFVDNTVMTSW 326
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|
gi 2793968422 327 IFEGNGVVEE 336
Cdd:TIGR03269 241 WLENGEIKEE 250
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
141-285 |
3.27e-12 |
|
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: 65.18 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKE-----IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKleVAYFDQY------- 208
Cdd:cd03250 4 EDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQEpwiqngt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 -RE-IL-----DPE--KSVI---------DNLADGKQ-EVTVGGRerhalsylqdflfspkrartpvkALSGGEKNRLLL 269
Cdd:cd03250 82 iREnILfgkpfDEEryEKVIkacalepdlEILPDGDLtEIGEKGI-----------------------NLSGGQKQRISL 138
|
170
....*....|....*.
gi 2793968422 270 ARIFLKSNNLLILDEP 285
Cdd:cd03250 139 ARAVYSDADIYLLDDP 154
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
150-352 |
3.50e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAYFDQY----REI----------LDP 214
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrGEPLAKLNRAQRkafrRDIqmvfqdsisaVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 215 EKSVIDNLADGKQEVTV---GGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK10419 105 RKTVREIIREPLRHLLSldkAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 292 ETLELLEDLLANYQ---GT-LLLVSHDRQFVDNTVMTSWIFEGNGVVEEFVGGY-----HDAQQQRKQAI 352
Cdd:PRK10419 185 VLQAGVIRLLKKLQqqfGTaCLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDkltfsSPAGRVLQNAV 254
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
153-291 |
4.18e-12 |
|
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: 65.47 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRlhcgtkLEVAYFDQYRE---------ILDPEKSVIDNLA 223
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGF------ATVDGFDVVKEpaearrrlgFVSDSTGLYDRLT 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2793968422 224 DGKQEVTVG---GRERHALSYLQDFLFSPKRAR----TPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:cd03266 95 ARENLEYFAglyGLKGDELTARLEELADRLGMEelldRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
133-290 |
5.97e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.44 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 133 SGKIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLldqlkpdsGRLH-----CGTKLEVAYFDQ 207
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL--------NRMNdlipgARVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 208 yrEILDPE---------------------KSVIDNLADG--------KQEVtvggRER--HALsylqdflfspKRA---- 252
Cdd:COG1117 79 --DIYDPDvdvvelrrrvgmvfqkpnpfpKSIYDNVAYGlrlhgiksKSEL----DEIveESL----------RKAalwd 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2793968422 253 ------RTPVKALSGGEKNRLLLAR-IFLKSNNLLiLDEPTNDLD 290
Cdd:COG1117 143 evkdrlKKSALGLSGGQQQRLCIARaLAVEPEVLL-MDEPTSALD 186
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
139-290 |
6.26e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKL--LLDQlkPDSGRLHCGTklevAYFD---------- 206
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVlnLLET--PDSGQLNIAG----HQFDfsqkpsekai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 ------------QYReiLDPEKSVIDNLADG--------KQEvtvgGRERhALSYLQDFLFSPKRARTPVkALSGGEKNR 266
Cdd:COG4161 78 rllrqkvgmvfqQYN--LWPHLTVMENLIEApckvlglsKEQ----AREK-AMKLLARLRLTDKADRFPL-HLSGGQQQR 149
|
170 180
....*....|....*....|....
gi 2793968422 267 LLLARIFLKSNNLLILDEPTNDLD 290
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALD 173
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
135-290 |
7.98e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.74 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 135 KIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGTKLEVAYFDQYREILD 213
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTlLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 214 -----PE---KSVIDNLADGKQEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEP 285
Cdd:PRK10247 85 ycaqtPTlfgDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
....*
gi 2793968422 286 TNDLD 290
Cdd:PRK10247 165 TSALD 169
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
155-316 |
8.72e-12 |
|
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: 66.29 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 155 DFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLE--------------VAY-FDQYReiLDPEKSV 218
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLnGRTLFdsrkgiflppekrrIGYvFQEAR--LFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 IDNLADGKQEVTVGGRERHALSYLQDFLFSPKRARTPVKaLSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLEL-- 296
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGR-LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEil 171
|
170 180
....*....|....*....|..
gi 2793968422 297 --LEDLLANYQGTLLLVSHDRQ 316
Cdd:TIGR02142 172 pyLERLHAEFGIPILYVSHSLQ 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
139-290 |
1.00e-11 |
|
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: 64.05 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhcgtKLEVAYFDQYREILDPEK-- 216
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIARGLly 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 -----------SVIDNL----ADGKQEVTVGGRERHALSYLQDflfspkrarTPVKALSGGEKNRLLLARIFLKSNNLLI 281
Cdd:cd03231 78 lghapgikttlSVLENLrfwhADHSDEQVEEALARVGLNGFED---------RPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
....*....
gi 2793968422 282 LDEPTNDLD 290
Cdd:cd03231 149 LDEPTTALD 157
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
140-291 |
1.02e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 140 AENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlEVAYFDQYREI-------- 211
Cdd:PRK13543 14 AHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-TATRGDRSRFMaylghlpg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 LDPEKSVIDNLadgkqevtvggrerHALSYLQDFlfSPKR--------------ARTPVKALSGGEKNRLLLARIFLKSN 277
Cdd:PRK13543 93 LKADLSTLENL--------------HFLCGLHGR--RAKQmpgsalaivglagyEDTLVRQLSAGQKKRLALARLWLSPA 156
|
170
....*....|....
gi 2793968422 278 NLLILDEPTNDLDI 291
Cdd:PRK13543 157 PLWLLDEPYANLDL 170
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
134-291 |
1.10e-11 |
|
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: 67.07 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEAENLNFGFeGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKL-----------EV 202
Cdd:TIGR01193 472 GDIVINDVSYSYGY-GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 203 AYFDQYREILDpeKSVIDNLADGKQEVTVGGRERHALSYLQ---DFLFSPKRARTPVKA----LSGGEKNRLLLARIFLK 275
Cdd:TIGR01193 551 NYLPQEPYIFS--GSILENLLLGAKENVSQDEIWAACEIAEikdDIENMPLGYQTELSEegssISGGQKQRIALARALLT 628
|
170
....*....|....*.
gi 2793968422 276 SNNLLILDEPTNDLDI 291
Cdd:TIGR01193 629 DSKVLILDESTSNLDT 644
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
150-314 |
1.14e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.49 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CG---TKLEVAY--------------------- 204
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGyvpFKRRKEFarrigvvfgqrsqlwwdlpai 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 205 --FDQYREI--LDPE--KSVIDNLADgkqevtvggrerhALSyLQDFLfspkraRTPVKALSGGEKNRLLLARIFLKSNN 278
Cdd:COG4586 115 dsFRLLKAIyrIPDAeyKKRLDELVE-------------LLD-LGELL------DTPVRQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2793968422 279 LLILDEPTNDLDIETLELL----EDLLANYQGTLLLVSHD 314
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIreflKEYNRERGTTILLTSHD 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
151-316 |
1.19e-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: 64.38 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 151 EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDQlkPDSGRLH-CGTKL--------------EVAYFDQyREILD 213
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLagLDR--PTSGTVRlAGQDLfaldedararlrarHVGFVFQ-SFQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 214 PEKSVIDN------LADGK----------QEVTVGGRERHAlsylqdflfsPKRartpvkaLSGGEKNRLLLARIFLKSN 277
Cdd:COG4181 103 PTLTALENvmlpleLAGRRdarararallERVGLGHRLDHY----------PAQ-------LSGGEQQRVALARAFATEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2793968422 278 NLLILDEPTNDLDietlelledlLAN--------------YQGTLLLVSHDRQ 316
Cdd:COG4181 166 AILFADEPTGNLD----------AATgeqiidllfelnreRGTTLVLVTHDPA 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
139-290 |
1.38e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.34 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC--------GTKLEVAYFDqyrE 210
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpvegpGAERGVVFQN---E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 211 ILDPEKSVIDNLADGKQEVTVGGRERH--ALSYLQDFLFSPKRARtPVKALSGGEKNRLLLARIFLKSNNLLILDEPTND 288
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLeiAHQMLKKVGLEGAEKR-YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
..
gi 2793968422 289 LD 290
Cdd:PRK11248 159 LD 160
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
146-193 |
1.88e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.95 E-value: 1.88e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2793968422 146 GFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR 193
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
139-314 |
4.28e-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: 62.70 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGF-EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlEVAYFDQY---REI--- 211
Cdd:cd03295 2 EFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPVelrRKIgyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 -----LDPEKSVIDNLA-----DGKQEVTvggRERHALSYLQDFLFSPK--RARTPvKALSGGEKNRLLLARIFLKSNNL 279
Cdd:cd03295 81 iqqigLFPHMTVEENIAlvpklLKWPKEK---IRERADELLALVGLDPAefADRYP-HELSGGQQQRVGVARALAADPPL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 2793968422 280 LILDEPTNDLDIETLELLEDLLANYQ----GTLLLVSHD 314
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHD 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
136-290 |
4.30e-11 |
|
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: 62.89 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 136 IVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGTKLEVAYFDQYR----- 209
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvLVDGHDLALADPAWLRrqvgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 210 ---EILDPEKSVIDNLADGKQEVTVGGRERHA-LSYLQDFLFS-PKRARTPV----KALSGGEKNRLLLARIFLKSNNLL 280
Cdd:cd03252 81 vlqENVLFNRSIRDNIALADPGMSMERVIEAAkLAGAHDFISElPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRIL 160
|
170
....*....|
gi 2793968422 281 ILDEPTNDLD 290
Cdd:cd03252 161 IFDEATSALD 170
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
148-316 |
4.44e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.53 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 148 EGK---EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGTKL--------------EVAYFDQYR 209
Cdd:PRK11629 17 EGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGQPMsklssaakaelrnqKLGFIYQFH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 210 EILdPEKSVIDNLAdgkQEVTVGGRER-HALSYLQDFLFS---PKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEP 285
Cdd:PRK11629 97 HLL-PDFTALENVA---MPLLIGKKKPaEINSRALEMLAAvglEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 2793968422 286 TNDLDIETLELLEDLLANY---QGT-LLLVSHDRQ 316
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELnrlQGTaFLVVTHDLQ 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
137-290 |
5.08e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.28 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEG-KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGTKLEVAYFDQYREIL-- 212
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvLIRGEPITKENIREVRKFVgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 ---DPEKSVIDNLAD----------GKQEVTVGGRERHALSYLQdflFSPKRARTPvKALSGGEKNRLLLARIFLKSNNL 279
Cdd:PRK13652 83 vfqNPDDQIFSPTVEqdiafgpinlGLDEETVAHRVSSALHMLG---LEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQV 158
|
170
....*....|.
gi 2793968422 280 LILDEPTNDLD 290
Cdd:PRK13652 159 LVLDEPTAGLD 169
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
150-290 |
6.13e-11 |
|
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: 61.90 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLldqlkpdSGRLHCGTKL--EVAYFDQYREILDPEKSV-----IDNL 222
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAI-------SGRVEGGGTTsgQILFNGQPRKPDQFQKCVayvrqDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 223 ADGkqeVTVggreRHALSYLQDFLF---SPKRARTP-------------------VKALSGGEKNRLLLARIFLKSNNLL 280
Cdd:cd03234 93 LPG---LTV----RETLTYTAILRLprkSSDAIRKKrvedvllrdlaltriggnlVKGISGGERRRVSIAVQLLWDPKVL 165
|
170
....*....|
gi 2793968422 281 ILDEPTNDLD 290
Cdd:cd03234 166 ILDEPTSGLD 175
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
141-290 |
6.80e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.34 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLEVA---------------- 203
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiAGNHFDFSktpsdkairelrrnvg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 204 -YFDQYReiLDPEKSVIDNLADGKQEVTVGGRER---HALSYLQDFLFSPKRARTPVKaLSGGEKNRLLLARIFLKSNNL 279
Cdd:PRK11124 86 mVFQQYN--LWPHLTVQQNLIEAPCRVLGLSKDQalaRAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQV 162
|
170
....*....|.
gi 2793968422 280 LILDEPTNDLD 290
Cdd:PRK11124 163 LLFDEPTAALD 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
155-313 |
6.87e-11 |
|
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: 61.74 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 155 DFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG----TKLEVAyfDQYREILDPEKSVIDNLaDGKQEVT 230
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvTAAPPA--DRPVSMLFQENNLFAHL-TVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 231 VG--------GRERHAL-SYLQDFLFSPKRARTPvKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELL---- 297
Cdd:cd03298 93 LGlspglkltAEDRQAIeVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMldlv 171
|
170
....*....|....*.
gi 2793968422 298 EDLLANYQGTLLLVSH 313
Cdd:cd03298 172 LDLHAETKMTVLMVTH 187
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
139-290 |
8.64e-11 |
|
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: 61.97 E-value: 8.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREI------- 211
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVgfvfqhy 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 -LDPEKSVIDNLADGKQEVTVGGRERHA--------------LSYLQDflfspkraRTPVKaLSGGEKNRLLLARIFLKS 276
Cdd:cd03296 84 aLFRHMTVFDNVAFGLRVKPRSERPPEAeirakvhellklvqLDWLAD--------RYPAQ-LSGGQRQRVALARALAVE 154
|
170
....*....|....
gi 2793968422 277 NNLLILDEPTNDLD 290
Cdd:cd03296 155 PKVLLLDEPFGALD 168
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
163-324 |
9.19e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.76 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 163 GDRIALIGPNGCGKSTVLKLLLDQLKPDSGR--LHCGTKLEVAYFDQYR-EildpEKSVIDNLADGKQEVTVGGRERHAL 239
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNvsLDPNERLGKLRQDQFAfE----EFTVLDTVIMGHTELWEVKQERDRI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 240 SYL--------------------QDFLFSPKRA--------------RTPVKALSGGEKNRLLLARIFLKSNNLLILDEP 285
Cdd:PRK15064 103 YALpemseedgmkvadlevkfaeMDGYTAEARAgelllgvgipeeqhYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEP 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 2793968422 286 TNDLDIETLELLEDLLANYQGTLLLVSHDRQFVdNTVMT 324
Cdd:PRK15064 183 TNNLDINTIRWLEDVLNERNSTMIIISHDRHFL-NSVCT 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
139-291 |
1.01e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.02 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGtKLEVAYFdqyreildPEKSV 218
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATT--------PSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 IDNLADGKQE------VTV------------GGR-----ERH---ALSYLQdflFSPKRARtPVKALSGGEKNRLLLARI 272
Cdd:COG4604 74 AKRLAILRQEnhinsrLTVrelvafgrfpysKGRltaedREIideAIAYLD---LEDLADR-YLDELSGGQRQRAFIAMV 149
|
170
....*....|....*....
gi 2793968422 273 FLKSNNLLILDEPTNDLDI 291
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDM 168
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
141-290 |
1.42e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.57 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPD---SGRLhcgtklevaYFDQyREI--LDPE 215
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV---------LLNG-RRLtaLPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 216 K----------------SVIDNLADGKQEvTVGGRERHA----------LSYLQDflfspkraRTPvKALSGGEKNRLLL 269
Cdd:COG4136 75 QrrigilfqddllfphlSVGENLAFALPP-TIGRAQRRArveqaleeagLAGFAD--------RDP-ATLSGGQRARVAL 144
|
170 180
....*....|....*....|.
gi 2793968422 270 ARIFLKSNNLLILDEPTNDLD 290
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLD 165
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
155-291 |
1.57e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 155 DFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC----GTKLEVAYFD--QYREILDPEKSVI-DNLADG-K 226
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYALSeaERRRLLRTEWGFVhQHPRDGlR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 227 QEVTVGGR---------ERH-------ALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK11701 104 MQVSAGGNigerlmavgARHygdiratAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
.
gi 2793968422 291 I 291
Cdd:PRK11701 184 V 184
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
99-291 |
2.18e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 99 NEGRVRALKKLREERINRREVQGkaviqiDDGqrsgkIVFEaenlNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKST 178
Cdd:TIGR01271 403 DEGIGELFEKIKQNNKARKQPNG------DDG-----LFFS----NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSS 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 179 VLKLLLDQLKPDSGRL-HCGtklEVAYFDQYREILdpEKSVIDNLADGkqeVTVGG-RERHALSYLQ---DFLFSPKRAR 253
Cdd:TIGR01271 468 LLMMIMGELEPSEGKIkHSG---RISFSPQTSWIM--PGTIKDNIIFG---LSYDEyRYTSVIKACQleeDIALFPEKDK 539
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2793968422 254 TPVK----ALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:TIGR01271 540 TVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
139-315 |
2.35e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 61.70 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDQlkPDSGRLHCGTklEVAYFD---QYREI-- 211
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagLET--PDSGRIVLNG--RDLFTNlppRERRVgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 ------LDPEKSVIDNLADGKQEVTVGGRERHA----------LSYLQDflfspkraRTPvKALSGGEKNRLLLARIfLK 275
Cdd:COG1118 80 vfqhyaLFPHMTVAENIAFGLRVRPPSKAEIRArveellelvqLEGLAD--------RYP-SQLSGGQRQRVALARA-LA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2793968422 276 SN-NLLILDEPTNDLDietlelledllA---------------NYQGTLLLVSHDR 315
Cdd:COG1118 150 VEpEVLLLDEPFGALD-----------AkvrkelrrwlrrlhdELGGTTVFVTHDQ 194
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
141-331 |
2.46e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.82 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKlLLDQLKPDSGRLHCGTKLEvaYFDQ--YREILDPEK-- 216
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRVE--FFNQniYERRVNLNRlr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 ---------------SVIDNLADGKQevTVGGRERHAL-----SYLQDF-LFSPKRARTPVKA--LSGGEKNRLLLARIF 273
Cdd:PRK14258 88 rqvsmvhpkpnlfpmSVYDNVAYGVK--IVGWRPKLEIddiveSALKDAdLWDEIKHKIHKSAldLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2793968422 274 LKSNNLLILDEPTNDLDIETLELLEDLLANY----QGTLLLVSHDRQFVDNTVMTSWIFEGN 331
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVSRLSDFTAFFKGN 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
157-394 |
2.61e-10 |
|
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: 63.04 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 157 SFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHcgTKLEVAYFDQYREILDpeKSVIDNLADGKQ-EVTVGGRE 235
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH--MKGSVAYVPQQAWIQN--DSLRENILFGKAlNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 236 RHALSYLQDFLFSPKRARTPVKA----LSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTL--- 308
Cdd:TIGR00957 734 LEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknk 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 309 --LLVSHDRQFVDNT----VMTSW----------IFEGNGVVEEFVGGYHDAQQQrkQAIEYRQVEKPSKPEKVVEETPK 372
Cdd:TIGR00957 814 trILVTHGISYLPQVdviiVMSGGkisemgsyqeLLQRDGAFAEFLRTYAPDEQQ--GHLEDSWTALVSGEGKEAKLIEN 891
|
250 260
....*....|....*....|..
gi 2793968422 373 TAPVKAKAKKlsyKLQRELEAL 394
Cdd:TIGR00957 892 GMLVTDVVGK---QLQRQLSAS 910
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
144-291 |
2.84e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.03 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 144 NFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL-HCGtklEVAYFDQYREILdpEKSVIDNL 222
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkHSG---RISFSSQFSWIM--PGTIKENI 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2793968422 223 ADGkqevtVGGRERHALSYL------QDFLFSPKRARTPVK----ALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:cd03291 119 IFG-----VSYDEYRYKSVVkacqleEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
155-285 |
3.57e-10 |
|
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: 61.27 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 155 DFSFNIMRGDRIALIGPNGCGKSTVLKLL--LdqLKPDSGRLHCGtklEVAYFDQYREI-----------------LDPE 215
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIagL--ERPDSGRIRLG---GEVLQDSARGIflpphrrrigyvfqearLFPH 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 216 KSVIDNLADGkQEVTVGGRERHALSYLQDFL-FSPKRARTPVkALSGGEKNRLLLARIFLKSNNLLILDEP 285
Cdd:COG4148 92 LSVRGNLLYG-RKRAPRAERRISFDEVVELLgIGHLLDRRPA-TLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
137-290 |
3.82e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.41 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKE--IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKL-EVAYFDQYREI- 211
Cdd:PRK13635 5 IIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVgGMVLsEETVWDVRRQVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 ---LDPEK-----SVIDNLADGKQEVTVG-----GRERHALS--YLQDFLfspkrARTPVKaLSGGEKNRLLLARIFLKS 276
Cdd:PRK13635 85 mvfQNPDNqfvgaTVQDDVAFGLENIGVPreemvERVDQALRqvGMEDFL-----NREPHR-LSGGQKQRVAIAGVLALQ 158
|
170
....*....|....
gi 2793968422 277 NNLLILDEPTNDLD 290
Cdd:PRK13635 159 PDIIILDEATSMLD 172
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
139-290 |
4.35e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.89 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG----TKLEVayfdQYREI--- 211
Cdd:PRK11432 8 VLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvTHRSI----QQRDIcmv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 -----LDPEKSVIDNLADG-------KQEVTVGGRERHALSYLQDFlfspkrARTPVKALSGGEKNRLLLARIFLKSNNL 279
Cdd:PRK11432 84 fqsyaLFPHMSLGENVGYGlkmlgvpKEERKQRVKEALELVDLAGF------EDRYVDQISGGQQQRVALARALILKPKV 157
|
170
....*....|.
gi 2793968422 280 LILDEPTNDLD 290
Cdd:PRK11432 158 LLFDEPLSNLD 168
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
159-330 |
4.42e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.73 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 159 NIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhcGTKLE-VAYFDQYREIlDPEKSVIDNLADGKQEVTVGgrerh 237
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--EIELDtVSYKPQYIKA-DYEGTVRDLLSSITKDFYTH----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 238 alSYLQDFLFSP----KRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD----IETLELLEDLLANYQGTLL 309
Cdd:cd03237 93 --PYFKTEIAKPlqieQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAF 170
|
170 180
....*....|....*....|.
gi 2793968422 310 LVSHDRQFVDNTVMTSWIFEG 330
Cdd:cd03237 171 VVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
142-290 |
4.80e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.81 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 142 NLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKL--EVA--------YFDQYreI 211
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmnDVPpaergvgmVFQSY--A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 LDPEKSVIDNLADGKQEVTVGGRER-----HALSYLQ-DFLFSpkraRTPvKALSGGEKNRLLLARIFLKSNNLLILDEP 285
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEInqrvnQVAEVLQlAHLLD----RKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
....*
gi 2793968422 286 TNDLD 290
Cdd:PRK11000 161 LSNLD 165
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
137-290 |
7.42e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.86 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGF-EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlEVAY----FDQYREI 211
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYsrkgLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 L-----DPEK-----SVIDNLADGK-----QEVTVGGRERHAL-----SYLQDflfspkrarTPVKALSGGEKNRLLLAR 271
Cdd:PRK13636 84 VgmvfqDPDNqlfsaSVYQDVSFGAvnlklPEDEVRKRVDNALkrtgiEHLKD---------KPTHCLSFGQKKRVAIAG 154
|
170
....*....|....*....
gi 2793968422 272 IFLKSNNLLILDEPTNDLD 290
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLD 173
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
150-352 |
8.23e-10 |
|
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: 59.43 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG----TKLEVAYFDQYREIL-----------DP 214
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlYQLDRKQRRAFRRDVqlvfqdspsavNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 215 EKSVIDNLADGKQEVT---VGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 292 ETLELLEDLLANYQ---GT-LLLVSHDRQFVDNTVMTSWIFEGNGVVEEFVGGY-----HDAQQQRKQAI 352
Cdd:TIGR02769 184 VLQAVILELLRKLQqafGTaYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQllsfkHPAGRNLQSAV 253
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
134-291 |
8.27e-10 |
|
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: 57.83 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEAENLNfgfeGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG------------TKLE 201
Cdd:cd03215 1 GEPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtrrsprdaIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 202 VAYF--DQYREILDPEKSVIDNLAdgkqevtvggrerhaLSYLqdflfspkrartpvkaLSGGEKNRLLLARIFLKSNNL 279
Cdd:cd03215 77 IAYVpeDRKREGLVLDLSVAENIA---------------LSSL----------------LSGGNQQKVVLARWLARDPRV 125
|
170
....*....|..
gi 2793968422 280 LILDEPTNDLDI 291
Cdd:cd03215 126 LILDEPTRGVDV 137
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
138-291 |
8.57e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKL-----------EVAYFD 206
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 QYreiLDPeksvidnlADG---KQEVTVG--------GR----------ERHALSYLQDFlfspkrARTPVKALSGGEKN 265
Cdd:PRK10575 92 QQ---LPA--------AEGmtvRELVAIGrypwhgalGRfgaadrekveEAISLVGLKPL------AHRLVDSLSGGERQ 154
|
170 180
....*....|....*....|....*.
gi 2793968422 266 RLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
153-320 |
1.04e-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: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG--------TKLEVA-----------YFDQYReiLD 213
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmTKPGPDgrgrakryigiLHQEYD--LY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 214 PEKSVIDNLADG-KQEVTVGGRERHALSYLQDFLFSPKRARTPVK----ALSGGEKNRLLLARIFLKSNNLLILDEPTND 288
Cdd:TIGR03269 378 PHRTVLDNLTEAiGLELPDELARMKAVITLKMVGFDEEKAEEILDkypdELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 2793968422 289 LD----IETLELLEDLLANYQGTLLLVSHDRQFVDN 320
Cdd:TIGR03269 458 MDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLD 493
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
142-315 |
1.21e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 142 NLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC---GTKLEVAYFDQ------YREIL 212
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqSIKKDLCTYQKqlcfvgHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 DPEKSVIDN------LADGKQEVTVGGReRHALSYLQDFlfspkrartPVKALSGGEKNRLLLARIFLKSNNLLILDEPT 286
Cdd:PRK13540 86 NPYLTLRENclydihFSPGAVGITELCR-LFSLEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|..
gi 2793968422 287 NDLD---IETLELLEDLLANYQGTLLLVSHDR 315
Cdd:PRK13540 156 VALDelsLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
163-291 |
1.32e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.53 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 163 GDRIALIGPNGCGKSTVLKLLLDQLKPDSGRlHC-------------GTKLEvAYFDQYRE-----ILDPEK-SVIDNLA 223
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDdppdwdeildefrGSELQ-NYFTKLLEgdvkvIVKPQYvDLIPKAV 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2793968422 224 DGK-QEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:cd03236 104 KGKvGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
137-290 |
1.35e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.94 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGF-EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLhcgtklevayfdqyreILDPE 215
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV----------------LIKGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 216 KSVIDNLADGKQEVTVG------GRERHALSYLQDFLFSP-----------KRARTPVKA-------------LSGGEKN 265
Cdd:PRK13639 65 PIKYDKKSLLEVRKTVGivfqnpDDQLFAPTVEEDVAFGPlnlglskeeveKRVKEALKAvgmegfenkpphhLSGGQKK 144
|
170 180
....*....|....*....|....*
gi 2793968422 266 RLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
139-290 |
1.39e-09 |
|
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: 60.15 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEG--KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSG--RL---------------HCGTk 199
Cdd:COG4618 332 SVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvRLdgadlsqwdreelgrHIGY- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 200 L--EVAYFD--------QYREIlDPEKSV-----------IDNLADG-KQEVTVGGRerhalsylqdflfspkrartpvk 257
Cdd:COG4618 411 LpqDVELFDgtiaeniaRFGDA-DPEKVVaaaklagvhemILRLPDGyDTRIGEGGA----------------------- 466
|
170 180 190
....*....|....*....|....*....|...
gi 2793968422 258 ALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
139-336 |
1.47e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.22 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKL--LLDQlkPDSGRLHCG------TKLEVAYFDQYRE 210
Cdd:PRK11264 5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQ--PEAGTIRVGditidtARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 211 I------------LDPEKSVIDNLADG--------KQEVTVGGRERHALSYLqdflfSPKRARTPvKALSGGEKNRLLLA 270
Cdd:PRK11264 83 LrqhvgfvfqnfnLFPHRTVLENIIEGpvivkgepKEEATARARELLAKVGL-----AGKETSYP-RRLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2793968422 271 RIFLKSNNLLILDEPTNDLD---IETLELLEDLLANYQGTLLLVSHDRQFVDNtVMTSWIFEGNGVVEE 336
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVTHEMSFARD-VADRAIFMDQGRIVE 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
139-290 |
1.73e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLEvAYFDQYREIL----- 212
Cdd:PRK13538 3 EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwQGEPIR-RQRDEYHQDLlylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 ----DPEKSVIDNLA-------DGKQEVTVGGRERHALSylqdflfspKRARTPVKALSGGEKNRLLLARIFLKSNNLLI 281
Cdd:PRK13538 82 qpgiKTELTALENLRfyqrlhgPGDDEALWEALAQVGLA---------GFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
....*....
gi 2793968422 282 LDEPTNDLD 290
Cdd:PRK13538 153 LDEPFTAID 161
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
162-291 |
1.85e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 162 RGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL-HCGTKLEVayFDQYR--EILDpeksVIDNLADGK-------QEV-- 229
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeEEPSWDEV--LKRFRgtELQN----YFKKLYNGEikvvhkpQYVdl 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2793968422 230 -------TVG-----GRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK13409 172 ipkvfkgKVRellkkVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
162-291 |
2.68e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 162 RGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC------------GTKLevayFDQYREILDPEKSV------IDNLA 223
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEepswdevlkrfrGTEL----QDYFKKLANGEIKVahkpqyVDLIP 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2793968422 224 ---DGK-QEVTVGGRERHALSYLQDFL-FSPKRARtPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:COG1245 174 kvfKGTvRELLEKVDERGKLDELAEKLgLENILDR-DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
139-318 |
2.72e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.33 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKE-----------IVKDFSFNIMRGDRIALIGPNGCGKST----VLKLLLDQ--LKPDSGRLHCGT--- 198
Cdd:PRK15134 277 DVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQgeIWFDGQPLHNLNrrq 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 199 ------KLEVAYFDQYREiLDPEKSVIDNLADGKQ----EVTVGGRERHALSYLQDFLFSPK-RARTPvKALSGGEKNRL 267
Cdd:PRK15134 357 llpvrhRIQVVFQDPNSS-LNPRLNVLQIIEEGLRvhqpTLSAAQREQQVIAVMEEVGLDPEtRHRYP-AEFSGGQRQRI 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2793968422 268 LLARIFLKSNNLLILDEPTNDLDIETLEL----LEDLLANYQGTLLLVSHDRQFV 318
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLDKTVQAQilalLKSLQQKHQLAYLFISHDLHVV 489
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
134-290 |
3.12e-09 |
|
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: 56.65 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH------CGTKLE------ 201
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidiSTIPLEdlrssl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 202 -------VAYFDQYREILDPEKSVIDNLADGKQEVTVGGRErhalsylqdflfspkrartpvkaLSGGEKNRLLLARIFL 274
Cdd:cd03369 85 tiipqdpTLFSGTIRSNLDPFDEYSDEEIYGALRVSEGGLN-----------------------LSQGQRQLLCLARALL 141
|
170
....*....|....*.
gi 2793968422 275 KSNNLLILDEPTNDLD 290
Cdd:cd03369 142 KRPRVLVLDEATASID 157
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
137-290 |
3.94e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.45 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKE--IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL----HCGTKLEVAYFDQYRE 210
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 211 IL--DPEKSVIDNLAdgKQEVTVgGRERHALSY----------LQDFLFSPKRARTPvKALSGGEKNRLLLARIFLKSNN 278
Cdd:PRK13648 87 IVfqNPDNQFVGSIV--KYDVAF-GLENHAVPYdemhrrvseaLKQVDMLERADYEP-NALSGGQKQRVAIAGVLALNPS 162
|
170
....*....|..
gi 2793968422 279 LLILDEPTNDLD 290
Cdd:PRK13648 163 VIILDEATSMLD 174
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
139-290 |
4.51e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.79 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDQ-----LK---PDSGRLHCGTKlEVAY-FDQ 207
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIagLEHqtsghIRfhgTDVSRLHARDR-KVGFvFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 208 YreILDPEKSVIDNLADG---------------KQEVTVgGRERHALSYLQDflfspkraRTPVKaLSGGEKNRLLLARI 272
Cdd:PRK10851 83 Y--ALFRHMTVFDNIAFGltvlprrerpnaaaiKAKVTQ-LLEMVQLAHLAD--------RYPAQ-LSGGQKQRVALARA 150
|
170
....*....|....*...
gi 2793968422 273 FLKSNNLLILDEPTNDLD 290
Cdd:PRK10851 151 LAVEPQILLLDEPFGALD 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
131-286 |
4.55e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 131 QRSGKIVFEAENLNfgfeGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLE-------- 201
Cdd:COG1129 250 AAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRlDGKPVRirsprdai 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 202 ---VAYF--DQYREILDPEKSVIDN--LADGKQEVTVG----GRER-HALSYLQDFLFSPKRARTPVKALSGGEKNRLLL 269
Cdd:COG1129 326 ragIAYVpeDRKGEGLVLDLSIRENitLASLDRLSRGGlldrRRERaLAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVL 405
|
170
....*....|....*..
gi 2793968422 270 ARIFLKSNNLLILDEPT 286
Cdd:COG1129 406 AKWLATDPKVLILDEPT 422
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
42-118 |
4.58e-09 |
|
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: 52.96 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 42 VDLDRGKLSSFPGDYENYLLEKEEALRVEEMQNAEFDKKLAQEEVWI-RQGIKARRTR-NEGRVRALKKLRE-ERINRRE 118
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKqAQSRIKALEKMERiEKPERDK 80
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
162-331 |
5.88e-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: 54.69 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 162 RGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHcgtklevayfdqyreILDPEKSVIDNLADGKQEVTVGGrerhalsy 241
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------YIDGEDILEEVLDQLLLIIVGGK-------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 242 lqdflfspkrartpVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSHDRQFVDNT 321
Cdd:smart00382 58 --------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
170
....*....|
gi 2793968422 322 VMTSWIFEGN 331
Cdd:smart00382 124 NDEKDLGPAL 133
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
149-290 |
6.20e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.89 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 149 GKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLdQLKPD-SGRLHCGTKLEVAYFDQ--Y------REIL---DPEK 216
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA-GLWPYgSGRIARPAGARVLFLPQrpYlplgtlREALlypATAE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 SVIDnladgkQEVT-----VGgrerhaLSYLQDFLFSPKR-ARTpvkaLSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:COG4178 454 AFSD------AELRealeaVG------LGHLAERLDEEADwDQV----LSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
147-290 |
6.50e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 147 FEGKEIVkDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKL---------------EVAYFDQYREI 211
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 LDPEKSVIDNLADGKQEVTVG-------GRERHALSYLQDFLFSpkraRTPVKaLSGGEKNRLLLARIFLKSNNLLILDE 284
Cdd:PRK13649 97 QLFEETVLKDVAFGPQNFGVSqeeaealAREKLALVGISESLFE----KNPFE-LSGGQMRRVAIAGILAMEPKILVLDE 171
|
....*.
gi 2793968422 285 PTNDLD 290
Cdd:PRK13649 172 PTAGLD 177
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
153-325 |
6.73e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 56.32 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGrlhcGTKLE-----------VAYFDQYReiLDPEKSVIDN 221
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSG----GVILEgkqitepgpdrMVVFQNYS--LLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 222 LA-----------DGKQEVTVggRERHALSYLQdflfspKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:TIGR01184 75 IAlavdrvlpdlsKSERRAIV--EEHIALVGLT------EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 2793968422 291 IETLELLEDLLAN----YQGTLLLVSHDrqfVDNTVMTS 325
Cdd:TIGR01184 147 ALTRGNLQEELMQiweeHRVTVLMVTHD---VDEALLLS 182
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
128-291 |
7.42e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 57.72 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 128 DDGQRS-----GKIVFEaeNLNFGFEGKEI--VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGTK 199
Cdd:PRK11176 329 DEGKRVierakGDIEFR--NVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEiLLDGHD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 200 LE----------VAYFDQYREILDpeKSVIDNLADGKQEV-TVGGRERHA-LSYLQDFLFSPKRARTPV-----KALSGG 262
Cdd:PRK11176 407 LRdytlaslrnqVALVSQNVHLFN--DTIANNIAYARTEQySREQIEEAArMAYAMDFINKMDNGLDTVigengVLLSGG 484
|
170 180
....*....|....*....|....*....
gi 2793968422 263 EKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDT 513
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
151-336 |
7.48e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.52 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 151 EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTK-----------LEVAYFDQYREI-------- 211
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqLKVADKNQLRLLrtrltmvf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 ----LDPEKSVIDNLADGKQEV----TVGGRERhALSYLQDFLFSPK-RARTPVKaLSGGEKNRLLLARIFLKSNNLLIL 282
Cdd:PRK10619 99 qhfnLWSHMTVLENVMEAPIQVlglsKQEARER-AVKYLAKVGIDERaQGKYPVH-LSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2793968422 283 DEPTNDLD---IETLELLEDLLANYQGTLLLVSHDRQFVDNtVMTSWIFEGNGVVEE 336
Cdd:PRK10619 177 DEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARH-VSSHVIFLHQGKIEE 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
136-290 |
8.28e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.33 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 136 IVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDQLKPDsgrlhCGTKLEVAYFDQ--YREI 211
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPG-----FRVEGKVTFHGKnlYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 LDP-----------------EKSVIDNLADGKQEVTVGGR-----ERhalSYLQDFLFS--PKRARTPVKALSGGEKNRL 267
Cdd:PRK14243 84 VDPvevrrrigmvfqkpnpfPKSIYDNIAYGARINGYKGDmdelvER---SLRQAALWDevKDKLKQSGLSLSGGQQQRL 160
|
170 180
....*....|....*....|...
gi 2793968422 268 LLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALD 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-291 |
1.75e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 23 SIIFISHDRAFIKSMATRIVDLDRGKLssfpgdyenyllekeealrVEEMQNAEFDKK-LAQEEVwirqgikarrtrneG 101
Cdd:COG3845 193 SIIFITHKLREVMAIADRVTVLRRGKV-------------------VGTVDTAETSEEeLAELMV--------------G 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 102 RVRALKKLREERinrrevqgkaviqiddgqRSGKIVFEAENLNF-GFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVL 180
Cdd:COG3845 240 REVLLRVEKAPA------------------EPGEVVLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 181 KLLLDQLKPDSGRLH-CGTKLE-----------VAYF--DQYREILDPEKSVIDNLADGKQ---EVTVGGR------ERH 237
Cdd:COG3845 302 EALAGLRPPASGSIRlDGEDITglsprerrrlgVAYIpeDRLGRGLVPDMSVAENLILGRYrrpPFSRGGFldrkaiRAF 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2793968422 238 ALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:COG3845 382 AEELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
142-290 |
1.80e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.40 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 142 NLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGTKLE------VAYFDQYREIL-D 213
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAvLWQGKPLDyskrglLALRQQVATVFqD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 214 PEKSV----ID--------NLadGKQEVTVGGRERHALSylqdfLFSPKRAR-TPVKALSGGEKNRLLLARIFLKSNNLL 280
Cdd:PRK13638 86 PEQQIfytdIDsdiafslrNL--GVPEAEITRRVDEALT-----LVDAQHFRhQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170
....*....|
gi 2793968422 281 ILDEPTNDLD 290
Cdd:PRK13638 159 LLDEPTAGLD 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
154-286 |
1.90e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 154 KDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLEvayFDQYREILD-------------PEKSVI 219
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILlDGEPVR---FRSPRDAQAagiaiihqelnlvPNLSVA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2793968422 220 DNLADGkQEVTVGGR------ERHALSYLQDF-L-FSPkraRTPVKALSGGEKNRLLLARIFLKSNNLLILDEPT 286
Cdd:COG1129 98 ENIFLG-REPRRGGLidwramRRRARELLARLgLdIDP---DTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
137-290 |
1.91e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.92 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDQLKPD---SGRLHCGT----KLEVAYFDQ 207
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGqdifKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 208 YREIL------DPEKSVIDNLADG-------KQEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFL 274
Cdd:PRK14247 83 RVQMVfqipnpIPNLSIFENVALGlklnrlvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALA 162
|
170
....*....|....*.
gi 2793968422 275 KSNNLLILDEPTNDLD 290
Cdd:PRK14247 163 FQPEVLLADEPTANLD 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
153-314 |
2.02e-08 |
|
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: 55.34 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlEVAYFD--QYREI-------------LDPEKS 217
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ-DIAAMSrkELRELrrkkismvfqsfaLLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 218 VIDNLADGKQEVTVGGRERH--ALSYLQDFLFSPKRARTPvKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD----I 291
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREerAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirR 197
|
170 180
....*....|....*....|...
gi 2793968422 292 ETLELLEDLLANYQGTLLLVSHD 314
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHD 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
141-313 |
2.69e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.05 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNF------GFEgKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC--------GTKL-----E 201
Cdd:PRK13637 6 ENLTHiymegtPFE-KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditdkKVKLsdirkK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 202 VAYFDQYREILDPEKSVIDNLADGKQEVTVGGRERH----------ALSYlQDFlfspkRARTPVKaLSGGEKNRLLLAR 271
Cdd:PRK13637 85 VGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIEnrvkramnivGLDY-EDY-----KDKSPFE-LSGGQKRRVAIAG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2793968422 272 IFLKSNNLLILDEPTNDLDIETL----ELLEDLLANYQGTLLLVSH 313
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRdeilNKIKELHKEYNMTIILVSH 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
134-291 |
3.61e-08 |
|
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: 53.65 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTK------LE------ 201
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskigLHdlrsri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 202 -------VAYFDQYREILDPE-----------------KSVIDNLADGKQ-EVTVGGrerhalsylqdflfspkrartpv 256
Cdd:cd03244 81 siipqdpVLFSGTIRSNLDPFgeysdeelwqalervglKEFVESLPGGLDtVVEEGG----------------------- 137
|
170 180 190
....*....|....*....|....*....|....*
gi 2793968422 257 KALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:cd03244 138 ENLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
137-314 |
4.46e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.35 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGF---EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKL-EVAYFDQYREI 211
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLtEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 ----LDPEK-----SVIDNLADGKQE-----VTVGGRERHALSY--LQDFlfspkRARTPVKaLSGGEKNRLLLARIFLK 275
Cdd:PRK13650 84 gmvfQNPDNqfvgaTVEDDVAFGLENkgiphEEMKERVNEALELvgMQDF-----KEREPAR-LSGGQKQRVAIAGAVAM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2793968422 276 SNNLLILDEPTNDLD----IETLELLEDLLANYQGTLLLVSHD 314
Cdd:PRK13650 158 RPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
139-290 |
5.73e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.56 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLK------------LLLDQLKPDSGRLH-CGTKLEVAY- 204
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVNDPKVDeRLIRQEAGMv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 205 FDQYReiLDPEKSVIDNLADGKQEVTVGGR---ERHALSYLQDFLFSPKRARTPVKaLSGGEKNRLLLARIFLKSNNLLI 281
Cdd:PRK09493 83 FQQFY--LFPHLTALENVMFGPLRVRGASKeeaEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKLML 159
|
....*....
gi 2793968422 282 LDEPTNDLD 290
Cdd:PRK09493 160 FDEPTSALD 168
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
135-290 |
6.07e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.69 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 135 KIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDQLKPDSgRLHCGTKL------------ 200
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEA-RVEGEVRLfgrniyspdvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 201 -----EVAYFDQYREILdPEKSVIDNLADG-------KQEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLL 268
Cdd:PRK14267 81 ievrrEVGMVFQYPNPF-PHLTIYDNVAIGvklnglvKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLV 159
|
170 180
....*....|....*....|..
gi 2793968422 269 LARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANID 181
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
127-284 |
6.38e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.72 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 127 IDDGQRS---GKIVFEAENLNFGFEG--KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSG--RLHcGTK 199
Cdd:PRK10789 300 VKDGSEPvpeGRGELDVNIRQFTYPQtdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGdiRFH-DIP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 200 LEVAYFDQYREIL-----DP---EKSVIDNLADGKQEVTVGGRERHA--LSYLQDFLFSPKRARTPVKA----LSGGEKN 265
Cdd:PRK10789 379 LTKLQLDSWRSRLavvsqTPflfSDTVANNIALGRPDATQQEIEHVArlASVHDDILRLPQGYDTEVGErgvmLSGGQKQ 458
|
170
....*....|....*....
gi 2793968422 266 RLLLARIFLKSNNLLILDE 284
Cdd:PRK10789 459 RISIARALLLNAEILILDD 477
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
139-290 |
7.84e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 53.57 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLEvayFDQYREI------ 211
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwDGEPLD---PEDRRRIgylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 --LDPEKSVIDNLAD-------GKQEVtvggRERhALSYLQDF-LfsPKRARTPVKALSGGEKNRLLLARIFLKSNNLLI 281
Cdd:COG4152 80 rgLYPKMKVGEQLVYlarlkglSKAEA----KRR-ADEWLERLgL--GDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
....*....
gi 2793968422 282 LDEPTNDLD 290
Cdd:COG4152 153 LDEPFSGLD 161
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
132-316 |
9.04e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.13 E-value: 9.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 132 RSGKIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLL-------DQLKPDSGRLHCGTKL---- 200
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIfqid 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 201 ------EVAYFDQYREILdPEKSVIDNLADGKQevTVGGRERHALSYLQDFLFSP--------KRARTPVKALSGGEKNR 266
Cdd:PRK14246 85 aiklrkEVGMVFQQPNPF-PHLSIYDNIAYPLK--SHGIKEKREIKKIVEECLRKvglwkevyDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2793968422 267 LLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQG--TLLLVSHDRQ 316
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQ 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
139-290 |
1.01e-07 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 53.52 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKE----IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKP---DSGR-LHCGTKLEVAYFDQYRE 210
Cdd:COG0444 3 EVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEiLFDGEDLLKLSEKELRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 211 I---------------LDPEKSVIDNLADG---KQEVTVGGRERHALSYLQDFLFSPKRARtpVKA----LSGGEKNRLL 268
Cdd:COG0444 83 IrgreiqmifqdpmtsLNPVMTVGDQIAEPlriHGGLSKAEARERAIELLERVGLPDPERR--LDRypheLSGGMRQRVM 160
|
170 180
....*....|....*....|..
gi 2793968422 269 LARIFLKSNNLLILDEPTNDLD 290
Cdd:COG0444 161 IARALALEPKLLIADEPTTALD 182
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
146-290 |
1.25e-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: 51.88 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 146 GFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPD---SGRLHCGTKlevayfdQYREILDPEKSVIdnl 222
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGI-------PYKEFAEKYPGEI--- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 223 adgkqeVTVGGRERH--ALSYLQDFLFSPK-RARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:cd03233 86 ------IYVSEEDVHfpTLTVRETLDFALRcKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
151-290 |
1.49e-07 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 52.20 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 151 EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKL--LLDqlKPDSGRLHC-GTKL-------------EVAYFDQYREILDp 214
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCinGLE--RPTSGSVLVdGTDLtllsgkelrkarrRIGMIFQHFNLLS- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2793968422 215 EKSVIDNLADGKQEVTVGGRERHALSY-LQDFL-FSPKRARTPvKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:cd03258 96 SRTVFENVALPLEIAGVPKAEIEERVLeLLELVgLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
139-318 |
1.59e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.43 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGF-EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlEVAYFDQY--REIL--- 212
Cdd:PRK13647 6 EVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR-EVNAENEKwvRSKVglv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 --DPE-----KSVIDNLADGKQEVTVGGRE-----RHALSY--LQDFlfspkRARTPVKaLSGGEKNRLLLARIFLKSNN 278
Cdd:PRK13647 85 fqDPDdqvfsSTVWDDVAFGPVNMGLDKDEverrvEEALKAvrMWDF-----RDKPPYH-LSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2793968422 279 LLILDEPTNDLDIETLELLEDLLA--NYQG-TLLLVSHDRQFV 318
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDrlHNQGkTVIVATHDVDLA 201
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
99-313 |
1.71e-07 |
|
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: 53.60 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 99 NEGRVRALKKLREERINRREVQGKAVIQIDDGqrsgKIVFEAENLnFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKST 178
Cdd:TIGR00954 419 KRPRVEEIESGREGGRNSNLVPGRGIVEYQDN----GIKFENIPL-VTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 179 VLKLLLDQLKPDSGRLHCGTKLEVAYFDQ--------YRE-ILDP-------EKSVID-NLADGKQEVTVGG--RERHAL 239
Cdd:TIGR00954 494 LFRILGELWPVYGGRLTKPAKGKLFYVPQrpymtlgtLRDqIIYPdssedmkRRGLSDkDLEQILDNVQLTHilEREGGW 573
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2793968422 240 SYLQDFLfspkrartpvKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQGTLLLVSH 313
Cdd:TIGR00954 574 SAVQDWM----------DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
135-290 |
2.35e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.92 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 135 KIVFEAENLNFGFEGKE--IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAYFDQYREI 211
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 L-----DPEK-----SVIDNLADGKQEVTVGGRERHALSY-------LQDFLfspkrARTPVKaLSGGEKNRLLLARIFL 274
Cdd:PRK13632 85 IgiifqNPDNqfigaTVEDDIAFGLENKKVPPKKMKDIIDdlakkvgMEDYL-----DKEPQN-LSGGQKQRVAIASVLA 158
|
170
....*....|....*.
gi 2793968422 275 KSNNLLILDEPTNDLD 290
Cdd:PRK13632 159 LNPEIIIFDESTSMLD 174
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
153-327 |
2.39e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.18 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVA-------YFDQYREILDPEKSVIDNlADG 225
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsfeatrSRNRYSVAYAAQKPWLLN-ATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 226 KQEVTVGG---RERH-----ALSYLQDFLFSPKRARTPVKA----LSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIET 293
Cdd:cd03290 96 EENITFGSpfnKQRYkavtdACSLQPDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2793968422 294 LELLEDL-----LANYQGTLLLVSHDRQFVDNtvmTSWI 327
Cdd:cd03290 176 SDHLMQEgilkfLQDDKRTLVLVTHKLQYLPH---ADWI 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
150-290 |
2.78e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC----GTKLEVAYFDQYREIL-----DPEK---- 216
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKitvdGITLTAKTVWDIREKVgivfqNPDNqfvg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 -SVIDNLADGKQEVTVGGRE-----RHALSY--LQDFLFSPKrartpvKALSGGEKNRLLLARIFLKSNNLLILDEPTND 288
Cdd:PRK13640 100 aTVGDDVAFGLENRAVPRPEmikivRDVLADvgMLDYIDSEP------ANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
..
gi 2793968422 289 LD 290
Cdd:PRK13640 174 LD 175
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
141-290 |
3.44e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGK---EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKP--DSGRLHCGTkleVAYFDQYREILDpe 215
Cdd:PLN03232 618 KNGYFSWDSKtskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRGS---VAYVPQVSWIFN-- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 216 KSVIDNLADG-KQEVTVGGRERHALSYLQDFLFSPKRARTPVKA----LSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PLN03232 693 ATVRENILFGsDFESERYWRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
155-290 |
3.57e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 51.66 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 155 DFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG---------------TKLEVAYFDQYREILDPEKSVI 219
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikpVRKKVGVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2793968422 220 DNLADGKQEVTVGGR--ERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK13643 104 KDVAFGPQNFGIPKEkaEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
139-291 |
3.94e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 50.84 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLL--DQLKPDSGRLH-CG---TKLEV---------- 202
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILlDGediLELSPderaragifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 203 AYfdQY-REIldPEKSVIDNL-----ADGKQEVTVGGRERHALSYLQDFLFSPKRARTPVKA-LSGGEKNRLLLARIFLK 275
Cdd:COG0396 82 AF--QYpVEI--PGVSVSNFLrtalnARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLL 157
|
170
....*....|....*.
gi 2793968422 276 SNNLLILDEPTNDLDI 291
Cdd:COG0396 158 EPKLAILDETDSGLDI 173
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
150-290 |
4.71e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.85 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlEVAYFDQYREIL-------DPEK------ 216
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-DVTKLPEYKRAKyigrvfqDPMMgtapsm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 SVIDNL--ADGKQE-------VTVGGRE--RHALSYLQDFLfsPKRARTPVKALSGGEknR----LLLARifLKSNNLLI 281
Cdd:COG1101 98 TIEENLalAYRRGKrrglrrgLTKKRRElfRELLATLGLGL--ENRLDTKVGLLSGGQ--RqalsLLMAT--LTKPKLLL 171
|
....*....
gi 2793968422 282 LDEPTNDLD 290
Cdd:COG1101 172 LDEHTAALD 180
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
149-318 |
5.16e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.26 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 149 GKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL----HCGTKL---EVAY--------FDQYREILD 213
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsgHDITRLknrEVPFlrrqigmiFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 214 peKSVIDNLADGKQEVTVGGRE-RHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLD-- 290
Cdd:PRK10908 94 --RTVYDNVAIPLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDda 171
|
170 180
....*....|....*....|....*....
gi 2793968422 291 IETLELLEDLLANYQG-TLLLVSHDRQFV 318
Cdd:PRK10908 172 LSEGILRLFEEFNRVGvTVLMATHDIGLI 200
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
139-291 |
5.46e-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: 49.83 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLL--DQLKPDSGRLhcgtklevaYFDQyREILD--P 214
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEI---------LFKG-EDITDlpP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 215 EKSVIDNLADGKQE------VTVGgrerhalsylqDFLfspkraRTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTND 288
Cdd:cd03217 72 EERARLGIFLAFQYppeipgVKNA-----------DFL------RYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
...
gi 2793968422 289 LDI 291
Cdd:cd03217 135 LDI 137
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
133-314 |
6.94e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.19 E-value: 6.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 133 SGKIVFEAENLNFGfegkeiVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGR-LHCGTKLEVAYFDQYREI 211
Cdd:PRK10070 30 SKEQILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQvLIDGVDIAKISDAELREV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 -------------LDPEKSVIDNLADGKQEVTVGGRERH--ALSYLQDFLFSPKRARTPvKALSGGEKNRLLLARIFLKS 276
Cdd:PRK10070 104 rrkkiamvfqsfaLMPHMTVLDNTAFGMELAGINAEERRekALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAIN 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2793968422 277 NNLLILDEPTNDLD----IETLELLEDLLANYQGTLLLVSHD 314
Cdd:PRK10070 183 PDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
151-291 |
8.02e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.17 E-value: 8.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 151 EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL----HCGTKLEVAYFDQ-YREIL-DPEKSV-----I 219
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddHPLHFGDYSYRSQrIRMIFqDPSTSLnprqrI 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2793968422 220 DNLADG----KQEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK15112 107 SQILDFplrlNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
112-290 |
9.23e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 9.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 112 ERINRREVqgkaVIQIDDGQRSGKIV-FEAENLNFGFEGK---EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQL 187
Cdd:PTZ00265 360 EIINRKPL----VENNDDGKKLKDIKkIQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 188 KPDSG------------------------------------------RLHCGTKLEvAYFDQYREILDPEKSVID----- 220
Cdd:PTZ00265 436 DPTEGdiiindshnlkdinlkwwrskigvvsqdpllfsnsiknnikySLYSLKDLE-ALSNYYNEDGNDSQENKNkrnsc 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 221 ------NLADGKQEVTVGGRERHALSY----------------LQDFLFS-PKRARTPVKA----LSGGEKNRLLLARIF 273
Cdd:PTZ00265 515 rakcagDLNDMSNTTDSNELIEMRKNYqtikdsevvdvskkvlIHDFVSAlPDKYETLVGSnaskLSGGQKQRISIARAI 594
|
250
....*....|....*..
gi 2793968422 274 LKSNNLLILDEPTNDLD 290
Cdd:PTZ00265 595 IRNPKILILDEATSSLD 611
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
157-291 |
9.29e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 157 SFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG-TKLEVAYFDQYREILDPE--KSVIDNLADGKQ------ 227
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfSHITRLSFEQLQKLVSDEwqRNNTDMLSPGEDdtgrtt 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2793968422 228 -EVTVGGRERHAL--SYLQDFLFSPKRARtPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK10938 103 aEIIQDEVKDPARceQLAQQFGITALLDR-RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
140-290 |
9.80e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.09 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 140 AENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKL--EVAYFDqYREILDPEK- 216
Cdd:PRK14271 24 AVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlgGRSIFN-YRDVLEFRRr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 -------------SVIDNLADG--------KQEVTVGGRERHALSYLQDFLfSPKRARTPVKaLSGGEKNRLLLARIFLK 275
Cdd:PRK14271 103 vgmlfqrpnpfpmSIMDNVLAGvrahklvpRKEFRGVAQARLTEVGLWDAV-KDRLSDSPFR-LSGGQQQLLCLARTLAV 180
|
170
....*....|....*
gi 2793968422 276 SNNLLILDEPTNDLD 290
Cdd:PRK14271 181 NPEVLLLDEPTSALD 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
146-289 |
1.05e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 146 GFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKlEVAY------FDQ-----YREI-LD 213
Cdd:PRK11288 13 TFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-EMRFasttaaLAAgvaiiYQELhLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 214 PEKSVIDNLADGkQEVTVGG--RERHALSYLQDFL------FSPkraRTPVKALSGGEKNRLLLARIFLKSNNLLILDEP 285
Cdd:PRK11288 92 PEMTVAENLYLG-QLPHKGGivNRRLLNYEAREQLehlgvdIDP---DTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
....
gi 2793968422 286 TNDL 289
Cdd:PRK11288 168 TSSL 171
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
149-323 |
1.44e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 149 GKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL--------HCGTKLEVAYFDQYREIlDPEKSVId 220
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQSEEV-DWSFPVL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 221 nladgKQEVTVGGRERHalsylQDFLFSPK-RARTPVKA-----------------LSGGEKNRLLLARIFLKSNNLLIL 282
Cdd:PRK15056 97 -----VEDVVMMGRYGH-----MGWLRRAKkRDRQIVTAalarvdmvefrhrqigeLSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2793968422 283 DEPTNDLDIETLELLEDLLANYQG---TLLLVSHD----RQFVDNTVM 323
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDegkTMLVSTHNlgsvTEFCDYTVM 214
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
141-290 |
1.47e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.60 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGF-EGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCgTKLEVAYFDQYREI-------- 211
Cdd:PRK13644 5 ENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV-SGIDTGDFSKLQGIrklvgivf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 LDPE-----KSVIDNLADGKQEVTVGGRERHAL--SYLQDFLFSPKRARTPvKALSGGEKNRLLLARIFLKSNNLLILDE 284
Cdd:PRK13644 84 QNPEtqfvgRTVEEDLAFGPENLCLPPIEIRKRvdRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDE 162
|
....*.
gi 2793968422 285 PTNDLD 290
Cdd:PRK13644 163 VTSMLD 168
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
153-290 |
1.69e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 49.73 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCG----TKLEVAYFDQYR-EI----------LDPEKS 217
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqdiTGLSGRELRPLRrRMqmvfqdpyasLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 218 VIDNLADG--------KQEV---------TVGGRERHAlsylqdflfspkrARTPvKALSGGEKNRLLLARIFLKSNNLL 280
Cdd:COG4608 114 VGDIIAEPlrihglasKAERrervaelleLVGLRPEHA-------------DRYP-HEFSGGQRQRIGIARALALNPKLI 179
|
170
....*....|
gi 2793968422 281 ILDEPTNDLD 290
Cdd:COG4608 180 VCDEPVSALD 189
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
155-314 |
1.71e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.44 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 155 DFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL---------HCGTK------LEVAYFDQYREILDPEKSVI 219
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhitpETGNKnlkklrKKVSLVFQFPEAQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 220 DNLADGKQEVTVGGRE--RHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELL 297
Cdd:PRK13641 105 KDVEFGPKNFGFSEDEakEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180
....*....|....*....|
gi 2793968422 298 EDLLANYQG---TLLLVSHD 314
Cdd:PRK13641 185 MQLFKDYQKaghTVILVTHN 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
147-291 |
1.75e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 147 FEGKEIVK---DFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAYFDQYREI----------- 211
Cdd:PRK11308 22 FKPERLVKaldGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKADPEAQKLLrqkiqivfqnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 ---LDPEKSVIDNLAD--------GKQE---------VTVGGRERHALSYLQDFlfspkrartpvkalSGGEKNRLLLAR 271
Cdd:PRK11308 102 ygsLNPRKKVGQILEEpllintslSAAErrekalammAKVGLRPEHYDRYPHMF--------------SGGQRQRIAIAR 167
|
170 180
....*....|....*....|
gi 2793968422 272 IFLKSNNLLILDEPTNDLDI 291
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDV 187
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
139-194 |
1.98e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.99 E-value: 1.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL 194
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
135-291 |
2.19e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 135 KIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL-------------------LDQLKPDSgRLH 195
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaykilegdilfkgesILDLEPEE-RAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 196 CGTKLevAYfdQYR-EIldPEKSVID--NLADGKQEVTVGGRERHALSYLQdfLFSPKR----------ARTPVKALSGG 262
Cdd:CHL00131 84 LGIFL--AF--QYPiEI--PGVSNADflRLAYNSKRKFQGLPELDPLEFLE--IINEKLklvgmdpsflSRNVNEGFSGG 155
|
170 180 190
....*....|....*....|....*....|
gi 2793968422 263 EKNR-LLLARIFLKSnNLLILDEPTNDLDI 291
Cdd:CHL00131 156 EKKRnEILQMALLDS-ELAILDETDSGLDI 184
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
148-289 |
2.99e-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: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 148 EGKEIVKDF---------SFNIMRGDRIALIGPNGCGKSTVLKLLldqlkpdSGRLHCGTKLEVAYFD----QYREILD- 213
Cdd:TIGR02633 3 EMKGIVKTFggvkaldgiDLEVRPGECVGLCGENGAGKSTLMKIL-------SGVYPHGTWDGEIYWSgsplKASNIRDt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 214 ---------------PEKSVIDNLADGKQEVTVGGRERHALSY------LQDFLFSPKRARTPVKALSGGEKNRLLLARI 272
Cdd:TIGR02633 76 eragiviihqeltlvPELSVAENIFLGNEITLPGGRMAYNAMYlraknlLRELQLDADNVTRPVGDYGGGQQQLVEIAKA 155
|
170
....*....|....*..
gi 2793968422 273 FLKSNNLLILDEPTNDL 289
Cdd:TIGR02633 156 LNKQARLLILDEPSSSL 172
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
135-290 |
3.67e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.47 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 135 KIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDS----------------GRLHCGT 198
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellgrtvqreGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 199 KLEVAY----FDQYReiLDPEKSVIDNLADGKQEVTVGGR----------ERHALSYLQDF---LFSPKRartpVKALSG 261
Cdd:PRK09984 82 RKSRANtgyiFQQFN--LVNRLSVLENVLIGALGSTPFWRtcfswftreqKQRALQALTRVgmvHFAHQR----VSTLSG 155
|
170 180
....*....|....*....|....*....
gi 2793968422 262 GEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
147-289 |
4.55e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 147 FEGKEIVKDF---------SFNIMRGDRIALIGPNGCGKSTVLKLLldqlkpdSGRLHCGTKLEVAYFD----QYREILD 213
Cdd:PRK13549 6 LEMKNITKTFggvkaldnvSLKVRAGEIVSLCGENGAGKSTLMKVL-------SGVYPHGTYEGEIIFEgeelQASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 214 ----------------PEKSVIDNLADGkQEVTVGGRERHALSYLqdflfspkRAR-------------TPVKALSGGEK 264
Cdd:PRK13549 79 teragiaiihqelalvKELSVLENIFLG-NEITPGGIMDYDAMYL--------RAQkllaqlkldinpaTPVGNLGLGQQ 149
|
170 180
....*....|....*....|....*
gi 2793968422 265 NRLLLARIFLKSNNLLILDEPTNDL 289
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASL 174
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
137-290 |
5.55e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.53 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEG----KEIVKDFSFNIMRGDRIALIGPNGCGKS----TVLKLLLDQLKPDSGRLH-CGTKLEVAYFDQ 207
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 208 YREI---------------LDPEKSVidnladGKQ--EV-----TVGGRE--RHALSYLQdfLFSPKRARTPVKA----L 259
Cdd:COG4172 86 LRRIrgnriamifqepmtsLNPLHTI------GKQiaEVlrlhrGLSGAAarARALELLE--RVGIPDPERRLDAyphqL 157
|
170 180 190
....*....|....*....|....*....|.
gi 2793968422 260 SGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
137-316 |
6.66e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.46 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDQLKPDsgrlhCGTKLEVAY---------- 204
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPE-----VTITGSIVYnghniysprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 205 --FDQYREI----LDPEK---SVIDNLADGKQevTVGGRERHAL------SYLQDFLFSPKRARTPVKA--LSGGEKNRL 267
Cdd:PRK14239 80 dtVDLRKEIgmvfQQPNPfpmSIYENVVYGLR--LKGIKDKQVLdeavekSLKGASIWDEVKDRLHDSAlgLSGGQQQRV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 268 LLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANY--QGTLLLVSHDRQ 316
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLkdDYTMLLVTRSMQ 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
134-286 |
7.36e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEAENLN--FGfegkeivkDF------SFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSG--RLhCG------ 197
Cdd:NF033858 263 DEPAIEARGLTmrFG--------DFtavdhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeaWL-FGqpvdag 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 198 ---TKLEVAYFDQ----YREIldpekSVIDNLadgkqevtvggrERHALsylqdfLFSPKRARTPVK------------- 257
Cdd:NF033858 334 diaTRRRVGYMSQafslYGEL-----TVRQNL------------ELHAR------LFHLPAAEIAARvaemlerfdladv 390
|
170 180 190
....*....|....*....|....*....|....*
gi 2793968422 258 ------ALSGGEKNRLLLARIFLKSNNLLILDEPT 286
Cdd:NF033858 391 adalpdSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
167-319 |
8.93e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 167 ALIGPNGCGKSTVLKLLLDQLKPD-----SGRLH----CGTKLEVAYFDQYREildpeksvidNLADGKQEVTvggRERH 237
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGElppnsKGGAHdpklIREGEVRAQVKLAFE----------NANGKKYTIT---RSLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 238 ALSYL----QDFLFSPkrARTPVKALSGGEKN------RLLLARIFLKSNNLLILDEPTNDLD-------IETLELLEDL 300
Cdd:cd03240 93 ILENVifchQGESNWP--LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieesLAEIIEERKS 170
|
170
....*....|....*....
gi 2793968422 301 LANYQgtLLLVSHDRQFVD 319
Cdd:cd03240 171 QKNFQ--LIVITHDEELVD 187
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
147-290 |
1.04e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.94 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 147 FEGKEIvKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKL---------------EVAYFDQYREI 211
Cdd:PRK13634 18 FERRAL-YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 LDPEKSVIDNLADGKQE--VTVGGRERHALSYLQDFLFSPK-RARTPVkALSGGEKNRLLLARIFLKSNNLLILDEPTND 288
Cdd:PRK13634 97 QLFEETVEKDICFGPMNfgVSEEDAKQKAREMIELVGLPEElLARSPF-ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
..
gi 2793968422 289 LD 290
Cdd:PRK13634 176 LD 177
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
139-318 |
1.05e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.91 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLE------------VAYF 205
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrGQHIEglpghqiarmgvVRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 206 DQYReiLDPEKSVIDNL--ADGKQEVT--VGG---------RERHALSYLQDFL-------FSPKRARTpvkaLSGGEKN 265
Cdd:PRK11300 87 QHVR--LFREMTVIENLlvAQHQQLKTglFSGllktpafrrAESEALDRAATWLervglleHANRQAGN----LAYGQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 266 RLLLARIFLKSNNLLILDEP--------TNDLDietlELLEDLLANYQGTLLLVSHDRQFV 318
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPaaglnpkeTKELD----ELIAELRNEHNVTVLLIEHDMKLV 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
109-290 |
1.20e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 109 LREERINRREVQGKAVIQIDDGQrsGKIvfEAENLNFGFEGKE---IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLD 185
Cdd:PTZ00265 1141 IRKSNIDVRDNGGIRIKNKNDIK--GKI--EIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMR 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 186 --QLKPD-----------------------------------SGRLHCGTKLEVAYFDQYREIL---------------- 212
Cdd:PTZ00265 1217 fyDLKNDhhivfknehtndmtneqdyqgdeeqnvgmknvnefSLTKEGGSGEDSTVFKNSGKILldgvdicdynlkdlrn 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 -------DP---EKSVIDNLADGKQEVTVGGRERHA-LSYLQDFLFS-PKRARTPV----KALSGGEKNRLLLARIFLKS 276
Cdd:PTZ00265 1297 lfsivsqEPmlfNMSIYENIKFGKEDATREDVKRACkFAAIDEFIESlPNKYDTNVgpygKSLSGGQKQRIAIARALLRE 1376
|
250
....*....|....
gi 2793968422 277 NNLLILDEPTNDLD 290
Cdd:PTZ00265 1377 PKILLLDEATSSLD 1390
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
150-286 |
1.83e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDF---------SFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGrlhcgtklEVAYFDQYREILDPEK---- 216
Cdd:COG3845 9 RGITKRFggvvanddvSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG--------EILIDGKPVRIRSPRDaial 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 ---------------SVIDNLadgkqevtVGGRERHALsylqdFLFSPKRAR-----------------TPVKALSGGEK 264
Cdd:COG3845 81 gigmvhqhfmlvpnlTVAENI--------VLGLEPTKG-----GRLDRKAARarirelserygldvdpdAKVEDLSVGEQ 147
|
170 180
....*....|....*....|..
gi 2793968422 265 NRLLLARIFLKSNNLLILDEPT 286
Cdd:COG3845 148 QRVEILKALYRGARILILDEPT 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
133-290 |
1.86e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 46.99 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 133 SGKIVFEAENLNFGFEGK-----------EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLdQLKPDSGRLH-CGTKL 200
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALL-RLIPSEGEIRfDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 201 EVAYFDQYREI--------------LDPEKSVIDNLADG----KQEVTVGGRERHALSYLQDFLFSPK-RARTPvKALSG 261
Cdd:COG4172 350 DGLSRRALRPLrrrmqvvfqdpfgsLSPRMTVGQIIAEGlrvhGPGLSAAERRARVAEALEEVGLDPAaRHRYP-HEFSG 428
|
170 180 190
....*....|....*....|....*....|
gi 2793968422 262 GEKNRLLLAR-IFLKSNnLLILDEPTNDLD 290
Cdd:COG4172 429 GQRQRIAIARaLILEPK-LLVLDEPTSALD 457
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
150-290 |
2.71e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.58 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL----LDQLKPDSGRLHCGTKLEV-------AYFDQYrEILDPEKSV 218
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGSGSVLLNGMPIDAkemraisAYVQQD-DLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 IDNL---AD---GKQEVTVGGRER-----HALSYL--QDFLF-SPKRartpVKALSGGEKNRLLLARIFLKSNNLLILDE 284
Cdd:TIGR00955 117 REHLmfqAHlrmPRRVTKKEKRERvdevlQALGLRkcANTRIgVPGR----VKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
....*.
gi 2793968422 285 PTNDLD 290
Cdd:TIGR00955 193 PTSGLD 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
81-290 |
3.79e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.55 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 81 LAQEEVWIrqGIKARRTRNEgrvRALKK---LREERINRREVQGkaviqIDDGqrsgkiVFEAE-----------NLNFG 146
Cdd:TIGR01257 874 LLQESYWL--GGEGCSTREE---RALEKtepLTEEMEDPEHPEG-----INDS------FFERElpglvpgvcvkNLVKI 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 147 FE--GKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREILD--PEKSVIdnl 222
Cdd:TIGR01257 938 FEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGmcPQHNIL--- 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 223 adgKQEVTVGgreRHALSYLQDFLFSPKRARTPVKA-----------------LSGGEKNRLLLARIFLKSNNLLILDEP 285
Cdd:TIGR01257 1015 ---FHHLTVA---EHILFYAQLKGRSWEEAQLEMEAmledtglhhkrneeaqdLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
....*
gi 2793968422 286 TNDLD 290
Cdd:TIGR01257 1089 TSGVD 1093
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
162-316 |
3.92e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.77 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 162 RGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLH-CGTKLEVAYFDQYREI-------------LDPEKSVIDN-----L 222
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlVGQPLHQMDEEARAKLrakhvgfvfqsfmLIPTLNALENvelpaL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 223 ADGKQEvtvgGRERHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLE---- 298
Cdd:PRK10584 115 LRGESS----RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAdllf 190
|
170
....*....|....*...
gi 2793968422 299 DLLANYQGTLLLVSHDRQ 316
Cdd:PRK10584 191 SLNREHGTTLILVTHDLQ 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
137-290 |
4.03e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.08 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGFEGKEIVKDF---SFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAYFDQYREIL 212
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 213 -----DPEK-----SVIDNLADGKQEVTVGGRErhALSYLQDFLFSPK----RARTPVKaLSGGEKNRLLLARIFLKSNN 278
Cdd:PRK13642 84 gmvfqNPDNqfvgaTVEDDVAFGMENQGIPREE--MIKRVDEALLAVNmldfKTREPAR-LSGGQKQRVAVAGIIALRPE 160
|
170
....*....|..
gi 2793968422 279 LLILDEPTNDLD 290
Cdd:PRK13642 161 IIILDESTSMLD 172
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
149-290 |
4.18e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.60 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 149 GKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDQLKpdSGRLHCG----TKLEVA------YFDQYreILDPEK 216
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagLERIT--SGEIWIGgrvvNELEPAdrdiamVFQNY--ALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 SVIDNLADG-------KQEVtvggRER--HA---LSyLQDFLfspkrARTPvKALSGGEKNRLLLARIFLKSNNLLILDE 284
Cdd:PRK11650 92 SVRENMAYGlkirgmpKAEI----EERvaEAariLE-LEPLL-----DRKP-RELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
....*.
gi 2793968422 285 PTNDLD 290
Cdd:PRK11650 161 PLSNLD 166
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
133-290 |
5.65e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.84 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 133 SGKIVFEAENLNFGFEGKE-----IVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQ 207
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 208 YREILDPEKSVIDNLADGKQEVT-VGGRERHAL---SYLQDFLFSP-----------KRA---------------RTPVK 257
Cdd:PRK13631 97 HELITNPYSKKIKNFKELRRRVSmVFQFPEYQLfkdTIEKDIMFGPvalgvkkseakKLAkfylnkmglddsyleRSPFG 176
|
170 180 190
....*....|....*....|....*....|...
gi 2793968422 258 aLSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK13631 177 -LSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
132-290 |
6.22e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 132 RSGKIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHcgTKLEVAYFDQYREI 211
Cdd:PTZ00243 655 RSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--AERSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 212 LDpeKSVIDNLADGKQEVTVGGRERHALSYLQ-DFLFSPKRARTPVKA----LSGGEKNRLLLARIFLKSNNLLILDEPT 286
Cdd:PTZ00243 733 MN--ATVRGNILFFDEEDAARLADAVRVSQLEaDLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
....
gi 2793968422 287 NDLD 290
Cdd:PTZ00243 811 SALD 814
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
150-323 |
6.24e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.31 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPD----SGRLHC-GTKLE--------VAYFDQY-REILDPE 215
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLdGKPVApcalrgrkIATIMQNpRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 216 KSVIDNLADGKQEVTVGGRERHALSYLQDF-LFSPKRA--RTPVKaLSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIE 292
Cdd:PRK10418 96 HTMHTHARETCLALGKPADDATLTAALEAVgLENAARVlkLYPFE-MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2793968422 293 TLELLEDLLANYQGT----LLLVSHDRQFV-----DNTVM 323
Cdd:PRK10418 175 AQARILDLLESIVQKralgMLLVTHDMGVVarladDVAVM 214
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
140-291 |
6.54e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 140 AENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLkPDSGRLHcGTKL--EVAYFDQYREILDPE-- 215
Cdd:PRK13547 4 ADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL-TGGGAPR-GARVtgDVTLNGEPLAAIDAPrl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 216 ---KSVIDNLAD-----GKQEVTVGGRERHA-----LSYLQDFLFSPKRART--------PVKALSGGEKNRLLLARIFL 274
Cdd:PRK13547 82 arlRAVLPQAAQpafafSAREIVLLGRYPHArragaLTHRDGEIAWQALALAgatalvgrDVTTLSGGELARVQFARVLA 161
|
170 180
....*....|....*....|....*.
gi 2793968422 275 K---------SNNLLILDEPTNDLDI 291
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDL 187
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
141-291 |
6.66e-05 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 44.17 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL-------------------LDQLKPDSgRLHCGtkLE 201
Cdd:TIGR01978 4 KDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpsyevtsgtilfkgqdLLELEPDE-RARAG--LF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 202 VAYfdQY-REIldPEKSVIDNLADGKQEVTvGGRERHALSyLQDF--LFSPKRA----------RTPVKALSGGEKNRLL 268
Cdd:TIGR01978 81 LAF--QYpEEI--PGVSNLEFLRSALNARR-SARGEEPLD-LLDFekLLKEKLAlldmdeeflnRSVNEGFSGGEKKRNE 154
|
170 180
....*....|....*....|...
gi 2793968422 269 LARIFLKSNNLLILDEPTNDLDI 291
Cdd:TIGR01978 155 ILQMALLEPKLAILDEIDSGLDI 177
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
149-290 |
6.76e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.67 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 149 GKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLL-----------DQLKPDSGRLHCGTKL------EVAYFD-QYRE 210
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLrllstegeiqiDGVSWNSVTLQTWRKAfgvipqKVFIFSgTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 211 ILDPEKSVIDnladgkQEVTVGGRERHALSYLQDFlfsPKRARTPVK----ALSGGEKNRLLLARIFLKSNNLLILDEPT 286
Cdd:TIGR01271 1311 NLDPYEQWSD------EEIWKVAEEVGLKSVIEQF---PDKLDFVLVdggyVLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
....
gi 2793968422 287 NDLD 290
Cdd:TIGR01271 1382 AHLD 1385
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
153-319 |
9.61e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTK----------------LEVAYFDQYREiLDPEK 216
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgklqalrrdIQFIFQDPYAS-LDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 SV---------IDNLADGKQEVT--------VGGRERHALSYLQDFlfspkrartpvkalSGGEKNRLLLARIFLKSNNL 279
Cdd:PRK10261 419 TVgdsimeplrVHGLLPGKAAAArvawllerVGLLPEHAWRYPHEF--------------SGGQRQRICIARALALNPKV 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2793968422 280 LILDEPTNDLDIETLELLEDLLANYQGTL----LLVSHDRQFVD 319
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISHDMAVVE 528
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
141-323 |
1.51e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGF----EGKEIVKDFSFNIMRGDRIALIGPNGCGKS----TVLKLL----------------LDQLKPDSGRLHC 196
Cdd:PRK15134 9 ENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypsgdirfhgESLLHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 197 --GTKLEVAyFDQYREILDP----EKSVIDNLA-------DGKQEVTVGGRER----HALSYLQDFlfsPKRartpvkaL 259
Cdd:PRK15134 89 vrGNKIAMI-FQEPMVSLNPlhtlEKQLYEVLSlhrgmrrEAARGEILNCLDRvgirQAAKRLTDY---PHQ-------L 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2793968422 260 SGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANYQG----TLLLVSHD----RQFVDN-TVM 323
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNlsivRKLADRvAVM 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
168-290 |
1.51e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.46 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 168 LIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREILD-----------PEKSVID------------NLAD 224
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRlrkeiglvfqfPEYQLFQetiekdiafgpvNLGE 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2793968422 225 GKQEVTvggrerHALSYLQDFLFSPKR--ARTPVKaLSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK13645 122 NKQEAY------KKVPELLKLVQLPEDyvKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
160-330 |
1.55e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 160 IMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHcgtklevayFDQYREILDPEKsvIDnladgkqevtvggrerhal 239
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE---------WDGITPVYKPQY--ID------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 240 sylqdflfspkrartpvkaLSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLEDLLANY----QGTLLLVSHDR 315
Cdd:cd03222 72 -------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDL 132
|
170
....*....|....*
gi 2793968422 316 QFVDNTVMTSWIFEG 330
Cdd:cd03222 133 AVLDYLSDRIHVFEG 147
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
139-289 |
2.74e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC------------GTKLEVAYFD 206
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITInninynkldhklAAQLGIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 QYREILDpEKSVIDNLADGKQEV-TVGG---------RERHALSYLQDFLfspKRA-RTPVKALSGGEKNRLLLARIFLK 275
Cdd:PRK09700 87 QELSVID-ELTVLENLYIGRHLTkKVCGvniidwremRVRAAMMLLRVGL---KVDlDEKVANLSISHKQMLEIAKTLML 162
|
170
....*....|....
gi 2793968422 276 SNNLLILDEPTNDL 289
Cdd:PRK09700 163 DAKVIIMDEPTSSL 176
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
139-314 |
2.85e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.77 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 139 EAENLNFGFEGK-----EIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL-----HCGTKLEVAYFDQY 208
Cdd:PRK13651 4 KVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkDEKNKKKTKEKEKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 RE---ILDPEKSVIDNLADGKQEVTV----GGRERHALSYLQDFLFSP-----------KRARTPVK------------- 257
Cdd:PRK13651 84 LEklvIQKTRFKKIKKIKEIRRRVGVvfqfAEYQLFEQTIEKDIIFGPvsmgvskeeakKRAAKYIElvgldesylqrsp 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 258 -ALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDIETLELLED--LLANYQG-TLLLVSHD 314
Cdd:PRK13651 164 fELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEifDNLNKQGkTIILVTHD 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
133-194 |
2.90e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.12 E-value: 2.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2793968422 133 SGKIVFEAENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL 194
Cdd:PRK15439 7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL 68
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
134-290 |
3.68e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 42.38 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEAENLNFGF----EGKEI--VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC---GTKLEVAY 204
Cdd:PRK13633 1 MNEMIKCKNVSYKYesneESTEKlaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdglDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 205 FDQYRE----ILDPEKSVI------------DNLADGKQEVtvggRER--HALSYLQDFLFSpkraRTPVKALSGGEKNR 266
Cdd:PRK13633 81 WDIRNKagmvFQNPDNQIVativeedvafgpENLGIPPEEI----RERvdESLKKVGMYEYR----RHAPHLLSGGQKQR 152
|
170 180
....*....|....*....|....
gi 2793968422 267 LLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLD 176
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-49 |
6.07e-04 |
|
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: 41.38 E-value: 6.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGS---IIFISHDRAFIKSMATRIVDLDRGKL 49
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEgktVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
153-290 |
8.63e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAYFDQYR--------------EILDPEKS 217
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEQPEDYRklfsavftdfhlfdQLLGPEGK 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2793968422 218 VIDNLADGKQEVTVGgrERHALSyLQDFLFSPKRartpvkaLSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:PRK10522 419 PANPALVEKWLERLK--MAHKLE-LEDGRISNLK-------LSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
155-210 |
9.65e-04 |
|
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: 41.71 E-value: 9.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2793968422 155 DFSFNimRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHC-GTKLEVAYFDQYRE 210
Cdd:COG4615 352 DLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLdGQPVTADNREAYRQ 406
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
146-290 |
1.01e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 41.63 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 146 GFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLL--LDqlKPDSG---------------------RLHCGTklev 202
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcLD--KPTSGtyrvagqdvatldadalaqlrREHFGF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 203 aYFDQYReiLDPEKSVIDNLadgkqEVTV--GGRERH-----ALSYLQDfLFSPKRARTPVKALSGGEKNRLLLARIFLK 275
Cdd:PRK10535 91 -IFQRYH--LLSHLTAAQNV-----EVPAvyAGLERKqrllrAQELLQR-LGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170
....*....|....*
gi 2793968422 276 SNNLLILDEPTNDLD 290
Cdd:PRK10535 162 GGQVILADEPTGALD 176
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
147-290 |
1.05e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.40 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 147 FEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDS--------GRLHCGTKLEVAYFDQYREILDPEKSV 218
Cdd:PLN03211 78 IQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftgtilanNRKPTKQILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 IDNL----------ADGKQEVTvggreRHALSYLQDFLFSPKR----ARTPVKALSGGEKNRLLLARIFLKSNNLLILDE 284
Cdd:PLN03211 158 RETLvfcsllrlpkSLTKQEKI-----LVAESVISELGLTKCEntiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
....*.
gi 2793968422 285 PTNDLD 290
Cdd:PLN03211 233 PTSGLD 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
252-291 |
1.06e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.19 E-value: 1.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2793968422 252 ARTPVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK15439 397 AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
153-291 |
1.11e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL------------HCGTKLEVAYF--DQYREILDPEKSV 218
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtldghevvtrspQDGLANGIVYIseDRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 219 IDN--LADGKQEVTVGGRERHALSYL--QDF--LFSPKrarTP-----VKALSGGEKNRLLLARIFLKSNNLLILDEPTN 287
Cdd:PRK10762 348 KENmsLTALRYFSRAGGSLKHADEQQavSDFirLFNIK---TPsmeqaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
....
gi 2793968422 288 DLDI 291
Cdd:PRK10762 425 GVDV 428
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
144-285 |
1.22e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 40.72 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 144 NFGfegkeIVKDFSFNImrGDRIALIGPNGCGKSTVLKLLL---------------------DQLKPDSGRLHCGTKLEV 202
Cdd:COG4938 8 NFG-----PFKEAELEL--KPLTLLIGPNGSGKSTLIQALLlllqsnfiylpaersgparlyPSLVRELSDLGSRGEYTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 203 AYFDQYREIL---DPEKSVIDNLADGKQEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGGEKNR-----LLLARIFL 274
Cdd:COG4938 81 DFLAELENLEildDKSKELLEQVEEWLEKIFPGKVEVDASSDLVRLVFRPSGNGKRIPLSNVGSGVSellpiLLALLSAA 160
|
170
....*....|.
gi 2793968422 275 KSNNLLILDEP 285
Cdd:COG4938 161 KPGSLLIIEEP 171
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
134-291 |
1.35e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.07 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 134 GKIVFEAENL------NfgfEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTVL-------------KLLLDQLKPDSGRL 194
Cdd:PRK13549 256 GEVILEVRNLtawdpvN---PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVqclfgaypgrwegEIFIDGKPVKIRNP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 195 HCGTKLEVAYF--DQYREILDPEKSVIDN--LADGKQeVTVGGRERHALSyLQDFLFSPKRART-------PVKALSGGE 263
Cdd:PRK13549 333 QQAIAQGIAMVpeDRKRDGIVPVMGVGKNitLAALDR-FTGGSRIDDAAE-LKTILESIQRLKVktaspelAIARLSGGN 410
|
170 180
....*....|....*....|....*...
gi 2793968422 264 KNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
137-291 |
1.66e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 137 VFEAENLNFGF--EGKEI--VKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKL------EVAYFD 206
Cdd:PRK10261 12 VLAVENLNIAFmqEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLlrrrsrQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 207 -----QYREI---------------LDPEKSVIDNLADGKQEVTVGGRERHALS--YLQDFLFSPKR----ARTPvKALS 260
Cdd:PRK10261 92 eqsaaQMRHVrgadmamifqepmtsLNPVFTVGEQIAESIRLHQGASREEAMVEakRMLDQVRIPEAqtilSRYP-HQLS 170
|
170 180 190
....*....|....*....|....*....|.
gi 2793968422 261 GGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDV 201
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
150-323 |
1.83e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 40.15 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLLDQLKPDSGRL-------HCGTK--------LEVAYFDQY------ 208
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvdditiTHKTKdkyirpvrKRIGMVFQFpesqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 209 -----REILDPEKSVIDNLADGKQevtvggrerHALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLLILD 283
Cdd:PRK13646 100 edtveREIIFGPKNFKMNLDEVKN---------YAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2793968422 284 EPTNDLDIETLELLEDLLANYQ----GTLLLVSHDR----QFVDNTVM 323
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMnevaRYADEVIV 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-48 |
1.89e-03 |
|
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: 38.77 E-value: 1.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRG---SIIFISHDRAFIKSMATRIVDLDRGK 48
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
153-290 |
2.10e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.84 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 153 VKDFSFNIMRGDRIALIGPNGCGKSTvlkLLLDQLKpDSGRLHCGTKLEvAYFDQYREILDPEKSVIDNladgkqevtvg 232
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKST---LVNEGLY-ASGKARLISFLP-KFSRNKLIFIDQLQFLIDV----------- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 233 grerhALSYLqdflfSPKRartPVKALSGGEKNRLLLARiFLKS---NNLLILDEPTNDLD 290
Cdd:cd03238 75 -----GLGYL-----TLGQ---KLSTLSGGELQRVKLAS-ELFSeppGTLFILDEPSTGLH 121
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
163-290 |
2.60e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 40.38 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 163 GDRIALIGPNGCGKSTVLKLLLDQLKPDSGRLHCGTKLEVAYFDQYREILD--PEKSVIDNLADGKQEVTVGGRERH--- 237
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGycPQFDAIDDLLTGREHLYLYARLRGvpa 2044
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2793968422 238 ---------ALSYLQDFLFSPKRARTpvkaLSGGEKNRLLLARIFLKSNNLLILDEPTNDLD 290
Cdd:TIGR01257 2045 eeiekvanwSIQSLGLSLYADRLAGT----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-59 |
2.67e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 2.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKLSSFPGDYENY 59
Cdd:PLN03073 654 PSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-64 |
3.33e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 38.91 E-value: 3.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2793968422 14 EGFLKDFR---GSIIFISHDRAFIKSMATRIVDLDRGKLSSFpGD-------YENYLLEKE 64
Cdd:COG1134 186 LARIRELResgRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD-GDpeeviaaYEALLAGRE 245
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
138-222 |
3.38e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.21 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 138 FEAENLnFGFEGKEIvkDFSFNimrgDRI-ALIGPNGCGKSTVLKLL----------LDQLKPDSGRLHCGTKLE----V 202
Cdd:COG3950 6 LTIENF-RGFEDLEI--DFDNP----PRLtVLVGENGSGKTTLLEAIalalsgllsrLDDVKFRKLLIRNGEFGDsaklI 78
|
90 100
....*....|....*....|
gi 2793968422 203 AYFDQYREILDPEKSVIDNL 222
Cdd:COG3950 79 LYYGTSRLLLDGPLKKLERL 98
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
255-291 |
3.77e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 39.42 E-value: 3.77e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2793968422 255 PVKALSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
150-290 |
3.93e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 150 KEIVKDFSFNIMRGDRIALIGPNGCGKSTVLKLLldqlkpdSGRLHCGTKLEVAYFDQYR----EILDPEK--------- 216
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-------TGDHPQGYSNDLTLFGRRRgsgeTIWDIKKhigyvsssl 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 217 --------SVIDNLADG-------KQEVTvgGRERH-ALSYLQDFLFSPKRARTPVKALSGGEKNRLLLARIFLKSNNLL 280
Cdd:PRK10938 346 hldyrvstSVRNVILSGffdsigiYQAVS--DRQQKlAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLL 423
|
170
....*....|
gi 2793968422 281 ILDEPTNDLD 290
Cdd:PRK10938 424 ILDEPLQGLD 433
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-49 |
4.61e-03 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 37.79 E-value: 4.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2793968422 1 PTNHLDVATIEWLEGFLKDFRG---SIIFISHDRAFIKSMATRIVDLDRGKL 49
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
141-179 |
5.17e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.62 E-value: 5.17e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2793968422 141 ENLNFGFEGKEIVKDFSFNIMRGDRIALIGPNGCGKSTV 179
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTL 43
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
144-288 |
5.35e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 144 NFG-FEGKEIVkDFSFNImrgdrIALIGPNGCGKSTVL---------------KLLLDQLKPDSGRL-------HCGTKL 200
Cdd:COG0419 9 NFRsYRDTETI-DFDDGL-----NLIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVGSEEAsvelefeHGGKRY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 201 EVAYFD------------QYREIL------DPEKSVIDNLADGKQEVTVGGRERHALSYLQDFLFSPKRARTPVKALSGG 262
Cdd:COG0419 83 RIERRQgefaefleakpsERKEALkrllglEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDPIETLSGG 162
|
170 180
....*....|....*....|....*.
gi 2793968422 263 EKNRLLLARIFlksnnLLILDEPTND 288
Cdd:COG0419 163 ERLRLALADLL-----SLILDFGSLD 183
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
141-313 |
5.96e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.93 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 141 ENLNFGFEGKEIvkdFSFNIMRGDR-IALI-GPNGCGKSTVLKLLLDQLKPDSG-------------RLHC-------GT 198
Cdd:PRK13541 5 HQLQFNIEQKNL---FDLSITFLPSaITYIkGANGCGKSSLLRMIAGIMQPSSGniyykncninniaKPYCtyighnlGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793968422 199 KLEVAYFDQ---YREILDPEKSVidnladgkqevtvggreRHALSY--LQDFLfSPKrartpVKALSGGEKNRLLLARIF 273
Cdd:PRK13541 82 KLEMTVFENlkfWSEIYNSAETL-----------------YAAIHYfkLHDLL-DEK-----CYSLSSGMQKIVAIARLI 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2793968422 274 LKSNNLLILDEPTNDLDIETLELLE---DLLANYQGTLLLVSH 313
Cdd:PRK13541 139 ACQSDLWLLDEVETNLSKENRDLLNnliVMKANSGGIVLLSSH 181
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
259-291 |
5.98e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 38.70 E-value: 5.98e-03
10 20 30
....*....|....*....|....*....|...
gi 2793968422 259 LSGGEKNRLLLARIFLKSNNLLILDEPTNDLDI 291
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-49 |
7.32e-03 |
|
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: 37.87 E-value: 7.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2793968422 1 PTNHLDVAT----IEWLEGFLKDFRGSIIFISHDRAFIKSMATRIVDLDRGKL 49
Cdd:cd03257 172 PTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
386-455 |
8.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 8.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2793968422 386 KLQRELEALPLRLEELETQIETLQEEVNDPSFFSKSVEQTQPVLDKLS-----AAEQELEVAFERWEELEALQQE 455
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlslATEEELQDLAEELEELQQRLAE 210
|
|
| |
