|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-593 |
6.67e-104 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 325.97 E-value: 6.67e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 1 MKKySLWNNLRWYIKYLRKDKPSLAWTASGLAIdkaaAALLGVFTPALL---VGAITGHATLGQFAWLATLTGLGLALTS 77
Cdd:COG1132 1 MSK-SPRKLLRRLLRYLRPYRGLLILALLLLLL----SALLELLLPLLLgriIDALLAGGDLSALLLLLLLLLGLALLRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 78 EVNYLLLTHDSIESSVLRTAIELDFHQKQWDLD---YDQISSGKLqglahtafIKGLSNTYAGAEAIYLYGRGTLVDLTT 154
Cdd:COG1132 76 LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPlsfFDRRRTGDL--------LSRLTNDVDAVEQFLAHGLPQLVRSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 155 LIVFLATLSFAVPWVFALVLVSAAISYAGMSWYRHWYLQNNVKwnklgRQQDYITR-NAYALEN--G-KDIRMFGMANW- 229
Cdd:COG1132 148 TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFR-----RVQEALAElNGRLQESlsGiRVVKAFGREERe 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 230 ---YHRHLDRLIQLQDAWQRRNSLRRFLGEQIGQLAGllrdAIVYGTLIVAIMRGSLSISQFTLMFGMTNSFITLLDQLL 306
Cdd:COG1132 223 lerFREANEELRRANLRAARLSALFFPLMELLGNLGL----ALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 307 DDFGKLQNASIDLQEVREFMNLQPQTPTRTltetEQKQLANRPVTITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVG 386
Cdd:COG1132 299 NVLNQLQRALASAERIFELLDEPPEIPDPP----GAVPLPPVRGEIEFENVSFSYPGDRPV-LKDISLTIPPGETVALVG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 387 INGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAM-TEHPDLNRVTTALTEA 465
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYgRPDATDEEVEEAAKAA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 466 GLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSL 545
Cdd:COG1132 454 QAHEFIEALPDGYDTVVG----ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTI 529
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 498176791 546 FISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQIQSK 593
Cdd:COG1132 530 VIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFG 577
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-591 |
4.05e-89 |
|
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: 290.97 E-value: 4.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 9 NLRWYIKYLRKDKPSLaWTASGLAIdkaAAALLGVFTPaLLVGAITGHATLGQ-FAWLATLT-GLGLALTSEVnylLLTh 86
Cdd:COG2274 143 GLRWFLRLLRRYRRLL-LQVLLASL---LINLLALATP-LFTQVVIDRVLPNQdLSTLWVLAiGLLLALLFEG---LLR- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 87 dsiessVLRTAIeLDFHQKQWDLdydQISSG---KLQGL-------AHTAFI-----------KGLSNTYAGaeaiylyg 145
Cdd:COG2274 214 ------LLRSYL-LLRLGQRIDL---RLSSRffrHLLRLplsffesRSVGDLasrfrdvesirEFLTGSLLT-------- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 146 rgTLVDLTTLIVFLATLSFAVPWVFALVLVSAAIsYAGMSWYrhwylqnnvkWNKLGRQQDYITRNAYALENG------- 218
Cdd:COG2274 276 --ALLDLLFVLIFLIVLFFYSPPLALVVLLLIPL-YVLLGLL----------FQPRLRRLSREESEASAKRQSllvetlr 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 219 --KDIRMFGMANWYHRHLDRLIQLQDAWQRRnslRRFLGEQIGQLAGLLRDAIVYGTLIVA---IMRGSLSISQFTLMFG 293
Cdd:COG2274 343 giETIKALGAESRFRRRWENLLAKYLNARFK---LRRLSNLLSTLSGLLQQLATVALLWLGaylVIDGQLTLGQLIAFNI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 294 MTNSFITLLDQLLDDFGKLQNASIDLQEVREFMNLQPQTPTrtltETEQKQLANRPVTITFAHVNYQYPEAKSASLKDVS 373
Cdd:COG2274 420 LSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREE----GRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNIS 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 374 FTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAMT-EH 452
Cdd:COG2274 496 LTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGdPD 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 453 PDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIY 532
Cdd:COG2274 576 ATDEEIIEAARLAGLHDFIEALPMGYDTVVG----EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 533 QDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQIQ 591
Cdd:COG2274 652 ENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
152-590 |
2.42e-76 |
|
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: 253.54 E-value: 2.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 152 LTTLIVFLATLSFAVPWVFALVLVSAAISYAGMSWYRHWylqnnvkwnkLGRQQDYITRNAYALENGKDIRMFGMANWYH 231
Cdd:COG4987 149 FLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRL----------AAARAALRARLTDLLQGAAELAAYGALDRAL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 232 RHLDRLIQLQDAWQRRNSLRRFLGEQIGQLAGLLrdaIVYGTLIVAIM---RGSLSISQFTLMFgmtnsFITLldQLLDD 308
Cdd:COG4987 219 ARLDAAEARLAAAQRRLARLSALAQALLQLAAGL---AVVAVLWLAAPlvaAGALSGPLLALLV-----LAAL--ALFEA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 309 FGKLQNASIDLQEVRE----FMNLQPQTPTrtLTETEQKQLANRPVTITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAI 384
Cdd:COG4987 289 LAPLPAAAQHLGRVRAaarrLNELLDAPPA--VTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 385 VGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAMT-EHPDLNRVTTALT 463
Cdd:COG4987 367 VGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLArPDATDEELWAALE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 464 EAGLGTFVKTLPQTTATPMtrytRDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKT 543
Cdd:COG4987 447 RVGLGDWLAALPDGLDTWL----GEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT 522
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 498176791 544 SLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQI 590
Cdd:COG4987 523 VLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
331-582 |
1.28e-71 |
|
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: 240.82 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 331 QTPTRTLTETEQKQLANRPVTITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTI 410
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPA-LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 411 TINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAM-TEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDD 489
Cdd:COG4988 395 LINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLgRPDASDEELEAALEAAGLDEFVAALPDGLDTPLG----EG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 490 GVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVL 569
Cdd:COG4988 471 GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIV 550
|
250
....*....|...
gi 498176791 570 ESGTHEQLMAKGG 582
Cdd:COG4988 551 EQGTHEELLAKNG 563
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
352-567 |
1.86e-61 |
|
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: 201.07 E-value: 1.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNVamtehpdlnrvttalteaglgtfvktlpqttatpmtrytrddgveLSGGQAQKLMLARALYKDA 511
Cdd:cd03228 81 VPQDPFLFSGTIRENI---------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 512 PVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQ 567
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
352-582 |
4.90e-59 |
|
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: 197.06 E-value: 4.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:cd03254 3 IEFENVNFSYDEKKPV-LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNVAM-TEHPDLNRVTTALTEAGLGTFVKTLPQTTATpmtrYTRDDGVELSGGQAQKLMLARALYKD 510
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLgRPNATDEEVIEAAKEAGAHDFIMKLPNGYDT----VLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 511 APVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGG 582
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
352-588 |
2.73e-57 |
|
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: 192.45 E-value: 2.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNVAM-TEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKD 510
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYgRPGATREEVEEAARAANAHEFIMELPEGYDTVIG----ERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 511 APVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMY 588
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
352-591 |
3.85e-57 |
|
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: 192.37 E-value: 3.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAS-LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFA 430
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQETIILAQSLANNVAMTEHP-DLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYK 509
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDaTDEEVEEAAKKANIHDFIMSLPDGYDTLVG----ERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQ 589
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
..
gi 498176791 590 IQ 591
Cdd:cd03249 237 AQ 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
148-591 |
5.23e-57 |
|
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: 201.48 E-value: 5.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 148 TLVDLTTLIVFLATLSFAVPWVFALV-LVSAAISYAGMSWYRHWYLQNNVKWNKLGRQQDYITrnAYALENGKDIRMFGM 226
Cdd:TIGR02203 134 VLVRETLTVIGLFIVLLYYSWQLTLIvVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVA--EETLQGYRVVKLFGG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 227 ANWYHRHLDRLIQLQDAWQRRNSLRRFLGEQIGQLAGLLRDAIVYGTLIVAIMRGSLSISQFTlmfgmtnSFITLLDQLL 306
Cdd:TIGR02203 212 QAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFT-------AFITAMIALI 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 307 DDFGKLQNASIDLQEvrefMNLQPQTPTRTLTETEQKQLANRPVT-----ITFAHVNYQYPEAKSASLKDVSFTLQAGQK 381
Cdd:TIGR02203 285 RPLKSLTNVNAPMQR----GLAAAESLFTLLDSPPEKDTGTRAIErargdVEFRNVTFRYPGRDRPALDSISLVIEPGET 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 382 LAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAM--TEHPDLNRVT 459
Cdd:TIGR02203 361 VALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYgrTEQADRAEIE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 460 TALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLA 539
Cdd:TIGR02203 441 RALAAAYAQDFVDKLPLGLDTPIG----ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 498176791 540 AGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQIQ 591
Cdd:TIGR02203 517 QGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
352-591 |
4.16e-56 |
|
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: 189.36 E-value: 4.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:cd03253 1 IEFENVTFAYDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNVAMTEhPDLN--RVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYK 509
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGR-PDATdeEVIEAAKAAQIHDKIMRFPDGYDTIVG----ERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQ 589
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
..
gi 498176791 590 IQ 591
Cdd:cd03253 235 AQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
148-592 |
1.16e-54 |
|
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: 195.81 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 148 TLVDLTTLIVFLAtlsFAVPWVFALVLVSAAISYAGMSWY-RHWYLQNNVKWNKLgrQQDYITRNAYALENGKDIRMFGM 226
Cdd:COG5265 162 TLLEIALVAGILL---VKYDWWFALITLVTVVLYIAFTVVvTEWRTKFRREMNEA--DSEANTRAVDSLLNYETVKYFGN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 227 ANWYHRHLDR-LIQLQDAWQR-RNSLRRFlgeQIGQlagllrdAIVYGTLIVAIM--------RGSLSISQFTLMfgmtN 296
Cdd:COG5265 237 EAREARRYDEaLARYERAAVKsQTSLALL---NFGQ-------ALIIALGLTAMMlmaaqgvvAGTMTVGDFVLV----N 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 297 SFITLLDQLLDDFG----KLQNASIDLQEVREFMNLQPQTPTRTltetEQKQLANRPVTITFAHVNYQYpEAKSASLKDV 372
Cdd:COG5265 303 AYLIQLYIPLNFLGfvyrEIRQALADMERMFDLLDQPPEVADAP----DAPPLVVGGGEVRFENVSFGY-DPERPILKGV 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 373 SFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAMTeH 452
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG-R 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 453 PDLNR--VTTALTEAGLGTFVKTLPQTTATPM-TRytrddGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAEN 529
Cdd:COG5265 457 PDASEeeVEAAARAAQIHDFIESLPDGYDTRVgER-----GLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTER 531
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498176791 530 EIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQIQS 592
Cdd:COG5265 532 AIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
352-591 |
2.99e-54 |
|
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: 184.61 E-value: 2.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNVAMT-EHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKD 510
Cdd:cd03252 81 VLQENVLFNRSIRDNIALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTIVG----EQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 511 APVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQI 590
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 498176791 591 Q 591
Cdd:cd03252 237 Q 237
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
148-580 |
3.56e-53 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 193.16 E-value: 3.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 148 TLVDLTTLIVFLATLSFAVPWVFALVLVSAAIsYAGMSWYRHWYLQNNVKWN-KLGRQqdyitRNAY---ALENGKDIRM 223
Cdd:TIGR03375 266 ALIDLPFALLFLLVIAIIGGPLVWVPLVAIPL-ILLPGLLLQRPLSRLAEESmRESAQ-----RNAVlveSLSGLETIKA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 224 FGMANWYHRHLDRLIQLQDAWQRRNslrRFLGEQIGQLAGLLRDAIVYGTLIV---AIMRGSLSisqftlMFGMTNSFI- 299
Cdd:TIGR03375 340 LNAEGRFQRRWEQTVAALARSGLKS---RFLSNLATNFAQFIQQLVSVAIVVVgvyLISDGELT------MGGLIACVMl 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 300 -----TLLDQLLDDFGKLQNASIDLQEVREFMNLQPQTPtrtltetEQKQLANRPV---TITFAHVNYQYPEAKSASLKD 371
Cdd:TIGR03375 411 sgralAPLGQLAGLLTRYQQAKTALQSLDELMQLPVERP-------EGTRFLHRPRlqgEIEFRNVSFAYPGQETPALDN 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 372 VSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAM-T 450
Cdd:TIGR03375 484 VSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALgA 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 451 EHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENE 530
Cdd:TIGR03375 564 PYADDEEILRAAELAGVTEFVRRHPDGLDMQIG----ERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEER 639
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 498176791 531 IYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAK 580
Cdd:TIGR03375 640 FKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
278-591 |
5.47e-51 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 185.29 E-value: 5.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 278 IMRGSLS---ISQFTLMFGMTNSFITLLDQLLddfGKLQNASIDLQEVREFMNLQPqtptrTLTETEQKQLANRPVT--I 352
Cdd:TIGR02204 267 VIAGKMSagtLGQFVFYAVMVAGSIGTLSEVW---GELQRAAGAAERLIELLQAEP-----DIKAPAHPKTLPVPLRgeI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 353 TFAHVNYQYPE-AKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:TIGR02204 339 EFEQVNFAYPArPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMAL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNVAMTeHPDLNR--VTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYK 509
Cdd:TIGR02204 419 VPQDPVLFAASVMENIRYG-RPDATDeeVEAAARAAHAHEFISALPEGYDTYLG----ERGVTLSGGQRQRIAIARAILK 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQ 589
Cdd:TIGR02204 494 DAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLAR 573
|
..
gi 498176791 590 IQ 591
Cdd:TIGR02204 574 LQ 575
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
352-572 |
5.37e-50 |
|
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: 172.39 E-value: 5.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNVAM--TEHPDlNRVTTALTEAGLGTFVKTLPQTtatpMTRYTRDDGVELSGGQAQKLMLARALYK 509
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLgaPLADD-ERILRAAELAGVTDFVNKHPNG----LDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESG 572
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
320-589 |
2.30e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 175.03 E-value: 2.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 320 QEVREFMNLQPQTPTRTltetEQKQLANRPVTITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLM 399
Cdd:PRK11174 322 ESLVTFLETPLAHPQQG----EKELASNDPVTIEAEDLEILSPDGKTL-AGPLNFTLPAGQRIALVGPSGAGKTSLLNAL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 400 MGLLhPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAMTeHPDLN--RVTTALTEAGLGTFVKTLPQT 477
Cdd:PRK11174 397 LGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-NPDASdeQLQQALENAWVSEFLPLLPQG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 478 TATPmtryTRDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFC 557
Cdd:PRK11174 475 LDTP----IGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW 550
|
250 260 270
....*....|....*....|....*....|..
gi 498176791 558 DSILFMNHGQVLESGTHEQLMAKGGRYAQMYQ 589
Cdd:PRK11174 551 DQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
270-587 |
1.69e-46 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 172.84 E-value: 1.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 270 VYGTLIVAimRGSLSISQFTLMFGMTNSFITLLDQLLDDFGKLQNASIDLQEvreFMNLQPQTPTRTLTEtEQKQLANRP 349
Cdd:PRK13657 259 VLGAALVQ--KGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEE---FFEVEDAVPDVRDPP-GAIDLGRVK 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 350 VTITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLarlmMGLLH----PISGTITINGLNANLLPLAER 425
Cdd:PRK13657 333 GAVEFDDVSFSYDNSRQG-VEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQrvfdPQSGRILIDGTDIRTVTRASL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 426 FALFAPVFQETIILAQSLANNVAMTEhPD--LNRVTTALTEAGLGTFVKTLPQTTATpmtrYTRDDGVELSGGQAQKLML 503
Cdd:PRK13657 408 RRNIAVVFQDAGLFNRSIEDNIRVGR-PDatDEEMRAAAERAQAHDFIERKPDGYDT----VVGERGRQLSGGERQRLAI 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 504 ARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGR 583
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGR 562
|
....
gi 498176791 584 YAQM 587
Cdd:PRK13657 563 FAAL 566
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
352-591 |
7.20e-46 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 170.97 E-value: 7.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNAN---LLPLAERFAL 428
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdytLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 fapVFQETIILAQSLANNVAMTEHPDLNR--VTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARA 506
Cdd:PRK11176 422 ---VSQNVHLFNDTIANNIAYARTEQYSReqIEEAARMAYAMDFINKMDNGLDTVIG----ENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 507 LYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQ 586
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
....*
gi 498176791 587 MYQIQ 591
Cdd:PRK11176 575 LHKMQ 579
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
331-589 |
1.80e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 169.62 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 331 QTPTRTLTETEQkqLANRPVTITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTI 410
Cdd:PRK11160 320 QKPEVTFPTTST--AAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 411 TINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAM-TEHPDLNRVTTALTEAGLGTFVktlpqTTATPMTRYTRDD 489
Cdd:PRK11160 398 LLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLaAPNASDEALIEVLQQVGLEKLL-----EDDKGLNAWLGEG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 490 GVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRL-ASTRFcDSILFMNHGQV 568
Cdd:PRK11160 473 GRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLtGLEQF-DRICVMDNGQI 551
|
250 260
....*....|....*....|.
gi 498176791 569 LESGTHEQLMAKGGRYAQMYQ 589
Cdd:PRK11160 552 IEQGTHQELLAQQGRYYQLKQ 572
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
345-563 |
6.69e-45 |
|
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: 167.08 E-value: 6.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 345 LANRPVTITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAE 424
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYPGRRPA-LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 425 RFALFAPVFQETIILAQSLANNVAMTEhPDLNR--VTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLM 502
Cdd:TIGR02857 394 WRDQIAWVPQHPFLFAGTIAENIRLAR-PDASDaeIREALERAGLDEFVAALPQGLDTPIG----EGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 503 LARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFM 563
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
278-587 |
4.20e-44 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 167.81 E-value: 4.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 278 IMRGSLSISQFTLMFGMTNSFITLLDQLLDDFGKLQNASIDLQEVREFMNlQPQTPTrtLTETEQKQLANRPVT-----I 352
Cdd:TIGR03796 402 VMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLR-NPVDPL--LEEPEGSAATSEPPRrlsgyV 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 353 TFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPV 432
Cdd:TIGR03796 479 ELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMV 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 433 FQETIILAQSLANNVAMTEH--PDLNRVTtALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKD 510
Cdd:TIGR03796 559 DQDIFLFEGTVRDNLTLWDPtiPDADLVR-ACKDAAIHDVITSRPGGYDAELA----EGGANLSGGQRQRLEIARALVRN 633
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 511 APVLILDEPTAALDAIAENEIYQDYAQlaAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQM 587
Cdd:TIGR03796 634 PSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
354-567 |
3.54e-43 |
|
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: 153.78 E-value: 3.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 354 FAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVF 433
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 434 Q--------ETII--LAQSLANNvAMTEHPDLNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLML 503
Cdd:cd03225 82 QnpddqffgPTVEeeVAFGLENL-GLPEEEIEERVEEALELVGLEGLRDRSPFT---------------LSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 504 ARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLASTR-FCDSILFMNHGQ 567
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
352-580 |
1.88e-42 |
|
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: 152.49 E-value: 1.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLN---ANLLPLAERFAL 428
Cdd:COG1122 1 IELENLSFSYPGGTPA-LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 fapVFQ--ETIILAQSLANNVA------------MTEhpdlnRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELS 494
Cdd:COG1122 80 ---VFQnpDDQLFAPTVEEDVAfgpenlglpreeIRE-----RVEEALELVGLEHLADRPPH---------------ELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 495 GGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLAS-TRFCDSILFMNHGQVLESG 572
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLvAELADRVIVLDDGRIVADG 216
|
....*...
gi 498176791 573 THEQLMAK 580
Cdd:COG1122 217 TPREVFSD 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
352-579 |
3.00e-42 |
|
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: 159.30 E-value: 3.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHP---ISGTITINGLNANLLPLAERFAL 428
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 FAPVFQE--------TII--LAQSLAN-NVAMTEHPDlnRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQ 497
Cdd:COG1123 85 IGMVFQDpmtqlnpvTVGdqIAEALENlGLSRAEARA--RVLELLEAVGLERRLDRYPH---------------QLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 498 AQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLAS-TRFCDSILFMNHGQVLESGTH 574
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPP 227
|
....*
gi 498176791 575 EQLMA 579
Cdd:COG1123 228 EEILA 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
278-587 |
7.65e-42 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 161.04 E-value: 7.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 278 IMRGSLSISQFTLMFGMTNSFITLLDQLLDDFGKLQNASIDLQEVREFMNLQPQTPtrtLTETeqkqLANRPVT--ITFA 355
Cdd:TIGR00958 410 VLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP---LTGT----LAPLNLEglIEFQ 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 356 HVNYQYPEAKSAS-LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLnanllPLAERFALF----- 429
Cdd:TIGR00958 483 DVSFSYPNRPDVPvLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV-----PLVQYDHHYlhrqv 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 430 APVFQETIILAQSLANNVA--MTEHPDlNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARAL 507
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAygLTDTPD-EEIMAAAKAANAHDFIMEFPNGYDTEVG----EKGSQLSGGQKQRIAIARAL 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 508 YKDAPVLILDEPTAALDAIAENEIYQDYAQlaAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQM 587
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
278-588 |
1.15e-41 |
|
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: 160.68 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 278 IMRGSLSISQFTLMFGMTNSFITLLDQLLDDFGKLQNASI---DLQEV----REFMNLQPQTPTRTLTETeqkqlanrpv 350
Cdd:TIGR01193 404 VMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVannRLNEVylvdSEFINKKKRTELNNLNGD---------- 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 351 tITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFA 430
Cdd:TIGR01193 474 -IVINDVSYSYGYGSNI-LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQETIILAQSLANNVAMTEHPDL--NRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALY 508
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLGAKENVsqDEIWAACEIAEIKDDIENMPLGYQTELS----EEGSSISGGQKQRIALARALL 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 509 KDAPVLILDEPTAALDAIAENEIYQDYAQLAAgKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMY 588
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
352-572 |
6.59e-41 |
|
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: 146.69 E-value: 6.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPlAERFALFAP 431
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNVamtehpdlnrvttalteaglgtfvktlpqttatpmtrytrddGVELSGGQAQKLMLARALYKDA 511
Cdd:cd03247 80 LNQRPYLFDTTLRNNL------------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 512 PVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESG 572
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
356-572 |
7.89e-41 |
|
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: 148.04 E-value: 7.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 356 HVNYQYPEAKSAS--LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING---LNANLLPLAERFALFA 430
Cdd:cd03257 6 NLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRRKEIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQE---------TI--ILAQSLANNVAMTEHPDLNRVTTALTEaGLGtfvktLPqttATPMTRYTRddgvELSGGQAQ 499
Cdd:cd03257 86 MVFQDpmsslnprmTIgeQIAEPLRIHGKLSKKEARKEAVLLLLV-GVG-----LP---EEVLNRYPH----ELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 500 KLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISH--RLAStRFCDSILFMNHGQVLESG 572
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHdlGVVA-KIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
346-579 |
8.64e-41 |
|
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: 155.45 E-value: 8.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 346 ANRPVTITFAHVNYQYPEAKSAS---LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPL 422
Cdd:COG1123 255 AAAEPLLEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 423 AERFAL---FAPVFQ---------ETI--ILAQSLANNVAMTEHPDLNRVTTALTEAGLGtfvktlpqttATPMTRYTRd 488
Cdd:COG1123 335 RSLRELrrrVQMVFQdpysslnprMTVgdIIAEPLRLHGLLSRAERRERVAELLERVGLP----------PDLADRYPH- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 489 dgvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAeneiyqdYAQLAA---------GKTSLFISHRLASTR-FCD 558
Cdd:COG1123 404 ---ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-------QAQILNllrdlqrelGLTYLFISHDLAVVRyIAD 473
|
250 260
....*....|....*....|.
gi 498176791 559 SILFMNHGQVLESGTHEQLMA 579
Cdd:COG1123 474 RVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
357-568 |
1.64e-40 |
|
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: 145.05 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 357 VNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQET 436
Cdd:cd03246 6 VSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 IILAQSLANNVamtehpdlnrvttalteaglgtfvktlpqttatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLIL 516
Cdd:cd03246 86 ELFSGSIAENI---------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498176791 517 DEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLASTRFCDSILFMNHGQV 568
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
143-551 |
1.15e-39 |
|
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: 152.51 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 143 LYGRGTLVDLTTLIVFLAT--LSFAVPWVFALVL-VSAAISYAGMSWYRHWYLQNNVKWNKLGRQQdYITRNAYALENGK 219
Cdd:TIGR02868 126 LYVRVIVPAGVALVVGAAAvaAIAVLSVPAALILaAGLLLAGFVAPLVSLRAARAAEQALARLRGE-LAAQLTDALDGAA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 220 DIRMFG-MANWYHRHLDRLIQLQDAWQRRNSLRRfLGEQIGQLAGLLrdaIVYGTLIVAI---MRGSLSisqftlmfGMT 295
Cdd:TIGR02868 205 ELVASGaLPAALAQVEEADRELTRAERRAAAATA-LGAALTLLAAGL---AVLGALWAGGpavADGRLA--------PVT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 296 NSFITLLD-QLLDDFGKLQNASIDLQEVRE----FMNLQPQTPTRTLTETEQ-KQLANRPVTITFAHVNYQYPEAkSASL 369
Cdd:TIGR02868 273 LAVLVLLPlAAFEAFAALPAAAQQLTRVRAaaerIVEVLDAAGPVAEGSAPAaGAVGLGKPTLELRDLSAGYPGA-PPVL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 370 KDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANN--V 447
Cdd:TIGR02868 352 DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlrL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 AMTEHPDlNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIA 527
Cdd:TIGR02868 432 ARPDATD-EELWAALERVGLADWLRALPDGLDTVLG----EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
410 420
....*....|....*....|....
gi 498176791 528 ENEIYQDYAQLAAGKTSLFISHRL 551
Cdd:TIGR02868 507 ADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
352-573 |
4.49e-39 |
|
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: 143.02 E-value: 4.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNVA-MTEHPD--LNRvttALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALY 508
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDpFGEYSDeeLWQ---ALERVGLKEFVESLPGGLDTVVE----EGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 509 KDAPVLILDEPTAALDAIAENEIyQDYAQLA-AGKTSLFISHRLASTRFCDSILFMNHGQVLESGT 573
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALI-QKTIREAfKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
157-580 |
9.47e-39 |
|
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: 150.28 E-value: 9.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 157 VFLATLsFAV-PWVFALVLVSAAISyAGMSWY-----RHWYLQNNVKWNKLGRQQDYITRNAYAlengkdIRMFGMAN-- 228
Cdd:COG4618 145 IFLAVL-FLFhPLLGLLALVGALVL-VALALLnerltRKPLKEANEAAIRANAFAEAALRNAEV------IEAMGMLPal 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 229 ---WYHRHlDRLIQLQDAWQRRNSLrrflgeqIGQLAGLLRDAIVYGTLIVA---IMRGSLSISqftLMFGmtNSFIT-- 300
Cdd:COG4618 217 rrrWQRAN-ARALALQARASDRAGG-------FSALSKFLRLLLQSAVLGLGaylVIQGEITPG---AMIA--ASILMgr 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 301 ---LLDQLLDDFGKLQNASIDLQEVREFMNLQPQTPTRTlteteqkQLAnRPV-TITFAHVNYQYPEAKSASLKDVSFTL 376
Cdd:COG4618 284 alaPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERM-------PLP-RPKgRLSVENLTVVPPGSKRPILRGVSFSL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 377 QAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAErfalFAPVF----QETIILAQSLANNVAMTEH 452
Cdd:COG4618 356 EPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE----LGRHIgylpQDVELFDGTIAENIARFGD 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 453 PDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIY 532
Cdd:COG4618 432 ADPEKVVAAAKLAGVHEMILRLPDGYDTRIG----EGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALA 507
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 498176791 533 QDYAQL-AAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAK 580
Cdd:COG4618 508 AAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
369-580 |
1.20e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 142.12 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERfALFAPVFQETIILAQ-SLANNV 447
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGYVPQEPALYPDlTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 A-------MTEHPDLNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLILDEPT 520
Cdd:COG1131 95 RffarlygLPRKEARERIDELLELFGLTDAADRKVGT---------------LSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 521 AALDAIAENEIYQDYAQLAA-GKTSLFISHRLAS-TRFCDSILFMNHGQVLESGTHEQLMAK 580
Cdd:COG1131 160 SGLDPEARRELWELLRELAAeGKTVLLSTHYLEEaERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
356-572 |
3.50e-38 |
|
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: 139.11 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 356 HVNYQYPeaKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERfalfapvfqe 435
Cdd:cd03214 4 NLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 tiilaqslANNVAMtehpdlnrVTTALTEAGLGTFVKtlpqttatpmtRYTRddgvELSGGQAQKLMLARALYKDAPVLI 515
Cdd:cd03214 72 --------ARKIAY--------VPQALELLGLAHLAD-----------RPFN----ELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 516 LDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISH--RLAStRFCDSILFMNHGQVLESG 572
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHdlNLAA-RYADRVILLKDGRIVAQG 180
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
356-579 |
3.72e-38 |
|
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: 141.09 E-value: 3.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 356 HVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQE 435
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 ---------TI--ILAQSLANNVaMTEHPDlnRVTTALTEAGLGtfvktlpqttATPMTRYTRddgvELSGGQAQKLMLA 504
Cdd:COG1124 88 pyaslhprhTVdrILAEPLRIHG-LPDREE--RIAELLEQVGLP----------PSFLDRYPH----QLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 505 RALYKDAPVLILDEPTAALDAIAENEI---YQDYaQLAAGKTSLFISHRLAS-TRFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEIlnlLKDL-REERGLTYLFVSHDLAVvAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
352-578 |
4.63e-38 |
|
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: 141.33 E-value: 4.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAksASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQ-SLANNVAMTEHP-----------DLNRVTTALTEAGLGTFVktlpqttatpMTRYTrddgvELSGGQAQ 499
Cdd:COG1120 80 VPQEPPAPFGlTVRELVALGRYPhlglfgrpsaeDREAVEEALERTGLEHLA----------DRPVD-----ELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 500 KLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISH--RLAStRFCDSILFMNHGQVLESGTHE 575
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHdlNLAA-RYADRLVLLKDGRIVAQGPPE 223
|
...
gi 498176791 576 QLM 578
Cdd:COG1120 224 EVL 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
351-591 |
1.56e-37 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 147.17 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 351 TITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFA 430
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLV-LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQETIILAQSLANNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKD 510
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLG----EQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 511 APVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQI 590
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQL 574
|
.
gi 498176791 591 Q 591
Cdd:PRK10790 575 Q 575
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
352-578 |
1.74e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYpEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANL-------LPLAE 424
Cdd:COG1121 7 IELENLTVSY-GGRPV-LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRarrrigyVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 425 RFALFAP--VFQetiILAQSLANNVAMTEHP---DLNRVTTALTEAGLGTFVKTlpqttatPMTrytrddgvELSGGQAQ 499
Cdd:COG1121 85 EVDWDFPitVRD---VVLMGRYGRRGLFRRPsraDREAVDEALERVGLEDLADR-------PIG--------ELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 500 KLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLAS-TRFCDSILFMNHGqVLESGTHEQL 577
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAvREYFDRVLLLNRG-LVAHGPPEEV 225
|
.
gi 498176791 578 M 578
Cdd:COG1121 226 L 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
352-579 |
7.35e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.50 E-value: 7.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAksasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERfalfaP 431
Cdd:COG3840 2 LRLDDLTYRYGDF----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER-----P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 V---FQETIILAQ-SLANNVAMTEHPDLN-------RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQK 500
Cdd:COG3840 73 VsmlFQENNLFPHlTVAQNIGLGLRPGLKltaeqraQVEQALERVGLAGLLDRLPG---------------QLSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 501 LMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLA-STRFCDSILFMNHGQVLESGTHEQL 577
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRerGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAAL 217
|
..
gi 498176791 578 MA 579
Cdd:COG3840 218 LD 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
148-580 |
1.54e-35 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 140.56 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 148 TLVDLTTLIVFLATLSFAVPWVFALVLVSAAISYaGMSWYRHWYLQNNVKWNKLGRQQDYITRNAyALENGKDIRMFGMA 227
Cdd:TIGR01842 122 AFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLV-GLALLNNRATKKPLKEATEASIRANNLADS-ALRNAEVIEAMGMM 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 228 NWYHRHLDRLIQLQDAWQRRNSLRrflGEQIGQLAGLLRdaIVYGTLIVAImRGSLSISQFTLMFGMTNSFITL------ 301
Cdd:TIGR01842 200 GNLTKRWGRFHSKYLSAQSAASDR---AGMLSNLSKYFR--IVLQSLVLGL-GAYLAIDGEITPGMMIAGSILVgralap 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 302 LDQLLDDFGKLQNASIDLQEVREFMNLQPQTPTRTlteteqkQLANRPVTITFAHVNYQYPEAKSASLKDVSFTLQAGQK 381
Cdd:TIGR01842 274 IDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAM-------PLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 382 LAIVGINGAGKSTLARLMMGLLHPISGTITINGLNAN------------LLPlaerfalfapvfQETIILAQSLANNVA- 448
Cdd:TIGR01842 347 LAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwdretfgkhigYLP------------QDVELFPGTVAENIAr 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEHPDLNRVTTALTEAGLGTFVKTLPQTTATpmtrYTRDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAE 528
Cdd:TIGR01842 415 FGENADPEKIIEAAKLAGVHELILRLPDGYDT----VIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 498176791 529 NEIYQDYAQL-AAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAK 580
Cdd:TIGR01842 491 QALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
369-566 |
1.65e-35 |
|
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: 132.66 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLnanllPLAERFALFAPVFQETIILAQ---SLAN 445
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQRRSIDRDfpiSVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 446 NVAM-----------TEHPDLNRVTTALTEAGLGTFVKtlpqttatpmtrytRDDGvELSGGQAQKLMLARALYKDAPVL 514
Cdd:cd03235 90 VVLMglyghkglfrrLSKADKAKVDEALERVGLSELAD--------------RQIG-ELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498176791 515 ILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRL-ASTRFCDSILFMNHG 566
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLgLVLEYFDRVLLLNRT 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
352-583 |
2.01e-35 |
|
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: 133.44 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPeaKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAp 431
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQET----------IILAQSLANNvaMTEHPDLNRVTTALTEAGLGTFVKtlpqttatpmtRYTRddgvELSGGQAQKL 501
Cdd:COG4555 79 LPDERglydrltvreNIRYFAELYG--LFDEELKKRIEELIELLGLEEFLD-----------RRVG----ELSTGMKKKV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 502 MLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLAS-TRFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEvEALCDRVVILHKGKVVAQGSLDELRE 221
|
....
gi 498176791 580 KGGR 583
Cdd:COG4555 222 EIGE 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
352-587 |
4.55e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.60 E-value: 4.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGL---NANLLPLAERFAL 428
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlsEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 fapVFQE--------TII--LAQSLANN-VAMTEHpdLNRVTTALTEAGlgtfvktlpqttatpMTRYTRDDGVELSGGQ 497
Cdd:PRK13635 86 ---VFQNpdnqfvgaTVQddVAFGLENIgVPREEM--VERVDQALRQVG---------------MEDFLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 498 AQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTRFCDSILFMNHGQVLESGTHE 575
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
250
....*....|..
gi 498176791 576 QLMAKGGRYAQM 587
Cdd:PRK13635 226 EIFKSGHMLQEI 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
352-568 |
1.93e-34 |
|
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: 130.28 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYP-EAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFA 430
Cdd:cd03248 12 VKFQNVTFAYPtRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQETIILAQSLANNVA--MTEHPDlNRVTTALTEAGLGTFVKTLPQTTATPmtryTRDDGVELSGGQAQKLMLARALY 508
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAygLQSCSF-ECVKEAAQKAHAHSFISELASGYDTE----VGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 509 KDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQV 568
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
369-579 |
2.00e-34 |
|
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: 130.48 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAPVFQE-------TIi 438
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrIGMLFQGgalfdslTV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 laqslANNVA--MTEHPDLN------RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKD 510
Cdd:COG1127 100 -----FENVAfpLREHTDLSeaeireLVLEKLELVGLPGAADKMPS---------------ELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 511 APVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISHRLAST-RFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
369-521 |
2.67e-34 |
|
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: 127.38 E-value: 2.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQ-----------ETI 437
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQdpqlfprltvrENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 ILAQSLAnnvAMTEHPDLNRVTTALTEAGLGTFVKtlpqttaTPMTRYTRddgvELSGGQAQKLMLARALYKDAPVLILD 517
Cdd:pfam00005 81 RLGLLLK---GLSKREKDARAEEALEKLGLGDLAD-------RPVGERPG----TLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 498176791 518 EPTA 521
Cdd:pfam00005 147 EPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
365-568 |
2.95e-34 |
|
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: 127.90 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 365 KSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNanllplaerfalfapVFQETIILAQSLA 444
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD---------------IKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 445 nnvAMTEHPDLNRVTTALteaglgtfvktlpqttatpmtrytrdDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALD 524
Cdd:cd03230 77 ---YLPEEPSLYENLTVR--------------------------ENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 498176791 525 AIAENEIYQDYAQLAA-GKTSLFISHRLAS-TRFCDSILFMNHGQV 568
Cdd:cd03230 128 PESRREFWELLRELKKeGKTILLSSHILEEaERLCDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
352-577 |
3.20e-34 |
|
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: 129.61 E-value: 3.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLH-----PISGTITING-----LNANLLP 421
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdiydLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 422 LAERFALfapVFQETIILAQSLANNVAM---------TEHPDLnRVTTALTEAGLGTFVKTlpqttatpmtrytRDDGVE 492
Cdd:cd03260 79 LRRRVGM---VFQKPNPFPGSIYDNVAYglrlhgiklKEELDE-RVEEALRKAALWDEVKD-------------RLHALG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 493 LSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLA-STRFCDSILFMNHGQVLES 571
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEF 221
|
....*.
gi 498176791 572 GTHEQL 577
Cdd:cd03260 222 GPTEQI 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
352-567 |
3.72e-34 |
|
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: 127.69 E-value: 3.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING-----LNANLLPLAERF 426
Cdd:cd03229 1 LELKNVSKRYGQKTV--LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 427 ALfapVFQetiilaqslannvamteHPDLNRVTTALTEAGLGtfvktlpqttatpmtrytrddgveLSGGQAQKLMLARA 506
Cdd:cd03229 79 GM---VFQ-----------------DFALFPHLTVLENIALG------------------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498176791 507 LYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLAST-RFCDSILFMNHGQ 567
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
353-567 |
5.37e-34 |
|
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: 126.59 E-value: 5.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 353 TFAHVNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPV 432
Cdd:cd00267 1 EIENLSFRYGGRTA--LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 433 FQetiilaqslannvamtehpdlnrvttalteaglgtfvktlpqttatpmtrytrddgveLSGGQAQKLMLARALYKDAP 512
Cdd:cd00267 79 PQ----------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 513 VLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLA-STRFCDSILFMNHGQ 567
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPElAELAADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
369-579 |
1.67e-33 |
|
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: 128.00 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAPVFQETIIL-AQSLA 444
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMGMLFQSGALFdSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 445 NNVA--MTEHPDLN------RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLIL 516
Cdd:cd03261 96 ENVAfpLREHTRLSeeeireIVLEKLEAVGLRGAEDLYPA---------------ELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 517 DEPTAALDAIAENEIyqdyAQL------AAGKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMA 579
Cdd:cd03261 161 DEPTAGLDPIASGVI----DDLirslkkELGLTSIMVTHDLDTAFaIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
352-568 |
2.89e-33 |
|
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: 126.84 E-value: 2.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAS--LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL- 428
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 -----FapVFQ-----------ETIILAQSLANNVAMTehpDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvE 492
Cdd:cd03255 81 rrhigF--VFQsfnllpdltalENVELPLLLAGVPKKE---RRERAEELLERVGLGDRLNHYPS---------------E 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 493 LSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLA--AGKTSLFISH--RLAStrFCDSILFMNHGQV 568
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHdpELAE--YADRIIELRDGKI 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
358-591 |
4.74e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 133.68 E-value: 4.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 358 NYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETI 437
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 ILAQSLANNVAMTeHPDLNR--VTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLI 515
Cdd:PRK10789 400 LFSDTVANNIALG-RPDATQqeIEHVARLASVHDDILRLPQGYDTEVG----ERGVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 516 LDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQIQ 591
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
369-572 |
2.81e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 126.11 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETiilaqSLANN-- 446
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLSFEfd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 ----VAMTEHPDLNRVTTAlTEAGLGTFVKTLPQTTATpmtRYTRDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAA 522
Cdd:PRK09536 94 vrqvVEMGRTPHRSRFDTW-TETDRAAVERAMERTGVA---QFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498176791 523 LD---AIAENEIYQDYAQlaAGKTSLFISHRL-ASTRFCDSILFMNHGQVLESG 572
Cdd:PRK09536 170 LDinhQVRTLELVRRLVD--DGKTAVAAIHDLdLAARYCDELVLLADGRVRAAG 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
352-570 |
3.81e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 120.92 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAS--LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL- 428
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 -----FapVFQ-----------ETIILAQSLANnvaMTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvE 492
Cdd:COG1136 85 rrhigF--VFQffnllpeltalENVALPLLLAG---VSRKERRERARELLERVGLGDRLDHRPS---------------Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 493 LSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISH--RLAStrFCDSILFMNHGQV 568
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHdpELAA--RADRVIRLRDGRI 222
|
..
gi 498176791 569 LE 570
Cdd:COG1136 223 VS 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
352-568 |
6.49e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.92 E-value: 6.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAE---RFAL 428
Cdd:COG4619 1 LELEGLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrrQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 fapVFQETIILAQSLANNVAMT-----EHPDLNRVTTALTEAGLGTFVktLPQTTAtpmtrytrddgvELSGGQAQKLML 503
Cdd:COG4619 79 ---VPQEPALWGGTVRDNLPFPfqlreRKFDRERALELLERLGLPPDI--LDKPVE------------RLSGGERQRLAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 504 ARALYKDAPVLILDEPTAALDA----IAENEIyQDYAQlAAGKTSLFISH-RLASTRFCDSILFMNHGQV 568
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPentrRVEELL-REYLA-EEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
352-577 |
1.75e-30 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 120.63 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQY----PEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNA------NLLP 421
Cdd:TIGR04521 1 IKLKNVSYIYqpgtPFEKKA-LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkkkKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 422 LAERFALfapVFQ--------ETIilaqslANNVA-------MTEHPDLNRVTTALTEAGLG-TFVKTLPqttatpmtry 485
Cdd:TIGR04521 80 LRKKVGL---VFQfpehqlfeETV------YKDIAfgpknlgLSEEEAEERVKEALELVGLDeEYLERSP---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 486 trddgVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISHRL---AstRFCDSI 560
Cdd:TIGR04521 141 -----FELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhkEKGLTVILVTHSMedvA--EYADRV 213
|
250
....*....|....*..
gi 498176791 561 LFMNHGQVLESGTHEQL 577
Cdd:TIGR04521 214 IVMHKGKIVLDGTPREV 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
371-572 |
1.79e-30 |
|
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: 118.75 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERfalfaPV---FQETIILAQ-SLANN 446
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR-----PVsmlFQENNLFAHlTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 VAMTEHPDLN-------RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLILDEP 519
Cdd:cd03298 91 VGLGLSPGLKltaedrqAIEVALARVGLAGLEKRLPG---------------ELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 520 TAALDAIAENEIYQDYAQLAA--GKTSLFISHRLA-STRFCDSILFMNHGQVLESG 572
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLHAetKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
369-572 |
2.89e-30 |
|
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: 118.01 E-value: 2.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAER-FALfapVFQETIILA-QSLANN 446
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRnIGM---VFQDYALFPhLTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 VA-------MTEHPDLNRVTTALTEAGLGTFvktlpqttatpMTRYTRddgvELSGGQAQKLMLARALYKDAPVLILDEP 519
Cdd:cd03259 93 IAfglklrgVPKAEIRARVRELLELVGLEGL-----------LNRYPH----ELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 520 TAALDAIAENEIYQDYAQL--AAGKTSLFISHRLA-STRFCDSILFMNHGQVLESG 572
Cdd:cd03259 158 LSALDAKLREELREELKELqrELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
366-580 |
9.56e-30 |
|
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: 118.51 E-value: 9.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 366 SASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL----FAPVFQETIILAQ 441
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 442 -SLANNVA-------MTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPV 513
Cdd:cd03294 117 rTVLENVAfglevqgVPRAEREERAAEALELVGLEGWEHKYPD---------------ELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 514 LILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLA-STRFCDSILFMNHGQVLESGTHEQLMAK 580
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
366-568 |
1.00e-29 |
|
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: 115.61 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 366 SASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAPV--FQETIILA 440
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiaYVPEdrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 441 QSLANNVAMTEHpdlnrvttalteaglgtfvktlpqttatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLILDEPT 520
Cdd:cd03215 93 LSVAENIALSSL----------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498176791 521 AALDAIAENEIYQDYAQLAA-GKTSLFISHRLAS-TRFCDSILFMNHGQV 568
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADaGKAVLLISSELDElLGLCDRILVMYEGRI 182
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
369-573 |
2.50e-29 |
|
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: 115.20 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVA 448
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEHPDLNRVTTAL--TEAGLgtfvktlpqttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAI 526
Cdd:cd03369 104 PFDEYSDEEIYGALrvSEGGL------------------------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498176791 527 AENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGT 573
Cdd:cd03369 160 TDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
352-567 |
2.88e-29 |
|
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: 114.87 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAS---LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanllplaeRFAL 428
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------SIAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 FApvfQETIILAQSLANNVAMTE---HPDLNRVTTA--------------LTEAGlgtfvktlpqttatpmtrytrDDGV 491
Cdd:cd03250 71 VS---QEPWIQNGTIRENILFGKpfdEERYEKVIKAcalepdleilpdgdLTEIG---------------------EKGI 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 492 ELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQ--LAAGKTSLFISHRLASTRFCDSILFMNHGQ 567
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILglLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
352-531 |
5.21e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 114.76 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPlAERFALF-- 429
Cdd:COG2884 2 IRFENVSKRYPGGREA-LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK-RREIPYLrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 430 --APVFQETIILAQ-SLANNVA-------MTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQ 499
Cdd:COG2884 80 riGVVFQDFRLLPDrTVYENVAlplrvtgKSRKEIRRRVREVLDLVGLSDKAKALPH---------------ELSGGEQQ 144
|
170 180 190
....*....|....*....|....*....|..
gi 498176791 500 KLMLARALYKDAPVLILDEPTAALDAIAENEI 531
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEI 176
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
352-579 |
1.12e-28 |
|
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: 114.71 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:cd03295 1 IEFENVTKRYGGGKKA-VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQ-SLANNVAMTehPDLN---------RVTTALTEAGLGtfvktlPQTTATpmtRYTRddgvELSGGQAQKL 501
Cdd:cd03295 80 VIQQIGLFPHmTVEENIALV--PKLLkwpkekireRADELLALVGLD------PAEFAD---RYPH----ELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 502 MLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISH------RLAstrfcDSILFMNHGQVLESGT 573
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHdideafRLA-----DRIAIMKNGEIVQVGT 219
|
....*.
gi 498176791 574 HEQLMA 579
Cdd:cd03295 220 PDEILR 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
352-580 |
1.20e-28 |
|
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: 114.22 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAS--LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL- 428
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 --FAPVFQETIILAQ-SLANNVA---------MTEHPDlnRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGG 496
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVAlpleiagvpKAEIEE--RVLELLELVGLEDKADAYPA---------------QLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 497 QAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGT 573
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKrICDRVAVMEKGEVVEEGT 224
|
....*..
gi 498176791 574 HEQLMAK 580
Cdd:cd03258 225 VEEVFAN 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
346-549 |
1.31e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.80 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 346 ANRPVTITFAHVNYQYPEAKSAS--LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLnanllPLA 423
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-----PVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 424 ERFALFAPVFQE-------T----IILAQSLANnVAMTEHPDlnRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvE 492
Cdd:COG1116 77 GPGPDRGVVFQEpallpwlTvldnVALGLELRG-VPKAERRE--RARELLELVGLAGFEDAYPH---------------Q 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 493 LSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISH 549
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
369-568 |
1.57e-28 |
|
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: 111.37 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLL-PLAERFALFAPVFQetiilaqslannv 447
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 amtehpdlnrvttalteaglgtfvktlpqttatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLILDEPTAALDAIA 527
Cdd:cd03216 83 ---------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 498176791 528 ENEIYQDYAQLAA-GKTSLFISHRLAS-TRFCDSILFMNHGQV 568
Cdd:cd03216 118 VERLFKVIRRLRAqGVAVIFISHRLDEvFEIADRVTVLRDGRV 160
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
356-568 |
2.53e-28 |
|
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: 112.35 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 356 HVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNAnllPLAERFALFAPVFQE 435
Cdd:cd03226 4 NISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 T--IILAQSLANNV---AMTEHPDLNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKD 510
Cdd:cd03226 80 VdyQLFTDSVREELllgLKELDAGNEQAETVLKDLDLYALKERHPLS---------------LSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 511 APVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLA-STRFCDSILFMNHGQV 568
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEfLAKVCDRVLLLANGAI 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
369-560 |
4.43e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.80 E-value: 4.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLP--LAERFALFAPvfQETIILAQSLANN 446
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARedYRRRLAYLGH--ADGLKPELTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 VAM-----TEHPDLNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLILDEPTA 521
Cdd:COG4133 96 LRFwaalyGLRADREAIDEALEAVGLAGLADLPVRQ---------------LSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 498176791 522 ALDAiAENEIYQDY--AQLAAGKTSLFISHRLASTRFCDSI 560
Cdd:COG4133 161 ALDA-AGVALLAELiaAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
369-579 |
5.23e-28 |
|
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: 118.25 E-value: 5.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLhPISGTITINGLNANLLPLAERFAL---FAPVFQE---------T 436
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDpfgslsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 I--ILAQSLA-NNVAMTEHPDLNRVTTALTEAGLgtfvktlpqtTATPMTRYTRddgvELSGGQAQKLMLARALYKDAPV 513
Cdd:COG4172 381 VgqIIAEGLRvHGPGLSAAERRARVAEALEEVGL----------DPAARHRYPH----EFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 514 LILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTRF-CDSILFMNHGQVLESGTHEQLMA 579
Cdd:COG4172 447 LVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
352-549 |
6.35e-28 |
|
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: 111.79 E-value: 6.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSA--SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanlLPLAERFALF 429
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 430 APVFQE-------TIIlaqslaNNVA----MTEHPD---LNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSG 495
Cdd:cd03293 76 GYVFQQdallpwlTVL------DNVAlgleLQGVPKaeaRERAEELLELVGLSGFENAYPH---------------QLSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 496 GQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISH 549
Cdd:cd03293 135 GMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTH 190
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
369-602 |
9.85e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.28 E-value: 9.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING--LNANL------LPlAERfALFA--PVfQETII 438
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepLDPEDrrrigyLP-EER-GLYPkmKV-GEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 -LAQsLANnvaMTEHPDLNRVTTALTEAGLGTFvktlpqttatpmtrytRDDGVE-LSGGQAQKLMLARALYKDAPVLIL 516
Cdd:COG4152 94 yLAR-LKG---LSKAEAKRRADEWLERLGLGDR----------------ANKKVEeLSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 517 DEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLAST-RFCDSILFMNHGQVLESGTHEQLMAKGGRyaQMYQIQSKY 594
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGR--NTLRLEADG 231
|
....*...
gi 498176791 595 YQPDAKEV 602
Cdd:COG4152 232 DAGWLRAL 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
371-579 |
1.43e-27 |
|
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: 113.22 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHP---ISGTITINGLNANLLPLAERFAL----FAPVFQE-------- 435
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIrgreIQMIFQDpmtslnpv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 -TI--ILAQSLANNVAMTEHPDLNRVTTALTEAGLgtfvkTLPQTTatpMTRYTrddgVELSGGQAQKLMLARALYKDAP 512
Cdd:COG0444 103 mTVgdQIAEPLRIHGGLSKAEARERAIELLERVGL-----PDPERR---LDRYP----HELSGGMRQRVMIARALALEPK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 513 VLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMA 579
Cdd:COG0444 171 LLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAeIADRVAVMYAGRIVEEGPVEELFE 240
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
352-568 |
2.81e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 110.53 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:COG3638 3 LELRNLSKRYPGGTPA-LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 ---VFQE-TIILAQSLANNV---AMTEHP------------DLNRVTTALTEAGLGTFVktlpqttatpmtrYTRDDgvE 492
Cdd:COG3638 82 igmIFQQfNLVPRLSVLTNVlagRLGRTStwrsllglfppeDRERALEALERVGLADKA-------------YQRAD--Q 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 493 LSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHR--LAsTRFCDSILFMNHGQV 568
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQvdLA-RRYADRIIGLRDGRV 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
352-581 |
8.87e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.84 E-value: 8.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGL---NANLLPLAERFAL 428
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 fapVFQ--ETIILAQSLANNVA------MTEHPDLNR-VTTALTEAGlgtfvktlpqttatpMTRYTRDDGVELSGGQAQ 499
Cdd:PRK13648 88 ---VFQnpDNQFVGSIVKYDVAfglenhAVPYDEMHRrVSEALKQVD---------------MLERADYEPNALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 500 KLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGK--TSLFISHRLASTRFCDSILFMNHGQVLESGTHEQL 577
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
....
gi 498176791 578 MAKG 581
Cdd:PRK13648 230 FDHA 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
369-577 |
1.17e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.39 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING--LNANLlPLAER--------FALFaP---VFQe 435
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdLFTNL-PPRERrvgfvfqhYALF-PhmtVAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 tiilaqslanNVA--MTEHPDLN-----RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALY 508
Cdd:COG1118 95 ----------NIAfgLRVRPPSKaeiraRVEELLELVQLEGLADRYPS---------------QLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 509 KDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISH-RLASTRFCDSILFMNHGQVLESGTHEQL 577
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
350-572 |
1.22e-26 |
|
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: 107.84 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 350 VTITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALf 429
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 430 aPVFQETIILAQSLANNVAMTEHPDLNRVTTALTEAGLGTFVKTLPqttatpMTRYTRDDGVELSGGQAQKLMLARALYK 509
Cdd:cd03266 81 -GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLG------MEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLAST-RFCDSILFMNHGQVLESG 572
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
352-577 |
2.35e-26 |
|
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: 108.04 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL--- 428
Cdd:cd03256 1 IEVENLSKTYPNGKKA-LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 FAPVFQE-TIILAQSLANNV---AMTEHP------------DLNRVTTALTEAGLGTFVktlpqttatpmtrYTRDDgvE 492
Cdd:cd03256 80 IGMIFQQfNLIERLSVLENVlsgRLGRRStwrslfglfpkeEKQRALAALERVGLLDKA-------------YQRAD--Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 493 LSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRL-ASTRFCDSILFMNHGQVL 569
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVdLAREYADRIVGLKDGRIV 224
|
....*...
gi 498176791 570 ESGTHEQL 577
Cdd:cd03256 225 FDGPPAEL 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
347-573 |
3.44e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.15 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 347 NRPVTITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERF 426
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 427 ALFAPVFQ-----------ETIIlAQSLAN-NVAMTEHPDLnrVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELS 494
Cdd:PRK13632 83 KKIGIIFQnpdnqfigatvEDDI-AFGLENkKVPPKKMKDI--IDDLAKKVGMEDYLDKEPQ---------------NLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 495 GGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLA--AGKTSLFISHRLASTRFCDSILFMNHGQVLESG 572
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRktRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
.
gi 498176791 573 T 573
Cdd:PRK13632 225 K 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
373-568 |
4.68e-26 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 106.10 E-value: 4.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 373 SFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERfaLFAPVFQETIILAQ-SLANNVAMTE 451
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQR--PVSMLFQENNLFAHlTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 452 HPDLN-------RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLILDEPTAALD 524
Cdd:TIGR01277 96 HPGLKlnaeqqeKVVDAAQQVGIADYLDRLPE---------------QLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498176791 525 AIAENEIYQDYAQLAAGK--TSLFISHRLA-STRFCDSILFMNHGQV 568
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERqrTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
351-577 |
8.16e-26 |
|
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: 106.27 E-value: 8.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 351 TITFAHVNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFa 430
Cdd:cd03296 2 SIEVRNVSKRFGDFVA--LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 pVFQETIILAQ-SLANNVAM-------TEHPDLN----RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQA 498
Cdd:cd03296 79 -VFQHYALFRHmTVFDNVAFglrvkprSERPPEAeiraKVHELLKLVQLDWLADRYPA---------------QLSGGQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 499 QKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISHRLA-STRFCDSILFMNHGQVLESGTHE 575
Cdd:cd03296 143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPD 222
|
..
gi 498176791 576 QL 577
Cdd:cd03296 223 EV 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
369-578 |
8.64e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 106.74 E-value: 8.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFApvfqetiILAQSLANN-- 446
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA-------VLPQHSSLAfp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 ------VAMTEHP-------DLNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARAL------ 507
Cdd:COG4559 90 ftveevVALGRAPhgssaaqDRQIVREALALVGLAHLAGRSYQT---------------LSGGEQQRVQLARVLaqlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 508 -YKDAPVLILDEPTAALDaiaeneIYQDYA------QLAAGKTSLF-ISH--RLAStRFCDSILFMNHGQVLESGTHEQL 577
Cdd:COG4559 155 vDGGPRWLFLDEPTSALD------LAHQHAvlrlarQLARRGGGVVaVLHdlNLAA-QYADRILLLHQGRLVAQGTPEEV 227
|
.
gi 498176791 578 M 578
Cdd:COG4559 228 L 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
369-560 |
1.11e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.88 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanllplaERFALFAP----------VFQETII 438
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---------EPVRFRSPrdaqaagiaiIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 LAQ-SLANNVAMTEHP---------DLNRVTTALTeAGLGtfVKTLPQTTATpmtrytrddgvELSGGQAQKLMLARALY 508
Cdd:COG1129 91 VPNlSVAENIFLGREPrrgglidwrAMRRRARELL-ARLG--LDIDPDTPVG-----------DLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 509 KDAPVLILDEPTAALDaiaENEIyqdyAQL--------AAGKTSLFISHRLAS-TRFCDSI 560
Cdd:COG1129 157 RDARVLILDEPTASLT---EREV----ERLfriirrlkAQGVAIIYISHRLDEvFEIADRV 210
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
348-570 |
1.98e-25 |
|
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: 106.04 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 348 RPVTITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFA 427
Cdd:TIGR02769 6 RDVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 428 L---FAPVFQETI-----------ILAQSLANNVAMTEHPDLNRVTTALTEAGLgtfvktlpqtTATPMTRYTRddgvEL 493
Cdd:TIGR02769 86 FrrdVQLVFQDSPsavnprmtvrqIIGEPLRHLTSLDESEQKARIAELLDMVGL----------RSEDADKLPR----QL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 494 SGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISHRL-ASTRFCDSILFMNHGQVLE 570
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLqqAFGTAYLFITHDLrLVQSFCQRVAVMDKGQIVE 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
352-549 |
2.29e-25 |
|
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: 104.41 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING-----LNANLLPLAERF 426
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 427 alFAPVFQET-IILAQSLANNVAM----TEHP--DLN-RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQA 498
Cdd:cd03292 80 --IGVVFQDFrLLPDRNVYENVAFalevTGVPprEIRkRVPAALELVGLSHKHRALPA---------------ELSGGEQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498176791 499 QKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISH 549
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
369-579 |
3.22e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLL-P---LAERFALfapV----FQETIILA 440
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRsPrdaIRAGIAY---VpedrKGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 441 QSLANNVAMtehPDLNRVTTAL-----TEAGL-GTFVKTL---PQTTATPMTrytrddgvELSGGQAQKLMLARALYKDA 511
Cdd:COG1129 345 LSIRENITL---ASLDRLSRGGlldrrRERALaEEYIKRLrikTPSPEQPVG--------NLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 512 PVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFIShrlaS-----TRFCDSILFMNHGQV---LESG--THEQLMA 579
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELAAeGKAVIVIS----SelpelLGLSDRILVMREGRIvgeLDREeaTEEAIMA 488
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
373-551 |
3.93e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.28 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 373 SFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERfalfaPV---FQETIILAQ-SLANNVA 448
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR-----PVsmlFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEHPDLN-------RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLILDEPTA 521
Cdd:PRK10771 94 LGLNPGLKlnaaqreKLHAIARQMGIEDLLARLPG---------------QLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|..
gi 498176791 522 ALDAIAENEIYQDYAQLAAGK--TSLFISHRL 551
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERqlTLLMVSHSL 190
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
365-579 |
4.53e-25 |
|
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: 103.67 E-value: 4.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 365 KSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAP----VFQEti 437
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgigYVPegrrIFPE-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 ilaQSLANNVAMTEHPDLNRVTTALTEAGLGTFvktlpqttatPM--TRYTRDDGvELSGGQAQKLMLARALYKDAPVLI 515
Cdd:cd03224 90 ---LTVEENLLLGAYARRRAKRKARLERVYELF----------PRlkERRKQLAG-TLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 516 LDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLAST-RFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDeGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
352-587 |
6.65e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.10 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQY----PEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITI-------NGLNANLL 420
Cdd:PRK13634 3 ITFQKVEHRYqyktPFERRA-LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitaGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 421 PLAERFALfapVFQ--------ETIilAQSLA---NNVAMTEHPDLNRVTTALTEAGLGTFVktlpqTTATPMtrytrdd 489
Cdd:PRK13634 82 PLRKKVGI---VFQfpehqlfeETV--EKDICfgpMNFGVSEEDAKQKAREMIELVGLPEEL-----LARSPF------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 490 gvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISHRLA-STRFCDSILFMNHG 566
Cdd:PRK13634 145 --ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEdAARYADQIVVMHKG 222
|
250 260
....*....|....*....|.
gi 498176791 567 QVLESGTHEQLMAKGGRYAQM 587
Cdd:PRK13634 223 TVFLQGTPREIFADPDELEAI 243
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
369-573 |
1.08e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.24 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAerfALFAPVF--QETIILAQSLANn 446
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELG---AGFHPELtgRENIYLNGRLLG- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 vaMTEHpDLNRVTTALTE-AGLGTFVKtlpqttaTPMTRYTrddgvelSGgqaqklMLAR-----ALYKDAPVLILDEPT 520
Cdd:COG1134 118 --LSRK-EIDEKFDEIVEfAELGDFID-------QPVKTYS-------SG------MRARlafavATAVDPDILLVDEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 521 AALDAI----AENEIYQdyaQLAAGKTSLFISHRLAS-TRFCDSILFMNHGQVLESGT 573
Cdd:COG1134 175 AVGDAAfqkkCLARIRE---LRESGRTVIFVSHSMGAvRRLCDRAIWLEKGRLVMDGD 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
352-580 |
1.09e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.11 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPIS---GTITINGLNAN---LLPLAER 425
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTaktVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 426 FALfapVFQ--ETIILAQSLANNVAM-TEHPDLNR------VTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGG 496
Cdd:PRK13640 86 VGI---VFQnpDNQFVGATVGDDVAFgLENRAVPRpemikiVRDVLADVGMLDYIDSEPAN---------------LSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 497 QAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGK--TSLFISHRLASTRFCDSILFMNHGQVLESGTH 574
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
....*.
gi 498176791 575 EQLMAK 580
Cdd:PRK13640 228 VEIFSK 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
369-577 |
2.39e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.99 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLN-----ANLLPLAERFALfapVFQ--------- 434
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdskKDINKLRRKVGM---VFQqfnlfphlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 --ETIILAQSL--------ANNVAMTEhpdLNRVttalteaGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLA 504
Cdd:COG1126 94 vlENVTLAPIKvkkmskaeAEERAMEL---LERV-------GLADKADAYPA---------------QLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 505 RALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLastRF----CDSILFMNHGQVLESGTHEQL 577
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKeGMTMVVVTHEM---GFarevADRVVFMDGGRIVEEGPPEEF 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
371-580 |
2.68e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 104.04 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP---VFQE---------TI- 437
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRmqmVFQDpyaslnprmTVg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 -ILAQSLANNVAMTEHPDLNRVTTALTEAGLGtfvktlpqttATPMTRYTRddgvELSGGQAQKLMLARALYKDAPVLIL 516
Cdd:COG4608 116 dIIAEPLRIHGLASKAERRERVAELLELVGLR----------PEHADRYPH----EFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498176791 517 DEPTAALD-AIaeneiyQdyAQ-------LAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMAK 580
Cdd:COG4608 182 DEPVSALDvSI------Q--AQvlnlledLQDelGLTYLFISHDLSVVRhISDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
352-579 |
2.71e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.76 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNA-NLLPLAERFALFA 430
Cdd:PRK13644 2 IRLENVSYSYPDGTPA-LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQ--ETIILAQSLANNVAMTEH----PDL---NRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKL 501
Cdd:PRK13644 81 IVFQnpETQFVGRTVEEDLAFGPEnlclPPIeirKRVDRALAEIGLEKYRHRSPKT---------------LSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 502 MLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
369-579 |
4.06e-24 |
|
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: 101.36 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL-FAPVFQETIILAQ-SLANN 446
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 VAMTEHPDL-----------------NRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYK 509
Cdd:cd03219 96 VMVAAQARTgsglllararreerearERAEELLERVGLADLADRPAG---------------ELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 510 DAPVLILDEPTAALdAIAENEiyqDYAQL-----AAGKTSLFISHRLAS-TRFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:cd03219 161 DPKLLLLDEPAAGL-NPEETE---ELAELirelrERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
352-578 |
5.03e-24 |
|
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: 101.31 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISG-TITING---LNANLLPLAERFA 427
Cdd:COG1119 4 LELRNVTVRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 428 LFAPVFQETIILAQSlANNVAMT---------EHP---DLNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSG 495
Cdd:COG1119 82 LVSPALQLRFPRDET-VLDVVLSgffdsiglyREPtdeQRERARELLELLGLAHLADRPFGT---------------LSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 496 GQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLAS-----TRfcdsILFMNHGQV 568
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEippgiTH----VLLLKDGRV 221
|
250
....*....|
gi 498176791 569 LESGTHEQLM 578
Cdd:COG1119 222 VAAGPKEEVL 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
362-573 |
6.60e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.05 E-value: 6.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 362 PEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLN-----ANLLPLAERFALfapVFQ-- 434
Cdd:PRK13637 17 PFEKKA-LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkVKLSDIRKKVGL---VFQyp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 ------ETIilAQSLA---NNVAMTEHPDLNRVTTALTEAGLgtfvktlpqttatPMTRYTRDDGVELSGGQAQKLMLAR 505
Cdd:PRK13637 93 eyqlfeETI--EKDIAfgpINLGLSEEEIENRVKRAMNIVGL-------------DYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 506 ALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGK--TSLFISHRLAS-TRFCDSILFMNHGQVLESGT 573
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDvAKLADRIIVMNKGKCELQGT 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
369-573 |
8.58e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 103.25 E-value: 8.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAER--------FALFaP---VFQeti 437
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRnvgmvfqdYALF-PhltVAE--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 ilaqslanNVA-------MTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKD 510
Cdd:COG3842 97 --------NVAfglrmrgVPKAEIRARVAELLELVGLEGLADRYPH---------------QLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 511 APVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISH------RLAstrfcDSILFMNHGQVLESGT 573
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHdqeealALA-----DRIAVMNDGRIEQVGT 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
369-580 |
1.10e-23 |
|
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: 106.53 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanllplaeRFAlFAPvfQETIILAQSLANNVA 448
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------RIS-FSP--QTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAE 528
Cdd:TIGR01271 509 FGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLG----EGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498176791 529 NEIYQD-YAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAK 580
Cdd:TIGR01271 585 KEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
362-580 |
2.36e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 101.19 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 362 PEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAPVFQ---- 434
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkIQIVFQnpyg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 -----ETI--ILAQSLANNVAMTEHPDLNRVTTALTEAGLGT-FVKTLPQttatpMtrytrddgveLSGGQAQKLMLARA 506
Cdd:PRK11308 104 slnprKKVgqILEEPLLINTSLSAAERREKALAMMAKVGLRPeHYDRYPH-----M----------FSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 507 LYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMAK 580
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEhIADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
312-607 |
4.06e-23 |
|
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: 105.03 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 312 LQNASIDLQEVREFMN---LQPQT-PTRTLTETEQKQLANRPVTITFAhvnyqypEAKSASLKDVSFTLQAGQKLAIVGI 387
Cdd:TIGR00957 600 IVQASVSLKRLRIFLSheeLEPDSiERRTIKPGEGNSITVHNATFTWA-------RDLPPTLNGITFSIPEGALVAVVGQ 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 388 NGAGKSTLARLMMGLLHPISGTITINGLNAnllplaerfalFAPvfQETIILAQSLANNVAMTEHPDLNRVTTALTEAGL 467
Cdd:TIGR00957 673 VGCGKSSLLSALLAEMDKVEGHVHMKGSVA-----------YVP--QQAWIQNDSLRENILFGKALNEKYYQQVLEACAL 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 468 GTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDY---AQLAAGKTS 544
Cdd:TIGR00957 740 LPDLEILPSGDRTEIG----EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTR 815
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498176791 545 LFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYqiqsKYYQPDAKEVIADGN 607
Cdd:TIGR00957 816 ILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL----RTYAPDEQQGHLEDS 874
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
214-586 |
5.96e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 104.34 E-value: 5.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 214 ALENGKDIRMFGMANWYHRHLDRLIQLQDAWQRRNSLRRFLGEQIGQLAGLLRDAIVYGTLIVAIMRGSLSI-----SQF 288
Cdd:PTZ00265 1028 AFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVddfmkSLF 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 289 TLMFgmTNSFItllDQLLDDFGKLQNASIDLQEVREFMNLQPQTPTRTLTETEQKQLANRPVTITFAHVNYQYPEAKSAS 368
Cdd:PTZ00265 1108 TFLF--TGSYA---GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVP 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 L-KDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLL-----HPI------------------------------------ 406
Cdd:PTZ00265 1183 IyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndHHIvfknehtndmtneqdyqgdeeqnvgmknvnefsltk 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 407 -------------SGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAM-TEHPDLNRVTTALTEAGLGTFVK 472
Cdd:PTZ00265 1263 eggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFgKEDATREDVKRACKFAAIDEFIE 1342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 473 TLPQTTATPMTRYtrddGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISHR 550
Cdd:PTZ00265 1343 SLPNKYDTNVGPY----GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHR 1418
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 498176791 551 LASTRFCDSILFMNH----GQVLES-GTHEQLM-AKGGRYAQ 586
Cdd:PTZ00265 1419 IASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLsVQDGVYKK 1460
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
369-568 |
6.11e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanllplaERFALFAP----------VFQ---- 434
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---------KPVRIRSPrdaialgigmVHQhfml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 -------ETIILAQSLANNVAmtehPDLNRVTTALTEA----GLgtfvktlpqttATPMTRYTRDdgveLSGGQAQKLML 503
Cdd:COG3845 92 vpnltvaENIVLGLEPTKGGR----LDRKAARARIRELseryGL-----------DVDPDAKVED----LSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 504 ARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLAS-TRFCDSILFMNHGQV 568
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAeGKSIIFITHKLREvMAIADRVTVLRRGKV 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
369-578 |
6.25e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.31 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFApvfqetiILAQSLANN-- 446
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA-------VLPQHSSLSfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 ------VAM-------TEHPDLNRVTTALTEAGLGTFVktlpqttatpmTRYTRddgvELSGGQAQKLMLARAL------ 507
Cdd:PRK13548 91 ftveevVAMgraphglSRAEDDALVAAALAQVDLAHLA-----------GRDYP----QLSGGEQQRVQLARVLaqlwep 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 508 YKDAPVLILDEPTAALDaiaeneIY--QDYAQLA------AGKTSLFISH--RLAStRFCDSILFMNHGQVLESGTHEQL 577
Cdd:PRK13548 156 DGPPRWLLLDEPTSALD------LAhqHHVLRLArqlaheRGLAVIVVLHdlNLAA-RYADRIVLLHQGRLVADGTPAEV 228
|
.
gi 498176791 578 M 578
Cdd:PRK13548 229 L 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
369-572 |
7.15e-23 |
|
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: 96.97 E-value: 7.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLP------LAERFALFAPV-FQETIILAQ 441
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigyLPEERGLYPKMkVIDQLVYLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 442 SLANnvaMTEHPDLNRVTTALTEAGLGTFvktlpqttatpmtRYTRDDgvELSGGQAQKLMLARALYKDAPVLILDEPTA 521
Cdd:cd03269 96 QLKG---LKKEEARRRIDEWLERLELSEY-------------ANKRVE--ELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498176791 522 ALDAIAENEIYQDYAQLA-AGKTSLFISHRLAST-RFCDSILFMNHGQVLESG 572
Cdd:cd03269 158 GLDPVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
369-577 |
7.52e-23 |
|
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: 98.78 E-value: 7.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanllplaeRFAlFAPvfQETIILAQSLANNVA 448
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------RIS-FSS--QFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAE 528
Cdd:cd03291 120 FGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLG----EGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498176791 529 NEIYQD-YAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQL 577
Cdd:cd03291 196 KEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
369-578 |
8.98e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLP---LAERFALFA--PVFQETIilaqSL 443
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsrqLARRLALLPqhHLTPEGI----TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 444 ANNVAMTEHPDLN-----------RVTTALTEAGLGTFVKTlpqttatPMTrytrddgvELSGGQAQKLMLARALYKDAP 512
Cdd:PRK11231 94 RELVAYGRSPWLSlwgrlsaednaRVNQAMEQTRINHLADR-------RLT--------DLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 513 VLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRL--AStRFCDSILFMNHGQVLESGTHEQLM 578
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLnqAS-RYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
369-568 |
2.45e-22 |
|
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: 95.29 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLN-----ANLLPLAERFALfapVFQ--------- 434
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddkKNINELRQKVGM---VFQqfnlfphlt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 --ETIILAQSLANNvaMTEHPDLNRVTTALTEAGLgtfvktLPQTTATPmtrytrddgVELSGGQAQKLMLARALYKDAP 512
Cdd:cd03262 93 vlENITLAPIKVKG--MSKAEAEERALELLEKVGL------ADKADAYP---------AQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 513 VLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLASTR-FCDSILFMNHGQV 568
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
269-587 |
2.66e-22 |
|
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: 102.33 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 269 IVYGTLIVAIMRGSLSISQFTLMFGMTNSFITLLDQLLDDFGKLQNASIDLQEVREFMNLQPQTPTRtLTETEQKQLANR 348
Cdd:TIGR00957 1203 VLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQ-IQETAPPSGWPP 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 349 PVTITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAE-RFA 427
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlRFK 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 428 LfAPVFQETIILAQSLANNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQTtatpMTRYTRDDGVELSGGQAQKLMLARAL 507
Cdd:TIGR00957 1362 I-TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDK----LDHECAEGGENLSVGQRQLVCLARAL 1436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 508 YKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQM 587
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
351-575 |
3.31e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 96.88 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 351 TITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING------LNANLL---P 421
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqptrqaLQKNLVayvP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 422 LAERFALFAPVFQETIILAQSLAnNVAMTEHP---DLNRVTTALTEAGLGTFvktlpqttatpmtRYtRDDGvELSGGQA 498
Cdd:PRK15056 85 QSEEVDWSFPVLVEDVVMMGRYG-HMGWLRRAkkrDRQIVTAALARVDMVEF-------------RH-RQIG-ELSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 499 QKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLAS-TRFCDSILfMNHGQVLESGTHE 575
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSvTEFCDYTV-MVKGTVLASGPTE 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
352-570 |
4.25e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 96.29 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEA----KSAS---LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAE 424
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgKHQHqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 425 RFAL---FAPVFQETI-----------ILAQSLANNVAMTEHPDLNRVTTALTEAGLG-TFVKTLPQttatpmtrytrdd 489
Cdd:PRK10419 84 RKAFrrdIQMVFQDSIsavnprktvreIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPP------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 490 gvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISH--RLAStRFCDSILFMNH 565
Cdd:PRK10419 151 --QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHdlRLVE-RFCQRVMVMDN 227
|
....*
gi 498176791 566 GQVLE 570
Cdd:PRK10419 228 GQIVE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
369-579 |
4.46e-22 |
|
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: 100.14 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHP----ISGTITINGlnANLLPLAERfAL-------FAPVFQE-- 435
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDG--QDLLGLSER-ELrrirgnrIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 -------TI--ILAQSLANNVAMTEHPDLNRVTTALTEAGLgtfvktlPQTtATPMTRYTRddgvELSGGQAQKLMLARA 506
Cdd:COG4172 103 tslnplhTIgkQIAEVLRLHRGLSGAAARARALELLERVGI-------PDP-ERRLDAYPH----QLSGGQRQRVMIAMA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 507 LYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMA 579
Cdd:COG4172 171 LANEPDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRrFADRVAVMRQGEIVEQGPTAELFA 246
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
369-584 |
4.50e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.47 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLN------ANL----------------LPLAERF 426
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrrkEFArrigvvfgqrsqlwwdLPAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 427 ALFAPVFQetiILAQSLANNVAMtehpdlnrvttaLTEA-GLGTFVKTlpqttatpMTRytrddgvELSGGQAQKLMLAR 505
Cdd:COG4586 118 RLLKAIYR---IPDAEYKKRLDE------------LVELlDLGELLDT--------PVR-------QLSLGQRMRCELAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 506 ALYKDAPVLILDEPTAALDAIAENEIYQ---DYAQlAAGKTSLFISHRLAS-TRFCDSILFMNHGQVLESGTHEQLMAKG 581
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREflkEYNR-ERGTTILLTSHDMDDiEALCDRVIVIDHGRIIYDGSLEELKERF 246
|
...
gi 498176791 582 GRY 584
Cdd:COG4586 247 GPY 249
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
352-577 |
4.54e-22 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 95.44 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLN------ANLLPLAER 425
Cdd:TIGR02315 2 LEVENLSKVYPNGKQA-LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitklrgKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 426 FALfapVFQE-TIILAQSLANNVAmteHPDLNRVTTalTEAGLGTFVKTLPQTTATPMTR-------YTRDDgvELSGGQ 497
Cdd:TIGR02315 81 IGM---IFQHyNLIERLTVLENVL---HGRLGYKPT--WRSLLGRFSEEDKERALSALERvgladkaYQRAD--QLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 498 AQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLA-STRFCDSILFMNHGQVLESGTH 574
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKedGITVIINLHQVDlAKKYADRIVGLKAGEIVFDGAP 230
|
...
gi 498176791 575 EQL 577
Cdd:TIGR02315 231 SEL 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
356-573 |
5.36e-22 |
|
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: 94.88 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 356 HVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNAnllpLAERFAlfapVFQE 435
Cdd:cd03263 5 NLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKA----ARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 TIILAQSLANNVAMT--EH------------PDLNRVTTALTEA-GLGTFVKTLPQTtatpmtrytrddgveLSGGQAQK 500
Cdd:cd03263 77 LGYCPQFDALFDELTvrEHlrfyarlkglpkSEIKEEVELLLRVlGLTDKANKRART---------------LSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498176791 501 LMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLA-STRFCDSILFMNHGQVLESGT 573
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDeAEALCDRIAIMSDGKLRCIGS 215
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
352-586 |
6.20e-22 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 96.08 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHpISGTITINGLNANLLPLAERFALFAP 431
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDA 511
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLV----DGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498176791 512 PVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQ 586
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
369-572 |
8.53e-22 |
|
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: 93.82 E-value: 8.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNA-NLLPLAERFAlfapvfqeTIILAQSLANNv 447
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqKNIEALRRIG--------ALIEAPGFYPN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 aMTEHPDL-----------NRVTTALTEAGLGTfvktlpqttatpmtryTRDDGV-ELSGGQAQKLMLARALYKDAPVLI 515
Cdd:cd03268 87 -LTARENLrllarllgirkKRIDEVLDVVGLKD----------------SAKKKVkGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 516 LDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLAS-TRFCDSILFMNHGQVLESG 572
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDqGITVLISSHLLSEiQKVADRIGIINKGKLIEEG 208
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
369-580 |
9.55e-22 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 94.98 E-value: 9.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVA 448
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAE 528
Cdd:cd03288 117 PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVT----EGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498176791 529 NeIYQDYAQLA-AGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAK 580
Cdd:cd03288 193 N-ILQKVVMTAfADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
369-579 |
1.25e-21 |
|
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: 94.72 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL-FAPVFQETIILAQ-SLANN 446
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 V--AMTEHPDLNRVTTALteaGLGTFVKTLPQTTATPM--------TRYTRDDGVELSGGQAQKLMLARALYKDAPVLIL 516
Cdd:COG0411 100 VlvAAHARLGRGLLAALL---RLPRARREEREARERAEellervglADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 517 DEPTAALDAiAE-NEIYQDYAQLAA--GKTSLFISHRL-ASTRFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:COG0411 177 DEPAAGLNP-EEtEELAELIRRLRDerGITILLIEHDMdLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
352-587 |
1.86e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.80 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQY-PEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFA 430
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQ--ETIILAQSLANNVAM------TEHPDL-NRVTTALTEAGLGTFVKTLPqttatpmtrytrddgVELSGGQAQKL 501
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFglenkgIPHEEMkERVNEALELVGMQDFKEREP---------------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 502 MLARALYKDAPVLILDEPTAALDAIAENE-------IYQDYaqlaaGKTSLFISHRLASTRFCDSILFMNHGQVLESGTH 574
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLEliktikgIRDDY-----QMTVISITHDLDEVALSDRVLVMKNGQVESTSTP 224
|
250
....*....|...
gi 498176791 575 EQLMAKGGRYAQM 587
Cdd:PRK13650 225 RELFSRGNDLLQL 237
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
369-570 |
1.94e-21 |
|
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: 93.27 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnANLLPLAE--RFAL------FapVFQETiila 440
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG--QDLFALDEdaRARLrarhvgF--VFQSF---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 441 QSLAN-----NVAM----TEHPDL-NRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKD 510
Cdd:COG4181 100 QLLPTltaleNVMLplelAGRRDArARARALLERVGLGHRLDHYPA---------------QLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 511 APVLILDEPTAALDA-----IAE-----NEiyqdyaqlAAGKTSLFISHRLASTRFCDSILFMNHGQVLE 570
Cdd:COG4181 165 PAILFADEPTGNLDAatgeqIIDllfelNR--------ERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
286-589 |
1.98e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 99.67 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 286 SQFTLMFGMTNSFITLLDQLLDDFGKLQNASIDLQEVREFMNLQPQTPTrtLTETeqkqlaNRPVT-------ITFAHVN 358
Cdd:PLN03232 1170 STMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATA--IIEN------NRPVSgwpsrgsIKFEDVH 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 359 YQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETII 438
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 LAQSLANNV-AMTEHPDLNrvttaLTEAGLGTFVKTLPQTTATPMTRYTRDDGVELSGGQAQKLMLARALYKDAPVLILD 517
Cdd:PLN03232 1322 FSGTVRFNIdPFSEHNDAD-----LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498176791 518 EPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAK-GGRYAQMYQ 589
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRdTSAFFRMVH 1469
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-577 |
2.17e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.81 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 342 QKQLANRPVTITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLN-ANLL 420
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 421 P-LAERFALFApVFQETIILA-QSLANNVA--MTEHPDLNRVTTALTeAGLGTFVKtLPQTTATpmtrytrddgVELSGG 496
Cdd:PRK15439 80 PaKAHQLGIYL-VPQEPLLFPnLSVKENILfgLPKRQASMQKMKQLL-AALGCQLD-LDSSAGS----------LEVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 497 QAQKLMlaRALYKDAPVLILDEPTAALDAIAENEIY-QDYAQLAAGKTSLFISHRLASTR-FCDSILFMNHGQVLESGTH 574
Cdd:PRK15439 147 QIVEIL--RGLMRDSRILILDEPTASLTPAETERLFsRIRELLAQGVGIVFISHKLPEIRqLADRISVMRDGTIALSGKT 224
|
...
gi 498176791 575 EQL 577
Cdd:PRK15439 225 ADL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
369-568 |
3.03e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING------------LNANLLPLAERFALFAPVFQet 436
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqeppLDDDLTVLDTVLDGDAELRA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 iILAQSLANNVAMTEH-PDLNRVTTALTE-----------------AGLGtfvktLPQTTA-TPMTrytrddgvELSGGQ 497
Cdd:COG0488 92 -LEAELEELEAKLAEPdEDLERLAELQEEfealggweaearaeeilSGLG-----FPEEDLdRPVS--------ELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 498 AQKLMLARALYKDAPVLILDEPTAALD--AIA--ENEIyQDYAqlaagKTSLFISH-RlastRF----CDSILFMNHGQV 568
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDleSIEwlEEFL-KNYP-----GTVLVVSHdR----YFldrvATRILELDRGKL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
369-572 |
3.80e-21 |
|
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: 92.21 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAerfALFAPVF--QETIILAQSLaNN 446
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG---GGFNPELtgRENIYLNGRL-LG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 VAMTEHPDLNRVTTALTEagLGTFVKtlpqttaTPMTRYtrddgvelSGGQAQKLMLARALYKDAPVLILDEPTAALDA- 525
Cdd:cd03220 114 LSRKEIDEKIDEIIEFSE--LGDFID-------LPVKTY--------SSGMKARLAFAIATALEPDILLIDEVLAVGDAa 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 526 --------IAEneiyqdyaQLAAGKTSLFISHRLASTR-FCDSILFMNHGQVLESG 572
Cdd:cd03220 177 fqekcqrrLRE--------LLKQGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
351-549 |
3.93e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.39 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 351 TITFAHVNYQYPEAKSA--SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlNANLLPLAERfal 428
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-VPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 fAPVFQETIILA-QSLANNVA-------MTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQK 500
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAfglrlrgVPKAERRARAEELLALVGLADFARRRIW---------------QLSGGMRQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498176791 501 LMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISH 549
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH 193
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
371-572 |
4.35e-21 |
|
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: 91.97 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQaGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING-------LNANLLPLAERFALfapVFQE-TIILAQS 442
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQRKIGL---VFQQyALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 443 LANNVA-----MTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLILD 517
Cdd:cd03297 92 VRENLAfglkrKRNREDRISVDELLDLLGLDHLLNRYPA---------------QLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 518 EPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLAST-RFCDSILFMNHGQVLESG 572
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
354-572 |
6.22e-21 |
|
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: 92.01 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 354 FAHVNYQYPEAksasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanLLPLAERFALFApvf 433
Cdd:cd03267 26 LFKRKYREVEA----LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKFLR--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 434 QETIILAQ--SLANNVAMTEHPDLNRVTTALTEAGLGTFVKTLpqttaTPMTRYTR--DDGV-ELSGGQAQKLMLARALY 508
Cdd:cd03267 95 RIGVVFGQktQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDEL-----SELLDLEEllDTPVrQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 509 KDAPVLILDEPTAALDAIAENEIYQ--DYAQLAAGKTSLFISHRLAS-TRFCDSILFMNHGQVLESG 572
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNflKEYNRERGTTVLLTSHYMKDiEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
350-579 |
1.55e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.20 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 350 VTITFAHVNYQY-PEA--KSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGL-------NANL 419
Cdd:PRK13641 1 MSIKFENVDYIYsPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpetgNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 420 LPLAERFALF-----APVFQETIILAQSLA-NNVAMTEHPDLNRVTTALTEAGLGTFVktlpqTTATPMtrytrddgvEL 493
Cdd:PRK13641 81 KKLRKKVSLVfqfpeAQLFENTVLKDVEFGpKNFGFSEDEAKEKALKWLKKVGLSEDL-----ISKSPF---------EL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 494 SGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENE---IYQDYAqlAAGKTSLFISHRLAS-TRFCDSILFMNHGQVL 569
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEmmqLFKDYQ--KAGHTVILVTHNMDDvAEYADDVLVLEHGKLI 224
|
250
....*....|
gi 498176791 570 ESGTHEQLMA 579
Cdd:PRK13641 225 KHASPKEIFS 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
350-588 |
1.95e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 350 VTITFAHVNYQY----PEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGL-------NAN 418
Cdd:PRK13646 1 MTIRFDNVSYTYqkgtPYEHQA-IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDItithktkDKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 419 LLPLAERFALfapVFQ--ETIILAQSL-------ANNVAMTEHPDLNRVTTALTEAGLGTFVKTLpqttaTPMtrytrdd 489
Cdd:PRK13646 80 IRPVRKRIGM---VFQfpESQLFEDTVereiifgPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQ-----SPF------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 490 gvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYA--QLAAGKTSLFISHRLAS-TRFCDSILFMNHG 566
Cdd:PRK13646 145 --QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSHDMNEvARYADEVIVMKEG 222
|
250 260
....*....|....*....|..
gi 498176791 567 QVLESGTHEQLMAKGGRYAQMY 588
Cdd:PRK13646 223 SIVSQTSPKELFKDKKKLADWH 244
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
369-561 |
2.02e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanllplAERFALfapVFQETII---LAQSLAN 445
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--------GARVAY---VPQRSEVpdsLPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 446 NVAM-----------TEHPDLNRVTTALTEAGLGTFVKtlpqttatpmtRYTRddgvELSGGQAQKLMLARALYKDAPVL 514
Cdd:NF040873 77 LVAMgrwarrglwrrLTRDDRAAVDDALERVGLADLAG-----------RQLG----ELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498176791 515 ILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLASTRFCDSIL 561
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCV 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
369-579 |
2.32e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLhPISGTITING-----LN-ANLLPLAERFALfapVFQE------- 435
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGqplhnLNrRQLLPVRHRIQV---VFQDpnsslnp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 ----TIILAQSLAnnvamTEHPDLN------RVTTALTEAGLgtfvktlpqttaTPMTRYTRDdgVELSGGQAQKLMLAR 505
Cdd:PRK15134 378 rlnvLQIIEEGLR-----VHQPTLSaaqreqQVIAVMEEVGL------------DPETRHRYP--AEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 506 ALYKDAPVLILDEPTAALDAIAENEI------YQDYAQLAagktSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLM 578
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQIlallksLQQKHQLA----YLFISHDLHVVRaLCHQVIVLRQGEVVEQGDCERVF 514
|
.
gi 498176791 579 A 579
Cdd:PRK15134 515 A 515
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
351-577 |
2.34e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.83 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 351 TITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFalFA 430
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRN--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQetiilaqSLAN--------NVAM------TEHPDLN-RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSG 495
Cdd:COG3839 79 MVFQ-------SYALyphmtvyeNIAFplklrkVPKAEIDrRVREAAELLGLEDLLDRKPK---------------QLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 496 GQAQKLMLARALYKDAPVLILDEPTAALDA----IAENEIYQDYAQLaaGKTSLFISH------RLAstrfcDSILFMNH 565
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL--GTTTIYVTHdqveamTLA-----DRIAVMND 209
|
250
....*....|..
gi 498176791 566 GQVLESGTHEQL 577
Cdd:COG3839 210 GRIQQVGTPEEL 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
360-577 |
3.72e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.08 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 360 QYPEAKSASLK---DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING---LNANLLPLAERFALFAPVF 433
Cdd:PRK15079 25 QWFWQPPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 434 QE---------TI--ILAQSLannvaMTEHPDL------NRVTTALTEAGLgtfvktLPQTtatpMTRYTRddgvELSGG 496
Cdd:PRK15079 105 QDplaslnprmTIgeIIAEPL-----RTYHPKLsrqevkDRVKAMMLKVGL------LPNL----INRYPH----EFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 497 QAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGT 573
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGT 245
|
....
gi 498176791 574 HEQL 577
Cdd:PRK15079 246 YDEV 249
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
351-575 |
5.83e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 89.30 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 351 TITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanllplaERFALFA 430
Cdd:COG4161 2 SIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG---------HQFDFSQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQETIilaQSLANNVAMTEH-----PDLNrVTTALTEAGlgtfVKTLPQTTATPM-------TRYTRDDGVE-----L 493
Cdd:COG4161 71 KPSEKAI---RLLRQKVGMVFQqynlwPHLT-VMENLIEAP----CKVLGLSKEQARekamkllARLRLTDKADrfplhL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 494 SGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLASTRFCDS-ILFMNHGQVLES 571
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASqVVYMEKGRIIEQ 222
|
....
gi 498176791 572 GTHE 575
Cdd:COG4161 223 GDAS 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
352-573 |
5.83e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 91.29 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSA--SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLnaNLLPLAER---- 425
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGV--DLTALSERelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 426 -----------FALFApvfQETIilaqslANNVAM------TEHPD-LNRVTTALTEAGLGTFVKTLPQttatpmtrytr 487
Cdd:COG1135 80 arrkigmifqhFNLLS---SRTV------AENVALpleiagVPKAEiRKRVAELLELVGLSDKADAYPS----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 488 ddgvELSGGQAQKLMLARALYKDAPVLILDEPTAALD-----AIAE--NEIYQDYaqlaaGKTSLFISH-----RlastR 555
Cdd:COG1135 140 ----QLSGGQKQRVGIARALANNPKVLLCDEATSALDpettrSILDllKDINREL-----GLTIVLITHemdvvR----R 206
|
250
....*....|....*...
gi 498176791 556 FCDSILFMNHGQVLESGT 573
Cdd:COG1135 207 ICDRVAVLENGRIVEQGP 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
371-581 |
7.24e-20 |
|
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: 91.33 E-value: 7.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNAN------LLPLAERfaLFAPVFQETII-----L 439
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrkgiFLPPEKR--RIGYVFQEARLfphlsV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 440 AQSLANNVAMTEHPDLNRVTTALTEA-GLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLILDE 518
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELlGIGHLLGRLPGR---------------LSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 519 PTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLAST-RFCDSILFMNHGQVLESGTHEQLMAKG 581
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
356-572 |
7.31e-20 |
|
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: 88.40 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 356 HVNYQYPeaKSASLKDVSFTLQAGQkLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL-FAPvfQ 434
Cdd:cd03264 5 NLTKRYG--KKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIgYLP--Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 ETIILAQ----------SLANNVAMTEHPdlNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLA 504
Cdd:cd03264 80 EFGVYPNftvrefldyiAWLKGIPSKEVK--ARVDEVLELVNLGDRAKKKIGS---------------LSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 505 RALYKDAPVLILDEPTAALDaIAENEIYQDY-AQLAAGKTSLFISH---RLASTrfCDSILFMNHGQVLESG 572
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLD-PEERIRFRNLlSELGEDRIVILSTHiveDVESL--CNQVAVLNKGKLVFEG 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
345-586 |
7.88e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.26 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 345 LANRPVTITFAHVNYQYPEAksasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANL----- 419
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEV----LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 420 --LPLAERFALfapvfqetiilaQSLANNVAMT-EHPDLNRVTTALtEAGLGTFVKTLPQTTATPMTRYTR-------DD 489
Cdd:PRK10619 77 gqLKVADKNQL------------RLLRTRLTMVfQHFNLWSHMTVL-ENVMEAPIQVLGLSKQEARERAVKylakvgiDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 490 G------VELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLA-AGKTSLFISHRLASTRFCDS-IL 561
Cdd:PRK10619 144 RaqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVSShVI 223
|
250 260
....*....|....*....|....*..
gi 498176791 562 FMNHGQVLESGTHEQLMA--KGGRYAQ 586
Cdd:PRK10619 224 FLHQGKIEEEGAPEQLFGnpQSPRLQQ 250
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
349-575 |
8.72e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 8.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 349 PVTITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNanlLPLAERFAL 428
Cdd:PRK13536 39 TVAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP---VPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 ----FAPVFqETIILAQSLANNVAMteHPDLNRVTTALTEAGLGTFVK--TLPQTTATPMTrytrddgvELSGGQAQKLM 502
Cdd:PRK13536 114 arigVVPQF-DNLDLEFTVRENLLV--FGRYFGMSTREIEAVIPSLLEfaRLESKADARVS--------DLSGGMKRRLT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 503 LARALYKDAPVLILDEPTAALDAIAENEIYQDY-AQLAAGKTSLFISHRL-ASTRFCDSILFMNHG-QVLESGTHE 575
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLrSLLARGKTILLTTHFMeEAERLCDRLCVLEAGrKIAEGRPHA 258
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
349-572 |
1.43e-19 |
|
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: 86.84 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 349 PVTITFAHVNYQYPEAKSAS----LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHP--ISGTITINGLNANLLPL 422
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 423 AERFALfapVFQETIIlaqslannvamteHPDLnrvttalteaglgTFVKTLpqttatpmtRYTrddgVEL---SGGQAQ 499
Cdd:cd03213 81 RKIIGY---VPQDDIL-------------HPTL-------------TVRETL---------MFA----AKLrglSGGERK 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 500 KLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLA-AGKTSLFISHRLASTRF--CDSILFMNHGQVLESG 572
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSEIFelFDKLLLLSQGRVIYFG 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
369-568 |
1.49e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAPV--FQETIILAQSL 443
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvaYIPEdrLGRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 444 ANNVAMTEHPD--------LNR-VTTALTEAGLGTF-VKTlpQTTATPMTRytrddgveLSGGQAQKLMLARALYKDAPV 513
Cdd:COG3845 354 AENLILGRYRRppfsrggfLDRkAIRAFAEELIEEFdVRT--PGPDTPARS--------LSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498176791 514 LILDEPTAALDAIAENEIYQdyaQL----AAGKTSLFISH------RLastrfCDSILFMNHGQV 568
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIHQ---RLlelrDAGAAVLLISEdldeilAL-----SDRIAVMYEGRI 480
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
369-579 |
1.72e-19 |
|
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: 87.60 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAPvfQETIILAQ-SLA 444
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgigYLP--QEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 445 NNV--AMTEHPDLNRVTTALTEAGLGTF-VKTLPQTTAtpmtrytrddgVELSGGQAQKLMLARALYKDAPVLILDEPTA 521
Cdd:cd03218 94 ENIlaVLEIRGLSKKEREEKLEELLEEFhITHLRKSKA-----------SSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 522 ALDAIAENEIYQDYAQLAAGKTSLFIS-HRLAST-RFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETlSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
366-578 |
1.81e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.86 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 366 SASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAE----RFALFAPVFQETIILAQ 441
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 442 -SLANNVA-------MTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPV 513
Cdd:PRK10070 121 mTVLDNTAfgmelagINAEERREKALDALRQVGLENYAHSYPD---------------ELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 514 LILDEPTAALDAIAENEIYQDYAQLAAG--KTSLFISHRL-ASTRFCDSILFMNHGQVLESGTHEQLM 578
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
352-577 |
1.90e-19 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 87.68 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERfaLFAP 431
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR--PVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQ-SLANNVA-------MTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLML 503
Cdd:cd03300 77 VFQNYALFPHlTVFENIAfglrlkkLPKAEIKERVAEALDLVQLEGYANRKPS---------------QLSGGQQQRVAI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 504 ARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISH--RLASTrFCDSILFMNHGQVLESGTHEQL 577
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHdqEEALT-MSDRIAVMNKGKIQQIGTPEEI 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
339-570 |
4.32e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 339 ETEQKQLANRPVTITFA-------------HVNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHP 405
Cdd:COG0488 290 EREEPPRRDKTVEIRFPpperlgkkvleleGLSKSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 406 ISGTITInGLNAnllplaeRFALFApvfQETIILaqslannvamteHPDLnRVTTALTEAGlgtfvktlPQTTATPMTRY 485
Cdd:COG0488 368 DSGTVKL-GETV-------KIGYFD---QHQEEL------------DPDK-TVLDELRDGA--------PGGTEQEVRGY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 486 ------TRDD-----GVeLSGGQAQKLMLARALYKDAPVLILDEPT-----AALDAIaeNEIYQDYaqlaAGkTSLFISH 549
Cdd:COG0488 416 lgrflfSGDDafkpvGV-LSGGEKARLALAKLLLSPPNVLLLDEPTnhldiETLEAL--EEALDDF----PG-TVLLVSH 487
|
250 260
....*....|....*....|..
gi 498176791 550 -RLASTRFCDSILFMNHGQVLE 570
Cdd:COG0488 488 dRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
361-549 |
4.55e-19 |
|
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: 85.55 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 361 YPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING--LNANLLPLAERFALFAPVFQ--ET 436
Cdd:TIGR01166 1 YPGGPEV-LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepLDYSRKGLLERRQRVGLVFQdpDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 IILAQSLANNVA-------MTEHPDLNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYK 509
Cdd:TIGR01166 80 QLFAADVDQDVAfgplnlgLSEAEVERRVREALTAVGASGLRERPTHC---------------LSGGEKKRVAIAGAVAM 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISH 549
Cdd:TIGR01166 145 RPDVLLLDEPTAGLDPAGREQMLAILRRLrAEGMTVVISTH 185
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
368-577 |
4.61e-19 |
|
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: 86.27 E-value: 4.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 368 SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERfalfapvfqETI-ILAQSLANN 446
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR---------RRIgIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 VAMTEHPDL---------------NRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDA 511
Cdd:cd03265 86 DELTGWENLyiharlygvpgaerrERIDELLDFVGLLEAADRLVKT---------------YSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 512 PVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRL-ASTRFCDSILFMNHGQVLESGTHEQL 577
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMeEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
369-579 |
4.76e-19 |
|
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: 86.57 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAP----VF-----QET 436
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgigYVPegrrIFpsltvEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 IILAQSLANNVAmTEHPDLNRVttalteagLGTFvktlpqttatPM--TRYTRdDGVELSGGQAQKLMLARALYKDAPVL 514
Cdd:COG0410 99 LLLGAYARRDRA-EVRADLERV--------YELF----------PRlkERRRQ-RAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 515 ILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRL-ASTRFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNReGVTILLVEQNArFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
352-567 |
4.84e-19 |
|
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: 84.04 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITInglnanllplaerfalfap 431
Cdd:cd03221 1 IELENLSKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 vfqetiilaqslannvamteHPDLNrvttalteaglgtfVKTLPQttatpmtrytrddgveLSGGQAQKLMLARALYKDA 511
Cdd:cd03221 60 --------------------GSTVK--------------IGYFEQ----------------LSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 512 PVLILDEPTAALDAIA----ENEIyQDYAQlaagkTSLFISH-RLASTRFCDSILFMNHGQ 567
Cdd:cd03221 90 NLLLLDEPTNHLDLESiealEEAL-KEYPG-----TVILVSHdRYFLDQVATKIIELEDGK 144
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
369-572 |
5.29e-19 |
|
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: 86.17 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHP---ISGTITING--LNANLLPlaERFA------LFAPVF--QE 435
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGqpRKPDQFQ--KCVAyvrqddILLPGLtvRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 TI----ILA----QSLANNVAMTEHPDLNRVttALTEAGlGTFVKTLpqttatpmtrytrddgvelSGGQAQKLMLARAL 507
Cdd:cd03234 101 TLtytaILRlprkSSDAIRKKRVEDVLLRDL--ALTRIG-GNLVKGI-------------------SGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 508 YKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFIS-HRLAST--RFCDSILFMNHGQVLESG 572
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiHQPRSDlfRLFDRILLLSSGEIVYSG 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
369-572 |
6.42e-19 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 85.77 E-value: 6.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFalFAPVFQETIILAQ-SLANNV 447
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--IAMVFQNYALYPHmTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 AmteHP-DLNRVTTALTEAGLGTFVKTLpqTTATPMTRYTRddgvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAI 526
Cdd:cd03301 94 A---FGlKLRKVPKDEIDERVREVAELL--QIEHLLDRKPK----QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498176791 527 AENEIYQDYAQLAA--GKTSLFISH-RLASTRFCDSILFMNHGQVLESG 572
Cdd:cd03301 165 LRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
369-577 |
6.73e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 86.63 E-value: 6.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLM--MGLLHP---ISGTITINGLN-----ANLLPLAERFALfapVFQETII 438
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPgarVEGEILLDGEDiydpdVDVVELRRRVGM---VFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 LAQSLANNVA-------MTEHPDLN-RVTTALTEAGLGTFVKT-LpqttatpmtrytRDDGVELSGGQAQKLMLARALYK 509
Cdd:COG1117 104 FPKSIYDNVAyglrlhgIKSKSELDeIVEESLRKAALWDEVKDrL------------KKSALGLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 510 DAPVLILDEPTAALDAIA----ENEIY---QDYaqlaagkTSLFISHRLA-STRFCDSILFMNHGQVLESGTHEQL 577
Cdd:COG1117 172 EPEVLLMDEPTSALDPIStakiEELILelkKDY-------TIVIVTHNMQqAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
352-578 |
6.92e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.29 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLP---LAERFAl 428
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsreLAKRLA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 fapvfqetiILAQSlaNNVAM--------------------TEHpDLNRVTTALTEAGLGTFVKtlpqttatpmtRYTrD 488
Cdd:COG4604 79 ---------ILRQE--NHINSrltvrelvafgrfpyskgrlTAE-DREIIDEAIAYLDLEDLAD-----------RYL-D 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 489 dgvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLA--AGKTSLFISHRL--AStRFCDSILFMN 564
Cdd:COG4604 135 ---ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDInfAS-CYADHIVAMK 210
|
250
....*....|....
gi 498176791 565 HGQVLESGTHEQLM 578
Cdd:COG4604 211 DGRVVAQGTPEEII 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
352-589 |
7.02e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 91.34 E-value: 7.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP 431
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQSLANNV-AMTEHPDLNrVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKD 510
Cdd:PLN03130 1318 IPQAPVLFSGTVRFNLdPFNEHNDAD-LWESLERAHLKDVIRRNSLGLDAEVS----EAGENFSVGQRQLLSLARALLRR 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 511 APVLILDEPTAAL----DAIAENEIYQDYAQLaagkTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAK-GGRYA 585
Cdd:PLN03130 1393 SKILVLDEATAAVdvrtDALIQKTIREEFKSC----TMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNeGSAFS 1468
|
....
gi 498176791 586 QMYQ 589
Cdd:PLN03130 1469 KMVQ 1472
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
352-573 |
8.86e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.93 E-value: 8.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSA--SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING-----LNANLLPLAE 424
Cdd:PRK11153 2 IELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltaLSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 425 RfaLFAPVFQETIILA-QSLANNVAM------TEHPDLN-RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGG 496
Cdd:PRK11153 82 R--QIGMIFQHFNLLSsRTVFDNVALplelagTPKAEIKaRVTELLELVGLSDKADRYPA---------------QLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 497 QAQKLMLARALYKDAPVLILDEPTAALD-----AIAE--NEIYQDYaqlaaGKTSLFISHRLAST-RFCDSILFMNHGQV 568
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDpattrSILEllKDINREL-----GLTIVLITHEMDVVkRICDRVAVIDAGRL 219
|
....*
gi 498176791 569 LESGT 573
Cdd:PRK11153 220 VEQGT 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
352-573 |
9.24e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.68 E-value: 9.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSA----SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNA----NLLPLA 423
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdeeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 424 ERFALfapVFQ--ETIILAQSLANNVAMTEH-----PD--LNRVTTALTEAGlgtfvktlpqttatpMTRYTRDDGVELS 494
Cdd:PRK13633 85 NKAGM---VFQnpDNQIVATIVEEDVAFGPEnlgipPEeiRERVDESLKKVG---------------MYEYRRHAPHLLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 495 GGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTRFCDSILFMNHGQVLESG 572
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
.
gi 498176791 573 T 573
Cdd:PRK13633 227 T 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
352-570 |
1.12e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.91 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLlPLAERfalfAP 431
Cdd:PRK11248 2 LQISHLYADYGGKPA--LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILA-QSLANNVAMtehpdlnrvttALTEAGLGtfvKTLPQTTATPMTRYTRDDGVE------LSGGQAQKLMLA 504
Cdd:PRK11248 75 VFQNEGLLPwRNVQDNVAF-----------GLQLAGVE---KMQRLEIAHQMLKKVGLEGAEkryiwqLSGGQRQRVGIA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 505 RALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTRFCDSILFM---NHGQVLE 570
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITHDIEEAVFMATELVLlspGPGRVVE 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
352-579 |
1.16e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.17 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEakSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnaNLLPLAERFAL--- 428
Cdd:PRK13537 8 IDFRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG---EPVPSRARHARqrv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 -FAPVF---------QETIILaqsLANNVAMTEHPDLNRVTTALTEAGLgtfvktlpQTTATPMTRytrddgvELSGGQA 498
Cdd:PRK13537 83 gVVPQFdnldpdftvRENLLV---FGRYFGLSAAAARALVPPLLEFAKL--------ENKADAKVG-------ELSGGMK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 499 QKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDY-AQLAAGKTSLFISHRL-ASTRFCDSILFMNHGQVLESGTHEQ 576
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLrSLLARGKTILLTTHFMeEAERLCDRLCVIEEGRKIAEGAPHA 224
|
...
gi 498176791 577 LMA 579
Cdd:PRK13537 225 LIE 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
356-580 |
1.32e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 356 HVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNAN-----LLPLAERFALfa 430
Cdd:PRK13636 10 ELNYNYSDGTHA-LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkgLMKLRESVGM-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 pVFQ--ETIILAQSL-------ANNVAMTEHPDLNRVTTALTEAGLgTFVKTLPQTTatpmtrytrddgveLSGGQAQKL 501
Cdd:PRK13636 87 -VFQdpDNQLFSASVyqdvsfgAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHC--------------LSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 502 MLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLM 578
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
..
gi 498176791 579 AK 580
Cdd:PRK13636 231 AE 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
369-577 |
1.59e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFapVFQETIILAQ-SLANNV 447
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGF--VFQHYALFRHmTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 AM-------TEHPDL----NRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLIL 516
Cdd:PRK10851 96 AFgltvlprRERPNAaaikAKVTQLLEMVQLAHLADRYPA---------------QLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498176791 517 DEPTAALDAIAENEIYQDYAQLAA--GKTSLFISH-RLASTRFCDSILFMNHGQVLESGTHEQL 577
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
369-575 |
2.07e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.17 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING------------LNANLLPLAERFALFAPVFQET 436
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklrigyvpqklyLDTTLPLTVNRFLRLRPGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 IILaqslannvamtehPDLNRVTTA-LTEAglgtfvktlpqttatPMTRytrddgveLSGGQAQKLMLARALYKDAPVLI 515
Cdd:PRK09544 100 DIL-------------PALKRVQAGhLIDA---------------PMQK--------LSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 516 LDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISHRL----ASTrfcDSILFMNHgQVLESGTHE 575
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLrrELDCAVLMVSHDLhlvmAKT---DEVLCLNH-HICCSGTPE 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
369-528 |
2.10e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPvfQETIILAQSLANNVA 448
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGH--RNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEH---PDLNRVTTALTEAGLGTfVKTLPqttatpmtrytrddGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDA 525
Cdd:PRK13539 96 FWAAflgGEELDIAAALEAVGLAP-LAHLP--------------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
...
gi 498176791 526 IAE 528
Cdd:PRK13539 161 AAV 163
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
372-578 |
2.56e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.60 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 372 VSFTLQAGQKLAIVGINGAGKSTLARLMMGLLhPISGTITINGLNANLLPLAE---RFALFA---------PVFQetiIL 439
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElarHRAYLSqqqtppfamPVFQ---YL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 440 AQSLANNVAMTEHPD-LNRVTTALteaGLGTFvktLPQTTATpmtrytrddgveLSGGQAQKLMLA-------RALYKDA 511
Cdd:PRK03695 91 TLHQPDKTRTEAVASaLNEVAEAL---GLDDK---LGRSVNQ------------LSGGEWQRVRLAavvlqvwPDINPAG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 512 PVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLAST-RFCDSILFMNHGQVLESGTHEQLM 578
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELCQqGIAVVMSSHDLNHTlRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
360-586 |
2.58e-18 |
|
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: 89.58 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 360 QYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHpISGTITINGLNANLLPLAERFALFAPVFQETIIL 439
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 440 AQSLANNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEP 519
Cdd:TIGR01271 1305 SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLV----DGGYVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 520 TAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQ 586
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
368-579 |
2.59e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.23 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 368 SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETI---------- 437
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 -ILAQSLANNVAMTEHPDLNRVTTALTEAGLgtfvktLP-QTTATPMTrytrddgveLSGGQAQKLMLARALYKDAPVLI 515
Cdd:PRK15112 108 qILDFPLRLNTDLEPEQREKQIIETLRQVGL------LPdHASYYPHM---------LAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 516 LDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMA 579
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
341-577 |
2.87e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.76 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 341 EQKQLANRPVTITFAHVNYQYPeaksaSLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGL----- 415
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIA-----AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 416 NANLLPLAE---------RFALFAPVFQETII-------LAQSLANNVAMteHPDLNRvTTALTEAGLGTFVKTLPQTTA 479
Cdd:PRK10261 84 SRQVIELSEqsaaqmrhvRGADMAMIFQEPMTslnpvftVGEQIAESIRL--HQGASR-EEAMVEAKRMLDQVRIPEAQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 480 TpMTRYTRddgvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQ--DYAQLAAGKTSLFISHRLA-STRF 556
Cdd:PRK10261 161 I-LSRYPH----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQKEMSMGVIFITHDMGvVAEI 235
|
250 260
....*....|....*....|.
gi 498176791 557 CDSILFMNHGQVLESGTHEQL 577
Cdd:PRK10261 236 ADRVLVMYQGEAVETGSVEQI 256
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
329-561 |
4.30e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.94 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 329 QPQTPTRTLTETEQKQLANRPVTITFAhvNYQypeaksASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISG 408
Cdd:COG4178 347 ALPEAASRIETSEDGALALEDLTLRTP--DGR------PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 409 TITinglnanlLPLAERfALFAPvfQETIILAQSLANNVA---MTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtry 485
Cdd:COG4178 419 RIA--------RPAGAR-VLFLP--QRPYLPLGTLREALLypaTAEAFSDAELREALEAVGLGHLAERLDE--------- 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 486 TRDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSIL 561
Cdd:COG4178 479 EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
371-579 |
4.34e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 86.31 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING-------LNANLLPLAERFALfapVFQETII----- 438
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsaRGIFLPPHRRRIGY---VFQEARLfphls 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 ----LAQSLANNVAMTEHPDLNRVTTALteaGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDAPVL 514
Cdd:COG4148 94 vrgnLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPAT---------------LSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 515 ILDEPTAALDAIAENEIYqDYAQLAAGKTS---LFISHRLAS-TRFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:COG4148 156 LMDEPLAALDLARKAEIL-PYLERLRDELDipiLYVSHSLDEvARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
330-586 |
6.93e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 330 PQTPTRTLTETEQKQLA---NRPVTITFAHVnYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPI 406
Cdd:PRK15439 238 PAAREKSLSASQKLWLElpgNRRQQAAGAPV-LTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 407 SGTITINGLNANLLPLAERFALfAPVF------QETIILAQSLANNVAmtehpdlnrvttALTEAGLGTFVKtlPQTTAT 480
Cdd:PRK15439 317 GGRIMLNGKEINALSTAQRLAR-GLVYlpedrqSSGLYLDAPLAWNVC------------ALTHNRRGFWIK--PARENA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 481 PMTRYTRDDGVE----------LSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTS-LFISH 549
Cdd:PRK15439 382 VLERYRRALNIKfnhaeqaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAvLFISS 461
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 498176791 550 RLAST-RFCDSILFMNHGQVLESGTHEQL-------MAKGGRYAQ 586
Cdd:PRK15439 462 DLEEIeQMADRVLVMHQGEISGALTGAAInvdtimrLAFGEHQAQ 506
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
359-573 |
7.59e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.97 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 359 YQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGL-----NANLLPLAERFA------ 427
Cdd:PRK13639 9 YSYPDGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydKKSLLEVRKTVGivfqnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 428 ---LFAPVFQETIILAQSlanNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLA 504
Cdd:PRK13639 88 ddqLFAPTVEEDVAFGPL---NLGLSKEEVEKRVKEALKAVGMEGFENKPPH---------------HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 505 RALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHR---LASTrFCDSILFMNHGQVLESGT 573
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHdvdLVPV-YADKVYVMSDGKIIKEGT 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
271-565 |
8.07e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.78 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 271 YGTLIVAIMRGSLsISQFTLMFGMTNsfitlldqlLDDFGKLQNASIDLQEVrefMNLQPqtptrtLTETEQ--KQLANR 348
Cdd:PTZ00265 320 HGGSVISILLGVL-ISMFMLTIILPN---------ITEYMKSLEATNSLYEI---INRKP------LVENNDdgKKLKDI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 349 PvTITFAHVNYQYPEAKSASL-KDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlNANLLPLAERF- 426
Cdd:PTZ00265 381 K-KIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-SHNLKDINLKWw 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 427 -ALFAPVFQETIILAQSLANNV-----------AMTEH-----------------------PDLNRVTTALTEAGL---- 467
Cdd:PTZ00265 459 rSKIGVVSQDPLLFSNSIKNNIkyslyslkdleALSNYynedgndsqenknkrnscrakcaGDLNDMSNTTDSNELiemr 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 468 --------------------GTFVKTLPQTTATpmtrYTRDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIA 527
Cdd:PTZ00265 539 knyqtikdsevvdvskkvliHDFVSALPDKYET----LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 498176791 528 ENEIYQDYAQLAA--GKTSLFISHRLASTRFCDSILFMNH 565
Cdd:PTZ00265 615 EYLVQKTINNLKGneNRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
372-576 |
8.63e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 8.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 372 VSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnANLLPLAERFALFAPVF-------QETIILAQSLA 444
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG--KPIDIRSPRDAIRAGIMlcpedrkAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 445 NNVAMTEHPDLNR---VTTALTEAGLG-TFVKTLPQTTATPmtrytRDDGVELSGGQAQKLMLARALYKDAPVLILDEPT 520
Cdd:PRK11288 350 DNINISARRHHLRagcLINNRWEAENAdRFIRSLNIKTPSR-----EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 521 AALDAIAENEIYQDYAQLAA-GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQ 576
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLPEVLgVADRIVVMREGRIAGELAREQ 482
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
280-593 |
1.01e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 87.72 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 280 RGSLSISQFTLMFGMTNSFITLLDQLLddfgklqNASIDLQEVREFMnlqpQTPTRTLTETEQKQLANRPVTITFAHVNY 359
Cdd:PLN03232 556 RAFTSLSLFAVLRSPLNMLPNLLSQVV-------NANVSLQRIEELL----LSEERILAQNPPLQPGAPAISIKNGYFSW 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 360 QYPEAKSaSLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGT-ITINGLNAnllplaerfalFAPvfQETII 438
Cdd:PLN03232 625 DSKTSKP-TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsVVIRGSVA-----------YVP--QVSWI 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 LAQSLANNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDE 518
Cdd:PLN03232 691 FNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIG----ERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 519 PTAALDAIAENEIYQDYAQLA-AGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQIQSK 593
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGK 842
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
369-579 |
1.11e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.88 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANL-LPLAERFALFAPVFQETIILAQSLannv 447
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTaRSLSQQKGLIRQLRQHVGFVFQNF---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 amtehpDLNRVTTALTEAGLG-TFVKTLPQTTATPMTR--------------YTRddgvELSGGQAQKLMLARALYKDAP 512
Cdd:PRK11264 95 ------NLFPHRTVLENIIEGpVIVKGEPKEEATARARellakvglagketsYPR----RLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 513 VLILDEPTAALDAIAENEIYQDYAQLAAGK-TSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMA 579
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
359-577 |
1.68e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.93 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 359 YQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQE--- 435
Cdd:PRK13652 11 YSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNpdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 ---TIILAQSLA---NNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYK 509
Cdd:PRK13652 90 qifSPTVEQDIAfgpINLGLDEETVAHRVSSALHMLGLEELRDRVPH---------------HLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLA-STRFCDSILFMNHGQVLESGTHEQL 577
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
356-577 |
1.80e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 84.01 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 356 HVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHP---ISGTITINGlnANLLPLAE------RF 426
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNG--REILNLPEkelnklRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 427 ALFAPVFQEtiilaqslannvAMTEhpdLN---RVTTALTEA-----GLG---TFVKTLPQTTATPMTRYTRDDGV---E 492
Cdd:PRK09473 97 EQISMIFQD------------PMTS---LNpymRVGEQLMEVlmlhkGMSkaeAFEESVRMLDAVKMPEARKRMKMyphE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 493 LSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAE-------NEIYQDYaqlaaGKTSLFISHRLASTR-FCDSILFMN 564
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQaqimtllNELKREF-----NTAIIMITHDLGVVAgICDKVLVMY 236
|
250
....*....|...
gi 498176791 565 HGQVLESGTHEQL 577
Cdd:PRK09473 237 AGRTMEYGNARDV 249
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
363-579 |
2.26e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.05 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 363 EAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHP----ISGTITINGLNanLLPLAERFALFAPVFQEtii 438
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKP--VAPCALRGRKIATIMQN--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 lAQSLANNV-AMTEH-----------PDLNRVTTALTEAGLGTfVKTLPQTTAtpmtrytrddgVELSGGQAQKLMLARA 506
Cdd:PRK10418 88 -PRSAFNPLhTMHTHaretclalgkpADDATLTAALEAVGLEN-AARVLKLYP-----------FEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 507 LYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLA-STRFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQkrALGMLLVTHDMGvVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-568 |
4.19e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.67 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 350 VTITFahvNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALF 429
Cdd:COG1101 7 LSKTF---NPGTVNEKRA-LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 430 APVFQ-------------ETIILAQ--------SLANNVAMTEHpdlnrVTTALTEAGLGtfvktLPQTTATPMtrytrd 488
Cdd:COG1101 83 GRVFQdpmmgtapsmtieENLALAYrrgkrrglRRGLTKKRREL-----FRELLATLGLG-----LENRLDTKV------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 489 dGVeLSGGQAQKLMLARALYKDAPVLILDEPTAALD-AIAE------NEIYQDYaQLaagkTSLFISHRLA-STRFCDSI 560
Cdd:COG1101 147 -GL-LSGGQRQALSLLMATLTKPKLLLLDEHTAALDpKTAAlvleltEKIVEEN-NL----TTLMVTHNMEqALDYGNRL 219
|
....*...
gi 498176791 561 LFMNHGQV 568
Cdd:COG1101 220 IMMHEGRI 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
368-572 |
5.95e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 368 SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL-FAPVFQE-TIILAQSLAN 445
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 446 NVAMTEHPdlnrvttalTEAGLGTFV---KTLPQTTATPMTRY----TRDDGV-ELSGGQAQKLMLARALYKDAPVLILD 517
Cdd:PRK09700 100 NLYIGRHL---------TKKVCGVNIidwREMRVRAAMMLLRVglkvDLDEKVaNLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 518 EPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLASTR-FCDSILFMNHGQVLESG 572
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRrICDRYTVMKDGSSVCSG 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
362-581 |
6.34e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 85.17 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 362 PEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPIS-GTITINGLnanllplaerfalFAPVFQETIILA 440
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------------VAYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 441 QSLANNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPT 520
Cdd:PLN03130 693 ATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIG----ERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 521 AALDAIAENEIYQDYAQLA-AGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMAKG 581
Cdd:PLN03130 769 SALDAHVGRQVFDKCIKDElRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNG 830
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
371-577 |
1.08e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.19 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAER--------FALFAPVFQEtiilaQS 442
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRpinmmfqsYALFPHMTVE-----QN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 443 LANNVAMTEHPD---LNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLILDEP 519
Cdd:PRK11607 112 IAFGLKQDKLPKaeiASRVNEMLGLVHMQEFAKRKPH---------------QLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 520 TAALDaiaenEIYQDYAQLA-------AGKTSLFISH-RLASTRFCDSILFMNHGQVLESGTHEQL 577
Cdd:PRK11607 177 MGALD-----KKLRDRMQLEvvdilerVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
369-579 |
1.16e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERF-ALFAPVFQE-----------T 436
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALaAGVAIIYQElhlvpemtvaeN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 IILAQsLANNVAMTEHPDLNRVTTALTEaGLGtfVKTLPQttaTPMTRytrddgveLSGGQAQKLMLARALYKDAPVLIL 516
Cdd:PRK11288 100 LYLGQ-LPHKGGIVNRRLLNYEAREQLE-HLG--VDIDPD---TPLKY--------LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498176791 517 DEPTAALDAiaeNEIYQDYA---QL-AAGKTSLFISHRLAST-RFCDSILFMNHGQV------LESGTHEQLMA 579
Cdd:PRK11288 165 DEPTSSLSA---REIEQLFRvirELrAEGRVILYVSHRMEEIfALCDAITVFKDGRYvatfddMAQVDRDQLVQ 235
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
369-578 |
1.26e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLhPISGTITINGLNANLLPLAE--RF---------ALFA-PVFQet 436
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElaRHraylsqqqsPPFAmPVFQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 iILAQSLAnnvAMTEHPDLNRVTTALTEA-GLGTFVktlpqttATPMTRytrddgveLSGGQAQKLMLARALYK------ 509
Cdd:COG4138 89 -YLALHQP---AGASSEAVEQLLAQLAEAlGLEDKL-------SRPLTQ--------LSGGEWQRVRLAAVLLQvwptin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 510 -DAPVLILDEPTAALDAIAENEIYQDYAQLA-AGKTSLFISHRLAST-RFCDSILFMNHGQVLESGTHEQLM 578
Cdd:COG4138 150 pEGQLLLLDEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNHTlRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
372-549 |
1.49e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.30 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 372 VSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAMTe 451
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 452 HPDLNR--VTTALTEAGLGTFvKTLPQTTatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAEN 529
Cdd:cd03231 98 HADHSDeqVEEALARVGLNGF-EDRPVAQ--------------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|.
gi 498176791 530 EIYQDYAQ-LAAGKTSLFISH 549
Cdd:cd03231 163 RFAEAMAGhCARGGMVVLTTH 183
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
365-580 |
1.56e-16 |
|
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: 79.30 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 365 KSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAER--------FALFAPV-FQE 435
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRdisyvpqnYALFPHMtVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 TIILAQSLANNVAMTEHPDLNRVTTALteaGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLI 515
Cdd:cd03299 91 NIAYGLKKRKVDKKEIERKVLEIAEML---GIDHLLNRKPET---------------LSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 516 LDEPTAALDA-IAENEIYQ-DYAQLAAGKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMAK 580
Cdd:cd03299 153 LDEPFSALDVrTKEKLREElKKIRKEFGVTVLHVTHDFEEAWaLADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
369-577 |
1.62e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTL-----ARLMMGLLhpISGTITINGLNANLLPLAERFA------LFAPVF--QE 435
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLmnalaFRSPKGVK--GSGSVLLNGMPIDAKEMRAISAyvqqddLFIPTLtvRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 TIILAQSLANNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQTTatpmtrytrDDGVELSGGQAQKLMLARALYKDAPVLI 515
Cdd:TIGR00955 119 HLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVP---------GRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498176791 516 LDEPTAALDAIAENEIYQDYAQLA-AGKTSLFISHRLASTRFC--DSILFMNHGQVLESGTHEQL 577
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQA 254
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
352-573 |
1.81e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.16 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQY-PEAKSAS--LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGL-------NANLLP 421
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 422 LAERFALF-----APVFQETIILAQSLA-NNVAMTEHPDLNRVTTALTEAGLGTfvktlpqttatpmtRYTRDDGVELSG 495
Cdd:PRK13643 82 VRKKVGVVfqfpeSQLFEETVLKDVAFGpQNFGIPKEKAEKIAAEKLEMVGLAD--------------EFWEKSPFELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 496 GQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLASTR-FCDSILFMNHGQVLESGT 573
Cdd:PRK13643 148 GQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGT 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
351-575 |
1.96e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 351 TITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanllplaERFALFA 430
Cdd:PRK11124 2 SIQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAG---------NHFDFSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQETIilaQSLANNVAMTEH-----PDLNrVTTALTEA-----GLGtfvKTLPQTTATP-MTRYTRDDGVE-----LS 494
Cdd:PRK11124 71 TPSDKAI---RELRRNVGMVFQqynlwPHLT-VQQNLIEApcrvlGLS---KDQALARAEKlLERLRLKPYADrfplhLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 495 GGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLASTRFCDS-ILFMNHGQVLESG 572
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASrVVYMENGHIVEQG 223
|
...
gi 498176791 573 THE 575
Cdd:PRK11124 224 DAS 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
369-573 |
2.40e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.15 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAER--------FALFaP---VFQeti 437
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRhvntvfqsYALF-PhmtVFE--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 ilaqslanNVA----MTEHPDLN---RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKD 510
Cdd:PRK09452 106 --------NVAfglrMQKTPAAEitpRVMEALRMVQLEEFAQRKPH---------------QLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 511 APVLILDEPTAALDA----IAENEIYQDYAQLaaGKTSLFISH----RLASTrfcDSILFMNHGQVLESGT 573
Cdd:PRK09452 163 PKVLLLDESLSALDYklrkQMQNELKALQRKL--GITFVFVTHdqeeALTMS---DRIVVMRDGRIEQDGT 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
156-570 |
2.52e-16 |
|
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: 82.15 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 156 IVFLATLSfavPWVFALVLVSAAIsyaGMSWYRHWYLQNNVKWNKLGRQQDYitrnayalengkdirmfgmanwYHRHLD 235
Cdd:COG4615 139 LAYLAWLS---PPLFLLTLVLLGL---GVAGYRLLVRRARRHLRRAREAEDR----------------------LFKHFR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 236 RLIQ----LQDAWQRRnslRRFLGEQIGQLAGLLRDAIV-----------------YGT--LIVAIMRGSLSISQFTL-M 291
Cdd:COG4615 191 ALLEgfkeLKLNRRRR---RAFFDEDLQPTAERYRDLRIradtifalannwgnllfFALigLILFLLPALGWADPAVLsG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 292 FGMTNSFITL-LDQLLDDFGKLQNASIDLQEVREfMNLQPQTPTRTLTETEQKQLANRPVTITFAHVNYQYPEAKSAS-- 368
Cdd:COG4615 268 FVLVLLFLRGpLSQLVGALPTLSRANVALRKIEE-LELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEgf 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 -LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING--LNANLLplaERF-ALFAPVFQEtIILAQSLA 444
Cdd:COG4615 347 tLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqpVTADNR---EAYrQLFSAVFSD-FHLFDRLL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 445 NnvaMTEHPDLNRVTTALTEAGLGTFVktlpqttatpmtryTRDDG----VELSGGQAQKLMLARALYKDAPVLILDEPT 520
Cdd:COG4615 423 G---LDGEADPARARELLERLELDHKV--------------SVEDGrfstTDLSQGQRKRLALLVALLEDRPILVFDEWA 485
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 521 AalDaiaeneiyQD-------YAQL-----AAGKTSLFISH-----RLAstrfcDSILFMNHGQVLE 570
Cdd:COG4615 486 A--D--------QDpefrrvfYTELlpelkARGKTVIAISHddryfDLA-----DRVLKMDYGKLVE 537
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
372-525 |
2.81e-16 |
|
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: 77.40 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 372 VSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLnanllPLAERfalfAPVFQETIIL---AQSLANNVA 448
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-----PLAEQ----RDEPHENILYlghLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTE-----HPDL----NRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLILDEP 519
Cdd:TIGR01189 90 ALEnlhfwAAIHggaqRTIEDALAAVGLTGFEDLPAAQ---------------LSAGQQRRLALARLWLSRRPLWILDEP 154
|
....*.
gi 498176791 520 TAALDA 525
Cdd:TIGR01189 155 TTALDK 160
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
359-568 |
3.33e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 359 YQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL----FAPVFQ 434
Cdd:PRK11629 15 YQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 ETIILAQSLA-NNVAMtehPDL----------NRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLML 503
Cdd:PRK11629 95 FHHLLPDFTAlENVAM---PLLigkkkpaeinSRALEMLAAVGLEHRANHRPS---------------ELSGGERQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 504 ARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISHRLASTRFCDSILFMNHGQV 568
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
369-579 |
4.00e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.15 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQklaIVGI---NGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAPvfQETIILAQ- 441
Cdd:COG1137 19 VKDVSLEVNQGE---IVGLlgpNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgigYLP--QEASIFRKl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 442 SLANNV-AMTEHPDLN------RVTTALTEAGLGTFVKTLpqttatpmtrytrddGVELSGGQAQKLMLARALYKDAPVL 514
Cdd:COG1137 94 TVEDNIlAVLELRKLSkkereeRLEELLEEFGITHLRKSK---------------AYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 515 ILDEPTAALDAIAENEIYQDYAQLAAGKTSLFIS-HRLAST-RFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITdHNVRETlGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
369-570 |
5.27e-16 |
|
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: 77.51 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLlPLAERFAlfapVFQETIILA-QSLANNV 447
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV----VFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 AMTehpdLNRVTTALTEAGLGTFVKTLPQTTATPMTRYTRDDgvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIA 527
Cdd:TIGR01184 76 ALA----VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPG--QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498176791 528 ENEIYQDYAQLA--AGKTSLFISHRLASTRF-CDSILFMNH------GQVLE 570
Cdd:TIGR01184 150 RGNLQEELMQIWeeHRVTVLMVTHDVDEALLlSDRVVMLTNgpaaniGQILE 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
371-579 |
8.45e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.36 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPIS-GTITINGLnanllPLAERfalfAPvfqetiilAQSLANNVAM 449
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGK-----PVKIR----NP--------QQAIAQGIAM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 450 TEH--------PDL-----------------NRVTTALTEAGLGTFVKTLPQTTATPMTRYTRddgveLSGGQAQKLMLA 504
Cdd:PRK13549 343 VPEdrkrdgivPVMgvgknitlaaldrftggSRIDDAAELKTILESIQRLKVKTASPELAIAR-----LSGGNQQKAVLA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 505 RALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLASTR-FCDSILFMNHGQ-----VLESGTHEQL 577
Cdd:PRK13549 418 KCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVLgLSDRVLVMHEGKlkgdlINHNLTQEQV 497
|
..
gi 498176791 578 MA 579
Cdd:PRK13549 498 ME 499
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
359-549 |
8.73e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.92 E-value: 8.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 359 YQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLL---PLAE-RFALFAPVFQ 434
Cdd:PRK10535 14 YPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQlRREHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 ETIILAQ-SLANNV-------AMTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARA 506
Cdd:PRK10535 94 RYHLLSHlTAAQNVevpavyaGLERKQRLLRAQELLQRLGLEDRVEYQPS---------------QLSGGQQQRVSIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498176791 507 LYKDAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISH 549
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTH 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
371-579 |
1.06e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLH--PI---SGTITING---LNANLLPL-AERFALFAPVFQETII--- 438
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGeslLHASEQTLrGVRGNKIAMIFQEPMVsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 ----LAQSLANNVAMteHPDLNRvttaltEAGLGTFVKTLPQTTATPMTRYTRDDGVELSGGQAQKLMLARALYKDAPVL 514
Cdd:PRK15134 107 plhtLEKQLYEVLSL--HRGMRR------EAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 515 ILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMA 579
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRkLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
328-577 |
1.69e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.59 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 328 LQPQTPTRTLTETEQkqlanrPVTITFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPIS 407
Cdd:PTZ00243 1291 IEPASPTSAAPHPVQ------AGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCG 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 408 GTITINGLNANLLPLAERFALFAPVFQETIILAQSLANNVAMTEHPDLNRVTTALTEAGLGTFVKTlpqtTATPMTRYTR 487
Cdd:PTZ00243 1365 GEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVAS----ESEGIDSRVL 1440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 488 DDGVELSGGQAQKLMLARALYKDAPVLIL-DEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLASTRFCDSILFMNHG 566
Cdd:PTZ00243 1441 EGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
250
....*....|.
gi 498176791 567 QVLESGTHEQL 577
Cdd:PTZ00243 1521 AVAEMGSPREL 1531
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
369-568 |
1.82e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.64 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTitingLNANLLPLAERFALFAPVFQETIILA-QSLANNV 447
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-----LLAGTAPLAEAREDTRLMFQDARLLPwKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 AMTEHPDL-NRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLILDEPTAALDAI 526
Cdd:PRK11247 103 GLGLKGQWrDAALQALAAVGLADRANEWPAA---------------LSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498176791 527 AENEIYQDYAQL--AAGKTSLFISHRLA-STRFCDSILFMNHGQV 568
Cdd:PRK11247 168 TRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
352-552 |
1.97e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.68 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING-----LNANLLPLAERf 426
Cdd:PRK10908 2 IRFEHVSKAYLGGRQA-LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrLKNREVPFLRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 427 aLFAPVFQE-TIILAQSLANNVAM------TEHPDL-NRVTTALTEAGLGTFVKTLPqttatpmtrytrddgVELSGGQA 498
Cdd:PRK10908 80 -QIGMIFQDhHLLMDRTVYDNVAIpliiagASGDDIrRRVSAALDKVGLLDKAKNFP---------------IQLSGGEQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 499 QKLMLARALYKDAPVLILDEPTAALD-AIAEN--EIYQDYAQLaaGKTSLFISHRLA 552
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTGNLDdALSEGilRLFEEFNRV--GVTVLMATHDIG 198
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
352-578 |
1.98e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 76.28 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAER-FALFA 430
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 P-VFQETIILAQSLA-NNVAM-------TEHPDLNRVTTAL-TEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQK 500
Cdd:PRK09493 80 GmVFQQFYLFPHLTAlENVMFgplrvrgASKEEAEKQARELlAKVGLAERAHHYPS---------------ELSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 501 LMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLA-AGKTSLFISHRLASTRFCDS-ILFMNHGQVLESGTHEQLM 578
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLI 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
323-579 |
4.05e-15 |
|
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: 78.33 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 323 REFMNLQPQTPTrtltETEQKQLANRPVTItfahvnYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGL 402
Cdd:TIGR02633 240 REITSLYPHEPH----EIGDVILEARNLTC------WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 403 lHP--ISGTITINGLNANLLPLAERFALFAPVFQET-----IILAQSLANNV---AMTEHPDLNRVTTALTEAGLGTFVK 472
Cdd:TIGR02633 310 -YPgkFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDrkrhgIVPILGVGKNItlsVLKSFCFKMRIDAAAELQIIGSAIQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 473 TLPQTTATPMTRYTRddgveLSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRL 551
Cdd:TIGR02633 389 RLKVKTASPFLPIGR-----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSEL 463
|
250 260 270
....*....|....*....|....*....|....
gi 498176791 552 ASTR-FCDSILFMNHGQVLESG-----THEQLMA 579
Cdd:TIGR02633 464 AEVLgLSDRVLVIGEGKLKGDFvnhalTQEQVLA 497
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-572 |
4.39e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.33 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGL--LHP---ISGTITINGLNANLLPLAERFALFAPVFQ-ETIILAQS 442
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPearVSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 443 LANNVAMTehPDLNR-----------VTTALTEAGLGTFVKTLPQTTATpmtrytrddgvELSGGQAQKLMLARALYKDA 511
Cdd:PRK14247 99 IFENVALG--LKLNRlvkskkelqerVRWALEKAQLWDEVKDRLDAPAG-----------KLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 512 PVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLA-STRFCDSILFMNHGQVLESG 572
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQqAARISDYVAFLYKGQIVEWG 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
369-525 |
4.42e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.44 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHP---ISGTITINGLNANLLPLAER-----F--ALFAP---VFQE 435
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRrigilFqdDLLFPhlsVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 436 tiiLAQSLANNVAMTEHPDlnRVTTALTEAGLGTFvktlpqttatpmtrYTRDDGvELSGGQAQKLMLARALYKDAPVLI 515
Cdd:COG4136 97 ---LAFALPPTIGRAQRRA--RVEQALEEAGLAGF--------------ADRDPA-TLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|
gi 498176791 516 LDEPTAALDA 525
Cdd:COG4136 157 LDEPFSKLDA 166
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
369-579 |
4.49e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.12 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITIN-----------GLNANLLPLAE-RFAlfapvfqET 436
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDghevvtrspqdGLANGIVYISEdRKR-------DG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 IILAQSLANNVAMTEHPDLNRVTTALTEA----GLGTFVKTLpqTTATPmtryTRDDGV-ELSGGQAQKLMLARALYKDA 511
Cdd:PRK10762 341 LVLGMSVKENMSLTALRYFSRAGGSLKHAdeqqAVSDFIRLF--NIKTP----SMEQAIgLLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 512 PVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFishrLASTR------FCDSILFMNHGQV-----LESGTHEQLMA 579
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSII----LVSSEmpevlgMSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
363-579 |
4.67e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 363 EAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING--LNA-NLLPLAERFALfapVFQ--ETI 437
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelLTAeNVWNLRRKIGM---VFQnpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 ILAQSLANNVAM-TEHPDLNR--VTTALTEAGLgtfvktlpqttATPMTRYTRDDGVELSGGQAQKLMLARALYKDAPVL 514
Cdd:PRK13642 94 FVGATVEDDVAFgMENQGIPReeMIKRVDEALL-----------AVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 515 ILDEPTAALDAIAENEIYQDYAQLAAGK--TSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
384-579 |
5.46e-15 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 76.38 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 384 IVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFalFAPVFQETIILAQ-SLANNVA----MTEHPDLN-- 456
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH--INMVFQSYALFPHmTVEENVAfglkMRKVPRAEik 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 457 -RVTTALTEAGLGTFVKTLPqttatpmtrytrddgVELSGGQAQKLMLARALYKDAPVLILDEPTAALD----AIAENEI 531
Cdd:TIGR01187 79 pRVLEALRLVQLEEFADRKP---------------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLEL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498176791 532 YQDYAQLaaGKTSLFISH--RLASTrFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:TIGR01187 144 KTIQEQL--GITFVFVTHdqEEAMT-MSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
365-578 |
5.75e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.20 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 365 KSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLM--MGLLHP---ISGTITINGLN-----ANLLPLAERFALfapVFQ 434
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNiysprTDTVDLRKEIGM---VFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 ETIILAQSLANNV-------AMTEHPDLNR-VTTALTEAGLGTFVKTlpqttatpmtrYTRDDGVELSGGQAQKLMLARA 506
Cdd:PRK14239 94 QPNPFPMSIYENVvyglrlkGIKDKQVLDEaVEKSLKGASIWDEVKD-----------RLHDSALGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498176791 507 LYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRL-ASTRFCDSILFMNHGQVLESG-THEQLM 578
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqQASRISDRTGFFLDGDLIEYNdTKQMFM 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
369-520 |
1.42e-14 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 73.33 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAPVFQEtIILAQSLAN 445
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgiaYVPQGRE-IFPRLTVEE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 446 N--VAMTEHPDLNRvttALTEAGLGTFvktlpqttatPMTRYTRD-DGVELSGGQAQKLMLARALYKDAPVLILDEPT 520
Cdd:TIGR03410 95 NllTGLAALPRRSR---KIPDEIYELF----------PVLKEMLGrRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
356-537 |
1.59e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.21 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 356 HVNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPlAERF--------- 426
Cdd:PRK10247 12 NVGYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK-PEIYrqqvsycaq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 427 --ALFAPVFQETIILAQSLANnvamtEHPDLNRVTtalteAGLGTFvkTLPQTTAT-PMTrytrddgvELSGGQAQKLML 503
Cdd:PRK10247 89 tpTLFGDTVYDNLIFPWQIRN-----QQPDPAIFL-----DDLERF--ALPDTILTkNIA--------ELSGGEKQRISL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 498176791 504 ARALYKDAPVLILDEPTAALD---AIAENEIYQDYAQ 537
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDesnKHNVNEIIHRYVR 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
352-573 |
1.93e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEA---KSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGL-------NANLLP 421
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstskNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 422 LAERFALfapVFQ--ETIILAQSLANNVAM---------TEHPDLNRVTTALTEAGLGTFVKtlpqttaTPMtrytrddg 490
Cdd:PRK13649 83 IRKKVGL---VFQfpESQLFEETVLKDVAFgpqnfgvsqEEAEALAREKLALVGISESLFEK-------NPF-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 491 vELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLAS-TRFCDSILFMNHGQV 568
Cdd:PRK13649 145 -ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDvANYADFVYVLEKGKL 223
|
....*
gi 498176791 569 LESGT 573
Cdd:PRK13649 224 VLSGK 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
369-574 |
2.05e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.12 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLlHP---ISGTITING--LNANLLPLAERfALFAPVFQETIILAQ-S 442
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPhgtYEGEIIFEGeeLQASNIRDTER-AGIAIIHQELALVKElS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 443 LANNVAMTEHP------DLN----RVTTALTEAGLGTFVktlpqttATPMTrytrddgvELSGGQAQKLMLARALYKDAP 512
Cdd:PRK13549 99 VLENIFLGNEItpggimDYDamylRAQKLLAQLKLDINP-------ATPVG--------NLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498176791 513 VLILDEPTAALDAiAENEIYQDYAQ--LAAGKTSLFISHRLAST-RFCDSILfmnhgqVLESGTH 574
Cdd:PRK13549 164 LLILDEPTASLTE-SETAVLLDIIRdlKAHGIACIYISHKLNEVkAISDTIC------VIRDGRH 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
369-579 |
2.16e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.13 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTItinglnanllpLAERFalFAPVFQETIILAQSLANNVA 448
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------WAERS--IAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAE 528
Cdd:PTZ00243 743 FFDEEDAARLADAVRVSQLEADLAQLGGGLETEIG----EKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498176791 529 NEIYQDYAQLA-AGKTSLFISHRLASTRFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:PTZ00243 819 ERVVEECFLGAlAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
372-580 |
2.59e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.17 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 372 VSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPiSGTIT-----INGLNANLLPLAERFAL----FAPVFQETIilaQS 442
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTadrfrWNGIDLLKLSPRERRKIigreIAMIFQEPS---SC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 443 LANNvamtehpdlNRVTTALTEAglgtfvktLPQTTAT------PMTRYTR-----------DDGV-------ELSGGQA 498
Cdd:COG4170 102 LDPS---------AKIGDQLIEA--------IPSWTFKgkwwqrFKWRKKRaiellhrvgikDHKDimnsyphELTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 499 QKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLA--AGKTSLFISHRLAS-TRFCDSILFMNHGQVLESGTHE 575
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqlQGTSILLISHDLESiSQWADTITVLYCGQTVESGPTE 244
|
....*
gi 498176791 576 QLMAK 580
Cdd:COG4170 245 QILKS 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
352-550 |
2.76e-14 |
|
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: 71.03 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKsASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITInglnanllplaerfalfaP 431
Cdd:cd03223 1 IELENLSLATPDGR-VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------------------P 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETIILAQslannvamteHPDLNRVTtaLTEAglgtfvktlpqttatpmTRYTRDDgvELSGGQAQKLMLARALYKDA 511
Cdd:cd03223 62 EGEDLLFLPQ----------RPYLPLGT--LREQ-----------------LIYPWDD--VLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 498176791 512 PVLILDEPTAALDAIAENEIYQdyAQLAAGKTSLFISHR 550
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQ--LLKELGITVISVGHR 147
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
351-570 |
2.94e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 351 TITFAHVNYQYPEaKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFA 430
Cdd:PRK10522 322 TLELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQETIILAQSLAnnvamtehPDLNRVTTALTEAGLGTFvktlpqttatPMTRYTRDDG-----VELSGGQAQKLMLAR 505
Cdd:PRK10522 401 AVFTDFHLFDQLLG--------PEGKPANPALVEKWLERL----------KMAHKLELEDgrisnLKLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 506 ALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISHRLASTRFCDSILFMNHGQVLE 570
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLlqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
369-579 |
3.15e-14 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 72.91 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING--------LNANLLP----LAERF-ALFAPVFQ- 434
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdRDGELVPadrrQLQRIrTRLGMVFQs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 ----------ETIILA------QSLANNVAMTEHPdLNRVttalteaGLGTFVKTLPqttatpmtrytrddgVELSGGQA 498
Cdd:COG4598 104 fnlwshmtvlENVIEApvhvlgRPKAEAIERAEAL-LAKV-------GLADKRDAYP---------------AHLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 499 QKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLASTRFCDS-ILFMNHGQVLESGTHEQ 576
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEeGRTMLVVTHEMGFARDVSShVVFLHQGRIEEQGPPAE 240
|
...
gi 498176791 577 LMA 579
Cdd:COG4598 241 VFG 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
368-567 |
5.79e-14 |
|
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: 74.48 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 368 SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLlHP---ISGTITING--LNANLLPLAERfALFAPVFQE-TIILAQ 441
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPhgtWDGEIYWSGspLKASNIRDTER-AGIVIIHQElTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 442 SLANNVAMTEHPDLNRVTTALTEAGLGTfvKTLPQTTATPMTRYTRDDGvELSGGQAQKLMLARALYKDAPVLILDEPTA 521
Cdd:TIGR02633 94 SVAENIFLGNEITLPGGRMAYNAMYLRA--KNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498176791 522 ALDAiAENEIYQDYAQ--LAAGKTSLFISHRLASTR-FCDSILFMNHGQ 567
Cdd:TIGR02633 171 SLTE-KETEILLDIIRdlKAHGVACVYISHKLNEVKaVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
359-590 |
2.17e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 359 YQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQ--ET 436
Cdd:PRK13647 12 FRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQdpDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 IILAQSLANNVA-----MTEHPD--LNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYK 509
Cdd:PRK13647 91 QVFSSTVWDDVAfgpvnMGLDKDevERRVEEALKAVRMWDFRDKPPY---------------HLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRL-ASTRFCDSILFMNHGQVLESG-----THEQLMAKGG 582
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVdLAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAG 235
|
....*....
gi 498176791 583 -RYAQMYQI 590
Cdd:PRK13647 236 lRLPLVAQI 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
370-579 |
2.75e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 370 KDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnANLLPLAERFAL---------------FAPVFq 434
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG--KDISPRSPLDAVkkgmayitesrrdngFFPNF- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 etiilaqSLANNVAmtehpdlnrVTTALTEAGLGTFVKTLPQTTATPMTRYTRDDG-----------VELSGGQAQKLML 503
Cdd:PRK09700 357 -------SIAQNMA---------ISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLalkchsvnqniTELSGGNQQKVLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 504 ARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLA-AGKTSLFISHRLAST-RFCDSILFMNHG---QVLESG---THE 575
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIiTVCDRIAVFCEGrltQILTNRddmSEE 500
|
....
gi 498176791 576 QLMA 579
Cdd:PRK09700 501 EIMA 504
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
365-577 |
3.24e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.29 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 365 KSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAER--------FALFAPVfqet 436
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdicmvfqsYALFPHM---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 iilaqSLANNVA----MTEHPD---LNRVTTALTEAGLGTFVKtlpqttatpmtRYTRddgvELSGGQAQKLMLARALYK 509
Cdd:PRK11432 94 -----SLGENVGyglkMLGVPKeerKQRVKEALELVDLAGFED-----------RYVD----QISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRlASTRFC--DSILFMNHGQVLESGTHEQL 577
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHD-QSEAFAvsDTVIVMNKGKIMQIGSPQEL 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
369-567 |
3.52e-13 |
|
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: 69.39 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNA--NLLPLAERFALfaPVFQETI--------- 437
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGwvDLAQASPREIL--ALRRRTIgyvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 --------ILAQSLannVAMTEHPDlnrvtTALTEAG--LGTFvkTLPQT--TATPMTrytrddgveLSGGQAQKLMLAR 505
Cdd:COG4778 105 iprvsaldVVAEPL---LERGVDRE-----EARARARelLARL--NLPERlwDLPPAT---------FSGGEQQRVNIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 506 ALYKDAPVLILDEPTAALDA---------IAEneiyqdyaQLAAGKTSLFISHRLAS-TRFCDSILFMNHGQ 567
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAanravvvelIEE--------AKARGTAIIGIFHDEEVrEAVADRVVDVTPFS 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
367-566 |
3.66e-13 |
|
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: 68.90 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 367 ASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL----FAPVFQETIILAQS 442
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 443 LANNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAA 522
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIG----ERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498176791 523 LDAIAENEIYQD----YAQlAAGKTSLFISHRLASTRFCDSILFMNHG 566
Cdd:cd03290 171 LDIHLSDHLMQEgilkFLQ-DDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
369-578 |
3.87e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.13 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLArlmMGLL-----HPISGTITINGLNANLLPLAE--------------RFALf 429
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELA---MSVFgrsygRNISGTVFKDGKEVDVSTVSDaidaglayvtedrkGYGL- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 430 apVFQETIILAQSLANNVAMTEHP--DLNRVTTALTEaglgtFVKTLpqTTATPmtrytrddGVE-----LSGGQAQKLM 502
Cdd:NF040905 352 --NLIDDIKRNITLANLGKVSRRGviDENEEIKVAEE-----YRKKM--NIKTP--------SVFqkvgnLSGGNQQKVV 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 503 LARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLASTR-FCDSILFMNHGQVL-----ESGTHE 575
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAeGKGVIVISSELPELLgMCDRIYVMNEGRITgelprEEASQE 494
|
...
gi 498176791 576 QLM 578
Cdd:NF040905 495 RIM 497
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
368-601 |
6.17e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.46 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 368 SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlNANLlplaerfalfapvfqetIILAQSLANNV 447
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-SAAL-----------------IAISSGLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 AMTEHPDLNRVTTALTE-------------AGLGTFVKtlpqttaTPMTRYtrddgvelSGGQAQKLMLARALYKDAPVL 514
Cdd:PRK13545 101 TGIENIELKGLMMGLTKekikeiipeiiefADIGKFIY-------QPVKTY--------SSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 515 ILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQIQS 592
Cdd:PRK13545 166 VIDEALSVGDQTFTKKCLDKMNEFKEqGKTIFFISHSLSQVKsFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQMS 245
|
....*....
gi 498176791 593 KYYQPDAKE 601
Cdd:PRK13545 246 VEERKDFRE 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
353-590 |
6.64e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.05 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 353 TFAHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARlMMGLLHPIS-GTITINGLnanllPLAE-RFALFA 430
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSeGEILLDAQ-----PLESwSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 pvfQETIILAQSLANN--------VAMTEHP-----------DLNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgv 491
Cdd:PRK10575 85 ---RKVAYLPQQLPAAegmtvrelVAIGRYPwhgalgrfgaaDREKVEEAISLVGLKPLAHRLVDS-------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 492 eLSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRL-ASTRFCDSILFMNHGQV 568
Cdd:PRK10575 148 -LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQerGLTVIAVLHDInMAARYCDYLVALRGGEM 226
|
250 260
....*....|....*....|..
gi 498176791 569 LESGTHEQLMaKGGRYAQMYQI 590
Cdd:PRK10575 227 IAQGTPAELM-RGETLEQIYGI 247
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
368-568 |
1.05e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 368 SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNAN----LLPLAERFALFAPVFQETIILAQ-- 441
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaNEAINHGFALVTEERRSTGIYAYld 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 442 ----SLANNVAMTEHP-----------DLNRVTTALTeaglgtfVKTLPQTTATPmtrytrddgvELSGGQAQKLMLARA 506
Cdd:PRK10982 343 igfnSLISNIRNYKNKvglldnsrmksDTQWVIDSMR-------VKTPGHRTQIG----------SLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498176791 507 LYKDAPVLILDEPTAALDAIAENEIYQDYAQLA-AGKTSLFISHRLASTR-FCDSILFMNHGQV 568
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLgITDRILVMSNGLV 469
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-579 |
1.17e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 355 AHVNYQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISG-----TITINGLNA----NLLPLAER 425
Cdd:PRK14271 23 AAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyrDVLEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 426 FALfapVFQETIILAQSLANNV-------AMTEHPDLNRVTTA-LTEAGLGTFVKTlpqttatpmtrYTRDDGVELSGGQ 497
Cdd:PRK14271 103 VGM---LFQRPNPFPMSIMDNVlagvrahKLVPRKEFRGVAQArLTEVGLWDAVKD-----------RLSDSPFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 498 AQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLA-STRFCDSILFMNHGQVLESGTHEQ 576
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQ 248
|
...
gi 498176791 577 LMA 579
Cdd:PRK14271 249 LFS 251
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
369-579 |
1.31e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAPvfQETIILAQ-SLA 444
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgigYLP--QEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 445 NNVA--------MTEHPDLNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLIL 516
Cdd:PRK10895 97 DNLMavlqirddLSAEQREDRANELMEEFHIEHLRDSMGQS---------------LSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498176791 517 DEPTAALDAIAENEIYQDYAQLA-AGKTSLFISHRLAST-RFCDSILFMNHGQVLESGTHEQLMA 579
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
369-581 |
1.31e-12 |
|
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: 66.78 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGllHP----ISGTITINGLNANLLPLAERFALfaPVFqetiilaqsla 444
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPkyevTEGEILFKGEDITDLPPEERARL--GIF----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 445 nnVAMTEHPDLNRVTTALteaglgtfvktlpqttatpmtrYTRDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALD 524
Cdd:cd03217 81 --LAFQYPPEIPGVKNAD----------------------FLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498176791 525 AIAENEIYQDYAQLAAGKTS-LFISH--RLASTRFCDSILFMNHGQVLESGTHE---QLMAKG 581
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSvLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElalEIEKKG 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
368-572 |
1.34e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 368 SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAL---FAPVFQE---TIILAQ 441
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrrdIQFIFQDpyaSLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 442 SLANNV--AMTEHPDLNRVTTALTEAGLGTFVKTLPQTTatpmTRYTRddgvELSGGQAQKLMLARALYKDAPVLILDEP 519
Cdd:PRK10261 419 TVGDSImePLRVHGLLPGKAAAARVAWLLERVGLLPEHA----WRYPH----EFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 520 TAALDAIAENEIYQDYAQLAA--GKTSLFISHRLAST-RFCDSILFMNHGQVLESG 572
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
357-524 |
1.54e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 357 VNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISG---------------------------- 408
Cdd:PRK11147 325 VNYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcgtklevayfdqhraeldpektvmd 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 409 -------TITINGLNANLLPLAERFaLFAPvfqetiilaqslanNVAMTehPdlnrvttalteaglgtfVKTlpqttatp 481
Cdd:PRK11147 403 nlaegkqEVMVNGRPRHVLGYLQDF-LFHP--------------KRAMT--P-----------------VKA-------- 440
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 498176791 482 mtrytrddgveLSGGQAQKLMLARALYKDAPVLILDEPTAALD 524
Cdd:PRK11147 441 -----------LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
369-571 |
1.78e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.82 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLlHPI---SGTITING-------LNAN-------------LLPL--- 422
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGevcrfkdIRDSealgiviihqelaLIPYlsi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 423 AERFALFAPV-------FQETIILAQSLANNVAMTEHPDlnrvttalteaglgTFVKTLpqttatpmtrytrddGVelsg 495
Cdd:NF040905 96 AENIFLGNERakrgvidWNETNRRARELLAKVGLDESPD--------------TLVTDI---------------GV---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 496 GQAQKLMLARALYKDAPVLILDEPTAALdaiaeNEiyQDYAQL--------AAGKTSLFISHRLAS-TRFCDSILFMNHG 566
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAAL-----NE--EDSAALldlllelkAQGITSIIISHKLNEiRRVADSITVLRDG 215
|
....*
gi 498176791 567 QVLES 571
Cdd:NF040905 216 RTIET 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
343-603 |
2.05e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 343 KQLANRPVTITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLM--MGLLHP---ISGTITING--L 415
Cdd:PRK14243 2 STLNGTETVLRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPgfrVEGKVTFHGknL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 416 NANLLPLAERFALFAPVFQETIILAQSLANNVAMTE-----HPDLNR-VTTALTEAGLGTFVKTlpqttatpmtrYTRDD 489
Cdd:PRK14243 80 YAPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGAringyKGDMDElVERSLRQAALWDEVKD-----------KLKQS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 490 GVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRL-ASTRFCDSILFMNhgqv 568
Cdd:PRK14243 149 GLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFFN---- 224
|
250 260 270
....*....|....*....|....*....|....*
gi 498176791 569 lesgthEQLMAKGGRYAQMYQIqskyyqpDAKEVI 603
Cdd:PRK14243 225 ------VELTEGGGRYGYLVEF-------DRTEKI 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
352-593 |
3.71e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYPEAKS---ASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTiTING---LNANLLPLAER 425
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGdyaIPANLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 426 FALFAPV-----FQETIILAQSLANNVAMTE-HPDLNRVTTALTEAGLGTFVKtLPQttatpmtRYTRDDGVELSGGQAQ 499
Cdd:PRK13645 86 KRLRKEIglvfqFPEYQLFQETIEKDIAFGPvNLGENKQEAYKKVPELLKLVQ-LPE-------DYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 500 KLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLAST-RFCDSILFMNHGQVLESG---- 572
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfe 237
|
250 260
....*....|....*....|....*...
gi 498176791 573 --THEQLMAK-----GGRYAQMYQIQSK 593
Cdd:PRK13645 238 ifSNQELLTKieidpPKLYQLMYKLKNK 265
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
369-573 |
3.75e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.57 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPvfQETIILAQSLANNVA 448
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPY--SKKIKNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MT-EHPDLNRV-TTALTEAGLGTFVKTLPQTTATPMTRYTRD-----------DGVELSGGQAQKLMLARALYKDAPVLI 515
Cdd:PRK13631 120 MVfQFPEYQLFkDTIEKDIMFGPVALGVKKSEAKKLAKFYLNkmglddsylerSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 516 LDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLAST-RFCDSILFMNHGQVLESGT 573
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
371-549 |
4.77e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.71 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNanlLPLAERFALFApVFQETIILAQSLA------ 444
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEN---IPAMSRSRLYT-VRKRMSMLFQSGAlftdmn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 445 --NNVA--MTEHPDL------NRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVL 514
Cdd:PRK11831 101 vfDNVAypLREHTQLpapllhSTVMMKLEAVGLRGAAKLMPS---------------ELSGGMARRAALARAIALEPDLI 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 498176791 515 ILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISH 549
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSH 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
372-579 |
5.17e-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: 68.68 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 372 VSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINgLNANLLPLAER-FALFAPVFQETIILAQSLAnnvaMT 450
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR-VGDEWVDMTKPgPDGRGRAKRYIGILHQEYD----LY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 451 EHPDlnrVTTALTEAGLGTFVKTLPQTTAT---PMTRYTRDDGV--------ELSGGQAQKLMLARALYKDAPVLILDEP 519
Cdd:TIGR03269 378 PHRT---VLDNLTEAIGLELPDELARMKAVitlKMVGFDEEKAEeildkypdELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498176791 520 TAALDAIAENEIYQD--YAQLAAGKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMA 579
Cdd:TIGR03269 455 TGTMDPITKVDVTHSilKAREEMEQTFIIVSHDMDFVLdVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
372-573 |
5.27e-12 |
|
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: 69.27 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 372 VSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING--LNANLLPLAERFALfAPvfQETIILaqslaNNVAM 449
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdIETNLDAVRQSLGM-CP--QHNILF-----HHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 450 TEHPDLNRVTTALTEAGLGTFVKTLPQTTATPMTRytRDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAEN 529
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKR--NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498176791 530 EIYQDYAQLAAGKTSLFISHRLASTRFC-DSILFMNHGQVLESGT 573
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-577 |
1.27e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.07 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 359 YQYPEAKsASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING---------LNANLLPLAERFALf 429
Cdd:PRK14246 17 YLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfgkdiFQIDAIKLRKEVGM- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 430 apVFQETIILAQ-SLANNVA-------MTEHPDLNRVTT-ALTEAGLGTFVKTLPQTTATpmtrytrddgvELSGGQAQK 500
Cdd:PRK14246 95 --VFQQPNPFPHlSIYDNIAyplkshgIKEKREIKKIVEeCLRKVGLWKEVYDRLNSPAS-----------QLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 501 LMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHR-LASTRFCDSILFMNHGQVLESGTHEQL 577
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
374-524 |
1.38e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 374 FTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFA--PVFQETIILAQSLANNVAMTE 451
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGhlPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498176791 452 HPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLILDEPTAALD 524
Cdd:PRK13543 112 RRAKQMPGSALAIVGLAGYEDTLVR---------------QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
368-589 |
1.73e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 368 SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLlhpISGTITING---LNANLLPLAERFA--LFAPVFQETIILAQ- 441
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGShieLLGRTVQREGRLArdIRKSRANTGYIFQQf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 442 SLANNVAMTEHPDLNRV-TTALTEAGLGTFVKTLPQTTATPMTR-----YTRDDGVELSGGQAQKLMLARALYKDAPVLI 515
Cdd:PRK09984 96 NLVNRLSVLENVLIGALgSTPFWRTCFSWFTREQKQRALQALTRvgmvhFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 516 LDEPTAALDAIAEN---EIYQDYAQlAAGKTSLFISHRL-ASTRFCDSILFMNHGQVLESGTHEQLmaKGGRYAQMYQ 589
Cdd:PRK09984 176 ADEPIASLDPESARivmDTLRDINQ-NDGITVVVTLHQVdYALRYCERIVALRQGHVFYDGSSQQF--DNERFDHLYR 250
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
368-608 |
1.91e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.84 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 368 SLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTIT---------IN-GLNANLLPLAE-RFALFAPVFQET 436
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrngevsviaISaGLSGQLTGIENiEFKMLCMGFKRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 IIlaqslannvamtehpdlNRVTTALTE-AGLGTFVKtlpqttaTPMTRYtrddgvelSGGQAQKLMLARALYKDAPVLI 515
Cdd:PRK13546 119 EI-----------------KAMTPKIIEfSELGEFIY-------QPVKKY--------SSGMRAKLGFSINITVNPDILV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 516 LDEPTAALD-AIAENEIYQDYAQLAAGKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLMAKGGRYAQMYQIQSK 593
Cdd:PRK13546 167 IDEALSVGDqTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRqFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSK 246
|
250
....*....|....*
gi 498176791 594 YYQPDAKEVIADGNF 608
Cdd:PRK13546 247 AEQKEFRNKLDESRF 261
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
357-567 |
3.88e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 357 VNYQYPEAKSasLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANllplaerfalfapvFQET 436
Cdd:PRK10982 4 ISKSFPGVKA--LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID--------------FKSS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 iilAQSLANNVAMTeHPDLNRV--TTALTEAGLGTFVKTLPQTTATPMTRYT-------------RDDGVELSGGQAQKL 501
Cdd:PRK10982 68 ---KEALENGISMV-HQELNLVlqRSVMDNMWLGRYPTKGMFVDQDKMYRDTkaifdeldididpRAKVATLSVSQMQMI 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 502 MLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLAST-RFCDSILFMNHGQ 567
Cdd:PRK10982 144 EIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKErGCGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-577 |
6.40e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLH-----PISGTITINGLN---ANLLPLAERFALfAPVFQ------ 434
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNiysPDVDPIEVRREV-GMVFQypnpfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 -----ETIILAQSLANNVAMTEHPDlNRVTTALTEAGLGTFVKTlpqttatpmtrYTRDDGVELSGGQAQKLMLARALYK 509
Cdd:PRK14267 99 hltiyDNVAIGVKLNGLVKSKKELD-ERVEWALKKAALWDEVKD-----------RLNDYPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLA-STRFCDSILFMNHGQVLESGTHEQL 577
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAqAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
351-573 |
8.03e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.09 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 351 TITFAHVNYQYPeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFalFA 430
Cdd:PRK11650 3 GLKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD--IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 431 PVFQEtiiLA----QSLANNVA-------MTEHPDLNRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQ 499
Cdd:PRK11650 80 MVFQN---YAlyphMSVRENMAyglkirgMPKAEIEERVAEAARILELEPLLDRKPR---------------ELSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 500 KLMLARALYKDAPVLILDEPTAALDAIAEN----EIYQDYAQLAAgkTSLFISH------RLAstrfcDSILFMNHGQVL 569
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDAKLRVqmrlEIQRLHRRLKT--TSLYVTHdqveamTLA-----DRVVVMNGGVAE 214
|
....
gi 498176791 570 ESGT 573
Cdd:PRK11650 215 QIGT 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
371-525 |
8.20e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING---------LNANLLPL-------AERFALfapvfq 434
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeYHQDLLYLghqpgikTELTAL------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 ETIILAQSLANNVamtehpDLNRVTTALTEAGLGTFvKTLPQTTatpmtrytrddgveLSGGQAQKLMLARALYKDAPVL 514
Cdd:PRK13538 93 ENLRFYQRLHGPG------DDEALWEALAQVGLAGF-EDVPVRQ--------------LSAGQQRRVALARLWLTRAPLW 151
|
170
....*....|.
gi 498176791 515 ILDEPTAALDA 525
Cdd:PRK13538 152 ILDEPFTAIDK 162
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
369-570 |
8.62e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLL--HPISGTITINGLnanllplaerfalfaPVFQETIILAQSLANN 446
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDN---------------QFGREASLIDAIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 vamtehpDLNRVTTALTEAGLGTFVKTLpqttatpmTRYTrddgvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAI 526
Cdd:COG2401 111 -------DFKDAVELLNAVGLSDAVLWL--------RRFK-----ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498176791 527 AENEIYQDYAQLA--AGKTSLFISHR--LASTRFCDSILFMNHGQVLE 570
Cdd:COG2401 171 TAKRVARNLQKLArrAGITLVVATHHydVIDDLQPDLLIFVGYGGVPE 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
369-577 |
9.60e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAlfapVFQETIILAQSLANNVA 448
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKE----KVLEKLVIQKTRFKKIK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEhpDL-NRVTTALTEAGLGTFVKTL-------PQTTATPMTR-----------------YTRDDGVELSGGQAQKLML 503
Cdd:PRK13651 99 KIK--EIrRRVGVVFQFAEYQLFEQTIekdiifgPVSMGVSKEEakkraakyielvgldesYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 504 ARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLAST-RFCDSILFMNHGQVLESG-THEQL 577
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGdTYDIL 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-577 |
1.30e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARlMMGLLHPISGTITING-----------LNANLLPLAERFALfapVFQETI 437
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGrveffnqniyeRRVNLNRLRRQVSM---VHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 ILAQSLANNVA-----MTEHPDL---NRVTTALTEAGLGTFVKTLPQTTAtpmtrytrddgVELSGGQAQKLMLARALYK 509
Cdd:PRK14258 99 LFPMSVYDNVAygvkiVGWRPKLeidDIVESALKDADLWDEIKHKIHKSA-----------LDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 510 DAPVLILDEPTAALDAIAENEIYQ--DYAQLAAGKTSLFISHRLAS-TRFCDSILFMNH-----GQVLESGTHEQL 577
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESliQSLRLRSELTMVIVSHNLHQvSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
369-581 |
1.87e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNAN-----LLPLAERFAlfaPVFQE-------T 436
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgLLALRQQVA---TVFQDpeqqifyT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 437 II---LAQSLaNNVAMTEHPDLNRVTTALTEAGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDAPV 513
Cdd:PRK13638 94 DIdsdIAFSL-RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQC---------------LSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 514 LILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRLAST-RFCDSILFMNHGQVLESGTHEQLMAKG 581
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
348-578 |
2.07e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 348 RPVTITFAHVNYQYPEAKSASLKDVSFTlqagqklAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLP---LAE 424
Cdd:PRK10253 9 RGEQLTLGYGKYTVAENLTVEIPDGHFT-------AIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAskeVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 425 RFALFApvfQETI----ILAQSLANNVAMTEHPDLNRVTTALTEAglgtFVKTLPQTTATPMTRYTRDdgvELSGGQAQK 500
Cdd:PRK10253 82 RIGLLA---QNATtpgdITVQELVARGRYPHQPLFTRWRKEDEEA----VTKAMQATGITHLADQSVD---TLSGGQRQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 501 LMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQL--AAGKTSLFISHRL-ASTRFCDSILFMNHGQVLESGTHEQL 577
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEI 231
|
.
gi 498176791 578 M 578
Cdd:PRK10253 232 V 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
369-578 |
4.13e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLH--------PISGTITINGLNANLLP---LAERFALFAPVFQETi 437
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDaprLARLRAVLPQAAQPA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 iLAQSLANNVAMTEHPDLNRvTTALTEAGLGTFVKTLPQTTATPMtryTRDDGVELSGGQAQKLMLARALYK-------- 509
Cdd:PRK13547 96 -FAFSAREIVLLGRYPHARR-AGALTHRDGEIAWQALALAGATAL---VGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498176791 510 -DAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISH--RLAStRFCDSILFMNHGQVLESGTHEQLM 578
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHdpNLAA-RHADRIAMLADGAIVAHGAPADVL 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
320-582 |
5.14e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 320 QEVREfmnlqpQTPTRTLTET------EQKQLANRPVTIT-FAHVNYQYP--EAKSASLK--------DVSFTLQAGQKL 382
Cdd:NF033858 222 AELLA------RTGADTLEAAfiallpEEKRRGHQPVVIPpRPADDDDEPaiEARGLTMRfgdftavdHVSFRIRRGEIF 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 383 AIVGINGAGKSTLARLMMGLLHPISGTITING--LNANllPLAER---------FALF------------APVFQetiil 439
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAG--DIATRrrvgymsqaFSLYgeltvrqnlelhARLFH----- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 440 aqslannVAMTEHPDlnRVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLILDEP 519
Cdd:NF033858 369 -------LPAAEIAA--RVAEMLERFDLADVADALPD---------------SLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 520 TAALDAIAENEIYQDYAQLA--AGKTsLFIshrlaSTRF------CDSILFMNHGQVLESGTHEQLMAKGG 582
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSreDGVT-IFI-----STHFmneaerCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
369-580 |
8.71e-10 |
|
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: 61.36 E-value: 8.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGL--LHPISGTI----------------------------TINGLNAN 418
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvgepcpvcggTLEPEEVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 419 LLPLAErfALFAPVFQETIILAQslaNNVAMTEHPD-LNRVTTALTEAG------LGTFVKTLPQTTAT-PMTRYTRDdg 490
Cdd:TIGR03269 96 FWNLSD--KLRRRIRKRIAIMLQ---RTFALYGDDTvLDNVLEALEEIGyegkeaVGRAVDLIEMVQLShRITHIARD-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 491 veLSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQdyAQLAAGKTSlFISHRLAS------TRFCDSILFMN 564
Cdd:TIGR03269 169 --LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHN--ALEEAVKAS-GISMVLTShwpeviEDLSDKAIWLE 243
|
250
....*....|....*.
gi 498176791 565 HGQVLESGTHEQLMAK 580
Cdd:TIGR03269 244 NGEIKEEGTPDEVVAV 259
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
372-577 |
1.18e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 372 VSFTLQAGQKLAIVGINGAGKSTLARLMMGLL-HP---ISGTITINGLNANLLPLAERFAL----FAPVFQETIilaQSL 443
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYPgrvMAEKLEFNGQDLQRISEKERRNLvgaeVAMIFQDPM---TSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 444 --ANNV------AMTEHPDLNRVTTALTEAGLGTFVKtLPQttatPMTR---YTRddgvELSGGQAQKLMLARALYKDAP 512
Cdd:PRK11022 103 npCYTVgfqimeAIKVHQGGNKKTRRQRAIDLLNQVG-IPD----PASRldvYPH----QLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 513 VLILDEPTAALDAIAENEIYQDYAQLAAGKTS--LFISHRLA-STRFCDSILFMNHGQVLESGTHEQL 577
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLAlVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
349-549 |
1.21e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 349 PVTITFAHVNYQYPeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTItinglnanLLPLAERFAL 428
Cdd:PLN03073 506 PPIISFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------FRSAKVRMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 FapvfqetiilAQSLANNVAMTEHPDL--NRVTTALTE----AGLGTFVKTlPQTTATPMtrYTrddgveLSGGQAQKLM 502
Cdd:PLN03073 577 F----------SQHHVDGLDLSSNPLLymMRCFPGVPEqklrAHLGSFGVT-GNLALQPM--YT------LSGGQKSRVA 637
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498176791 503 LARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGktSLFISH 549
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSH 682
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
369-570 |
1.56e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.64 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAP----VFQETIILAQSLA 444
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhvgfVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 445 -NNV-------AMTEHPDLNRVTTALTEAGLGTFVKTLPqttatpmtrytrddgVELSGGQAQKLMLARALYKDAPVLIL 516
Cdd:PRK10584 106 lENVelpallrGESSRQSRNGAKALLEQLGLGKRLDHLP---------------AQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498176791 517 DEPTAALDAIAENEIY-------QDYAqlaagKTSLFISHRLASTRFCDSILFMNHGQVLE 570
Cdd:PRK10584 171 DEPTGNLDRQTGDKIAdllfslnREHG-----TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
369-524 |
1.77e-09 |
|
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: 60.33 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINglnanllplaerfalfapvfqETIILA---QS--- 442
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------------------ETVKLAyvdQSrda 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 443 LANNVAM-------TEHPDLNRVTTAlTEAGLGTF----------VKtlpqttatpmtrytrddgvELSGGQAQKLMLAR 505
Cdd:TIGR03719 397 LDPNKTVweeisggLDIIKLGKREIP-SRAYVGRFnfkgsdqqkkVG-------------------QLSGGERNRVHLAK 456
|
170
....*....|....*....
gi 498176791 506 ALYKDAPVLILDEPTAALD 524
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLD 475
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
372-577 |
2.09e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.46 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 372 VSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPlAERFALFAPV--FQ-----------ETII 438
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVrtFQhvrlfremtviENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 LAQSLANNVAM------------TEHPDLNRVTTALTEAGLGTFVktlpqttatpmtryTRDDGvELSGGQAQKLMLARA 506
Cdd:PRK11300 103 VAQHQQLKTGLfsgllktpafrrAESEALDRAATWLERVGLLEHA--------------NRQAG-NLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498176791 507 LYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQL 577
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMgISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
370-572 |
2.82e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.27 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 370 KDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFAlfAPVFQETIILAQ-SLANN-- 446
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGV--GMVFQSYALYPHlSVAENms 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 ----VAMTEHPDLN-RVTTALTEAGLGTFVKTLPQttatpmtrytrddgvELSGGQAQKLMLARALYKDAPVLILDEPTA 521
Cdd:PRK11000 98 fglkLAGAKKEEINqRVNQVAEVLQLAHLLDRKPK---------------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 522 ALDAI----AENEIYQDYAQLaaGKTSLFISH-RLASTRFCDSILFMNHGQVLESG 572
Cdd:PRK11000 163 NLDAAlrvqMRIEISRLHKRL--GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
373-579 |
3.35e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 373 SFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFAPVFQEtiilaqslaNNVAM-TE 451
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQR---------NNTDMlSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 452 HPDLNRVTTA------LTEAGLGTFVKTLPQTTATPMTRYTRddgveLSGGQAQKLMLARALYKDAPVLILDEPTAALDA 525
Cdd:PRK10938 94 GEDDTGRTTAeiiqdeVKDPARCEQLAQQFGITALLDRRFKY-----LSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 526 IAENEIYQDYAQLAAGKTSLFishrLASTRFCDSILFMNHGQVL------ESGTHEQLMA 579
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLV----LVLNRFDEIPDFVQFAGVLadctlaETGEREEILQ 224
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
492-579 |
5.07e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 492 ELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLAS-TRFCDSILFMNHGQV 568
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMlSQWADKINVLYCGQT 237
|
90
....*....|.
gi 498176791 569 LESGTHEQLMA 579
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
369-567 |
6.45e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLL-PLAERFALFAPVFQETIILAQ-SLANN 446
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgPKSSQEAGIGIIHQELNLIPQlTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 447 VAM----------TEHPDLNRVTTALTeAGLGtfVKTLPQTTATpmtrytrddgvELSGGQAQKLMLARALYKDAPVLIL 516
Cdd:PRK10762 100 IFLgrefvnrfgrIDWKKMYAEADKLL-ARLN--LRFSSDKLVG-----------ELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498176791 517 DEPTAALDAIAENEIYQDYAQL-AAGKTSLFISHRLAST-RFCDSILFMNHGQ 567
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRELkSQGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
359-524 |
1.32e-08 |
|
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: 55.88 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 359 YQYPEAKSAslkDVSFTLQA-------GQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPlaerfALFAP 431
Cdd:cd03237 1 YTYPTMKKT---LGEFTLEVeggsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP-----QYIKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 432 VFQETI--ILAQSLANnvaMTEHPDLN-RVTTALTEAGLgtfvktlpqttatpMTRYTRddgvELSGGQAQKLMLARALY 508
Cdd:cd03237 73 DYEGTVrdLLSSITKD---FYTHPYFKtEIAKPLQIEQI--------------LDREVP----ELSGGELQRVAIAACLS 131
|
170
....*....|....*.
gi 498176791 509 KDAPVLILDEPTAALD 524
Cdd:cd03237 132 KDADIYLLDEPSAYLD 147
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
383-576 |
1.42e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.81 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 383 AIVGINGAGKSTLARLMMGLLHPISGTITINGlnaNLLPLAERFALFAP-------VFQETII-----LAQSLANNVAMT 450
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLFDAEKGICLPPekrrigyVFQDARLfphykVRGNLRYGMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 451 EHPDLNRVTTALteaGLGTFVKTLPQTtatpmtrytrddgveLSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENE 530
Cdd:PRK11144 105 MVAQFDKIVALL---GIEPLLDRYPGS---------------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498176791 531 IYqDYAQLAAGKTS---LFISH------RLAstrfcDSILFMNHGQVLESGTHEQ 576
Cdd:PRK11144 167 LL-PYLERLAREINipiLYVSHsldeilRLA-----DRVVVLEQGKVKAFGPLEE 215
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
379-579 |
1.42e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.58 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 379 GQKLAIVGINGAGKSTLARLMMGLLHP--ISGTITINGLNANLlPLAERFALFAP--------VFQETIILAQSLANNVA 448
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRKPTK-QILKRTGFVTQddilyphlTVRETLVFCSLLRLPKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEHPDLNRVTTALTEAGLGTFVKTLPQTTatpmtrYTRDdgveLSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAE 528
Cdd:PLN03211 173 LTKQEKILVAESVISELGLTKCENTIIGNS------FIRG----ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498176791 529 NEIYQDYAQLA-AGKTSLFISHRLASTRF--CDSILFMNHGQVLESGTHEQLMA 579
Cdd:PLN03211 243 YRLVLTLGSLAqKGKTIVTSMHQPSSRVYqmFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
369-410 |
1.74e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 1.74e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTI 410
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
375-549 |
2.39e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 375 TLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINglnanlLPLAerfalFAPvfqetiilaQSLANNVAMTEHPD 454
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIS-----YKP---------QYIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 455 LNRVTTALTeaglGTFVKTL---PQTTATPMTRYTRDdgveLSGGQAQKLMLARALYKDAPVLILDEPTAALDA------ 525
Cdd:PRK13409 421 LRSITDDLG----SSYYKSEiikPLQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlav 492
|
170 180 190
....*....|....*....|....*....|
gi 498176791 526 ------IAENEiyqdyaqlaaGKTSLFISH 549
Cdd:PRK13409 493 akairrIAEER----------EATALVVDH 512
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
369-550 |
3.05e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANllplAERFAlfapvFQETIILA---QSLAN 445
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCT-----YQKQLCFVghrSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 446 NVAMTEHP--DLNRVTTALTEAGLGTFVKtLPQTTATPMtrytrddGVeLSGGQAQKLMLARALYKDAPVLILDEPTAAL 523
Cdd:PRK13540 88 YLTLRENClyDIHFSPGAVGITELCRLFS-LEHLIDYPC-------GL-LSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*...
gi 498176791 524 DAIA-ENEIYQDYAQLAAGKTSLFISHR 550
Cdd:PRK13540 159 DELSlLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
350-572 |
3.33e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.50 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 350 VTITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAErfalf 429
Cdd:PRK11614 4 VMLSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 430 apVFQETIILAqslannvamtehPDLNRVTTALT---EAGLGTF----------VKTLPQTTATPMTRYTRDDGVeLSGG 496
Cdd:PRK11614 77 --IMREAVAIV------------PEGRRVFSRMTveeNLAMGGFfaerdqfqerIKWVYELFPRLHERRIQRAGT-MSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498176791 497 QAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFISHRLAStrfcDSILFMNHGQVLESG 572
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAN----QALKLADRGYVLENG 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
370-524 |
3.61e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 370 KDVSFTLQAGqklAIVGI---NGAGKSTLARLMMGLLHPISGTITINglnanllplaerfalfapvfqETIILA---QS- 442
Cdd:PRK11819 341 DDLSFSLPPG---GIVGIigpNGAGKSTLFKMITGQEQPDSGTIKIG---------------------ETVKLAyvdQSr 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 443 --LANNVAM-------TEHPDLNRVTTAlTEAGLGTF----------VKTlpqttatpmtrytrddgveLSGGQAQKLML 503
Cdd:PRK11819 397 daLDPNKTVweeisggLDIIKVGNREIP-SRAYVGRFnfkggdqqkkVGV-------------------LSGGERNRLHL 456
|
170 180
....*....|....*....|.
gi 498176791 504 ARALYKDAPVLILDEPTAALD 524
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLD 477
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
371-578 |
4.09e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.55 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPL-----AERFALF----APVFQ---ETII 438
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseAERRRLLrtewGFVHQhprDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 439 LAQSLANNVA---MtehpdlnrvttALTEAGLGtfvkTLPQTTATPMTRytrddgVEL------------SGGQAQKLML 503
Cdd:PRK11701 104 MQVSAGGNIGerlM-----------AVGARHYG----DIRATAGDWLER------VEIdaariddlpttfSGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498176791 504 ARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA--GKTSLFISHRLASTR-FCDSILFMNHGQVLESGTHEQLM 578
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARlLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
375-524 |
1.87e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 375 TLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTItinglnanllplaerfalfapvfQETIILA---QSLANNVAMTe 451
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------------------DEDLKISykpQYISPDYDGT- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 452 hpdlnrVTTALTEAGLGTFVKTLPQT-TATP------MTRYTRDdgveLSGGQAQKLMLARALYKDAPVLILDEPTAALD 524
Cdd:COG1245 418 ------VEEFLRSANTDDFGSSYYKTeIIKPlgleklLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
264-550 |
3.74e-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: 53.21 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 264 LLRDAIVYGTLIV----AIMRGSLSISQFTLMFGMTNSFITLLdQLLDDfgklqNASIDLQEVREFMNLQPQTPTRTLTE 339
Cdd:TIGR00954 365 LMQEFYNNGRLLLkaadALGRLMLAGRDMTRLAGFTARVDTLL-QVLDD-----VKSGNFKRPRVEEIESGREGGRNSNL 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 340 TEQK-QLANRPVTITFAHVNYQYPEAKSAsLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNaN 418
Cdd:TIGR00954 439 VPGRgIVEYQDNGIKFENIPLVTPNGDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG-K 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 419 LLPLAERFALFAPVFQETIILAQSL----------ANNVAMTEHPDLNRVttaLTEAGLGTFVktlpqttatpmtrytRD 488
Cdd:TIGR00954 517 LFYVPQRPYMTLGTLRDQIIYPDSSedmkrrglsdKDLEQILDNVQLTHI---LEREGGWSAV---------------QD 578
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 489 DGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQlaAGKTSLFISHR 550
Cdd:TIGR00954 579 WMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
369-558 |
9.63e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITING-LNANLL----PLAERFALFAPVFQETIILAQSL 443
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdLIVARLqqdpPRNVEGTVYDFVAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 444 -----ANNVAMTEHPD-----LNRVTTALTEAGLGTF----VKTLPQTTATPMTRYTrddgvELSGGQAQKLMLARALYK 509
Cdd:PRK11147 99 kryhdISHLVETDPSEknlneLAKLQEQLDHHNLWQLenriNEVLAQLGLDPDAALS-----SLSGGWLRKAALGRALVS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498176791 510 DAPVLILDEPTAALDaIAENEIYQDYaqLAAGKTSL-FISH-----RLASTRFCD 558
Cdd:PRK11147 174 NPDVLLLDEPTNHLD-IETIEWLEGF--LKTFQGSIiFISHdrsfiRNMATRIVD 225
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
369-581 |
1.22e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGllHP----ISGTITINGLNANLLPLAER--FALFApVFQETI-ILAQ 441
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPEERahLGIFL-AFQYPIeIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 442 S------LANNVamtehpdlNRVTTALTEAGLGTFVK------TLPQTTATPMTRYTrDDGveLSGGQAQK-LMLARALY 508
Cdd:CHL00131 100 SnadflrLAYNS--------KRKFQGLPELDPLEFLEiineklKLVGMDPSFLSRNV-NEG--FSGGEKKRnEILQMALL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 509 kDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTS-LFISH--RLASTRFCDSILFMNHGQVLESGTHE---QLMAKG 581
Cdd:CHL00131 169 -DSELAILDETDSGLDIDALKIIAEGINKLMTSENSiILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElakELEKKG 246
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
379-531 |
1.89e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.75 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 379 GQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGLNANLLPLAERFALFapvfqetiilaqslannvamtehpdlnrv 458
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLI----------------------------- 52
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498176791 459 ttalteaglgtfvktlpqttatpmtrYTRDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEI 531
Cdd:smart00382 53 --------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALL 99
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
492-552 |
2.03e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 2.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 492 ELSGGQAQKLMLARALYKDAPVLILDEPTAALDaiaeneIYQDYA------QLAAGKTSLFISHRLA 552
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQRLNvarlirELAEGKYVLVVEHDLA 272
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
359-573 |
2.57e-06 |
|
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: 48.09 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 359 YQYPEAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARlmmgllhpisgtitiNGLNANLlplAERFALFAPVFQET-I 437
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------EGLYASG---KARLISFLPKFSRNkL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 438 ILAQSLANnvamtehpdlnrvttaLTEAGLGTFvkTLPQTTATpmtrytrddgveLSGGQAQKLMLARALYKDAP--VLI 515
Cdd:cd03238 63 IFIDQLQF----------------LIDVGLGYL--TLGQKLST------------LSGGELQRVKLASELFSEPPgtLFI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 516 LDEPTAALDaiaENEIYQDYAQL----AAGKTSLFISHRLASTRFCDSILFMNHGQVLESGT 573
Cdd:cd03238 113 LDEPSTGLH---QQDINQLLEVIkgliDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGK 171
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
369-525 |
2.60e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITIN-GLNANLLP----LAERFALFAPVFQ--ETIILAQ 441
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLPqepqLDPTKTVRENVEEgvAEIKDAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 442 SLANNVAM---TEHPDLNRVTTALTE-------AGLGTFVKTLPQttATPMTRYTRDDG--VELSGGQAQKLMLARALYK 509
Cdd:TIGR03719 101 DRFNEISAkyaEPDADFDKLAAEQAElqeiidaADAWDLDSQLEI--AMDALRCPPWDAdvTKLSGGERRRVALCRLLLS 178
|
170
....*....|....*.
gi 498176791 510 DAPVLILDEPTAALDA 525
Cdd:TIGR03719 179 KPDMLLLDEPTNHLDA 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
369-572 |
3.73e-06 |
|
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: 48.03 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHP---ISGTITINGLNanllplaerFALFAPVFQETIILaqslan 445
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIP---------YKEFAEKYPGEIIY------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 446 NVAMTEH-PDLnrvttalteaglgtfvkTLPQT--TATPM--TRYTRddGVelSGGQAQKLMLARALYKDAPVLILDEPT 520
Cdd:cd03233 88 VSEEDVHfPTL-----------------TVRETldFALRCkgNEFVR--GI--SGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498176791 521 AALDAIAENEIYQDYAQLA-AGKTSLFISHRLASTR----FcDSILFMNHGQVLESG 572
Cdd:cd03233 147 RGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEiydlF-DKVLVLYEGRQIYYG 202
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
452-573 |
5.01e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.38 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 452 HPDLNRVTTALTEAGLGtFVKtLPQTTATpmtrytrddgveLSGGQAQKLMLARALYKDAP---VLILDEPTAALDaiae 528
Cdd:cd03271 143 IPKIARKLQTLCDVGLG-YIK-LGQPATT------------LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLH---- 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 529 neiYQDYAQL--------AAGKTSLFISHRLASTRFCDSILFM------NHGQVLESGT 573
Cdd:cd03271 205 ---FHDVKKLlevlqrlvDKGNTVVVIEHNLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
371-563 |
5.28e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.97 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 371 DVSFTlqAGQKLAIVGINGAGKSTLARlmmgllhpisgtitinglnanllplaerfalfapvfqeTIILAQSLANNVAMT 450
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTILD--------------------------------------AIGLALGGAQSATRR 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 451 EHPDLNRVTTALTEAglgTFVKTLPQttatpmtrytrddgveLSGGQAQKLMLARAL----YKDAPVLILDEPTAALD-- 524
Cdd:cd03227 55 RSGVKAGCIVAAVSA---ELIFTRLQ----------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDpr 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498176791 525 ---AIAE--NEIYQDYAQLaagktsLFISHRLASTRFCDSILFM 563
Cdd:cd03227 116 dgqALAEaiLEHLVKGAQV------IVITHLPELAELADKLIHI 153
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
369-408 |
1.01e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.01e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISG 408
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG 62
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
352-582 |
1.10e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 352 ITFAHVNYQYpeAKSASLKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITIngLNANLLPLAERFAL--- 428
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV--LGGDMADARHRRAVcpr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 429 --FAPvfqetiilaQSLANNVamteHPDL--------------------NRVTTALTEA-GLGTFVktlpqttatpmtry 485
Cdd:NF033858 78 iaYMP---------QGLGKNL----YPTLsvfenldffgrlfgqdaaerRRRIDELLRAtGLAPFA-------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 486 TRDDGvELSGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAAGKTSLFIshrLAST-------RFcD 558
Cdd:NF033858 131 DRPAG-KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSV---LVATaymeeaeRF-D 205
|
250 260
....*....|....*....|....
gi 498176791 559 SILFMNHGQVLESGTHEQLMAKGG 582
Cdd:NF033858 206 WLVAMDAGRVLATGTPAELLARTG 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
349-566 |
1.73e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 45.70 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 349 PVTITFAHVNYQYPEAKSAS--LKDVSFTLQAGQKLAIVGINGAGKSTL-----ARLMMGLlhpISGTITINGlnanlLP 421
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRqlLNNISGYVKPGTLTALMGESGAGKTTLldvlaGRKTAGV---ITGEILING-----RP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 422 LAERFALF-APVFQETIilaqslannvamteHPDLNRVTTALTeaglgtfvktlpqttatpMTRYTRDDGVElsggQAQK 500
Cdd:cd03232 73 LDKNFQRStGYVEQQDV--------------HSPNLTVREALR------------------FSALLRGLSVE----QRKR 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498176791 501 LMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLA-AGKTSLFISHRLASTRF--CDSILFMNHG 566
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAdSGQAILCTIHQPSASIFekFDRLLLLKRG 185
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
369-549 |
2.13e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLlHPISgtitinglNANLLPLAERfalfapvfQ----ETIILAQSLA 444
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQG--------YSNDLTLFGR--------RrgsgETIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 445 NNVAMTEHPDLnRVTTALTEAGLGTFVKTLPQTTATP----------MTRYTRDDGV------ELSGGQAQKLMLARALY 508
Cdd:PRK10938 339 GYVSSSLHLDY-RVSTSVRNVILSGFFDSIGIYQAVSdrqqklaqqwLDILGIDKRTadapfhSLSWGQQRLALIVRALV 417
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 498176791 509 KDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSL-FISH 549
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETQLlFVSH 460
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
492-552 |
2.52e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 2.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 492 ELSGGQAQKLMLARALYKDAPVLILDEPTAALDaiaeneIYQ---------DYAQlaAGKTSLFISHRLA 552
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD------IYQrlnvarlirELAE--EGKYVLVVEHDLA 273
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
355-567 |
3.02e-05 |
|
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: 44.87 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 355 AHVNYQYPEAKSaslkdvsftlqaGQKLAIVGINGAGKSTLARLMMGLLHPISGTItinglnanllplaerfalfapvfq 434
Cdd:cd03222 13 FFLLVELGVVKE------------GEVIGIVGPNGTGKTTAVKILAGQLIPNGDND------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 435 etiilaqslannvamtehpDLNRVTTALTeaglgtfvktlPQTtatpmtrytrddgVELSGGQAQKLMLARALYKDAPVL 514
Cdd:cd03222 57 -------------------EWDGITPVYK-----------PQY-------------IDLSGGELQRVAIAAALLRNATFY 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498176791 515 ILDEPTAALDAIAENEIYQDYAQLA--AGKTSLFISHRLASTRFCDSILFMNHGQ 567
Cdd:cd03222 94 LFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
452-577 |
7.89e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 452 HPDLNRVTTALTEAGLGtFVKtLPQTTATpmtrytrddgveLSGGQAQKLMLARALYKDA---PVLILDEPTAALDaiae 528
Cdd:TIGR00630 803 VPSISRKLQTLCDVGLG-YIR-LGQPATT------------LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLH---- 864
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498176791 529 neiYQDYAQL--------AAGKTSLFISHRLASTRFCDSILFM------NHGQVLESGTHEQL 577
Cdd:TIGR00630 865 ---FDDIKKLlevlqrlvDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
494-587 |
8.54e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 494 SGGQAQKLMLARALYKDAPVLILDEPTAALDAIAENEIYQDYAQLAA-GKTSLFISHRL-ASTRFCDSILFMNHGQVLES 571
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMeEAEQLAHELTVIDRGRVIAD 225
|
90
....*....|....*..
gi 498176791 572 GTHEQLMAK-GGRYAQM 587
Cdd:NF000106 226 GKVDELKTKvGGRTLQI 242
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
369-524 |
1.97e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTITINGlnanllplaeRFALfAPVFQETIILAQSLANNV- 447
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----------NWQL-AWVNQETPALPQPALEYVi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 448 -AMTEHPDLNRVTTALTEAGLGTFVKTLP-----------QTTA-----------TPMTRYTRDdgveLSGGQAQKLMLA 504
Cdd:PRK10636 86 dGDREYRQLEAQLHDANERNDGHAIATIHgkldaidawtiRSRAasllhglgfsnEQLERPVSD----FSGGWRMRLNLA 161
|
170 180
....*....|....*....|
gi 498176791 505 RALYKDAPVLILDEPTAALD 524
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLD 181
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
491-524 |
2.35e-04 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 43.06 E-value: 2.35e-04
10 20 30
....*....|....*....|....*....|....*...
gi 498176791 491 VELSGGQ----AQKLMLARALYKDAPVLILDEPTAALD 524
Cdd:cd03273 165 TELSGGQrslvALSLILALLLFKPAPMYILDEVDAALD 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
369-524 |
2.96e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 369 LKDVSFTLQAGQKLAIVGINGAGKSTLARLMMGLLHPISGTItinGLNANLlplaeRFALFApvfQETIilaQSLANNVA 448
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GLAKGI-----KLGYFA---QHQL---EFLRADES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498176791 449 MTEHpdLNRVTTALTEAG----LGTFVKTLPQTTatpmtrytrDDGVELSGGQAQKLMLARALYKDAPVLILDEPTAALD 524
Cdd:PRK10636 394 PLQH--LARLAPQELEQKlrdyLGGFGFQGDKVT---------EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
452-520 |
9.11e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 9.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498176791 452 HPDLNRVTTALTEAGLGtFVKtLPQTTATpmtrytrddgveLSGGQAQKLMLARALYKDAP---VLILDEPT 520
Cdd:COG0178 800 IPKIARKLQTLQDVGLG-YIK-LGQPATT------------LSGGEAQRVKLASELSKRSTgktLYILDEPT 857
|
|
| |
