|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
170-694 |
1.60e-158 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 477.73 E-value: 1.60e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 170 SEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIAD 249
Cdd:COG1132 58 SALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 250 QMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFG 329
Cdd:COG1132 138 GLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 330 GEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSV--IVGALN- 406
Cdd:COG1132 218 REERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLS-GSLTVGDLVAFILYLlrLFGPLRq 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 407 LGNAspcLEAFATGRAAATSIFETIDRKPIIDCmSEDGYKLDRIKGEIEFHNVTFHYPsrPEVKILNDLNMVIKPGEMTA 486
Cdd:COG1132 297 LANV---LNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 487 LVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAA 566
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAA 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 567 KEANAYNFIMDLPQQFDTLVgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIIS 646
Cdd:COG1132 451 KAAQAHEFIEALPDGYDTVVgergvnlsggqrqRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIV 530
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 767920343 647 VAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQG 694
Cdd:COG1132 531 IAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
454-691 |
2.03e-131 |
|
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: 394.60 E-value: 2.03e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKI 613
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920343 614 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
180-691 |
1.51e-126 |
|
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: 398.82 E-value: 1.51e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITGYIQIC-FWVIA-AARQIQ-KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDdINKINDAIADQMALFIQ 256
Cdd:COG2274 200 IGLLLALLFEGLLRLLrSYLLLrLGQRIDlRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 257 RMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVE 336
Cdd:COG2274 279 DLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 337 RYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV--QIFLSVIVGAL-NLGNAspc 413
Cdd:COG2274 359 RWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVID-GQLTLGQLIafNILSGRFLAPVaQLIGL--- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 414 LEAFATGRAAATSIFETIDRKPiiDCMSEDGYK-LDRIKGEIEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSG 492
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPP--EREEGRSKLsLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 493 AGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAY 572
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLH 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 573 NFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLS 652
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLS 671
|
490 500 510
....*....|....*....|....*....|....*....
gi 767920343 653 TVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
199-688 |
4.51e-117 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 374.06 E-value: 4.51e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 199 IAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLV 278
Cdd:TIGR00958 227 YTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 279 IISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVmgf 358
Cdd:TIGR00958 307 TLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALA--- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 359 FTGFVWC------LIFLcyaLAFWYGSTLVLdEGEYTPGTLVqiflSVIVGALNLGNASPCLEAFATGR----AAATSIF 428
Cdd:TIGR00958 384 YAGYLWTtsvlgmLIQV---LVLYYGGQLVL-TGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSGMmqavGASEKVF 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 429 ETIDRKPiidCMSEDG-YKLDRIKGEIEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD 507
Cdd:TIGR00958 456 EYLDRKP---NIPLTGtLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 508 PCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVG 587
Cdd:TIGR00958 533 PTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVG 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 588 EGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEvlSKIQHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:TIGR00958 613 EKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGS 690
|
490 500
....*....|....*....|.
gi 767920343 668 AVERGTHEELLERKGVYFTLV 688
Cdd:TIGR00958 691 VVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
96-427 |
2.83e-115 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 354.86 E-value: 2.83e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 96 MFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVELQELQipgkacvnntivwtnsslnqnmtngtrcgllNIESEMIKF 175
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPD-------------------------------EFLDDVNKY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 176 ASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFI 255
Cdd:cd18577 50 ALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 256 QRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREV 335
Cdd:cd18577 130 QSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 336 ERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVIVGALNLGNASPCLE 415
Cdd:cd18577 210 KRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRD-GEISPGDVLTVFFAVLIGAFSLGQIAPNLQ 288
|
330
....*....|..
gi 767920343 416 AFATGRAAATSI 427
Cdd:cd18577 289 AFAKARAAAAKI 300
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
164-691 |
5.90e-112 |
|
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: 356.32 E-value: 5.90e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 164 GLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIA-AARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINK 242
Cdd:TIGR02204 48 GFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWlGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 243 INDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSM 322
Cdd:TIGR02204 128 LQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 323 RTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQ-IFLSVI 401
Cdd:TIGR02204 208 RTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVI-AGKMSAGTLGQfVFYAVM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 402 VGAlNLGNASPCLEAFATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIKGEIEFHNVTFHYPSRPEVKILNDLNMVIKP 481
Cdd:TIGR02204 287 VAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 482 GEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMED 561
Cdd:TIGR02204 366 GETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 562 IVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHG 641
Cdd:TIGR02204 446 VEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKG 525
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 767920343 642 HTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:TIGR02204 526 RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
181-691 |
9.25e-106 |
|
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: 339.77 E-value: 9.25e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 181 GIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTS 260
Cdd:TIGR02203 62 GLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 261 TICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEK 340
Cdd:TIGR02203 142 VIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 341 NLVFAQRWGIRKGIVMGFFTGFVWCLIFLcyALAFWYGSTLVL-DEGEYTPGTLVQIFLSVIVGALNLGNASPCLEAFAT 419
Cdd:TIGR02203 222 VSNRNRRLAMKMTSAGSISSPITQLIASL--ALAVVLFIALFQaQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 420 GRAAATSIFETIDRKPIIDcmsEDGYKLDRIKGEIEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKSTAL 499
Cdd:TIGR02203 300 GLAAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 500 QLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGR-EDATMEDIVQAAKEANAYNFIMDL 578
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 579 PQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAAD 658
Cdd:TIGR02203 456 PLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKAD 535
|
490 500 510
....*....|....*....|....*....|...
gi 767920343 659 TIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
324-697 |
2.90e-100 |
|
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: 326.01 E-value: 2.90e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 324 TVAAFGGEKREVERYEKNLvfaQRW---GIRKGIVMGFFtGFVWCLIF-LCYALAFWYGSTLVLDeGEYTPGTLVQI--F 397
Cdd:COG5265 230 TVKYFGNEAREARRYDEAL---ARYeraAVKSQTSLALL-NFGQALIIaLGLTAMMLMAAQGVVA-GTMTVGDFVLVnaY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 398 LSVIVGALN-LGNAspcleaFATGRAAATSI---FETIDRKP-IIDcmSEDGYKLDRIKGEIEFHNVTFHY-PSRPevkI 471
Cdd:COG5265 305 LIQLYIPLNfLGFV------YREIRQALADMermFDLLDQPPeVAD--APDAPPLVVGGGEVRFENVSFGYdPERP---I 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIR 551
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIA 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 552 YGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMV 631
Cdd:COG5265 454 YGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVgerglklsggekqRVAIARTLLKNPPILIFDEATSALDSRTERAI 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 632 QEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQA 697
Cdd:COG5265 534 QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEA 599
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
454-687 |
2.07e-98 |
|
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: 308.01 E-value: 2.07e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKI 613
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 614 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTL 687
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
96-427 |
1.04e-96 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 306.51 E-value: 1.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 96 MFVGSLCAFLHGIAQPGVLLIFGTMTDVFIdydvelqelqipgkacvnnTIVWTNSSLNQNMTNGTRCGLLNIESEMIKF 175
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFT-------------------NGGMTNITGNSSGLNSSAGPFEKLEEEMTLY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 176 ASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFI 255
Cdd:cd18558 62 AYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 256 QRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREV 335
Cdd:cd18558 142 QNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 336 ERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDEgEYTPGTLVQIFLSVIVGALNLGNASPCLE 415
Cdd:cd18558 222 TRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQ-EYSIGEVLTVFFSVLIGAFSAGQQVPSIE 300
|
330
....*....|..
gi 767920343 416 AFATGRAAATSI 427
Cdd:cd18558 301 AFANARGAAYHI 312
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
188-691 |
3.70e-96 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 314.65 E-value: 3.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 188 ITGYIQ-ICF-WViaAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKIndAIADQMALF-IQRMTSTICG 264
Cdd:PRK11176 80 ITSFISsYCIsWV--SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQV--ASSSSGALItVVREGASIIG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 265 -FLLGFFRGWKLTLVIISVSPLIGIgaaTIGLsVSK-FTDYELKAYAKAGVV---ADEVISSMRTVAAFGGEKREVERYE 339
Cdd:PRK11176 156 lFIMMFYYSWQLSLILIVIAPIVSI---AIRV-VSKrFRNISKNMQNTMGQVttsAEQMLKGHKEVLIFGGQEVETKRFD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 340 KNLVFAQRWGIRKGIVMGFFTGFVWCLIFLcyALAF-WYGSTLVLDEGEYTPGTLVQIFLSVIvgAL-----NLGNASpc 413
Cdd:PRK11176 232 KVSNRMRQQGMKMVSASSISDPIIQLIASL--ALAFvLYAASFPSVMDTLTAGTITVVFSSMI--ALmrplkSLTNVN-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 414 lEAFATGRAAATSIFETIDRKPIIDcmsEDGYKLDRIKGEIEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGA 493
Cdd:PRK11176 306 -AQFQRGMAACQTLFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGS 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 494 GKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDA-TMEDIVQAAKEANAY 572
Cdd:PRK11176 381 GKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAM 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 573 NFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLS 652
Cdd:PRK11176 461 DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS 540
|
490 500 510
....*....|....*....|....*....|....*....
gi 767920343 653 TVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:PRK11176 541 TIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
454-691 |
1.20e-86 |
|
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: 276.80 E-value: 1.20e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKI 613
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920343 614 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
452-682 |
1.68e-86 |
|
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: 276.41 E-value: 1.68e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHYpsRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ 531
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 611
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 612 KILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKG 682
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
176-682 |
1.08e-84 |
|
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: 283.19 E-value: 1.08e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 176 ASYYAGIAVAVL---ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADQMA 252
Cdd:COG4988 58 LPLLGLLLAVLLlraLLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV----EALDGYFA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 253 LFI-QRM-TSTICGFLLG--FFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAK-AGVVADeVISSMRTVAA 327
Cdd:COG4988 134 RYLpQLFlAALVPLLILVavFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARlSGHFLD-RLRGLTTLKL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 328 FGGEKREVERYEKNlvfAQRWgiRK------------GIVMGFFTgfvwcliFLCYALAfwygstlvldegeytpgtLVQ 395
Cdd:COG4988 213 FGRAKAEAERIAEA---SEDF--RKrtmkvlrvaflsSAVLEFFA-------SLSIALV------------------AVY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 396 IFLSVIVGALNLGNA------SPclEAF-------------ATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIkGEIEF 456
Cdd:COG4988 263 IGFRLLGGSLTLFAAlfvlllAP--EFFlplrdlgsfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGP-PSIEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 457 HNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVE 536
Cdd:COG4988 340 EDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 537 QEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVgegggqmsggqkqRVAIARALIRNPKILLL 616
Cdd:COG4988 418 QNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLgeggrglsggqaqRLALARALLRDAPLLLL 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 617 DMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKG 682
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
52-898 |
5.90e-84 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 296.17 E-value: 5.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 52 KEQKKISNNNN---------------DKKSRLQDEKKGDGVRVGFFQLFRFSSSTDIWLMFVGSLCAFLHGIAQPGVLLI 116
Cdd:PTZ00265 3 KDQRQKKDNNSgggnlsikdevekelNKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 117 FGtmtdvfidydvelqelqipgkacvnntIVWTNSSLNQNMTNgtrcgllniesemIKFASYYAGIAVAVL--ITGYiqi 194
Cdd:PTZ00265 83 FG---------------------------VIMKNMNLGENVND-------------IIFSLVLIGIFQFILsfISSF--- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 195 CFWVIAAarQIQKMRKFYFRRIMRMEIGWFDCNSVG-ELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGW 273
Cdd:PTZ00265 120 CMDVVTT--KILKTLKLEFLKSVFYQDGQFHDNNPGsKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 274 KLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKG 353
Cdd:PTZ00265 198 RLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKAN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 354 IVMGFFTGFVWCLIFLCYALAFWYGSTLVLDE-------GEYTPGTLVQIFLSVIVGALNLGNASPCLEAFATGRAAATS 426
Cdd:PTZ00265 278 FMESLHIGMINGFILASYAFGFWYGTRIIISDlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNS 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 427 IFETIDRKPIIDcMSEDGYKLDRIKgEIEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFY 506
Cdd:PTZ00265 358 LYEIINRKPLVE-NNDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 507 DPCEGMVTV-DGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYG-------------------------------- 553
Cdd:PTZ00265 436 DPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscr 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 554 -----------------------REDATMED--IVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALI 608
Cdd:PTZ00265 516 akcagdlndmsnttdsneliemrKNYQTIKDseVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAII 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 609 RNPKILLLDMATSALDNESEAMVQEVLSKIQHGH---TIIsVAHRLSTVRAADTI------------------------- 660
Cdd:PTZ00265 596 RNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnriTII-IAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdn 674
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 661 ----------------------IGFEHGTAVERGTHEELLERK-GVYFTLVTLQS-QGNQALNEEDIKDATEDDMLARTF 716
Cdd:PTZ00265 675 kennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKvSSKKSSNNDNDKDSDMKSSAYKDS 754
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 717 SRGSYQDSLRASIRQRSKSqlsylvhepplaVVDHKSTYEEDRKDKDIPVQEEVepAPVRRILKfSAPEWPYML------ 790
Cdd:PTZ00265 755 ERGYDPDEMNGNSKHENES------------ASNKKSCKMSDENASENNAGGKL--PFLRNLFK-RKPKAPNNLrivyre 819
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 791 ---------VGSVGAAVNGTVTPLYAFLFSQILGT-FSIPDKEEQRSQINgvclLFVAMGCVSLF-TQFLQGYAFAKSGE 859
Cdd:PTZ00265 820 ifsykkdvtIIALSILVAGGLYPVFALLYAKYVSTlFDFANLEANSNKYS----LYILVIAIAMFiSETLKNYYNNVIGE 895
|
970 980 990
....*....|....*....|....*....|....*....
gi 767920343 860 LLTKRLRKFGFRAMLGQDIAWFDDLRNSPGALTTRLATD 898
Cdd:PTZ00265 896 KVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRD 934
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
454-691 |
4.16e-79 |
|
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: 256.64 E-value: 4.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHY-PSRPEvkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQI 532
Cdd:cd03252 1 ITFEHVRFRYkPDGPV--ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPK 612
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 613 ILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 691
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
447-691 |
2.73e-77 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 263.75 E-value: 2.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 447 LDRIKGEIEFHNVTFHYP-SRPEVKilnDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI 525
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 526 QWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIAR 605
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYF 685
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
....*.
gi 767920343 686 TLVTLQ 691
Cdd:PRK13657 565 ALLRAQ 570
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
92-437 |
9.21e-76 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 250.83 E-value: 9.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 92 DIWLMFVGSLCAFLHGIAQPGVLLIFGTMTDVFidydvelqelqipgkacvnntivwtnsslnqnmtngTRCGLLNIESE 171
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVF------------------------------------SLPDDDELRSE 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 172 MIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFD--CNSVGELNTRFSDDINKINDAIAD 249
Cdd:cd18578 51 ANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 250 QMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFG 329
Cdd:cd18578 131 RLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 330 GEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVIVGALNLGN 409
Cdd:cd18578 211 LEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVAN-GEYTFEQFFIVFMALIFGAQSAGQ 289
|
330 340
....*....|....*....|....*...
gi 767920343 410 ASPCLEAFATGRAAATSIFETIDRKPII 437
Cdd:cd18578 290 AFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
200-690 |
4.13e-75 |
|
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: 257.00 E-value: 4.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 200 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADqmaLFIqR---------MTSTICGFLLGFF 270
Cdd:COG4987 82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV----DALDN---LYL-RvllpllvalLVILAAVAFLAFF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 271 rGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAyAKAGVVAD--EVISSMRTVAAFGGEKREVERY---EKNLVFA 345
Cdd:COG4987 154 -SPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAA-ARAALRARltDLLQGAAELAAYGALDRALARLdaaEARLAAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 346 QRwgiRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVIVGALNLGNASPCLEAFATGRAAAT 425
Cdd:COG4987 232 QR---RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAA-GALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAAR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 426 SIFETIDRKPIIDcMSEDGYKLDRiKGEIEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRF 505
Cdd:COG4987 308 RLNELLDAPPAVT-EPAEPAPAPG-GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 506 YDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTL 585
Cdd:COG4987 385 LDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTW 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 586 VGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEH 665
Cdd:COG4987 465 LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLED 544
|
490 500
....*....|....*....|....*
gi 767920343 666 GTAVERGTHEELLERKGVYFTLVTL 690
Cdd:COG4987 545 GRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
448-666 |
1.78e-71 |
|
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: 235.83 E-value: 1.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 448 DRIKGEIEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW 527
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 528 LRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARAL 607
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 608 IRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHG 666
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
454-666 |
2.37e-70 |
|
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: 230.35 E-value: 2.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFSTTIAENIRYGREdatmedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKI 613
Cdd:cd03228 80 YVPQDPFLFSGTIRENILSGGQ------------------------RQ------------------RIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920343 614 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHG 666
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
37-690 |
5.99e-64 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 236.08 E-value: 5.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 37 TRRGENKSRTSWSSFKEQKKISNNNNDKKSRLQDEKKGDGVRVGFFQ-LFR----------------FSSSTDIWLMFVG 99
Cdd:PTZ00265 754 SERGYDPDEMNGNSKHENESASNKKSCKMSDENASENNAGGKLPFLRnLFKrkpkapnnlrivyreiFSYKKDVTIIALS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 100 SLCAflhGIAQPGVLLIFGTMTDVFIDYdvelqelqipgkacvnntivwtnsslnqnmtngtrcglLNIESEMIKFASYY 179
Cdd:PTZ00265 834 ILVA---GGLYPVFALLYAKYVSTLFDF--------------------------------------ANLEANSNKYSLYI 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFD--CNSVGELNTRFSDDINKINDAIADQMALFIQR 257
Cdd:PTZ00265 873 LVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHF 952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 258 MTSTICGFLLGFFRgWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVV----------------ADEVISS 321
Cdd:PTZ00265 953 IVLFLVSMVMSFYF-CPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVfaynsddeifkdpsflIQEAFYN 1031
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 322 MRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVldegeyTPGT-LVQIFLSV 400
Cdd:PTZ00265 1032 MNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLI------RRGTiLVDDFMKS 1105
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 401 IVGALNLGNASPCLEAFATGRAAATSIFET----IDRKPIIDCMSEDGYKL---DRIKGEIEFHNVTFHYPSRPEVKILN 473
Cdd:PTZ00265 1106 LFTFLFTGSYAGKLMSLKGDSENAKLSFEKyyplIIRKSNIDVRDNGGIRIknkNDIKGKIEIMDVNFRYISRPNVPIYK 1185
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 474 DLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD---------------------------------------------- 507
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkegg 1265
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 508 --------PCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLP 579
Cdd:PTZ00265 1266 sgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLP 1345
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 580 QQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAA 657
Cdd:PTZ00265 1346 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRS 1425
|
730 740 750
....*....|....*....|....*....|....*....
gi 767920343 658 DTIIGFEH----GTAVE-RGTHEELLE-RKGVYFTLVTL 690
Cdd:PTZ00265 1426 DKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
215-691 |
1.61e-63 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 227.92 E-value: 1.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 215 RIMRMEIGWFDCNSVGELNTRfSDDINKINDAIADqmALFIQRMTSTICGFLLG--FFRGWKLTLVIISVSPLIGIGAAT 292
Cdd:TIGR03797 218 RLLRLPVSFFRQYSTGDLASR-AMGISQIRRILSG--STLTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 293 IGLsvsKFTDYELKAYAKAGVVADEV------ISSMRTVAAfggEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCL 366
Cdd:TIGR03797 295 LGL---LQVRKERRLLELSGKISGLTvqlingISKLRVAGA---ENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 367 IFLCYALAFWYGSTLvLDEGEYTPGTLVQ---IFLSVIVGALNLGNAspcleafATGRAAATSIFETIdrKPIIDCMSE- 442
Cdd:TIGR03797 369 PVLTSAALFAAAISL-LGGAGLSLGSFLAfntAFGSFSGAVTQLSNT-------LISILAVIPLWERA--KPILEALPEv 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 443 DGYKLD--RIKGEIEFHNVTFHY-PSRPevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHD 519
Cdd:TIGR03797 439 DEAKTDpgKLSGAIEVDRVTFRYrPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 520 IRSLNIQWLRDQIGIVEQEPVLFSTTIAENIrYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQ 599
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhgHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLE 679
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK--VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
490
....*....|..
gi 767920343 680 RKGVYFTLVTLQ 691
Cdd:TIGR03797 674 REGLFAQLARRQ 685
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
212-688 |
1.83e-63 |
|
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: 227.90 E-value: 1.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 212 YFRRIMRMEIGWFDCNSVGELNTRFSddinkINDAIADQMAlfiQRMTSTICGFLLGFFRG-------WKLTLVIISvsp 284
Cdd:TIGR03796 233 FLWHILRLPVRFFAQRHAGDIASRVQ-----LNDQVAEFLS---GQLATTALDAVMLVFYAllmllydPVLTLIGIA--- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 285 LIGIGAATIGLSVSKFTDYELKA---YAKAGVVADEVISSMRTVAAFGGEKREVER---YEKNLVFAQRwgiRKGIVMGF 358
Cdd:TIGR03796 302 FAAINVLALQLVSRRRVDANRRLqqdAGKLTGVAISGLQSIETLKASGLESDFFSRwagYQAKLLNAQQ---ELGVLTQI 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 359 FTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV------QIFLSVIVGALNLGNASPCLEA----------FATGRA 422
Cdd:TIGR03796 379 LGVLPTLLTSLNSALILVVGGLRVME-GQLTIGMLVafqslmSSFLEPVNNLVGFGGTLQELEGdlnrlddvlrNPVDPL 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 423 AatsifetIDRKPIIDCMSEDGykldRIKGEIEFHNVTFHYpSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI 502
Cdd:TIGR03796 458 L-------EEPEGSAATSEPPR----RLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLV 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 503 QRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGreDATM--EDIVQAAKEANAYNFIMDLPQ 580
Cdd:TIGR03796 526 AGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLW--DPTIpdADLVRACKDAAIHDVITSRPG 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 581 QFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSkiQHGHTIISVAHRLSTVRAADTI 660
Cdd:TIGR03796 604 GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEI 681
|
490 500
....*....|....*....|....*...
gi 767920343 661 IGFEHGTAVERGTHEELLERKGVYFTLV 688
Cdd:TIGR03796 682 IVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
96-405 |
4.99e-61 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 208.65 E-value: 4.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 96 MFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVelqelqipgkacvnntivwtnsslnqnmtngtrcgllNIESEMIKF 175
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD-------------------------------------PETQALNVY 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 176 ASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFI 255
Cdd:pfam00664 44 SLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 256 QRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREV 335
Cdd:pfam00664 124 QSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYEL 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 336 ERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQI--FLSVIVGAL 405
Cdd:pfam00664 204 EKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVIS-GELSVGDLVAFlsLFAQLFGPL 274
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
180-661 |
1.17e-59 |
|
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: 212.92 E-value: 1.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADQMALFI-QRM 258
Cdd:TIGR02857 51 ALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGV----EALDGYFARYLpQLV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 259 TSTICGFLLG---FFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAK-AGVVADeVISSMRTVAAFGGEKRE 334
Cdd:TIGR02857 127 LAVIVPLAILaavFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRlSGHFLD-RLRGLPTLKLFGRAKAQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 335 VER-YEKNLVFAQRwgirkgiVMGfftgfVWCLIFLcyalafwygSTLVLdegEY-----TPGTLVQIFLSVIVGALNLG 408
Cdd:TIGR02857 206 AAAiRRSSEEYRER-------TMR-----VLRIAFL---------SSAVL---ELfatlsVALVAVYIGFRLLAGDLDLA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 409 NASPCL----EAF-------------ATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIkgEIEFHNVTFHYPSRPEVki 471
Cdd:TIGR02857 262 TGLFVLllapEFYlplrqlgaqyharADGVAAAEALFAVLDAAPRPLAGKAPVTAAPAS--SLEFSGVSVAYPGRRPA-- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIR 551
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 552 YGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMV 631
Cdd:TIGR02857 418 LARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
490 500 510
....*....|....*....|....*....|
gi 767920343 632 QEVLSKIQHGHTIISVAHRLSTVRAADTII 661
Cdd:TIGR02857 498 LEALRALAQGRTVLLVTHRLALAALADRIV 527
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
182-710 |
4.25e-57 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 206.87 E-value: 4.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 182 IAVAVLITGYIQIcFWVIAAARQIQ-KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKIN-----------DAIAD 249
Cdd:PRK10789 45 IAVVVYLLRYVWR-VLLFGASYQLAvELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVfaagegvltlvDSLVM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 250 QMALFIQrMTSTIcgfllgffrGWKLTLVIISVSPLIGIGAATIGLSV-SKFTDYElKAYAKAGVVADEVISSMRTVAAF 328
Cdd:PRK10789 124 GCAVLIV-MSTQI---------SWQLTLLALLPMPVMAIMIKRYGDQLhERFKLAQ-AAFSSLNDRTQESLTSIRMIKAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 329 GGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQ--IFLSVIVGaln 406
Cdd:PRK10789 193 GLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVV-NGSLTLGQLTSfvMYLGLMIW--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 407 lgnasPCLeAFA-------TGRAAATSIFETIDRKPIIdcmsEDGYK-LDRIKGEIEFHNVTFHYPSRpEVKILNDLNMV 478
Cdd:PRK10789 269 -----PML-ALAwmfniveRGSAAYSRIRAMLAEAPVV----KDGSEpVPEGRGELDVNIRQFTYPQT-DHPALENVNFT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 479 IKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDAT 558
Cdd:PRK10789 338 LKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDAT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 559 MEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI 638
Cdd:PRK10789 418 QQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 639 QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQsQGNQALNEEDIKDATEDD 710
Cdd:PRK10789 498 GEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ-QLEAALDDAPEIREEAVD 568
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
443-688 |
4.86e-57 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 207.05 E-value: 4.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 443 DGYKLDRIKGEIEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRS 522
Cdd:TIGR01192 324 DAPELPNVKGAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 523 LNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVA 602
Cdd:TIGR01192 402 VTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKG 682
Cdd:TIGR01192 482 IARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDG 561
|
....*.
gi 767920343 683 VYFTLV 688
Cdd:TIGR01192 562 RFYKLL 567
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
452-672 |
5.20e-53 |
|
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: 184.33 E-value: 5.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ 531
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 611
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 612 KILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 672
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
452-673 |
1.50e-52 |
|
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: 183.08 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHYpsRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 530
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFSTTIAENIrygreD----ATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARA 606
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL-----DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920343 607 LIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 673
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
779-905 |
1.58e-50 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 180.73 E-value: 1.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 779 LKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSG 858
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767920343 859 ELLTKRLRKFGFRAMLGQDIAWFDDLRNSPGALTTRLATDASQVQGL 905
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGL 127
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
188-689 |
3.16e-50 |
|
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: 189.57 E-value: 3.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 188 ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDdINKINDAIADQM-ALFIQRMTSTICGFL 266
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTIlSLFLDMWILVIVGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 267 LGFfRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKrevERY-------- 338
Cdd:TIGR01193 290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEA---ERYskidsefg 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 339 ---EKNLVFAQRWGIRKGIVMGFftgfvwCLIFLCYALafWYGSTLVLdEGEYTPGTLV--QIFLSVIVGAL-NLGNASP 412
Cdd:TIGR01193 366 dylNKSFKYQKADQGQQAIKAVT------KLILNVVIL--WTGAYLVM-RGKLTLGQLItfNALLSYFLTPLeNIINLQP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 413 CLEAfatGRAAATSIFETIdrkpIIDCMSEDGYKLD---RIKGEIEFHNVTFHYPSRPEvkILNDLNMVIKPGEMTALVG 489
Cdd:TIGR01193 437 KLQA---ARVANNRLNEVY----LVDSEFINKKKRTelnNLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 490 PSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYG-REDATMEDIVQAAKE 568
Cdd:TIGR01193 508 MSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEI 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 569 ANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHgHTIISVA 648
Cdd:TIGR01193 588 AEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVA 666
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 767920343 649 HRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVT 689
Cdd:TIGR01193 667 HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
180-696 |
1.04e-45 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 174.14 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITG-------YIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA 252
Cdd:PRK10790 65 AGLAAAYVGLQllaaglhYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 253 LFIqRMTSTICGFLLGFFR-GWKLTLVIISVSPLIgIGAATIGLSVSKFTDYELKAYakagvVAD------EVISSM--- 322
Cdd:PRK10790 145 TVL-RSAALIGAMLVAMFSlDWRMALVAIMIFPAV-LVVMVIYQRYSTPIVRRVRAY-----LADindgfnEVINGMsvi 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 323 ---RTVAAFGGEKREVER--YEKNLVFAQRWGIRKGIVMGFFTGFVWC-LIFLcyalaFWYGSTLVLDEGeytpgtLVQI 396
Cdd:PRK10790 218 qqfRQQARFGERMGEASRshYMARMQTLRLDGFLLRPLLSLFSALILCgLLML-----FGFSASGTIEVG------VLYA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 397 FLSVIvGALNlgnaSPCLEaFATGRA-------AATSIFETIDRkpiidcmSEDGYKLDRI---KGEIEFHNVTFHYpsR 466
Cdd:PRK10790 287 FISYL-GRLN----EPLIE-LTTQQSmlqqavvAGERVFELMDG-------PRQQYGNDDRplqSGRIDIDNVSFAY--R 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 467 PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTI 546
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 547 AENIRYGReDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNE 626
Cdd:PRK10790 432 LANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 627 SEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQ 696
Cdd:PRK10790 511 TEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
378-680 |
7.65e-45 |
|
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: 171.08 E-value: 7.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 378 GSTLVLdEGEYTPGTLvqIFLSVIVG-ALnlgnaSPcLE-------AFATGRAAATSIFETIDRKPiidcMSEDGYKLDR 449
Cdd:COG4618 260 GAYLVI-QGEITPGAM--IAASILMGrAL-----AP-IEqaiggwkQFVSARQAYRRLNELLAAVP----AEPERMPLPR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 450 IKGEIEFHNVTFHYPSRPEVkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRslniQWLR 529
Cdd:COG4618 327 PKGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 530 DQ----IGIVEQEPVLFSTTIAENI-RYGreDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIA 604
Cdd:COG4618 402 EElgrhIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920343 605 RALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLER 680
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
328-687 |
1.11e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 170.78 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 328 FGGEKR---EVERYEKNLVFAQRwgirkgiVMGFFTGFVWCLIFLCYALA----FWYGSTLVldEGEYTPGTLVQIF--- 397
Cdd:PRK11160 216 FGAEDRyrqQLEQTEQQWLAAQR-------RQANLTGLSQALMILANGLTvvlmLWLAAGGV--GGNAQPGALIALFvfa 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 398 -------LSVIVGA-LNLGNaspCLeafatgrAAATSIFETIDRKPIIDCMSEDGYKLDRikGEIEFHNVTFHYPSRPEv 469
Cdd:PRK11160 287 alaafeaLMPVAGAfQHLGQ---VI-------ASARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 470 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAEN 549
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDN 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 550 IRYGREDATMEDIVQAAKEANAYNFIMDlPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEA 629
Cdd:PRK11160 434 LLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETER 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920343 630 MVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTL 687
Cdd:PRK11160 513 QILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
200-651 |
9.88e-44 |
|
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: 167.15 E-value: 9.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 200 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADqmaLFIQRMTSTICGFLLG-------FFRG 272
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADV----DALQD---LYVRVIVPAGVALVVGaaavaaiAVLS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 273 WKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAyaKAGVVADEVISSMRTVA---AFGGEKREVERYEKnlvfAQRWG 349
Cdd:TIGR02868 153 VPAALILAAGLLLAGFVAPLVSLRAARAAEQALAR--LRGELAAQLTDALDGAAelvASGALPAALAQVEE----ADREL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 350 IRKGIVMGFFTGFVWCLIFLCYALAFWygSTLVLDEGEYTPGTLVQIFLSVIV-GALNLGNA----SPCLEAFATGRAAA 424
Cdd:TIGR02868 227 TRAERRAAAATALGAALTLLAAGLAVL--GALWAGGPAVADGRLAPVTLAVLVlLPLAAFEAfaalPAAAQQLTRVRAAA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 425 TSIFETIDRKPIIDCMS---EDGYKLDRIKgeIEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQL 501
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSapaAGAVGLGKPT--LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 502 IQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQ 581
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDG 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 582 FDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRL 651
Cdd:TIGR02868 461 LDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
454-677 |
1.37e-42 |
|
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: 155.03 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQ-- 526
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 527 WLRDQIGIVEQEPVLFSTTIAENIRYG------REDATMEDIVQAA-------KEANAYNFIMDLP---QQfdtlvgegg 590
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEAlrkaalwDEVKDRLHALGLSggqQQ--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 591 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAV 669
Cdd:cd03260 149 ---------RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLV 219
|
....*...
gi 767920343 670 ERGTHEEL 677
Cdd:cd03260 220 EFGPTEQI 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
467-693 |
2.24e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 164.25 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 467 PEVKILND-LNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTT 545
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 546 IAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDN 625
Cdd:PRK11174 439 LRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920343 626 ESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQ 693
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
174-424 |
1.37e-41 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 154.26 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 174 KFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMAL 253
Cdd:cd18557 37 ELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 254 FIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKR 333
Cdd:cd18557 117 LLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 334 EVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQIFLSVIVGALNLGNASPC 413
Cdd:cd18557 197 EIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVL-SGQLTVGELTSFILYTIMVASSVGGLSSL 275
|
250
....*....|.
gi 767920343 414 LEAFATGRAAA 424
Cdd:cd18557 276 LADIMKALGAS 286
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
454-681 |
3.92e-41 |
|
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: 150.95 E-value: 3.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPV--LFSTTIAENI-----RYGREDATMEDIV-QAAKEANAYNF----IMDLP---QQfdtlvgegggqmsggqk 598
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVafgpeNLGLPREEIRERVeEALELVGLEHLadrpPHELSggqKQ----------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 599 qRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEE 676
Cdd:COG1122 142 -RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPRE 220
|
....*
gi 767920343 677 LLERK 681
Cdd:COG1122 221 VFSDY 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
454-668 |
1.70e-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: 146.98 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFSTTIAENIRYGREdatmediVQaakeanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIRNPKI 613
Cdd:cd03246 80 YLPQDDELFSGSIAENILSGGQ-------RQ-----------------------------------RLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 614 LLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRAADTIIGFEHGTA 668
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
178-394 |
3.49e-38 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 144.22 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 178 YYAGIAVAVLITGYIQ-ICFWvIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQ 256
Cdd:cd18572 41 LLLLLSVLSGLFSGLRgGCFS-YAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 257 RMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVE 336
Cdd:cd18572 120 NLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREAR 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920343 337 RYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLV 394
Cdd:cd18572 200 RYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVL-SGRMSAGQLV 256
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
454-649 |
7.04e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.72 E-value: 7.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFSTTIAENI----RYGREDATMEDIVQAAKEANAYNFIMDLP--------QQfdtlvgegggqmsggqkqRV 601
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPverlsggeRQ------------------RL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767920343 602 AIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 649
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSH 189
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
179-393 |
1.21e-37 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 143.16 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 179 YAGIAVAVLITGYiqiCFwVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRM 258
Cdd:cd18780 52 VLIGSIATFLRSW---LF-TLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 259 TSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERY 338
Cdd:cd18780 128 VQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRY 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 339 EKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTL 393
Cdd:cd18780 208 SEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVID-GELTTGLL 261
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
454-667 |
5.17e-37 |
|
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: 137.32 E-value: 5.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW--LRDQ 531
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFST-TIAENIRYGredatmedivqaakeanaynfimdLP---QQfdtlvgegggqmsggqkqRVAIARAL 607
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG------------------------LSggqQQ------------------RVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 608 IRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGT 667
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
455-667 |
6.92e-37 |
|
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: 137.98 E-value: 6.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 455 EFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGI 534
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 535 VEQEP--VLFSTTIAENIRYGREDATM--EDIVQAAKEANAYNFIMDLP-----------QQfdtlvgegggqmsggqkq 599
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLpeEEIEERVEEALELVGLEGLRdrspftlsggqKQ------------------ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRA-ADTIIGFEHGT 667
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
454-680 |
3.46e-36 |
|
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: 144.28 E-value: 3.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRP--EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWL 528
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 529 RDQIGIVEQEPV--LF-STTIAENIRYG---REDATMEDIVQAAKE-----------ANAYnfimdlPQQFdtlvgeggg 591
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAEllervglppdlADRY------PHELsgg------ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 592 qmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTA 668
Cdd:COG1123 409 -----qrqRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
250
....*....|..
gi 767920343 669 VERGTHEELLER 680
Cdd:COG1123 484 VEDGPTEEVFAN 495
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
454-672 |
4.78e-36 |
|
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: 134.36 E-value: 4.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIG 533
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFSTTIAENIryGREDATMEdivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKI 613
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--GRRFSGGE-------------------RQ------------------RLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 614 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 672
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
454-661 |
2.20e-35 |
|
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: 134.14 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSR-PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlrDQI 532
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVLFS-TTIAENIRYGREDATM-----EDIVQAAKE-------ANAYnfimdlP-------QQfdtlvgegggq 592
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVpkaeaRERAEELLElvglsgfENAY------PhqlsggmRQ----------- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 593 msggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTII 661
Cdd:cd03293 139 -------RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVV 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
455-667 |
2.84e-35 |
|
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: 131.60 E-value: 2.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 455 EFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGI 534
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 535 VEQepvlFSttiaeniryGREdatmedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKIL 614
Cdd:cd00267 78 VPQ----LS---------GGQ------------------------RQ------------------RVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 615 LLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGT 667
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
452-673 |
3.20e-35 |
|
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: 133.31 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHY-PSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 530
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFSTTIAENI-RYGREDAtmEDIVQAAKEANAYNfimDLPQQFDTLVgegggqmsggqkqrvAIARALIR 609
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYSD--EEIYGALRVSEGGL---NLSQGQRQLL---------------CLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 610 NPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 673
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
454-678 |
3.75e-35 |
|
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: 134.40 E-value: 3.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVL-FSTTIAENIRYGR---------EDATMEDIVQAA-KEANAYNFIMdlpQQFDTLvgegggqmsggqkqRVA 602
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAVEEAlERTGLEHLAD---RPVDELsgg--------erqRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 603 IARALIRNPKILLLDMATSALD--NESEAMvqEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEEL 677
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlaHQLEVL--ELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 767920343 678 L 678
Cdd:COG1120 226 L 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
454-678 |
5.36e-35 |
|
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: 133.48 E-value: 5.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLR 529
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 530 DQIGIVEQEPVLFST-TIAENIRYGREDATMEDIVQAAK------------EANAYnfimdlPQQFdtlvgegggqmSGG 596
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERvlellelvgledKADAY------PAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 597 QKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGT 673
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....*
gi 767920343 674 HEELL 678
Cdd:cd03258 225 VEEVF 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
454-666 |
1.13e-34 |
|
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: 131.84 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPE-VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQWL 528
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 529 RDQIGIVEQEPVLFST-TIAENIRY-----GREDATMEDIVQAAKE-----ANAYNFIMDLP---QQfdtlvgegggqms 594
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELLErvglgDRLNHYPSELSggqQQ------------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 595 ggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAADTIIGFEHG 666
Cdd:cd03255 148 -----RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
454-670 |
1.52e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.70 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPS-RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI---QRfydPCEGMVTVDGHDIRSLNI---- 525
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSErela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 526 QWLRDQIGIVEQEPVLFST-TIAENI----RYGREDAtmEDIVQAAKEA--------NAYNFIMDLP---QQfdtlvgeg 589
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENValplLLAGVSR--KERRERARELlervglgdRLDHRPSQLSggqQQ-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 590 ggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:COG1136 152 ----------RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGR 221
|
...
gi 767920343 668 AVE 670
Cdd:COG1136 222 IVS 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
454-682 |
1.87e-34 |
|
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: 132.29 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqWLRDQIG 533
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFST-TIAENIRYgreDATMEDIVQAAKEANAYNFI--MDLPQQFDTLVgeggGQMSGGQKQRVAIARALIRN 610
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELIelLGLEEFLDRRV----GELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 611 PKILLLDMATSALDNES-EAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERKG 682
Cdd:COG4555 151 PKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
472-621 |
2.90e-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: 128.15 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFS-TTIAENI 550
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 551 RYGREdatMEDIVQAAKEANAYNFI--MDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATS 621
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
454-680 |
4.61e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 130.88 E-value: 4.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI--RSLNIQWLRDQ 531
Cdd:COG1126 2 IEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFS-TTIAENIRYG--------REDAT---ME--DIVQAAKEANAYnfimdlP-------QQfdtlvgegg 590
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvkkmsKAEAEeraMEllERVGLADKADAY------PaqlsggqQQ--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 591 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQH----GHTIISVAHRLSTVR-AADTIIGFEH 665
Cdd:COG1126 144 ---------RVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDVMRDlakeGMTMVVVTHEMGFAReVADRVVFMDG 211
|
250
....*....|....*
gi 767920343 666 GTAVERGTHEELLER 680
Cdd:COG1126 212 GRIVEEGPPEEFFEN 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
454-678 |
6.55e-34 |
|
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: 130.50 E-value: 6.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFS-TTIAENI-------RYGRedatmEDIVQAAKEANAynfIMDLPQQfdTLVGEGGGQMSGGQKQRVAIAR 605
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalvpkllKWPK-----EKIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRL-STVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
454-679 |
3.45e-33 |
|
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: 128.56 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFST-TIAENIRYG-RE-----DATMEDIVQAAKEAnaynfiMDLPQQFDTLvgegggqmsggqkqRVAI 603
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREhtdlsEAEIRELVLEKLEL------VGLPGAADKMpsels----ggmrkRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 679
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
454-670 |
5.06e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.48 E-value: 5.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQE-PVLFSTTIAENIRY-----GREDATMEDIVQAA--------KeanAYNFIMDLP---QQfdtlvgegggqm 593
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVldlvglsdK---AKALPHELSggeQQ------------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 594 sggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADT-IIGFEHGTAVE 670
Cdd:COG2884 145 ------RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
454-672 |
5.80e-33 |
|
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: 126.87 E-value: 5.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDqIG 533
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRN-IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFST-TIAENIRYGREDATM--EDIVQAAKEANAynfIMDLP--------------QQfdtlvgegggqmsgg 596
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRARVRELLE---LVGLEgllnryphelsggqQQ--------------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 597 qkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHGTAVERG 672
Cdd:cd03259 138 ---RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
454-680 |
6.52e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.49 E-value: 6.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRdQIG 533
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFST-TIAENIR-----YGREDATMEDIVQAAKEAnaynfiMDLPQQFDTLVgegggqmsggqKQ-------R 600
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEARERIDELLEL------FGLTDAADRKV-----------GTlsggmkqR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 601 VAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 678
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELK 219
|
..
gi 767920343 679 ER 680
Cdd:COG1131 220 AR 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
454-672 |
6.66e-33 |
|
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: 127.24 E-value: 6.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD-- 530
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 -QIGIVEQEPvlFST-----TIAENIRYGREDATMEDIVQAAKEANAYNFI-MDLP---------------QQfdtlvge 588
Cdd:cd03257 82 kEIQMVFQDP--MSSlnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPeevlnryphelsggqRQ------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 589 gggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEH 665
Cdd:cd03257 153 -----------RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeeLGLTLLFITHDLGVVAKiADRVAVMYA 221
|
....*..
gi 767920343 666 GTAVERG 672
Cdd:cd03257 222 GKIVEEG 228
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
173-424 |
8.15e-33 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 128.82 E-value: 8.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 173 IKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA 252
Cdd:cd07346 39 LWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 253 LFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEK 332
Cdd:cd07346 119 QLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 333 REVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV------QIFLSVIVGALN 406
Cdd:cd07346 199 REIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQ-GSLTIGELVaflaylGMLFGPIQRLAN 277
|
250
....*....|....*...
gi 767920343 407 LGNaspcleAFATGRAAA 424
Cdd:cd07346 278 LYN------QLQQALASL 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
180-404 |
8.50e-33 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 128.76 E-value: 8.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 259
Cdd:cd18576 43 LGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 260 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYE 339
Cdd:cd18576 123 TLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYR 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 340 KNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQ-IFLSVIVGA 404
Cdd:cd18576 203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLA-GELTAGDLVAfLLYTLFIAG 267
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
454-680 |
1.53e-32 |
|
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: 133.10 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGHDIRSLNIQWLRD 530
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEP--VLFSTTIAENIRYGRE--DATMEDIVQAAKEANAYNFIMDL----PQQFdtlvgegggqmSGGQKQRVA 602
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVLELLEAVGLERRldryPHQL-----------SGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLE 679
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 767920343 680 R 680
Cdd:COG1123 233 A 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
454-677 |
3.80e-32 |
|
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: 125.37 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL---NIQWLRD 530
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFS-TTIAENIRYGREDA-----------TMEDIVQAAKEANAYNFIMDLPQQFDTLvgegggqmSGGQK 598
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRrstwrslfglfPKEEKQRALAALERVGLLDKAYQRADQL--------SGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 599 QRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHE 675
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPA 230
|
..
gi 767920343 676 EL 677
Cdd:cd03256 231 EL 232
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
199-393 |
9.22e-32 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 126.09 E-value: 9.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 199 IAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLV 278
Cdd:cd18573 67 IAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 279 IISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGF 358
Cdd:cd18573 147 MLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGL 226
|
170 180 190
....*....|....*....|....*....|....*...
gi 767920343 359 F---TGFVWCLIFLCyalAFWYGSTLVLdEGEYTPGTL 393
Cdd:cd18573 227 FfgsTGFSGNLSLLS---VLYYGGSLVA-SGELTVGDL 260
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
454-680 |
1.36e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 127.14 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIG 533
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFS-TTIAENIRYG----------REDATME--DIVQAAKEANAYnfIMDLP---QQfdtlvgegggqmsggq 597
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrmrgvpkaeIRARVAEllELVGLEGLADRY--PHQLSggqQQ---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 598 kqRVAIARALIRNPKILLLDMATSALDNES-EAMVQEvLSKIQH--GHTIISVAHRLS---TVraADTIIGFEHGTAVER 671
Cdd:COG3842 143 --RVALARALAPEPRVLLLDEPLSALDAKLrEEMREE-LRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQV 217
|
....*....
gi 767920343 672 GTHEELLER 680
Cdd:COG3842 218 GTPEEIYER 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
454-649 |
1.52e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.43 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniqwLRDQI 532
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVLFS-TTIAENIRYGREDATM-----EDIVQAAKE-------ANAYnfimdlP-------QQfdtlvgegggq 592
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVpkaerRERARELLElvglagfEDAY------PhqlsggmRQ----------- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 593 msggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 649
Cdd:COG1116 146 -------RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH 197
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
454-681 |
5.22e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 122.92 E-value: 5.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL-NIQWLRDQI 532
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEP--VLFSTTIAENIRYGRED-----ATMEDIVQ-AAKEANAYNFIMDLPQ-------Qfdtlvgegggqmsggq 597
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgvprEEMRKRVDeALKLVGMEDFRDREPHllsggqkQ---------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 598 kqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHE 675
Cdd:TIGR04520 144 --RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnkEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
....*.
gi 767920343 676 ELLERK 681
Cdd:TIGR04520 222 EIFSQV 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
147-694 |
8.82e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 131.25 E-value: 8.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 147 VWTNSSLNQNMtngtRCGLLNIESEMIKFASyyagiaVAVLITGyiqiCFWVIAAARQIQK-MRKFYFRRIMRMEIGWFD 225
Cdd:PLN03232 937 IWTDQSTPKSY----SPGFYIVVYALLGFGQ------VAVTFTN----SFWLISSSLHAAKrLHDAMLNSILRAPMLFFH 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 226 CNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLgffRGWKLTLVIISVSPLIGIGAATIGLSVSkfTDYEL 305
Cdd:PLN03232 1003 TNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFAL---IGTVSTISLWAIMPLLILFYAAYLYYQS--TSREV 1077
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 306 K---------AYAKAGVvADEVISSMRTVAAFGGEKREVERY-EKNLVF------AQRW-GIRKGIVMGFftgfvwcLIF 368
Cdd:PLN03232 1078 RrldsvtrspIYAQFGE-ALNGLSSIRAYKAYDRMAKINGKSmDNNIRFtlantsSNRWlTIRLETLGGV-------MIW 1149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 369 LCYALA-FWYGSTlvldEGEYTPGTLVQIFLSVIVgalnlgNASPCLEAFATGRAAATSIFETIDR-KPIIDCMSE--DG 444
Cdd:PLN03232 1150 LTATFAvLRNGNA----ENQAGFASTMGLLLSYTL------NITTLLSGVLRQASKAENSLNSVERvGNYIDLPSEatAI 1219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 445 YKLDR------IKGEIEFHNVTFHYpsRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG 517
Cdd:PLN03232 1220 IENNRpvsgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD 1297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 518 HDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGRE--DAtmeDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSG 595
Cdd:PLN03232 1298 CDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEhnDA---DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSV 1374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 596 GQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHE 675
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQ 1454
|
570 580
....*....|....*....|
gi 767920343 676 ELLERKG-VYFTLVtlQSQG 694
Cdd:PLN03232 1455 ELLSRDTsAFFRMV--HSTG 1472
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
147-687 |
1.18e-30 |
|
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: 130.84 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 147 VWTNSSLNQNMTNGTRcgllniESEMIKFASYYA-GIAVAVLITGY-IQICFWVIAAARQIQKMrkfYFRRIMRMEIGWF 224
Cdd:TIGR00957 986 YWLSLWTDDPMVNGTQ------NNTSLRLSVYGAlGILQGFAVFGYsMAVSIGGIQASRVLHQD---LLHNKLRSPMSFF 1056
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 225 DCNSVGELNTRFSDDINKINDAIADQMALFIQrmtsticgfllGFFRGWKLTLVIISVSPLIGIGAATIGLS---VSKF- 300
Cdd:TIGR00957 1057 ERTPSGNLVNRFSKELDTVDSMIPPVIKMFMG-----------SLFNVIGALIVILLATPIAAVIIPPLGLLyffVQRFy 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 301 --TDYELK---AYAKAGVVA--DEVISSMRTVAAFGGEKR-------EVERYEKNL---VFAQRW-GIRKGIVMGfftgf 362
Cdd:TIGR00957 1126 vaSSRQLKrleSVSRSPVYShfNETLLGVSVIRAFEEQERfihqsdlKVDENQKAYypsIVANRWlAVRLECVGN----- 1200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 363 vwCLIFLCYALAfwygstlVLDEGEYTPGtLVQIFLSV---IVGALN-LGNASPCLEA--FATGRAAATSIFETIDRKPI 436
Cdd:TIGR00957 1201 --CIVLFAALFA-------VISRHSLSAG-LVGLSVSYslqVTFYLNwLVRMSSEMETniVAVERLKEYSETEKEAPWQI 1270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 437 IDCMSEDGYKLdriKGEIEFHNVTFHYpsRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTV 515
Cdd:TIGR00957 1271 QETAPPSGWPP---RGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 516 DGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENI----RYGREDATMedivqAAKEANAYNFIMDLPQQFDTLVGEGGG 591
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEEVWW-----ALELAHLKTFVSALPDKLDHECAEGGE 1420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 592 QMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVER 671
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
570
....*....|....*.
gi 767920343 672 GTHEELLERKGVYFTL 687
Cdd:TIGR00957 1501 GAPSNLLQQRGIFYSM 1516
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
454-677 |
1.23e-30 |
|
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: 120.68 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLF-STTIAENIRYG-RE-----DATMEDIVQAAKEAnaynfiMDLPQQFDTLVgeggGQMSGGQKQRVAI 603
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFPlREhtrlsEEEIREIVLEKLEA------VGLRGAEDLYP----AELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920343 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 677
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
454-666 |
1.36e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 121.32 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFS-TTIAENI----------------RYGREDatmediVQAAKEANAynfIMDLP-------------- 579
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagrlgrtstwrsllgLFPPED------RERALEALE---RVGLAdkayqradqlsggq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 580 QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA- 656
Cdd:COG3638 152 QQ------------------RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRy 213
|
250
....*....|
gi 767920343 657 ADTIIGFEHG 666
Cdd:COG3638 214 ADRIIGLRDG 223
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
452-688 |
1.46e-30 |
|
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: 121.55 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHYPS--RPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLR 529
Cdd:cd03288 18 GEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 530 DQIGIVEQEPVLFSTTIAENIRYGREdATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIR 609
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 610 NPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERK-GVYFTLV 688
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
454-678 |
1.76e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 123.26 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD-- 530
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 -QIGIVEQEPVLFST-TIAENIRYGREDATM--EDIVQAAKE----------ANAYnfimdlP-------QQfdtlvgeg 589
Cdd:COG1135 82 rKIGMIFQHFNLLSSrTVAENVALPLEIAGVpkAEIRKRVAEllelvglsdkADAY------PsqlsggqKQ-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 590 ggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHG 666
Cdd:COG1135 148 ----------RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInrELGLTIVLITHEMDVVRRiCDRVAVLENG 217
|
250
....*....|..
gi 767920343 667 TAVERGTHEELL 678
Cdd:COG1135 218 RIVEQGPVLDVF 229
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
454-680 |
1.88e-30 |
|
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: 120.68 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPE-VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQI 532
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVL-----FS--TTIAENIRYGREDATMEDIVQAAKEanaynfiMDLP---------------QQfdtlvgegg 590
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRIHGLPDREERIAELLEQ-------VGLPpsfldryphqlsggqRQ--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 591 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGT 667
Cdd:COG1124 146 ---------RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVaHLCDRVAVMQNGR 216
|
250
....*....|...
gi 767920343 668 AVERGTHEELLER 680
Cdd:COG1124 217 IVEELTVADLLAG 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
454-666 |
1.00e-29 |
|
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: 117.63 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI--RSLNIQWLRDQ 531
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFS-TTIAENIRYG--------REDAT---ME--DIVQAAKEANAYnfimdlP-------QQfdtlvgegg 590
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLApikvkgmsKAEAEeraLEllEKVGLADKADAY------PaqlsggqQQ--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 591 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKI----QHGHTIISVAHRLSTVR-AADTIIGFEH 665
Cdd:cd03262 143 ---------RVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVMkdlaEEGMTMVVVTHEMGFAReVADRVIFMDD 210
|
.
gi 767920343 666 G 666
Cdd:cd03262 211 G 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
440-680 |
1.54e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 118.22 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 440 MSEDGYKLDRIkgeIEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD--P---CEGMVT 514
Cdd:COG1117 1 MTAPASTLEPK---IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 515 VDGHDI--RSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYG------REDATMEDIVQAA-KEA------------NAyn 573
Cdd:COG1117 75 LDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESlRKAalwdevkdrlkkSA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 574 fiMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR 650
Cdd:COG1117 153 --LGLSggqQQ------------------RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHN 212
|
250 260 270
....*....|....*....|....*....|.
gi 767920343 651 LS-TVRAADTIIGFEHGTAVERGTHEELLER 680
Cdd:COG1117 213 MQqAARVSDYTAFFYLGELVEFGPTEQIFTN 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
454-677 |
1.64e-29 |
|
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: 117.78 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkkLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFS-TTIAENIRYGREDA-----------TMEDIvQAAKEANAYNFIMDLP-QQFDTLvgegggqmSGGQ 597
Cdd:TIGR02315 80 RIGMIFQHYNLIErLTVLENVLHGRLGYkptwrsllgrfSEEDK-ERALSALERVGLADKAyQRADQL--------SGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 598 KQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTH 674
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInkEDGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAP 230
|
...
gi 767920343 675 EEL 677
Cdd:TIGR02315 231 SEL 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
454-681 |
1.84e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.55 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEP---VLFSTT---IA---ENIRYGREDatMEDIV-QAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAI 603
Cdd:PRK13632 87 IIFQNPdnqFIGATVeddIAfglENKKVPPKK--MKDIIdDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
452-694 |
2.75e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 126.39 E-value: 2.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHYpsRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 530
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFSTTIAENIRYGRE--DAtmeDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALI 608
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDPFNEhnDA---DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 609 RNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLV 688
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
....*.
gi 767920343 689 tLQSQG 694
Cdd:PLN03130 1471 -VQSTG 1475
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
454-679 |
3.09e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.11 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniqwLRDQIG 533
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVL---FSTTIAENI------------RYGREDatmEDIVQAA-KEANAYNF----IMDLP---QQfdtlvgegg 590
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgrygrrglfrRPSRAD---REAVDEAlERVGLEDLadrpIGELSggqQQ--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 591 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTII-----GF 663
Cdd:COG1121 147 ---------RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLllnrgLV 217
|
250
....*....|....*.
gi 767920343 664 EHGTAVERGTHEELLE 679
Cdd:COG1121 218 AHGPPEEVLTPENLSR 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
455-672 |
5.15e-29 |
|
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: 114.45 E-value: 5.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 455 EFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGI 534
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 535 VEqepvlfsttiaenirygredatmedivQAAKEANAYNFIMdlpQQFDTLvgegggqmsggqkqRVAIARALIRNPKIL 614
Cdd:cd03214 78 VP---------------------------QALELLGLAHLAD---RPFNELsgg--------erqRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 615 LLDMATSALD--NESEAMvqEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERG 672
Cdd:cd03214 120 LLDEPTSHLDiaHQIELL--ELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
454-661 |
6.58e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 113.65 E-value: 6.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRdQIG 533
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFST-TIAENIRY--GredatMedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRN 610
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKLsgG-----M--------------------KQ------------------RLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920343 611 PKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTII 661
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAeRLCDRVA 166
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
455-661 |
2.17e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 113.78 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 455 EFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhdirsLNIQWLRDQIGI 534
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 535 VEQEPVL---FSTTIAENI------------RYGREDatMEDIVQAAKEANAYNFImdlPQQFDTLvgegggqmSGGQKQ 599
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmglyghkglfrRLSKAD--KAKVDEALERVGLSELA---DRQIGEL--------SGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTII 661
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVL 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
454-666 |
2.41e-28 |
|
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: 113.66 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 530
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFST-TIAENIRYGRE--DATMEDIVQAAKEANAynfIMDLPQQFDTLvgegGGQMSGGQKQRVAIARAL 607
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 608 IRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHG 666
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVdTTRHRVIALERG 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
470-677 |
6.40e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 113.72 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 470 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQW--LRDQIGIVEQEPVLF 542
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 543 STTIAENIRYG------REDATMEDIVQAA-KEANAYNFIMDlpQQFDTLVGEGGGQMSggqkqRVAIARALIRNPKILL 615
Cdd:PRK14239 99 PMSIYENVVYGlrlkgiKDKQVLDEAVEKSlKGASIWDEVKD--RLHDSALGLSGGQQQ-----RVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 616 LDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEEL 677
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
182-410 |
7.29e-27 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 111.63 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 182 IAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIqRMTST 261
Cdd:cd18784 45 LAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFL-RSLVK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 262 ICGFLLGFFR-GWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEK 340
Cdd:cd18784 124 AIGVIVFMFKlSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSE 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 341 NLVFAQRWGIRKGIVMGfftGFVWCLIFLCYALA---FWYGSTLVLdEGEYTPGTLVqiflSVIVGALNLGNA 410
Cdd:cd18784 204 KLKDTYKLKIKEALAYG---GYVWSNELTELALTvstLYYGGHLVI-TGQISGGNLI----SFILYQLELGSC 268
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
454-680 |
1.76e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.03 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR--SLNIQWLRDQ 531
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFSTTIA-ENIRYG--------REDA-----TMEDIVQAAKEANAYNFIMDLPQQfdtlvgegggqmsggq 597
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGplrvrgasKEEAekqarELLAKVGLAERAHHYPSELSGGQQ---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 598 kQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQ----HGHTIISVAHRLSTVR-AADTIIGFEHGTAVERG 672
Cdd:PRK09493 143 -QRVAIARALAVKPKLMLFDEPTSALDPE---LRHEVLKVMQdlaeEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDG 218
|
....*...
gi 767920343 673 THEELLER 680
Cdd:PRK09493 219 DPQVLIKN 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
453-653 |
2.06e-26 |
|
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: 107.25 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 453 EIEFHNVTF---HYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI--QRFYDPCEGMVTVDGHDIRslnIQW 527
Cdd:cd03213 3 TLSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 528 LRDQIGIVEQEPVLFST-TIAENIRYgredatmedivqAAK-------EAnaynfimdlpqqfdtlvgegggqmsggqkQ 599
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMF------------AAKlrglsggER-----------------------------K 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLST 653
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSS 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
472-680 |
7.42e-26 |
|
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: 107.04 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIGIVEQEPVLF-STTIAENI 550
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 551 RYGREdatMEDIVQAAKEANAYNFIMDLpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAM 630
Cdd:cd03299 93 AYGLK---KRKVDKKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920343 631 VQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLER 680
Cdd:cd03299 168 LREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
789-903 |
1.27e-25 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 108.33 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 789 MLVGSVGAAVNGTVTPLYAFLFSQILGTFS-----IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTK 863
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767920343 864 RLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQ 903
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQ 118
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
454-679 |
1.69e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.14 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEP--VLFSTTIAENIRYGREDAT-----MEDIV-QAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIAR 605
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAvpydeMHRRVsEALKQVDMLERADYEPNALS-----------GGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920343 606 ALIRNPKILLLDMATSALDNESEA----MVQEVlsKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLE 679
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQnlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
454-680 |
2.12e-25 |
|
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: 105.78 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrsLNIQWLRDQIG 533
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFS-TTIAENIRYG------------REDATMEDIVQAakEANAYNFIMDLP---QQfdtlvgegggqmsggq 597
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrlkklpkaeikERVAEALDLVQL--EGYANRKPSQLSggqQQ---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 598 kqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTH 674
Cdd:cd03300 138 --RVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTP 215
|
....*.
gi 767920343 675 EELLER 680
Cdd:cd03300 216 EEIYEE 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
454-673 |
2.75e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.35 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYP-SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL---R 529
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 530 DQIGIVEQE-PVLFSTTIAENIRYGREDATME------------DIVQAAKEANAYnfimdlP-------QQfdtlvgeg 589
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALPLELAGTPkaeikarvtellELVGLSDKADRY------PaqlsggqKQ-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 590 ggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHG 666
Cdd:PRK11153 148 ----------RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAG 217
|
....*..
gi 767920343 667 TAVERGT 673
Cdd:PRK11153 218 RLVEQGT 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
472-679 |
5.84e-25 |
|
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: 105.42 E-value: 5.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL----RDQIGIVEQEPVLF-STTI 546
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 547 AENIRYG----------REDATMEDIVQAAKEANAYNFIMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKI 613
Cdd:cd03294 120 LENVAFGlevqgvpraeREERAAEALELVGLEGWEHKYPDELSggmQQ------------------RVGLARALAVDPDI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 614 LLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELLE 679
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQaeLQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
454-680 |
6.66e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.07 E-value: 6.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkiLNdLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlrDQ-- 531
Cdd:COG3840 2 LRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFS-TTIAENI--------RYGREDAtmEDIVQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsg 595
Cdd:COG3840 73 VSMLFQENNLFPhLTVAQNIglglrpglKLTAEQR--AQVEQALERVGLAGLLDRLPgqlsggqRQ-------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 596 gqkqRVAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSkiQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 670
Cdd:COG3840 137 ----RVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEDAaRIADRVLLVADGRIAA 210
|
250
....*....|
gi 767920343 671 RGTHEELLER 680
Cdd:COG3840 211 DGPTAALLDG 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
454-676 |
7.20e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.51 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHY-PSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI--RSLNIQWLR 529
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 530 DQIGIVEQEP--VLFSTTIAENIRYGREDATMED--IVQAAKEAnaynfiMDLPQ-QFDTLVGEGGGQMSGGQKQRVAIA 604
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEeeIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920343 605 RALIRNPKILLLDMATSALDNESEamvQEVLSKIQHGH-----TIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 676
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGR---DEILNKIKELHkeynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
453-680 |
8.22e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 106.77 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 453 EIEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniqWL--RD 530
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLppRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 -QIGIVEQEPVLF-STTIAENIRYG-----------REDAtME--DIVQAAKEANAYnfimdlP-------QQfdtlvge 588
Cdd:COG1118 75 rRVGFVFQHYALFpHMTVAENIAFGlrvrppskaeiRARV-EEllELVQLEGLADRY------PsqlsggqRQ------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 589 gggqmsggqkqRVAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSKIqhGHTIISVAH-RLSTVRAADTIIGF 663
Cdd:COG1118 141 -----------RVALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL--GGTTVFVTHdQEEALELADRVVVM 207
|
250
....*....|....*..
gi 767920343 664 EHGTAVERGTHEELLER 680
Cdd:COG1118 208 NQGRIEQVGTPDEVYDR 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
454-680 |
2.29e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.11 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGHDIRSLNIQWLRD 530
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEP--VLFSTTIAENIRYGRED-----ATMEDIV-QAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVA 602
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENravprPEMIKIVrDVLADVGMLDYIDSEPANLS-----------GGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
453-685 |
4.39e-24 |
|
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: 102.03 E-value: 4.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 453 EIEFHNVTFHYPSRPEvkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQI 532
Cdd:cd03296 2 SIEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVLFS-TTIAENIRYGREdatMEDIVQAAKEANAYNFIMDLPQ--QFDTLVGEGGGQMSGGQKQRVAIARALIR 609
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGLR---VKPRSERPPEAEIRAKVHELLKlvQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 610 NPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELLERKGVYF 685
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
454-679 |
6.07e-24 |
|
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: 100.97 E-value: 6.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN-IQWLRDQI 532
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVLFST-TIAENIRYGREDATMEDIvqAAKEANAYNFIMDLP--------------QQFdtlvgegggqmsggq 597
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKR--KARLERVYELFPRLKerrkqlagtlsggeQQM--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 598 kqrVAIARALIRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 672
Cdd:cd03224 141 ---LAIARALMSRPKLLLLDEPSEGL---APKIVEEIFEAIRElrdeGVTILLVEQNARFALEiADRAYVLERGRVVLEG 214
|
....*..
gi 767920343 673 THEELLE 679
Cdd:cd03224 215 TAAELLA 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
470-675 |
6.11e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.33 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 470 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAEN 549
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 550 IRYGREdatmedIVQAAKEANAynFIMDLpQQF---DTLVGEGGGQMSGGQKQRVaiarALIRN----PKILLLDMATSA 622
Cdd:PRK10247 101 LIFPWQ------IRNQQPDPAI--FLDDL-ERFalpDTILTKNIAELSGGEKQRI----SLIRNlqfmPKVLLLDEITSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 623 LDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFE-HGTAVERGTHE 675
Cdd:PRK10247 168 LDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQpHAGEMQEARYE 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
452-649 |
9.09e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.00 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDq 531
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-DRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLF-STTIAENIRYG----REDAtmEDIVQAAKEANAynfIMDL-------P-------QQfdtlvgegggq 592
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrKVPK--AEIDRRVREAAE---LLGLedlldrkPkqlsggqRQ----------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 593 msggqkqRVAIARALIRNPKILLLDMATSALDNES-EAMVQEvLSKIQH--GHTIISVAH 649
Cdd:COG3839 141 -------RVALGRALVREPKVFLLDEPLSNLDAKLrVEMRAE-IKRLHRrlGTTTIYVTH 192
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
454-660 |
1.48e-23 |
|
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: 99.48 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWlRDQIG 533
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFST-TIAENIR-----YGReDATMEDIVQAAKEanaynfiMDLPQQFDTLVGEgggqmsggqkqRVAIARAL 607
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVRQlsag----qkrRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767920343 608 IRNPKILLLDMATSALDNESEAMVQEVLSK-IQHGHTIISVAHRLSTVRAADTI 660
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
454-660 |
2.15e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ-I 532
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVLFST-TIAENIRYGRE--------DATMEDivQAAKEANAYNF-------IMDLP---QQFdtlvgegggqm 593
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREprrgglidWRAMRR--RARELLARLGLdidpdtpVGDLSvaqQQL----------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 594 sggqkqrVAIARALIRNPKILLLDMATSALdNESEAmvqEVLSKI-----QHGHTIISVAHRLSTVRA-ADTI 660
Cdd:COG1129 149 -------VEIARALSRDARVLILDEPTASL-TEREV---ERLFRIirrlkAQGVAIIYISHRLDEVFEiADRV 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
454-680 |
2.17e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.96 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEP--VLFSTTIAENIRYGREDATM--EDIVQAAKEA----NAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIAR 605
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIphEEMKERVNEAlelvGMQDFKEREPARLS-----------GGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920343 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrdDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
182-427 |
3.54e-23 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 100.96 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 182 IAVAVL--ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 259
Cdd:cd18552 46 IGLFLLrgLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 260 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERY- 338
Cdd:cd18552 126 TVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFr 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 339 ---EKNLVFAQRWGIRKGI---VMGFFTGFVwclIflcyALAFWYGSTLVLDeGEYTPGTlvqiFLSVIVGAL------- 405
Cdd:cd18552 206 kanERLRRLSMKIARARALsspLMELLGAIA---I----ALVLWYGGYQVIS-GELTPGE----FISFITALLllyqpik 273
|
250 260
....*....|....*....|..
gi 767920343 406 NLGNASpclEAFATGRAAATSI 427
Cdd:cd18552 274 RLSNVN---ANLQRGLAAAERI 292
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
454-678 |
3.94e-23 |
|
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: 99.39 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGM-VTVDGHDIRSLNIQWLRDQI 532
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVeqepvlfSTTIAENIrygREDATMEDIV-------------------QAAKEanaynfIMDL-------PQQFDTLv 586
Cdd:COG1119 81 GLV-------SPALQLRF---PRDETVLDVVlsgffdsiglyreptdeqrERARE------LLELlglahlaDRPFGTL- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 587 gegggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLStvraaDTIIGFE 664
Cdd:COG1119 144 -------SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVE-----EIPPGIT 211
|
250 260
....*....|....*....|
gi 767920343 665 H------GTAVERGTHEELL 678
Cdd:COG1119 212 HvlllkdGRVVAAGPKEEVL 231
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
182-399 |
4.25e-23 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 100.58 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 182 IAVAVL--ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 259
Cdd:cd18542 46 LGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 260 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSK-FTDYElKAYAKAGVVADEVISSMRTVAAFGGEKREVERY 338
Cdd:cd18542 126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPaFEEIR-EQEGELNTVLQENLTGVRVVKAFAREDYEIEKF 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 339 EK-NLVFAQRWgIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQiFLS 399
Cdd:cd18542 205 DKeNEEYRDLN-IKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVIN-GEITLGELVA-FIS 263
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
471-678 |
4.52e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 471 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI---RSLN-----IQWLRDQIGIVEQEPVLF 542
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 543 S-TTIAENIRYG--------REDAT------MEDIVQAAKEaNAYNFIMDLPQQfdtlvgegggqmsggqkQRVAIARAL 607
Cdd:PRK11264 98 PhRTVLENIIEGpvivkgepKEEATararelLAKVGLAGKE-TSYPRRLSGGQQ-----------------QRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 608 IRNPKILLLDMATSALDNEseaMVQEVLSKI----QHGHTIISVAHRLSTVR-AADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPE---LVGEVLNTIrqlaQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALF 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
454-667 |
5.38e-23 |
|
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: 97.93 E-value: 5.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEV--KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHdirslniqwlrdq 531
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFSTTIAENIRYGRE-DATM-EDIVQA-AKEAnaynfimDLpQQFD----TLVGEGGGQMSGGQKQRVAIA 604
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKAcALEP-------DL-EILPdgdlTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 605 RALIRNPKILLLDMATSALDNESEAMVQE--VLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
454-708 |
9.70e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 9.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEP--VLFSTTIAENIRYG------REDATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIAR 605
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPYHLS-----------YGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERG-----THEELL 678
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250 260 270
....*....|....*....|....*....|....*
gi 767920343 679 ERKGVYFTLVT-----LQSQGNQALnEEDIKDATE 708
Cdd:PRK13647 232 EQAGLRLPLVAqifedLPELGQSKL-PLTVKEAVQ 265
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
454-680 |
1.10e-22 |
|
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: 100.13 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPC---EGMVTVDGHDIRSLN---IQ 526
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 527 WLR-DQIGIVEQEPvlFS---------TTIAENIRY----GREDAT------MED--IVQAAKEANAYnfimdlPQQFdt 584
Cdd:COG0444 82 KIRgREIQMIFQDP--MTslnpvmtvgDQIAEPLRIhgglSKAEAReraielLERvgLPDPERRLDRY------PHELsg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 585 lvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTII 661
Cdd:COG0444 154 g-----------mrqRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQreLGLAILFITHDLGVVAEiADRVA 222
|
250
....*....|....*....
gi 767920343 662 GFEHGTAVERGTHEELLER 680
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
471-680 |
1.57e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.18 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 471 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWlRDqIGIVEQEPVLFS-TTIAEN 549
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-ICMVFQSYALFPhMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 550 IRYG--REDATMEDIVQAAKEANAynfIMDLPQQFDTLVgeggGQMSGGQKQRVAIARALIRNPKILLLDMATSALD-NE 626
Cdd:PRK11432 99 VGYGlkMLGVPKEERKQRVKEALE---LVDLAGFEDRYV----DQISGGQQQRVALARALILKPKVLLFDEPLSNLDaNL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920343 627 SEAMvQEVLSKIQHGHTIIS--VAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK11432 172 RRSM-REKIRELQQQFNITSlyVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
454-680 |
1.65e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.55 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYP--SRPEVKilnDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ 531
Cdd:PRK13635 6 IRVEHISFRYPdaATYALK---DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEP--VLFSTTIAENIRYGRE------DATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAI 603
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLEnigvprEEMVERVDQALRQVGMEDFLNREPHRLS-----------GGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 604 ARALIRNPKILLLDMATSALDNESEamvQEVLSKI-----QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGR---REVLETVrqlkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
..
gi 767920343 679 ER 680
Cdd:PRK13635 229 KS 230
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
170-395 |
2.71e-22 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 98.25 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 170 SEMIKFASYYAGIAVAVLITGYIQiCFWVIAAARQIQK-MRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIA 248
Cdd:cd18541 37 SQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIEYdLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 249 DQMALFIQrmTSTICGFLLG--FFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVA 326
Cdd:cd18541 116 PGILYLVD--ALFLGVLVLVmmFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIK 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920343 327 AFGGEKREVER--------YEKNLVFAQrwgirkgiVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQ 395
Cdd:cd18541 194 AFVQEEAEIERfdklneeyVEKNLRLAR--------VDALFFPLIGLLIGLSFLIVLWYGGRLVIR-GTITLGDLVA 261
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
454-678 |
3.94e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.47 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEP--VLFSTTIAENIRYGREDATM--EDIVQAAKEA----NAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIAR 605
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIprEEMIKRVDEAllavNMLDFKTREPARLS-----------GGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
454-672 |
4.27e-22 |
|
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: 95.34 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpevKILNDLNMVIKPGeMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 533
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFST-TIAENIRY---------GREDATmedIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAI 603
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkgipsKEVKAR---VDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 672
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
180-427 |
9.19e-22 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 96.73 E-value: 9.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 259
Cdd:cd18551 43 VALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 260 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYE 339
Cdd:cd18551 123 TVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 340 KNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVlDEGEYTPGTLVQIFLSV--IVGAL-NLGNAspcLEA 416
Cdd:cd18551 203 EAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARV-ASGALTVGTLVAFLLYLfqLITPLsQLSSF---FTQ 278
|
250
....*....|.
gi 767920343 417 FATGRAAATSI 427
Cdd:cd18551 279 LQKALGALERI 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
209-404 |
9.65e-22 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 96.40 E-value: 9.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 209 RKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGI 288
Cdd:cd18575 72 RKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 289 GAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERY----EKNLVFAQRW-GIRkgivmGFFTGFV 363
Cdd:cd18575 152 PIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFatavEAAFAAALRRiRAR-----ALLTALV 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767920343 364 WCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQ-IFLSVIVGA 404
Cdd:cd18575 227 IFLVFGAIVFVLWLGAHDVL-AGRMSAGELSQfVFYAVLAAG 267
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
454-680 |
1.20e-21 |
|
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: 99.76 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSR--------PEVKILNDLNMVIKPGEMTALVGPSGAGKST----ALQLIqrfydPCEGMVTVDGHDIR 521
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 522 SLN---IQWLRDQIGIVEQEPvlFST-----TIAENI-------RYGREDATMEDIVQAAKE--------ANAYnfimdl 578
Cdd:COG4172 351 GLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIaeglrvhGPGLSAAERRARVAEALEevgldpaaRHRY------ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 579 PQQFdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA 656
Cdd:COG4172 423 PHEFsgg-----------qrqRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQreHGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|....*
gi 767920343 657 -ADTIIGFEHGTAVERGTHEELLER 680
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
453-677 |
1.77e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 453 EIEFHNVTFHY-PSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI----RSLNIQ 526
Cdd:PRK13634 2 DITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 527 WLRDQIGIVEQ--EPVLFSTTIAENIRYGRED--ATMEDIVQAAKEANAynfIMDLPQQfdtLVGEGGGQMSGGQKQRVA 602
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPEE---LLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920343 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEEL 677
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
454-683 |
2.49e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--DIRSLNIQWLRDQ 531
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEP--VLFSTTIAENIRYGREDATM-EDIVQA----AKEANAYNFIMDLPQQFDTLvgegggqmsgGQKQRVAIA 604
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLpEDEVRKrvdnALKRTGIEHLKDKPTHCLSF----------GQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 605 RALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEK 233
|
..
gi 767920343 682 GV 683
Cdd:PRK13636 234 EM 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
470-672 |
3.29e-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: 93.13 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 470 KILNDLNMVIK---PGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG---HDIR-SLNIQWLRDQIGIVEQEPVLF 542
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRkKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 543 S-TTIAENIRYG-REDATMEDIVQAAKeanaynfIMDLpQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMAT 620
Cdd:cd03297 88 PhLNVRENLAFGlKRKRNREDRISVDE-------LLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 621 SALDNESEAMVQEVLSKIQ---HGHTIIsVAHRLSTV-RAADTIIGFEHGTAVERG 672
Cdd:cd03297 160 SALDRALRLQLLPELKQIKknlNIPVIF-VTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
454-669 |
3.38e-21 |
|
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: 91.34 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ-I 532
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVlfsttiAEnirygredatmedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPK 612
Cdd:cd03216 78 AMVYQLSV------GE-------------------------------RQ------------------MVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 613 ILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 669
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
454-681 |
3.70e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.85 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHY-PSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG----HDIRSLNIQW 527
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 528 LRDQIGIVEQ--EPVLFSTTIAENIRYGREDATMEdiVQAAKEaNAYNFIMDLPQQFDTLvGEGGGQMSGGQKQRVAIAR 605
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVKN-YAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
454-681 |
7.89e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.74 E-value: 7.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHY-PSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR----SLNIQW 527
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 528 LRDQIGIVEQ--EPVLFSTTIAENIRYGREDATMEDivQAAKEAnAYNFI--MDLPQQfdtLVGEGGGQMSGGQKQRVAI 603
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE--DEAKEK-ALKWLkkVGLSED---LISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 604 ARALIRNPKILLLDMATSALDNES-EAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-666 |
9.44e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 9.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDI--RSLNIQ 526
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 527 WLRDQIGIVEQEPVLFSTTIAENIRYG------REDATMEDIVQAAKEAnaynfiMDLPQQFDTLVGEGGGQMSGGQKQR 600
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920343 601 VAIARALIRNPKILLLDMATSALDNESEAMVQEVLS--KIQHGHTIISVAHRLSTVRAADTIIGFEHG 666
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
789-904 |
1.32e-20 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 93.88 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 789 MLVGSVGAAVNGTVTPLYAFLFSQILGTF-------------SIPDK----EEQRSQINGVCLLFVAMGCVSLFTQFLQG 851
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnssGLNSSagpfEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 767920343 852 YAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQG 904
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINE 131
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
454-678 |
1.67e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.10 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:COG4559 2 LEAENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVL-FSTTIAENIRYGR-----EDATMEDIVQAAKEAnaynfiMDLP--------------QQfdtlvgegggqm 593
Cdd:COG4559 79 VLPQHSSLaFPFTVEEVVALGRaphgsSAAQDRQIVREALAL------VGLAhlagrsyqtlsggeQQ------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 594 sggqkqRVAIARALI-------RNPKILLLDMATSALDneseamvqevlskIQHGHTIISVAHRLS-------------- 652
Cdd:COG4559 141 ------RVQLARVLAqlwepvdGGPRWLFLDEPTSALD-------------LAHQHAVLRLARQLArrgggvvavlhdln 201
|
250 260
....*....|....*....|....*..
gi 767920343 653 -TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:COG4559 202 lAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
469-676 |
1.83e-20 |
|
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: 91.34 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 469 VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIGIVE--QEPVLFST-T 545
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 546 IAENIRYG-----REDATMEDIVQAAKEANAYNF----IMDLPQQFDTLVgeggGQMSGGQKQRVAIARALIRNPKILLL 616
Cdd:cd03219 92 VLENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPA----GELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 617 DMATSAL-DNESEAMVqEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEE 676
Cdd:cd03219 168 DEPAAGLnPEETEELA-ELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
454-681 |
1.98e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPS-RP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL----NIQW 527
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 528 LRDQIGIVEQ--EPVLFSTTIAENIRYGRED--ATMEDIVQAAKEANAYNFIMdlpqqfDTLVGEGGGQMSGGQKQRVAI 603
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGT------HE 675
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKpkdifqDV 236
|
....*.
gi 767920343 676 ELLERK 681
Cdd:PRK13649 237 DFLEEK 242
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
464-672 |
3.31e-20 |
|
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: 90.12 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 464 PSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLRDQIGIVEQEPVLFS 543
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 544 -TTIAENIRY-GRedatmediVQAAKEANAYNFIMDLPQQFDT--LVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMA 619
Cdd:cd03266 92 rLTARENLEYfAG--------LYGLKGDELTARLEELADRLGMeeLLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 620 TSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTV-RAADTIIGFEHGTAVERG 672
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
452-685 |
3.65e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 96.77 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHY-PSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 530
Cdd:PTZ00243 1307 GSLVFEGVQMRYrEGLPLV--LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFSTTIAENIRYGREDATMEdiVQAAKE-ANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALI- 608
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASSAE--VWAALElVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLk 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 609 RNPKILLLDMATS----ALDNESEAMVQEVLSkiqhGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVY 684
Cdd:PTZ00243 1463 KGSGFILMDEATAnidpALDRQIQATVMSAFS----AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSI 1538
|
.
gi 767920343 685 F 685
Cdd:PTZ00243 1539 F 1539
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
454-649 |
4.55e-20 |
|
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: 89.62 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDqIG 533
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLF-STTIAENIRYG------REDATMEDIVQAAKeanaynfIMDLpqqfDTLVGEGGGQMSGGQKQRVAIARA 606
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAE-------LLQI----EHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767920343 607 LIRNPKILLLDMATSALDNE-SEAMVQEvLSKIQ--HGHTIISVAH 649
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKlRVQMRAE-LKRLQqrLGTTTIYVTH 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
454-672 |
4.96e-20 |
|
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: 89.47 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEvkilnDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIG 533
Cdd:cd03298 1 VRLDKIRFSYGEQPM-----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFS-TTIAENIRYGREDA---TMED---IVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIARA 606
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSPGlklTAEDrqaIEVALARVGLAGLEKRLPGELS-----------GGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 607 LIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 672
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
454-678 |
5.21e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.60 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVL-FSTTIAENIRYGR-----EDATMEDIVQAAKEAN-----AYNFIMDLP---QQfdtlvgegggqmsggqkq 599
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRaphglSRAEDDALVAAALAQVdlahlAGRDYPQLSggeQQ------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 600 RVAIARALIR------NPKILLLDMATSALDneseamvqevlskIQHGHTIISVAHRLS----------------TVRAA 657
Cdd:PRK13548 142 RVQLARVLAQlwepdgPPRWLLLDEPTSALD-------------LAHQHHVLRLARQLAherglavivvlhdlnlAARYA 208
|
250 260
....*....|....*....|.
gi 767920343 658 DTIIGFEHGTAVERGTHEELL 678
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPAEVL 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
454-649 |
5.76e-20 |
|
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: 89.80 E-value: 5.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQWL 528
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 529 RDQIGIVEQ-EPVLFSTTIAENI-----RYGREDATmedivQAAKE----------ANAYnfimdlP-------QQfdtl 585
Cdd:COG4181 89 ARHVGFVFQsFQLLPTLTALENVmlpleLAGRRDAR-----ARARAllervglghrLDHY------PaqlsggeQQ---- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 586 vgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 649
Cdd:COG4181 154 --------------RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnrERGTTLVLVTH 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
453-675 |
6.12e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.07 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 453 EIEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH------DIRSLNIQ 526
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 527 WLRDQIGIVEQE----PVLfstTIAENI--------RYGREDATMEDI-----VQAAKEANAYNFIMDLPQQfdtlvgeg 589
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLieapckvlGLSKEQAREKAMkllarLRLTDKADRFPLHLSGGQQ-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 590 ggqmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVR-AADTIIGFEHGT 667
Cdd:COG4161 148 ---------QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARkVASQVVYMEKGR 218
|
....*...
gi 767920343 668 AVERGTHE 675
Cdd:COG4161 219 IIEQGDAS 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
469-676 |
1.32e-19 |
|
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: 89.33 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 469 VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiQWLRDQIGIVE--QEPVLFST-T 545
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIARtfQNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 546 IAENI--------------------RYGREDATMEDIVQA-------AKEANAYnfIMDLP--QQfdtlvgegggqmsgg 596
Cdd:COG0411 96 VLENVlvaaharlgrgllaallrlpRARREEREARERAEEllervglADRADEP--AGNLSygQQ--------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 597 qkQRVAIARALIRNPKILLLD-----MATSaldnESEAMVqEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTA 668
Cdd:COG0411 159 --RRLEIARALATEPKLLLLDepaagLNPE----ETEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
....*...
gi 767920343 669 VERGTHEE 676
Cdd:COG0411 232 IAEGTPAE 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
454-677 |
1.77e-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: 88.20 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIG 533
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPvlfsttIAENIRYGREDATMEDIVQAAKEANAYNFI------MDLPQQFDTLVgeggGQMSGGQKQRVAIARAL 607
Cdd:cd03265 77 IVFQDL------SVDDELTGWENLYIHARLYGVPGAERRERIdelldfVGLLEAADRLV----KTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 608 IRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 677
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
454-649 |
2.67e-19 |
|
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: 87.56 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 533
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFST-TIAENIRY-----GREDATMEDIVQAAKEanaynfIMDLPQQFDTLVgeggGQMSGGQKQRVAIARAL 607
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRA----RTLSGGMKRKLSLAIAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767920343 608 IRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAH 649
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
472-678 |
2.72e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.25 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD----QIGIVEQEPVLFS-TTI 546
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 547 AENIRYGREDATM------EDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIARALIRNPKILLLDMAT 620
Cdd:PRK10070 124 LDNTAFGMELAGInaeerrEKALDALRQVGLENYAHSYPDELS-----------GGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 621 SALDNESEAMVQEVLSKIQ--HGHTIISVAHRL-STVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
455-683 |
3.39e-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: 87.73 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 455 EFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL-RDQIG 533
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFST-TIAENIRYGREDATMEDIVQAAKEanaynFIMDL-P-----------------QQFdtlvgegggqms 594
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLE-----RVYELfPrlkerrrqragtlsggeQQM------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 595 ggqkqrVAIARALIRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLSTVRA-ADTIIGFEHGTAV 669
Cdd:COG0410 145 ------LAIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIIRRlnreGVTILLVEQNARFALEiADRAYVLERGRIV 215
|
250
....*....|....
gi 767920343 670 ERGTHEELLERKGV 683
Cdd:COG0410 216 LEGTAAELLADPEV 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
457-649 |
3.94e-19 |
|
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: 86.54 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 457 HNVTFHYpsRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniQWLRDQIGIVE 536
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 537 QEP--VLFSTTIAENIRYGREDA--TMEDIVQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsggqkqRVAIAR 605
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELdaGNEQAETVLKDLDLYALKERHPlslsggqKQ------------------RLAIAA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767920343 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAH 649
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITH 184
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
454-680 |
7.56e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.62 E-value: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIG 533
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFS-TTIAENIRYG------REDATMEDIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAIARA 606
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrmqktPAAEITPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 607 LIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAH----RLSTvraADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
454-660 |
1.30e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--DIRSLNiQWLRDQ 531
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPR-DAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFST-TIAENIRYGREDATME--DIVQAAKE----ANAYNF-------IMDLP---QQfdtlvgegggqms 594
Cdd:COG3845 82 IGMVHQHFMLVPNlTVAENIVLGLEPTKGGrlDRKAARARirelSERYGLdvdpdakVEDLSvgeQQ------------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 595 ggqkqRVAIARALIRNPKILLLDMATSAL-DNESE-------AMVQEvlskiqhGHTIISVAHRLSTVRA-ADTI 660
Cdd:COG3845 149 -----RVEILKALYRGARILILDEPTAVLtPQEADelfeilrRLAAE-------GKSIIFITHKLREVMAiADRV 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
454-710 |
1.55e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.09 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIG 533
Cdd:COG4152 2 LELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLF-STTIAENIRY-GR-EDATMEDIVQAAKE--------ANAYNFIMDLP---QQfdtlvgegggqmsggqkq 599
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlARlKGLSKAEAKRRADEwlerlglgDRANKKVEELSkgnQQ------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 600 RVAIARALIRNPKILLLDMATSALD--NeSEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 676
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDpvN-VELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDE 215
|
250 260 270
....*....|....*....|....*....|....
gi 767920343 677 LLERKGVYFTLVTLQSQGNQALNEEDIKDATEDD 710
Cdd:COG4152 216 IRRQFGRNTLRLEADGDAGWLRALPGVTVVEEDG 249
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
468-680 |
2.91e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.35 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 468 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLF 542
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 543 ST-TIAENIRYGREdatMEDIVQAAKEANA-YNFIMDLPQQFDTL---VGEGGGQMSGGQKQRVAIARALIRNPKILLLD 617
Cdd:PRK14247 95 PNlSIFENVALGLK---LNRLVKSKKELQErVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 618 MATSALDNESEAMVQEVLSKIQHGHTIISVAH-RLSTVRAADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
454-680 |
9.66e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 85.55 E-value: 9.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYP--------SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN- 524
Cdd:COG4608 8 LEVRDLKKHFPvrgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 525 --IQWLRDQIGIVEQEPvlFS---------TTIAENIRY-------GREDATME--DIVQAAKE-ANAYnfimdlPQQFd 583
Cdd:COG4608 88 reLRPLRRRMQMVFQDP--YAslnprmtvgDIIAEPLRIhglaskaERRERVAEllELVGLRPEhADRY------PHEFs 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 584 tlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVR-AADTI 660
Cdd:COG4608 160 gg-----------qrqRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQdeLGLTYLFISHDLSVVRhISDRV 228
|
250 260
....*....|....*....|
gi 767920343 661 IGFEHGTAVERGTHEELLER 680
Cdd:COG4608 229 AVMYLGKIVEIAPRDELYAR 248
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
474-680 |
1.32e-17 |
|
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: 85.54 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 474 DLNMVIKPGEMTALVGPSGAGKSTALQLI---QRfydPCEGMVTVDGH---DIRSLniQWL---RDQIGIVEQEPVLFST 544
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEvlqDSARG--IFLpphRRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 545 -TIAENIRYGREdatmedivQAAKEANAYNF--IMDL----------P-------QQfdtlvgegggqmsggqkqRVAIA 604
Cdd:COG4148 92 lSVRGNLLYGRK--------RAPRAERRISFdeVVELlgighlldrrPatlsggeRQ------------------RVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 605 RALIRNPKILLLDMATSALDNESEamvQEVLSKIQ--HGHT---IISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 678
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARK---AEILPYLErlRDELdipILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222
|
..
gi 767920343 679 ER 680
Cdd:COG4148 223 SR 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
463-661 |
1.71e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 463 YPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlrdQIGIVEQEPVlf 542
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ----RSEVPDSLPL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 543 stTIAENI------------RYGREDatmEDIVQAAKEANAynfIMDL-PQQFDTLvgegggqmSGGQKQRVAIARALIR 609
Cdd:NF040873 73 --TVRDLVamgrwarrglwrRLTRDD---RAAVDDALERVG---LADLaGRQLGEL--------SGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920343 610 NPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRAADTII 661
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
454-678 |
2.14e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpEVKILNDLNMVIKPGEMTALVGPSGAGKST-ALQLiQRFYDPCEGMVTVDGHDIRSLN-IQWLRDQ 531
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTlALHL-NGLLRPQKGKVLVSGIDTGDFSkLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEP--VLFSTTIAENIRYGREDATMEDIV------QAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAI 603
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEirkrvdRALAEIGLEKYRHRSPKTLS-----------GGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
474-681 |
2.82e-17 |
|
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: 84.39 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 474 DLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRS------LNIQwlRDQIGIVEQEPVLFS-TTI 546
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPE--KRRIGYVFQEARLFPhLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 547 AENIRYGREDATMEDiVQAAKEAnaynfIMDLpQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNE 626
Cdd:TIGR02142 93 RGNLRYGMKRARPSE-RRISFER-----VIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 627 SEAMVQEVLSKIqHGHT---IISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:TIGR02142 166 RKYEILPYLERL-HAEFgipILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
452-650 |
3.24e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.01 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHYPS-RPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDiRSLniqwlrd 530
Cdd:COG4178 361 GALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-RVL------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 qigIVEQEPVLFSTTIAENIRY--GREDATMEDIVQAAKEANaynfimdLP--------------------QQfdtlvge 588
Cdd:COG4178 430 ---FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG-------LGhlaerldeeadwdqvlslgeQQ------- 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 589 gggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR 650
Cdd:COG4178 493 -----------RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
454-651 |
3.86e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.55 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTF---HYPSRpevkilndLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRD 530
Cdd:PRK10771 2 LKLTDITWlyhHLPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFS-TTIAENIRYG---------REDATMEDIvqaAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQR 600
Cdd:PRK10771 72 PVSMLFQENNLFShLTVAQNIGLGlnpglklnaAQREKLHAI---ARQMGIEDLLARLPGQL-----------SGGQRQR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 601 VAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSKIQhgHTIISVAHRL 651
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQ--LTLLMVSHSL 190
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
453-673 |
4.20e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.14 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 453 EIEFHNVTFHYPSRPEVKilnDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQ- 526
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 527 -WLRDQIGIVEQEPVLFSTTIAENIRYGRE----DATMEDIVQAA-KEANAYNFIMD-LPQQFDTLvgegggqmSGGQKQ 599
Cdd:PRK14243 87 vEVRRRIGMVFQKPNPFPKSIYDNIAYGARingyKGDMDELVERSlRQAALWDEVKDkLKQSGLSL--------SGGQQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 673
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
454-624 |
4.71e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.98 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTfhyPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlRD-QI 532
Cdd:PRK10851 3 IEIANIK---KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDrKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVLFS-TTIAENIRYG------REDATME----------DIVQAAKEANAYnfimdlPQQFDtlvgegggqmsG 595
Cdd:PRK10851 77 GFVFQHYALFRhMTVFDNIAFGltvlprRERPNAAaikakvtqllEMVQLAHLADRY------PAQLS-----------G 139
|
170 180
....*....|....*....|....*....
gi 767920343 596 GQKQRVAIARALIRNPKILLLDMATSALD 624
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
454-677 |
5.20e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.43 E-value: 5.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL--RDQ 531
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEP--VLFSTTIAENIRYG------REDATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAI 603
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPHHLS-----------GGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 677
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
454-679 |
1.26e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHY-PSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQW 527
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 528 LRDQIGIVEQEP--VLFSTTIAENIRYGREDATMEDiVQAAKEANAYNFIMDLPQQFdtlVGEGGGQMSGGQKQRVAIAR 605
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPK-EKAEKIAAEKLEMVGLADEF---WEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 606 ALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 679
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
449-678 |
1.55e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 449 RIKGEiefhNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL 528
Cdd:PRK10253 7 RLRGE----QLTLGYGKY---TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 529 RDQIGIVEQEPVL-FSTTIAENIRYGR------------EDatmEDIVQAAKEANAynfIMDLP-QQFDTLvgegggqmS 594
Cdd:PRK10253 80 ARRIGLLAQNATTpGDITVQELVARGRyphqplftrwrkED---EEAVTKAMQATG---ITHLAdQSVDTL--------S 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 595 GGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVER 671
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQ 225
|
....*..
gi 767920343 672 GTHEELL 678
Cdd:PRK10253 226 GAPKEIV 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-678 |
1.99e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.09 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 471 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH------DIRSLNIQWLRDQIGIVEQEPVLFS- 543
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 544 TTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSAL 623
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 624 DNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
469-660 |
2.18e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 469 VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIGI--VEQEPVLF-STT 545
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 546 IAENIRYG--REDATMEDIVQAAKEANAYnfiMDLPQQFDTLvgegggqmSGGQKQRVAIARALIRNPKILLLDMATSAL 623
Cdd:PRK15439 103 VKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSL--------EVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 767920343 624 D-NESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTI 660
Cdd:PRK15439 172 TpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRI 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
470-678 |
2.30e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.06 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 470 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVL-FSTTIAE 548
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 549 NIRYGR------------EDatmEDIVQAAKEANaynfimdlpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLL 616
Cdd:PRK11231 96 LVAYGRspwlslwgrlsaED---NARVNQAMEQT----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 617 DMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
455-661 |
2.46e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.68 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 455 EFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGHDIRSLNIQwlRDQ 531
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFS-TTIAENIRYG---------REDAtmedIVQAAKEANAYNFIMDLPqqfDTLvgegggqmSGGQKQRV 601
Cdd:COG4136 78 IGILFQDDLLFPhLSVGENLAFAlpptigraqRRAR----VEQALEEAGLAGFADRDP---ATL--------SGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 602 AIARALIRNPKILLLDMATSALDNESEAMVQE-VLSKI-QHGHTIISVAHRLSTVRAADTII 661
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIrQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
202-398 |
2.58e-16 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 80.46 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 202 ARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTI--CGFLLGFfrGWKLTLVI 279
Cdd:cd18590 65 SRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLgmLGFMLSL--SWQLTLLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 280 ISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFF 359
Cdd:cd18590 143 LIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVY 222
|
170 180 190
....*....|....*....|....*....|....*....
gi 767920343 360 TGFVWCLIFLCYALAFWYGSTLvLDEGEYTPGTLVQIFL 398
Cdd:cd18590 223 LLVRRVLQLGVQVLMLYCGRQL-IQSGHLTTGSLVSFIL 260
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
172-394 |
2.71e-16 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 80.51 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 172 MIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQM 251
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 252 ALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIgaatiglSVSKFTDYELKAYAKA-GVVAD------EVISSMRT 324
Cdd:cd18544 120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL-------ATYLFRKKSRKAYREVrEKLSRlnaflqESISGMSV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 325 VAAFGGEKREVERYEK---NLVFAQRWGIRkgiVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18544 193 IQLFNREKREFEEFDEinqEYRKANLKSIK---LFALFRPLVELLSSLALALVLWYGGGQVLS-GAVTLGVLY 261
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
789-921 |
4.23e-16 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 79.61 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 789 MLVGSVGAAVNGTVTPLYAFLFSQILGTFsIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 868
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-LPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 767920343 869 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGLEAEPGHLVLLPLLGFI 921
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIV 130
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
454-675 |
4.79e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.52 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH------DIRSLNIQW 527
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 528 LRDQIGIVEQEPVLFS-TTIAENIRygreDATME----DIVQAAKEAN-----------AYNFIMDLP---QQfdtlvge 588
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLI----EAPCRvlglSKDQALARAEkllerlrlkpyADRFPLHLSggqQQ------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 589 gggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVR-AADTIIGFEHG 666
Cdd:PRK11124 149 -----------RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARkTASRVVYMENG 217
|
....*....
gi 767920343 667 TAVERGTHE 675
Cdd:PRK11124 218 HIVEQGDAS 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
454-677 |
4.82e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVK---ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW-LR 529
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 530 DQIGIVEQEP--VLFSTTIAENIRYGRE------DATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRV 601
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPEnlgippEEIRERVDESLKKVGMYEYRRHAPHLLS-----------GGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 602 AIARALIRNPKILLLDMATSALDNESEamvQEVLSKIQ-----HGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEE 676
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGR---REVVNTIKelnkkYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
.
gi 767920343 677 L 677
Cdd:PRK13633 231 I 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
454-679 |
5.39e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVkilNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLRdQIG 533
Cdd:PRK11607 20 LEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQR-PIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFS-TTIAENIRYG-REDATMEDIVQAAKE-----ANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIARA 606
Cdd:PRK11607 95 MMFQSYALFPhMTVEQNIAFGlKQDKLPKAEIASRVNemlglVHMQEFAKRKPHQLS-----------GGQRQRVALARS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 607 LIRNPKILLLDMATSALDNE-SEAMVQEVLSKIQH-GHTIISVAH-RLSTVRAADTIIGFEHGTAVERGTHEELLE 679
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
471-679 |
5.97e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 471 ILNDLNMVIKPGEMTALVGPSGAGKSTA----LQLIqrfydPCEGMVTVDGHDIRSLNIQWL---RDQIGIVEQEP---- 539
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTglalLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 540 -----VLfsTTIAENIRY--------GRED---ATMEDIVQAAKEANAYnfimdlPQQFDtlvgegggqmsGGQKQRVAI 603
Cdd:PRK15134 376 nprlnVL--QIIEEGLRVhqptlsaaQREQqviAVMEEVGLDPETRHRY------PAEFS-----------GGQRQRIAI 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTI--ISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 679
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
180-399 |
6.86e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 79.48 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQM-ALFIQRM 258
Cdd:cd18563 50 AGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLpDFLTNIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 259 TSTICGFLLgFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAK-AGVVADeVISSMRTVAAFGGEKREVER 337
Cdd:cd18563 130 MIIGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRlNSVLND-TLPGIRVVKAFGQEKREIKR 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 338 YEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQiFLS 399
Cdd:cd18563 208 FDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLS-GTMTLGTLVA-FLS 267
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
468-667 |
7.40e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 77.86 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 468 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDgHDIRSLNI------QWL---RDQIGIVEQe 538
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLaqasprEILalrRRTIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 539 pvlFSTTI---------AENIRygrEDATMEDIVQA-AKEANAYnfiMDLP---------------QQfdtlvgegggqm 593
Cdd:COG4778 101 ---FLRVIprvsaldvvAEPLL---ERGVDREEARArARELLAR---LNLPerlwdlppatfsggeQQ------------ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 594 sggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGT 667
Cdd:COG4778 160 ------RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIeEAKARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
454-681 |
7.82e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 533
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVL-FSTTIAENI----RYGREDA-TMEDIVQAAKEanaynfIMDLPQQFDTLVGEGGGQMSGgqkqRVAIARAL 607
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLlvfgRYFGMSTrEIEAVIPSLLE------FARLESKADARVSDLSGGMKR----RLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 608 IRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLrSLLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-399 |
9.53e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 79.09 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 179 YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQ-MALFIQr 257
Cdd:cd18564 60 LVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGvLPLLTN- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 258 mTSTICGFL-LGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVE 336
Cdd:cd18564 139 -LLTLVGMLgVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEER 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 337 RYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVqIFLS 399
Cdd:cd18564 218 RFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLA-GRLTPGDLL-VFLA 278
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
454-654 |
1.00e-15 |
|
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: 76.51 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQ-LIQRFYD-PCEGMVTVDGhdiRSLNIQWLRd 530
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAgVITGEILING---RPLDKNFQR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFST-TIAENIRYgreDATMEDIVQAAKEanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIR 609
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALRF---SALLRGLSVEQRK-------------------------------RLTIGVELAA 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767920343 610 NPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV 654
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSAS 171
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
465-678 |
1.27e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.89 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 465 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVL-FS 543
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 544 TTIAENIRYGR---------EDATMEDIVQAAKEANAYNFIMDLPqqFDTLvgegggqmSGGQKQRVAIARALIRNPKIL 614
Cdd:PRK09536 92 FDVRQVVEMGRtphrsrfdtWTETDRAAVERAMERTGVAQFADRP--VTSL--------SGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 615 LLDMATSALD-NESEAMVQEVLSKIQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK09536 162 LLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
458-678 |
1.35e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.70 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 458 NVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL-------------N 524
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 525 IQWLRDQIGIVEQEPVLFS-TTIAENIrygredatMEDIVQA-------AKEANAynFIMDLPQQFDTLVGEGGGQMSGG 596
Cdd:PRK10619 87 LRLLRTRLTMVFQHFNLWShMTVLENV--------MEAPIQVlglskqeARERAV--KYLAKVGIDERAQGKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 597 QKQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQH----GHTIISVAHRLSTVRAADTIIGFEH-GTAVER 671
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQQlaeeGKTMVVVTHEMGFARHVSSHVIFLHqGKIEEE 233
|
....*..
gi 767920343 672 GTHEELL 678
Cdd:PRK10619 234 GAPEQLF 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
454-678 |
1.49e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFST-TIAENIRYGR----------EDatmEDIVQaakEANAYNFIMDLPQQF-DTLvgegggqmsggqkqRV 601
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFGRfpyskgrltaED---REIID---EAIAYLDLEDLADRYlDELsgg--------qrqRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 602 AIARALIRNPKILLLDMATSALD-NESEAMVQeVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 677
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMK-LLRRLadELGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEI 223
|
.
gi 767920343 678 L 678
Cdd:COG4604 224 I 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
454-667 |
1.56e-15 |
|
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: 74.41 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVdGHDIRslniqwlrdqIG 533
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQepvlFSttiaeniryGREDAtmedivqaakeanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIRNPKI 613
Cdd:cd03221 67 YFEQ----LS---------GGEKM------------------------------------------RLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920343 614 LLLDMATSALDNESEAMVQEVLSKIQhgHTIISVAH-R--LSTVraADTIIGFEHGT 667
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
468-672 |
2.07e-15 |
|
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: 76.10 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 468 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLRdQIGIVEQEPVLF-STTI 546
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALR-RIGALIEAPGFYpNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 547 AENIR-----YGREDATME---DIV----QAAKEANAYNFIMdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKIL 614
Cdd:cd03268 90 RENLRllarlLGIRKKRIDevlDVVglkdSAKKKVKGFSLGM---KQ------------------RLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 615 LLDMATSALDNESEAMVQE-VLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERG 672
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRElILSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
458-681 |
3.41e-15 |
|
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: 76.02 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 458 NVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL-RDQIGIVE 536
Cdd:TIGR03410 5 NLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 537 QEPVLFST-TIAENIRYGREdatmediVQAAKEANAYNFIMDL-P-----------------QQfdtlvgegggqmsggq 597
Cdd:TIGR03410 82 QGREIFPRlTVEENLLTGLA-------ALPRRSRKIPDEIYELfPvlkemlgrrggdlsggqQQ---------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 598 kqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTH 674
Cdd:TIGR03410 139 --QLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAG 216
|
....*..
gi 767920343 675 EELLERK 681
Cdd:TIGR03410 217 DELDEDK 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
467-660 |
4.11e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.20 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 467 PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPC---EGMVTVDGHDIRSLNIqwlRDQ----IGIVEQEP 539
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNI---RDTeragIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 540 VLFST-TIAENIRYGRE--------DATM----EDIVQAAK-EANAYNFIMDLP---QQFdtlvgegggqmsggqkqrVA 602
Cdd:PRK13549 92 ALVKElSVLENIFLGNEitpggimdYDAMylraQKLLAQLKlDINPATPVGNLGlgqQQL------------------VE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 603 IARALIRNPKILLLDMATSALdNESEAmvqEVLSKI-----QHGHTIISVAHRLSTVRA-ADTI 660
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASL-TESET---AVLLDIirdlkAHGIACIYISHKLNEVKAiSDTI 213
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
452-700 |
4.25e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.97 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHYPSRP--EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI-----RSLN 524
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 525 IQWLRDQIGIVEQEP--VLFSTTIAENIRYGREDATmEDIVQAAKEANAYNFIMDLPQQFdtlVGEGGGQMSGGQKQRVA 602
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERG------T 673
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfeifS 240
|
250 260 270
....*....|....*....|....*....|..
gi 767920343 674 HEELL-----ERKGVYFTLVTLQSQGNQALNE 700
Cdd:PRK13645 241 NQELLtkieiDPPKLYQLMYKLKNKGIDLLNK 272
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
454-661 |
7.13e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.00 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPE-VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL---- 528
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 529 RDQIGIVEQEPVLFS-TTIAENIRYgreDATMEDIVQAAKEANAYNFIMDL---------PQQFDtlvgegggqmsGGQK 598
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRLgledrveyqPSQLS-----------GGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 599 QRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTII 661
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-679 |
8.80e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQWL 528
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 529 --RDQIGIVEQEPVLFS-TTIAENIRYG-------REDATMEDIVQ-AAKEANAY----NFIMDLPQQFDtlvgegggqm 593
Cdd:PRK14267 82 evRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDERVEwALKKAALWdevkDRLNDYPSNLS---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 594 sGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR-LSTVRAADTIIGFEHGTAVERG 672
Cdd:PRK14267 152 -GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
....*..
gi 767920343 673 THEELLE 679
Cdd:PRK14267 231 PTRKVFE 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
454-680 |
9.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 9.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYpsRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEP--VLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFImdlpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 611
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 612 KILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLER 680
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
470-677 |
9.93e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.28 E-value: 9.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 470 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN-IQWL--RDQIGIVEQEPvLFSTT- 545
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDP-LASLNp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 546 -------IAENIRYGREDATMEDIVQAAKEANAY-----NFIMDLPQQFDtlvgegggqmsGGQKQRVAIARALIRNPKI 613
Cdd:PRK15079 114 rmtigeiIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPHEFS-----------GGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920343 614 LLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFEHGTAVERGTHEEL 677
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 249
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
429-702 |
1.01e-14 |
|
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: 79.22 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 429 ETIDRKPIIDcmsEDGYKldrikgeIEFHNVTFHYpSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDP 508
Cdd:TIGR00957 622 DSIERRTIKP---GEGNS-------ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 509 CEGMVTVDGhdirslniqwlrdQIGIVEQEPVLFSTTIAENIRYGRedATMEDIVQAAKEANAynFIMDL---PQQFDTL 585
Cdd:TIGR00957 691 VEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK--ALNEKYYQQVLEACA--LLPDLeilPSGDRTE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 586 VGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNE-SEAMVQEVLSK--IQHGHTIISVAHRLSTVRAADTIIG 662
Cdd:TIGR00957 754 IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIV 833
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767920343 663 FEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQALNEED 702
Cdd:TIGR00957 834 MSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLED 873
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
165-565 |
1.19e-14 |
|
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: 77.92 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 165 LLNIESEMIKFASYYAGIAVAVLITGYIQicfwVIAAARQIQ----KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDI 240
Cdd:COG4615 40 LNATGAALARLLLLFAGLLVLLLLSRLAS----QLLLTRLGQhavaRLRLRLSRRILAAPLERLERIGAARLLAALTEDV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 241 NKINDAIAdQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVsplIGIGAATIGLSVSKFtdyeLKAYAKAGVVADEVIS 320
Cdd:COG4615 116 RTISQAFV-RLPELLQSVALVLGCLAYLAWLSPPLFLLTLVL---LGLGVAGYRLLVRRA----RRHLRRAREAEDRLFK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 321 SMRTVaaFGG--------EKRE----------VERYEKNLVFAQRWgirkgivmgFFTGFVW--CLIFLCYALAFWYGST 380
Cdd:COG4615 188 HFRAL--LEGfkelklnrRRRRaffdedlqptAERYRDLRIRADTI---------FALANNWgnLLFFALIGLILFLLPA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 381 LVLDEGEYTPG-TLVQIF----LSVIVGALnlgnasPcleAFATGRAAATSIfETIDRKpiIDCMSEDGYKLDRIK---- 451
Cdd:COG4615 257 LGWADPAVLSGfVLVLLFlrgpLSQLVGAL------P---TLSRANVALRKI-EELELA--LAAAEPAAADAAAPPapad 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 -GEIEFHNVTFHYPSRPEVK--ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL 528
Cdd:COG4615 325 fQTLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAY 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 767920343 529 RDQIGIVEQEPVLFSTTiaenirYGREDATMEDIVQA 565
Cdd:COG4615 405 RQLFSAVFSDFHLFDRL------LGLDGEADPARARE 435
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
456-627 |
1.34e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 456 FHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhDIRslniqwlrdqIGIV 535
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 536 EQEPVLFST-TIAENIR----------------YGREDATMEDIVQAAK------EANAYNF------IM--------DL 578
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLdgdaelraleaeleelEAKLAEPDEDLERLAElqeefeALGGWEAearaeeILsglgfpeeDL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767920343 579 PQQFDTL-----VgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNES 627
Cdd:COG0488 147 DRPVSELsggwrR-------------RVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
460-701 |
1.48e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 74.87 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 460 TFHYPS----RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH------------DIR-- 521
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdykyrckHIRmi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 522 ------SLNIqwlRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQfdtlvgegggqmsg 595
Cdd:COG4167 93 fqdpntSLNP---RLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQK-------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 596 gqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVR-AADTIIGFEHGTAVERG 672
Cdd:COG4167 156 ---QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQekLGISYIYVSQHLGIVKhISDKVLVMHQGEVVEYG 232
|
250 260
....*....|....*....|....*....
gi 767920343 673 THEELLERKGVYFTLVTLQSQGNQALNEE 701
Cdd:COG4167 233 KTAEVFANPQHEVTKRLIESHFGEALTAD 261
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
458-680 |
1.65e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.77 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 458 NVTFHYPSR-----PE--VKILNDLNMVIKPGEMTALVGPSGAGKST---ALQLIQRfydPCEGMVTVDGHDIRSLN--- 524
Cdd:PRK11308 10 DLKKHYPVKrglfkPErlVKALDGVSFTLERGKTLAVVGESGCGKSTlarLLTMIET---PTGGELYYQGQDLLKADpea 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 525 IQWLRDQIGIVEQ-----------------EPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYnfimdlPQQFdtlvg 587
Cdd:PRK11308 87 QKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY------PHMF----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 588 egggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFE 664
Cdd:PRK11308 156 ------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEhIADEVMVMY 229
|
250
....*....|....*.
gi 767920343 665 HGTAVERGTHEELLER 680
Cdd:PRK11308 230 LGRCVEKGTKEQIFNN 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
454-672 |
1.66e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.47 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIG 533
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLF-STTIAENIRYGREDATMEdIVQAAKEANAYNFIMDLP----QQFDTLvgegggqmSGGQKQRVAIARALI 608
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYLAQLKGLK-KEEARRRIDEWLERLELSeyanKRVEEL--------SKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 609 RNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTV-RAADTIIGFEHGTAVERG 672
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
466-645 |
2.60e-14 |
|
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: 73.07 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 466 RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI---QRFYDPCEGMVTVDGhdiRSLNIQWLRDQIGIVEQEPVLF 542
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 543 ST-TIAENIRYGREDATMEDIVQAAKEANAYnfIMDLPQQFDTLVGEGGGQMSGG-QKQRVAIARALIRNPKILLLDMAT 620
Cdd:cd03234 94 PGlTVRETLTYTAILRLPRKSSDAIRKKRVE--DVLLRDLALTRIGGNLVKGISGgERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180
....*....|....*....|....*
gi 767920343 621 SALDNESEAMVQEVLSKIQHGHTII 645
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIV 196
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
472-654 |
3.12e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI---RSLNIQWLRDQIGIVEQE-PVLFSTTIA 547
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDhHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 548 ENIRYGR--EDATMEDI---VQAAKEA-----NAYNFIMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKIL 614
Cdd:PRK10908 98 DNVAIPLiiAGASGDDIrrrVSAALDKvglldKAKNFPIQLSggeQQ------------------RVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767920343 615 LLDMATSALDNE-SEAMVQ--EVLSKIqhGHTIISVAHRLSTV 654
Cdd:PRK10908 160 LADEPTGNLDDAlSEGILRlfEEFNRV--GVTVLMATHDIGLI 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
454-650 |
3.76e-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: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPS-RPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdpcegmvtvdghdirslniQWLRDQI 532
Cdd:cd03223 1 IELENLSLATPDgRV---LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-------------------PWGSGRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVLF--------STTIAENIRYGREDATMEDivqaakEanaynfimdlpQQfdtlvgegggqmsggqkqRVAIA 604
Cdd:cd03223 59 GMPEGEDLLFlpqrpylpLGTLREQLIYPWDDVLSGG------E-----------QQ------------------RLAFA 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767920343 605 RALIRNPKILLLDMATSALDNESEAMVQEVLSkiQHGHTIISVAHR 650
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEDRLYQLLK--ELGITVISVGHR 147
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
212-394 |
5.30e-14 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 73.63 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 212 YFRRIMRMEIGWFDCNSVGELNTRFSdDINKINDAIADQM-ALFIQRMTSTICGFLLgFFRGWKLTLVIISVSPLIGIga 290
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTiSLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYIL-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 291 aTIGLSVSKFTDY---ELKAYAK--AGVVadEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKG---IVMGFFTGF 362
Cdd:cd18570 157 -IILLFNKPFKKKnreVMESNAElnSYLI--ESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGklsNLQSSIKGL 233
|
170 180 190
....*....|....*....|....*....|..
gi 767920343 363 VwCLIFLcyALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18570 234 I-SLIGS--LLILWIGSYLVIK-GQLSLGQLI 261
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
470-617 |
9.12e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.81 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 470 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI-QWLRDQIGIVEQEPVLF-STTIA 547
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFrKLTVE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 548 ENIRYGREDATmEDIVQAAKEANAynFIMDLpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLD 617
Cdd:cd03218 94 ENILAVLEIRG-LSKKEREEKLEE--LLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
472-649 |
1.44e-13 |
|
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: 70.96 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIGIVEQEPVLFSTTIAENIr 551
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----PDRMVVFQNYSLLPWLTVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 552 YGREDATMEDIVQAAKEAnaynfIMDLPQQFDTLVGEGGGQMSGGQ---KQRVAIARALIRNPKILLLDMATSALDNESE 628
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRA-----IVEEHIALVGLTEAADKRPGQLSggmKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|...
gi 767920343 629 AMVQEVLSKI--QHGHTIISVAH 649
Cdd:TIGR01184 151 GNLQEELMQIweEHRVTVLMVTH 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
457-670 |
2.27e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 457 HNVTFHYPS------RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN------ 524
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrka 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 525 ----IQWL-RDQIGIVE---------QEPVLFSTTIAENIRYGREDAtMEDIVQAAKEanaynfIMD-LPQQFDtlvgeg 589
Cdd:PRK10419 87 frrdIQMVfQDSISAVNprktvreiiREPLRHLLSLDKAERLARASE-MLRAVDLDDS------VLDkRPPQLS------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 590 ggqmsGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTV-RAADTIIGFEHG 666
Cdd:PRK10419 154 -----GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRVMVMDNG 228
|
....
gi 767920343 667 TAVE 670
Cdd:PRK10419 229 QIVE 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
453-677 |
2.58e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 453 EIEFHNVTFHYPSRP--EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL------- 523
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 524 -----------------NIQWLRDQIGIVEQ--EPVLFSTTIAENIRYGREDATMEDiVQAAKEANAYNFIMDLPQQFdt 584
Cdd:PRK13651 82 kvleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 585 lVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIG 662
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIF 237
|
250
....*....|....*.
gi 767920343 663 FEHGTAVERG-THEEL 677
Cdd:PRK13651 238 FKDGKIIKDGdTYDIL 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
458-680 |
2.70e-13 |
|
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: 73.57 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 458 NVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKS-TAL---QLIQRFYDPCEGMVTVDGHDIRSLNIQWLR---- 529
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALsilRLLPDPAAHPSGSILFDGQDLLGLSERELRrirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 530 DQIGIVEQEPV-----LFS--TTIAENIR----YGREDATME--------DIVQAAKEANAYnfimdlP-------QQfd 583
Cdd:COG4172 92 NRIAMIFQEPMtslnpLHTigKQIAEVLRlhrgLSGAAARARalellervGIPDPERRLDAY------PhqlsggqRQ-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 584 tlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTI 660
Cdd:COG4172 164 ----------------RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQreLGMALLLITHDLGVVRRfADRV 227
|
250 260
....*....|....*....|
gi 767920343 661 IGFEHGTAVERGTHEELLER 680
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFAA 247
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
452-684 |
2.74e-13 |
|
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: 71.04 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHYPSRPEVkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDpCEGMVTVDGHDIRSLNIQWLRDQ 531
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFSTTIAENIR-YGREDAtmEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRN 610
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 611 PKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVY 684
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
173-394 |
3.30e-13 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 71.42 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 173 IKFASYYAgiAVAVLITGYIQicFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA 252
Cdd:cd18574 46 LKLLGLYL--LQSLLTFAYIS--LLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 253 LFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIG-----LSVSkftdyeLKAY-AKAGVVADEVISSMRTVA 326
Cdd:cd18574 122 QGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGsflrkLSRR------AQAQvAKATGVADEALGNIRTVR 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 327 AFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTG----FVWCLIFLCYalafWYGSTLVlDEGEYTPGTLV 394
Cdd:cd18574 196 AFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGlsnlALNGIVLGVL----YYGGSLV-SRGELTAGDLM 262
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
465-672 |
3.83e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 465 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQ--IGIVEQE-PVL 541
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQElSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 542 FSTTIAENIRYGRE------DATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGqkqrVAIARALIRNPKILL 615
Cdd:PRK09700 93 DELTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM----LEIAKTLMLDAKVII 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 616 LDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 672
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
454-681 |
4.37e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 533
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQ----EPvlfSTTIAENIR-----YGREDATMEDIVQAAKEanaynfIMDLPQQFDTLVGEGGGQMSGgqkqRVAIA 604
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLvfgryFGLSAAAARALVPPLLE------FAKLENKADAKVGELSGGMKR----RLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 605 RALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 681
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLrSLLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
182-342 |
4.58e-13 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 70.96 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 182 IAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTST 261
Cdd:cd18589 45 LTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 262 ICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKN 341
Cdd:cd18589 125 LFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQR 204
|
.
gi 767920343 342 L 342
Cdd:cd18589 205 L 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
454-672 |
5.42e-13 |
|
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: 69.10 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPS-------------------RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT 514
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 515 VDGhdirslNIQWLRD-QIGIveqEPVLfstTIAENIR-----YGREDATMEDIvqaakeanaYNFIMD---LPQQFDTL 585
Cdd:cd03220 81 VRG------RVSSLLGlGGGF---NPEL---TGRENIYlngrlLGLSRKEIDEK---------IDEIIEfseLGDFIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 586 VgeggGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRA-ADTIIGF 663
Cdd:cd03220 140 V----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVL 215
|
....*....
gi 767920343 664 EHGTAVERG 672
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
466-679 |
5.74e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 466 RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQrFYDP----CEGMVTVDGHDIrslNIQWLRDQIGIVEQEPVL 541
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 542 FST-TIAENI------RYGREDAT------MEDIVQAAKEANAYNFIMDLPQQFDTLvgegggqmSGGQKQRVAIARALI 608
Cdd:TIGR00955 111 IPTlTVREHLmfqahlRMPRRVTKkekrerVDEVLQALGLRKCANTRIGVPGRVKGL--------SGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 609 RNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLST--VRAADTIIGFEHGTAVERGTHEELLE 679
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
458-679 |
5.86e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 458 NVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQ 537
Cdd:PRK10575 16 NVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 538 E-PVLFSTTIAENI------------RYGREDAtmedivQAAKEANAYNFIMDLPQQF-DTLvgegggqmSGGQKQRVAI 603
Cdd:PRK10575 93 QlPAAEGMTVRELVaigrypwhgalgRFGAADR------EKVEEAISLVGLKPLAHRLvDSL--------SGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 604 ARALIRNPKILLLDMATSALD----NESEAMVQEvLSKiQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDiahqVDVLALVHR-LSQ-ERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
.
gi 767920343 679 E 679
Cdd:PRK10575 237 R 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
467-670 |
8.17e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 467 PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPC---EGMVTVDG-----HDIRSlniqwlRDQIGIV--E 536
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRD------SEALGIViiH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 537 QE----PVLfstTIAENIRYGREDATM------EDIVQAAK-------EANAYNFIMDL---PQQFdtlvgegggqmsgg 596
Cdd:NF040905 85 QElaliPYL---SIAENIFLGNERAKRgvidwnETNRRAREllakvglDESPDTLVTDIgvgKQQL-------------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 597 qkqrVAIARALIRNPKILLLDMATSAL-DNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 670
Cdd:NF040905 148 ----VEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
181-404 |
8.60e-13 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 70.12 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 181 GIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRM---EIGWFdcnSVGELNTRFSDDINKIndaiadQMALF-IQ 256
Cdd:cd18548 47 LLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFsfaEIDKF---GTSSLITRLTNDVTQV------QNFVMmLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 257 RMTST-----ICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGE 331
Cdd:cd18548 118 RMLVRapimlIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNRE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 332 KREVERYEK-NLVFAQRwGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVlDEGEYTPGTLV-------QIFLSVIVG 403
Cdd:cd18548 198 DYEEERFDKaNDDLTDT-SLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLI-NAGSLQVGDLVafinylmQILMSLMML 275
|
.
gi 767920343 404 A 404
Cdd:cd18548 276 S 276
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
468-682 |
1.20e-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: 67.55 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 468 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRF--YDPCEGMVTVDGHDIRSLNIQwLRDQIGI--VEQEPVLFS 543
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 544 -TTIAENIRY------GREdatmedivqaakeanaynfimdlpqqfdtlvgegggqmsggqKQRVAIARALIRNPKILLL 616
Cdd:cd03217 91 gVKNADFLRYvnegfsGGE------------------------------------------KKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 617 DMATSALDNESEAMVQEVLSKIQH-GHTIISVAH--RLSTVRAADTIIGFEHGTAVERGTHE--ELLERKG 682
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
454-678 |
1.31e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.05 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNV--TFHYPS----RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI------- 520
Cdd:PRK15112 5 LEVRNLskTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 521 RSLNIQWL----------RDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQfdtlvgegg 590
Cdd:PRK15112 85 RSQRIRMIfqdpstslnpRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQK--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 591 gqmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTI--ISVAHRLSTVR-AADTIIGFEHGT 667
Cdd:PRK15112 156 --------QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKhISDQVLVMHQGE 227
|
250
....*....|.
gi 767920343 668 AVERGTHEELL 678
Cdd:PRK15112 228 VVERGSTADVL 238
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
463-711 |
1.35e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.12 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 463 YPSRPEVkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVtvdghdirslniqWLRDQIGIVEQEPVLF 542
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 543 STTIAENIRYGRED--ATMEDIVQAAK-EANaynfIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMA 619
Cdd:PTZ00243 734 NATVRGNILFFDEEdaARLADAVRVSQlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 620 TSALDNE-SEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLeRKGVYFTLVTlQSQGNQAL 698
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATLAA-ELKENKDS 887
|
250
....*....|...
gi 767920343 699 NEEDiKDATEDDM 711
Cdd:PTZ00243 888 KEGD-ADAEVAEV 899
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
440-654 |
1.39e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.06 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 440 MSEDGYKLDRIKGEIEFH--NVTFHYPSRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQ-LIQRFydpCEGMVT- 514
Cdd:TIGR00956 744 DVNDEKDMEKESGEDIFHwrNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERV---TTGVITg 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 515 ----VDGHDIRSLniqwLRDQIGIVEQEPV-LFSTTIAENIRYG---REDATMEDivqaaKEANAY-NFIMDL---PQQF 582
Cdd:TIGR00956 821 gdrlVNGRPLDSS----FQRSIGYVQQQDLhLPTSTVRESLRFSaylRQPKSVSK-----SEKMEYvEEVIKLlemESYA 891
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 583 DTLVGEGGGQMSGGQKQRVAIARALIRNPKILL-LDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV 654
Cdd:TIGR00956 892 DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLaDHGQAILCTIHQPSAI 965
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
452-651 |
1.48e-12 |
|
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: 71.87 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEIEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDpCEGMVTVDGHDIRSLNIQWLRDQ 531
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFSTTIAENIRyGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 611
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767920343 612 KILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRL 651
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
454-638 |
1.58e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.74 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYP-SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI------Rslniq 526
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 527 wlrdqiGIVEQEPVLFS-TTIAENIRYG----------REDATMEDIVQAAKEANAYNFIMDLP---QQfdtlvgegggq 592
Cdd:COG4525 79 ------GVVFQKDALLPwLNVLDNVAFGlrlrgvpkaeRRARAEELLALVGLADFARRRIWQLSggmRQ----------- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767920343 593 msggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI 638
Cdd:COG4525 142 -------RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
468-684 |
1.95e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.49 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 468 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVD----GHDIRSL------------NIQWLRDQ 531
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHelitnpyskkikNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEP--VLFSTTIAENIRYGREDATMEDIvQAAKEANAYNFIMDLPQQFdtlVGEGGGQMSGGQKQRVAIARALIR 609
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKS-EAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767920343 610 NPKILLLDMATSALDNESEA-MVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERKGVY 684
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
773-905 |
2.79e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.58 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 773 APVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPdkeEQRSQINGVCLLFVAMGCVSLFTQFLQGY 852
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG---GDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 767920343 853 AFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGL 905
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQF 134
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
458-666 |
2.90e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 458 NVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQrfydpceGMVTVDGHDIRSLN--IQWLRDQIGIV 535
Cdd:PRK11247 17 AVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLA-------GLETPSAGELLAGTapLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 536 EQEPVLFS-TTIAENIRYG-----REDATME-DIVQAAKEANAYNFIMDLPQQfdtlvgegggqmsggqkQRVAIARALI 608
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGlkgqwRDAALQAlAAVGLADRANEWPAALSGGQK-----------------QRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 609 RNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHG 666
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEG 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
462-640 |
3.22e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.80 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 462 HYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWlrdqiGIVEQ-EPV 540
Cdd:PRK11248 10 DYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQnEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 541 LFSTTIAENIRYG----------REDATMEDIVQAAKEANAYNFIMDLpqqfdtlvgegggqmSGGQKQRVAIARALIRN 610
Cdd:PRK11248 82 LPWRNVQDNVAFGlqlagvekmqRLEIAHQMLKKVGLEGAEKRYIWQL---------------SGGQRQRVGIARALAAN 146
|
170 180 190
....*....|....*....|....*....|
gi 767920343 611 PKILLLDMATSALDNESEAMVQEVLSKIQH 640
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQ 176
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
461-694 |
3.63e-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: 70.81 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 461 FHYPSRPEVkilNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIGIVEQEPV 540
Cdd:TIGR01257 938 FEPSGRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 541 LFS-TTIAENIRY-----GR--EDATMEdiVQAAKEANAYNFIMDLPQQfdtlvgegggQMSGGQKQRVAIARALIRNPK 612
Cdd:TIGR01257 1014 LFHhLTVAEHILFyaqlkGRswEEAQLE--MEAMLEDTGLHHKRNEEAQ----------DLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 613 ILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE--RKGVYFTLV- 688
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPLFLKNcfGTGFYLTLVr 1161
|
....*....
gi 767920343 689 ---TLQSQG 694
Cdd:TIGR01257 1162 kmkNIQSQR 1170
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-678 |
3.78e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.81 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 471 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGM-----VTVDGHDIRSL-NIQWLRDQIGIVEQEPVLFST 544
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 545 TIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALD 624
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 625 NESEAMVQEVLSKIQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
458-651 |
4.52e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.42 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 458 NVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiQWLRDQ-IGIVE 536
Cdd:COG1101 8 SKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRAKyIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 537 QEPVL---FSTTIAEN------------IRYGREDATMEDIVQAAKEANaynfiMDLPQQFDTlvgegggqmsggqkqRV 601
Cdd:COG1101 87 QDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-----LGLENRLDT---------------KV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 602 ---------AIA--RALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRL 651
Cdd:COG1101 147 gllsggqrqALSllMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
454-680 |
4.61e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.71 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVdGHDIRslniqwlrdqIG 533
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLF--STTIAENIRYGREDATMEDIVQAAKeanAYNFImdlPQQFDTLVgegggqmsggqKQ-------RVAIA 604
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLG---RFLFS---GDDAFKPV-----------GVlsggekaRLALA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 605 RALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhGhTIISVAH-R--LSTVraADTIIGFEHGTAVER-GTHEELLER 680
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDDYLEK 520
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
454-649 |
5.85e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHY-PSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW---LR 529
Cdd:PRK10584 7 VEVHHLKKSVgQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 530 DQ-IGIVEQEPVLFSTTIA-ENI------RYGREDATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRV 601
Cdd:PRK10584 87 AKhVGFVFQSFMLIPTLNAlENVelpallRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLS-----------GGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767920343 602 AIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAH 649
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
179-394 |
5.89e-12 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 67.49 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 179 YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRM 258
Cdd:cd18545 46 FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 259 TSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIG-LSVSKFTDYELKayaKAGVVAD--EVISSMRTVAAFGGEKREV 335
Cdd:cd18545 126 LTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRrRARKAWQRVRKK---ISNLNAYlhESISGIRVIQSFAREDENE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 336 ERYE---KNLVFAQRWGIRkgivmgfFTGFVWCLIFLCYALA----FWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18545 203 EIFDelnRENRKANMRAVR-------LNALFWPLVELISALGtalvYWYGGKLVLG-GAITVGVLV 260
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
461-667 |
9.35e-12 |
|
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: 65.82 E-value: 9.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 461 FHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRdQIGIV--EQE 538
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 539 PVLFSTTIAENIRYGREDATMEDiVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGgqkqRVAIARALIRNPKILLLDM 618
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDLPP-ARFKKRLDELSELLDLEELLDTPVRQLSLGQRM----RAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767920343 619 ATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGT 667
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNreRGTTVLLTSHYMKDIEAlARRVLVIDKGR 231
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
170-340 |
1.13e-11 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 66.66 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 170 SEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIAD 249
Cdd:cd18547 42 SGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 250 QMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFG 329
Cdd:cd18547 122 SLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFN 201
|
170
....*....|.
gi 767920343 330 GEKREVERYEK 340
Cdd:cd18547 202 REEEAIEEFDE 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
213-731 |
1.35e-11 |
|
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: 68.78 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 213 FRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIAdqMALFIQrMTSTICGFLLGFFrgWKLtlviISVSPLIGIGA-- 290
Cdd:TIGR01271 162 YKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLA--LAHFVW-IAPLQVILLMGLI--WEL----LEVNGFCGLGFli 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 291 ------ATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKrEVERYEKNLVFAQRWGIRKGIVMGFFtgfvw 364
Cdd:TIGR01271 233 llalfqACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEE-AMEKIIKNIRQDELKLTRKIAYLRYF----- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 365 cliflcYALAFWYGSTLVldegeytpgtlvqIFLSVIVGALNLG--------NASPCLE-AFATGRAAATSIFETIDR-- 433
Cdd:TIGR01271 307 ------YSSAFFFSGFFV-------------VFLSVVPYALIKGiilrriftTISYCIVlRMTVTRQFPGAIQTWYDSlg 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 434 --KPIIDCMSEDGYKL---DRIKGEIEFHNVT-------------------------------FHYPSRPEVKILNDLNM 477
Cdd:TIGR01271 368 aiTKIQDFLCKEEYKTleyNLTTTEVEMVNVTaswdegigelfekikqnnkarkqpngddglfFSNFSLYVTPVLKNISF 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 478 VIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhdirslniqwlrdQIGIVEQEPVLFSTTIAENIRYG--RE 555
Cdd:TIGR01271 448 KLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFGlsYD 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 556 DATMEDIVQAAK-EANaynfIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQE- 633
Cdd:TIGR01271 515 EYRYTSVIKACQlEED----IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEs 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 634 VLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTlqsqGNQALNEedIKDATEDDMLA 713
Cdd:TIGR01271 591 CLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLL----GLEAFDN--FSAERRNSILT 664
|
570 580
....*....|....*....|....*..
gi 767920343 714 RTFSR---------GSYQDSLRASIRQ 731
Cdd:TIGR01271 665 ETLRRvsidgdstvFSGPETIKQSFKQ 691
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
454-680 |
1.61e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.49 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYP-------------------SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT 514
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 515 VDGhdirslNIQWLrdqIGiveqepvlFST------TIAENIR-----YG---RE-DATMEDIVQAAkeanaynfimDLP 579
Cdd:COG1134 85 VNG------RVSAL---LE--------LGAgfhpelTGRENIYlngrlLGlsrKEiDEKFDEIVEFA----------ELG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 580 QQFDT---------LVgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNE----SEAMVQEvlsKIQHGHTIIS 646
Cdd:COG1134 138 DFIDQpvktyssgmRA-------------RLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE---LRESGRTVIF 201
|
250 260 270
....*....|....*....|....*....|....*
gi 767920343 647 VAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLER 680
Cdd:COG1134 202 VSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
467-667 |
1.98e-11 |
|
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: 64.66 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 467 PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMV--------TVDGHDIRSLNiqwlRDQIGIVEQE 538
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesEPSFEATRSRN----RYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 539 PVLFSTTIAENIRYGreDATMEDIVQAAKEANAYNFIMD-LPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLD 617
Cdd:cd03290 88 PWLLNATVEENITFG--SPFNKQRYKAVTDACSLQPDIDlLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920343 618 MATSALD-NESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:cd03290 166 DPFSALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
466-636 |
2.17e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 466 RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQWL--RDQIgiveqEP 539
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeaCHYLghRNAM-----KP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 540 VLfstTIAENIR-----YGREDATmediVQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsggqkQRVAIARAL 607
Cdd:PRK13539 87 AL---TVAENLEfwaafLGGEELD----IAAALEAVGLAPLAHLPfgylsagQK-----------------RRVALARLL 142
|
170 180
....*....|....*....|....*....
gi 767920343 608 IRNPKILLLDMATSALDNESEAMVQEVLS 636
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAELIR 171
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
458-666 |
2.64e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.21 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 458 NVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDghDIRSLNIQWLRDQIGIVEQ 537
Cdd:PRK11000 8 NVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 538 EPVLFS-TTIAENIRYGREDATMEDIvQAAKEANAYNFIMdlpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLL 616
Cdd:PRK11000 83 SYALYPhLSVAENMSFGLKLAGAKKE-EINQRVNQVAEVL----QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 617 DMATSALDNESEAMVQEVLSKIQH--GHTIISVAHrlSTVRA---ADTIIGFEHG 666
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTH--DQVEAmtlADKIVVLDAG 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
455-677 |
3.23e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 455 EFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlRDQ--- 531
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST---TAAlaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 -IGIVEQE----PVLfstTIAENIRYGR--EDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGqkqrVAIA 604
Cdd:PRK11288 80 gVAIIYQElhlvPEM---TVAENLYLGQlpHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQM----VEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 605 RALIRNPKILLLDMATSALD-NESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVErgTHEEL 677
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSaREIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
471-678 |
3.80e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 471 ILNDLNMVIKPGEMTALVGPSGAGKS-TALQLIQRFYDP----CEGMVTVDGHDIRSLNIQWLR----DQIGIVEQEPVL 541
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 542 fSTTIAENI-----------RYGREDATMEDIV---------QAAKEANaynfimDLPQQFDtlvgegggqmsGGQKQRV 601
Cdd:PRK15134 104 -SLNPLHTLekqlyevlslhRGMRREAARGEILncldrvgirQAAKRLT------DYPHQLS-----------GGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 602 AIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLF 245
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
460-666 |
3.89e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.65 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 460 TFHypsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQ----LIQRFYDPcEGMVTVDGHDIR-----SLNIQWLRD 530
Cdd:PRK09984 13 TFN-----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSA-GSHIELLGRTVQregrlARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIG-IVEQEPVLFSTTIAENIRYGREDAT--------------MEDIVQAAKEANAYNFIMdlpQQFDTLvgegggqmSG 595
Cdd:PRK09984 87 NTGyIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfswftreqKQRALQALTRVGMVHFAH---QRVSTL--------SG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 596 GQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHG 666
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQG 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
471-677 |
4.10e-11 |
|
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: 64.88 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 471 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLrdqigiveqepvlFSTTIAENI 550
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWI-------------MPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 551 RYG--REDATMEDIVQAAKEANAynfIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESE 628
Cdd:cd03291 119 IFGvsYDEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767920343 629 AMVQE-VLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEEL 677
Cdd:cd03291 196 KEIFEsCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
473-677 |
5.67e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.86 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 473 NDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlrdQI---GIVE--QEPVLF-STTI 546
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH----QIarmGVVRtfQHVRLFrEMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 547 AENI--------------------RYGRedATMEDIVQAA---------KEAN------AYNfimdlpQQfdtlvgeggg 591
Cdd:PRK11300 98 IENLlvaqhqqlktglfsgllktpAFRR--AESEALDRAAtwlervgllEHANrqagnlAYG------QQ---------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 592 qmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTA 668
Cdd:PRK11300 160 -------RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrnEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTP 232
|
....*....
gi 767920343 669 VERGTHEEL 677
Cdd:PRK11300 233 LANGTPEEI 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
469-660 |
5.77e-11 |
|
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: 66.00 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 469 VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPC---EGMVTVDGHDIRSLNIQWL-RDQIGIVEQEPVLF-S 543
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 544 TTIAENIRYGRE---------DATM----EDIVQAAK--EANAYNFIMDLPQQFDTLVgegggqmsggqkqrvAIARALI 608
Cdd:TIGR02633 93 LSVAENIFLGNEitlpggrmaYNAMylraKNLLRELQldADNVTRPVGDYGGGQQQLV---------------EIAKALN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767920343 609 RNPKILLLDMATSAL-DNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTI 660
Cdd:TIGR02633 158 KQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTI 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
454-683 |
6.19e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrslnIQW-----L 528
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----TDWqtakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 529 RDQIGIVEQEPVLFS-TTIAENIRYGREDATMEDIVQAAKEanaynfIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARAL 607
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKW------VYELFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 608 IRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELLERKG 682
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
.
gi 767920343 683 V 683
Cdd:PRK11614 230 V 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
457-617 |
6.59e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.51 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 457 HNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTAlqliqrFY------DPCEGMVTVDGHDIRSLNIqWLRD 530
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGI--VEQEPVLF-STTIAENIRygredATMEDIVQAAKEANAYnfIMDLPQQF----------DTLvgegggqmsggq 597
Cdd:COG1137 77 RLGIgyLPQEASIFrKLTVEDNIL-----AVLELRKLSKKEREER--LEELLEEFgithlrkskaYSLsgg--------e 141
|
170 180
....*....|....*....|
gi 767920343 598 kqRVAIARALIRNPKILLLD 617
Cdd:COG1137 142 rrRVEIARALATNPKFILLD 161
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
458-680 |
6.72e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 6.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 458 NVTFHYpSRPEVKILNDLNMVIKPGEMTALVGPSGAGKS-TALQLIqRFYDPCEGMVTVDGHDIRSLNIQW--LRDQ--- 531
Cdd:PRK10261 19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMLLRRRSRQVieLSEQsaa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 ---------IGIVEQEPV-----LFST--TIAENIR----YGREDATME--DIVQAAKEANAYNFIMDLPQQFDtlvgeg 589
Cdd:PRK10261 97 qmrhvrgadMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREEAMVEakRMLDQVRIPEAQTILSRYPHQLS------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 590 ggqmsGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHT--IISVAHRLSTV-RAADTIIGFEHG 666
Cdd:PRK10261 171 -----GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRVLVMYQG 245
|
250
....*....|....
gi 767920343 667 TAVERGTHEELLER 680
Cdd:PRK10261 246 EAVETGSVEQIFHA 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
454-679 |
8.15e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.59 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPS--RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT-------VDGHDIRSLN 524
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 525 IQWLRDQIGIVEQEPVLFS-TTIAENI----------RYGREDATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqm 593
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLteaiglelpdELARMKAVITLKMVGFDEEKAEEILDKYPDELS---------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 594 sGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL--SKIQHGHTIISVAHRLSTVR-AADTIIGFEHGTAVE 670
Cdd:TIGR03269 430 -EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLdVCDRAALMRDGKIVK 508
|
....*....
gi 767920343 671 RGTHEELLE 679
Cdd:TIGR03269 509 IGDPEEIVE 517
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
180-394 |
9.08e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 63.76 E-value: 9.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITGYIQIC---FWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDdINKINDAIADQMALFIQ 256
Cdd:cd18566 46 IGVVIAILLESLLRLLrsyILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNS-LEQIREFLTGQALLALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 257 RMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGlsvskftdYELKAYAKAGVVAD--------EVISSMRTVAAF 328
Cdd:cd18566 125 DLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLG--------PILRRALKERSRADerrqnfliETLTGIHTIKAM 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 329 GGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18566 197 AMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVIN-GDLTVGALI 261
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
471-652 |
1.54e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.14 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 471 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW---LRDQ-IGIVEQ-EPVLFSTT 545
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 546 IAENIrygredaTMEDIVQAAK--EANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSAL 623
Cdd:PRK11629 104 ALENV-------AMPLLIGKKKpaEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 767920343 624 DNESEAMVQEVLSKI--QHGHTIISVAHRLS 652
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
454-656 |
1.91e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHdirslniqwLRdqIG 533
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFST---TIAENIRYgREDATMEDIVQAAKEANAYNFImDLPQQfdtlvgegggQMSGGQKQRVAIARALIRN 610
Cdd:PRK09544 71 YVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767920343 611 PKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA 656
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMA 186
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
208-400 |
3.48e-10 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 62.08 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 208 MRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDaiadqMA------LFIQrmTSTICG-FLLGFFRGWKLTLVII 280
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISE-----LAhhgpedLFIS--IITIIGsFIILLTINVPLTLIVF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 281 SVSPLIGIGAATIGLsvsKFTDYELKAYAKAGVVADEV---ISSMRTVAAFGGEKREVERYEK-NLVF--AQRWGIRkgi 354
Cdd:cd18549 150 ALLPLMIIFTIYFNK---KMKKAFRRVREKIGEINAQLedsLSGIRVVKAFANEEYEIEKFDEgNDRFleSKKKAYK--- 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767920343 355 VMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQIFLSV 400
Cdd:cd18549 224 AMAYFFSGMNFFTNLLNLVVLVAGGYFII-KGEITLGDLVAFLLYV 268
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
465-649 |
3.57e-10 |
|
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: 60.58 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 465 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFST 544
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 545 TIAENIRYGREDATMEDIVQAAKEANAYNFiMDLPqqFDTLvgegggqmSGGQKQRVAIARALIRNPKILLLDMATSALD 624
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGF-EDRP--VAQL--------SAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*.
gi 767920343 625 NESEAMVQEVL-SKIQHGHTIISVAH 649
Cdd:cd03231 158 KAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
461-693 |
3.98e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.56 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 461 FHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--DIRSLNIQWLRDQIGIVEQE 538
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 539 P--VLFSTTIAENIRYGREDATM--EDIVQAAKEA----NAYNFiMDLPQQfdtlvgegggQMSGGQKQRVAIARALIRN 610
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVpeAEITRRVDEAltlvDAQHF-RHQPIQ----------CLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 611 PKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISvAHRLSTV-RAADTIIGFEHGTAVERG------THEELLERK 681
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNHVIIS-SHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQA 233
|
250
....*....|...
gi 767920343 682 GVYFT-LVTLQSQ 693
Cdd:PRK13638 234 GLTQPwLVKLHTQ 246
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
470-640 |
4.26e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.06 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 470 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI-QWLRDQIGIVEQEPVLFST-TIA 547
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 548 ENIRYG---REDATMEdivQAAKEANaynfimDLPQQFDT--LVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSA 622
Cdd:PRK10895 97 DNLMAVlqiRDDLSAE---QREDRAN------ELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170
....*....|....*...
gi 767920343 623 LDNESeamVQEVLSKIQH 640
Cdd:PRK10895 168 VDPIS---VIDIKRIIEH 182
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
823-902 |
6.10e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 61.41 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 823 EEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQV 902
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKV 106
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
200-424 |
1.26e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 60.24 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 200 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIqrmTST-----ICGFLlgFFRGWK 274
Cdd:cd18778 67 AEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI---TNVltlvgVAIIL--FSINPK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 275 LTLVIISVSPLIGIGAAtiglsvsKFTDYELKAYAKA--------GVVADEvISSMRTVAAFGGEKREVERYEK------ 340
Cdd:cd18778 142 LALLTLIPIPFLALGAW-------LYSKKVRPRYRKVrealgelnALLQDN-LSGIREIQAFGREEEEAKRFEAlsrryr 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 341 --NLVFAQRWGIrKGIVMGFFTGfvwclifLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVI-----VGALNLGNaspc 413
Cdd:cd18778 214 kaQLRAMKLWAI-FHPLMEFLTS-------LGTVLVLGFGGRLVLA-GELTIGDLVAFLLYLGlfyepITSLHGLN---- 280
|
250
....*....|.
gi 767920343 414 lEAFATGRAAA 424
Cdd:cd18778 281 -EMLQRALAGA 290
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
454-714 |
1.47e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVdghdirslniqwLRDQIG 533
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFSTTIAENIRYGrEDATMEDIVQAAkEANAYNFIMDL-PQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPK 612
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFG-SDFESERYWRAI-DVTALQHDLDLlPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 613 ILLLDMATSALDNESEAMVQEvlSKIQH---GHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVT 689
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVFD--SCMKDelkGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
250 260
....*....|....*....|....*
gi 767920343 690 lqsqgNQALNEEDIKDATEDDMLAR 714
Cdd:PLN03232 839 -----NAGKMDATQEVNTNDENILK 858
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
454-670 |
2.08e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRP--------------------EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFY--DPCEG 511
Cdd:COG2401 8 FVLMRVTKVYSSVLdlservaivleafgvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 512 MVTVDghdirslNIQWLRDqigiveqepvlfsTTIAENI-RYGREDATMEdIVQAAKEANAYNFI-----MDLPQQFdtl 585
Cdd:COG2401 88 CVDVP-------DNQFGRE-------------ASLIDAIgRKGDFKDAVE-LLNAVGLSDAVLWLrrfkeLSTGQKF--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 586 vgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA--ADTII 661
Cdd:COG2401 144 --------------RFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarRAGITLVVATHHYDVIDDlqPDLLI 209
|
....*....
gi 767920343 662 GFEHGTAVE 670
Cdd:COG2401 210 FVGYGGVPE 218
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
789-905 |
3.30e-09 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 59.10 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 789 MLVGSVGAAVNGTVTPLYAFLFSQILGTFsIPDKeeQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 868
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV-IPAG--DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 767920343 869 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGL 905
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNL 112
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
178-382 |
3.47e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 59.05 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 178 YYAGIAVAVLITGYIQICFWVIA---AARQI-QKMrkfyFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMAL 253
Cdd:cd18580 44 YAALLVLASVLLVLLRWLLFVLAglrASRRLhDKL----LRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 254 FIQRMTSTICGFllgffrgwkltLVIISVSPLIGIGAATIGLSVSKFTDY------ELK---AYAKAGVVA--DEVISSM 322
Cdd:cd18580 120 FLQSLFSVLGSL-----------IVIAIVSPYFLIVLPPLLVVYYLLQRYylrtsrQLRrleSESRSPLYShfSETLSGL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 323 RTVAAFGGEKREVERYEKNL----------VFAQRWgirKGIVMGFF-TGFVWCLIFLCYALAFWYGSTLV 382
Cdd:cd18580 189 STIRAFGWQERFIEENLRLLdasqrafyllLAVQRW---LGLRLDLLgALLALVVALLAVLLRSSISAGLV 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
465-651 |
3.62e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 465 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhdiRSLNIQWLRDQ----IGIVEQEPV 540
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 541 LFST-TIAENIRYGREDATMEDIVQAAK---EANAYNFIMDLPQQFDTLVGEGGGQMSGGqkqrVAIARALIRNPKILLL 616
Cdd:PRK10762 90 LIPQlTIAENIFLGREFVNRFGRIDWKKmyaEADKLLARLNLRFSSDKLVGELSIGEQQM----VEIAKVLSFESKVIIM 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 767920343 617 DMATSAL-DNESEAMVQeVLSKIQ-HGHTIISVAHRL 651
Cdd:PRK10762 166 DEPTDALtDTETESLFR-VIRELKsQGRGIVYISHRL 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
457-649 |
3.85e-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: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 457 HNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLiqrfydpcegMVTVD----GHDIRSLNIQwlrdqI 532
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI----------MAGVDkdfnGEARPQPGIK-----V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVLFST-TIAENI-------------------RYGREDATM----------EDIVQAAkeaNAYNFIMDLPQQF 582
Cdd:TIGR03719 71 GYLPQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFdklaaeqaelQEIIDAA---DAWDLDSQLEIAM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 583 DTLVGEGGGQMSGGQK----QRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLskIQHGHTIISVAH 649
Cdd:TIGR03719 148 DALRCPPWDADVTKLSggerRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL--QEYPGTVVAVTH 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
464-647 |
8.89e-09 |
|
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: 56.50 E-value: 8.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 464 PSRPEVKILNDLNMVIKPGEMTALVGPSGAGKST---ALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIgIVEQEPV 540
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEII-YVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 541 LFSTTiaenirygredaTMEDIVQAAKEANAYNFIMDLP--QQfdtlvgegggqmsggqkQRVAIARALIRNPKILLLDM 618
Cdd:cd03233 94 HFPTL------------TVRETLDFALRCKGNEFVRGISggER-----------------KRVSIAEALVSRASVLCWDN 144
|
170 180 190
....*....|....*....|....*....|..
gi 767920343 619 ATSALDNESE---AMVQEVLSKIQHGHTIISV 647
Cdd:cd03233 145 STRGLDSSTAleiLKCIRTMADVLKTTTFVSL 176
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
806-903 |
9.07e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 57.57 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 806 YAFLFSQILGTFSIP-------D---KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLG 875
Cdd:cd18557 2 LLFLLISSAAQLLLPyligrliDtiiKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100
....*....|....*....|....*...
gi 767920343 876 QDIAWFDdlRNSPGALTTRLATDASQVQ 903
Cdd:cd18557 82 QEIAFFD--KHKTGELTSRLSSDTSVLQ 107
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
179-362 |
9.62e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 57.87 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 179 YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRM 258
Cdd:cd18606 41 YAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 259 TSTICGFLLgffrgwkltlvIISVSPLIGIGAATIGLSVSKFTDY------ELK---AYAKAGVVA--DEVISSMRTVAA 327
Cdd:cd18606 121 SSIIGTFIL-----------IIIYLPWFAIALPPLLVLYYFIANYyrassrELKrleSILRSFVYAnfSESLSGLSTIRA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767920343 328 FGGEKREVERYEKN---------LVFA-QRW-GIR---KGIVMGFFTGF 362
Cdd:cd18606 190 YGAQDRFIKKNEKLidnmnrayfLTIAnQRWlAIRldlLGSLLVLIVAL 238
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
481-673 |
1.04e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 481 PGEMTALVGPSGAGKSTALQLIQRFYDP-CEGMVTVDGHDIRSLNIQWLRdqigiveqepvlfsttiaeNIRYGREDATM 559
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPpGGGVIYIDGEDILEEVLDQLL-------------------LIIVGGKKASG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 560 EDIVQAakeanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLS--- 636
Cdd:smart00382 62 SGELRL----------------------------------RLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767920343 637 ----KIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 673
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
465-649 |
1.25e-08 |
|
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: 55.83 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 465 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG------HDIRSLNIQWLRDQIGIveqE 538
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqRDEPHENILYLGHLPGL---K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 539 PVLfstTIAENIRYGREDATMEDI-VQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsggqkQRVAIARALIRN 610
Cdd:TIGR01189 86 PEL---SALENLHFWAAIHGGAQRtIEDALAAVGLTGFEDLPaaqlsagQQ-----------------RRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767920343 611 PKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAH 649
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLrAHLARGGIVLLTTH 185
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
213-398 |
1.28e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 57.58 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 213 FRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGaat 292
Cdd:cd18565 94 YDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAG--- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 293 iglsVSKFTDYELKAYA----KAGVVA---DEVISSMRTVAAFGGEKREVERYEK--NLVFAQRWG-IRKGIVmgfFTGF 362
Cdd:cd18565 171 ----TYWFQRRIEPRYRavreAVGDLNarlENNLSGIAVIKAFTAEDFERERVADasEEYRDANWRaIRLRAA---FFPV 243
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767920343 363 VWCLIFLCYALAFWYGSTLVLD-----EGEYTPGTLVqIFL 398
Cdd:cd18565 244 IRLVAGAGFVATFVVGGYWVLDgpplfTGTLTVGTLV-TFL 283
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
180-394 |
1.35e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 57.11 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 259
Cdd:cd18550 46 VAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 260 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEV--ISSMRTVAAFGGEKREVER 337
Cdd:cd18550 126 TLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAAR 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767920343 338 YEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18550 206 FARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIG-GGLTIGTLV 261
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
182-394 |
1.66e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 57.18 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 182 IAVAVLITGYIQIcfwVIAAARQI---QKMRKF-------YFRRIMRMEIGWFDCNSVGELNTRFSDDiNKINDAIADQ- 250
Cdd:cd18568 44 ILIGLLIVGIFQI---LLSAVRQYlldYFANRIdlsllsdFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSa 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 251 MALFIQRMTSTICGFLLgFFRGWKLTLVIISVSPLIgigaATIGLSVSKFTDYELKAYAKAGVVAD----EVISSMRTVA 326
Cdd:cd18568 120 LTTILDLLMVFIYLGLM-FYYNLQLTLIVLAFIPLY----VLLTLLSSPKLKRNSREIFQANAEQQsflvEALTGIATIK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 327 AFGGEKREVERYEK---NLVFAQRWGIRKGIVMGFFTGFvwcLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18568 195 ALAAERPIRWRWENkfaKALNTRFRGQKLSIVLQLISSL---INHLGTIAVLWYGAYLVIS-GQLTIGQLV 261
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
465-649 |
2.14e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 465 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL------NIQWLRDQIGIveqE 538
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 539 PVLfstTIAENIRY---GREDATMEDIVQAAKEANAYNFiMDLP-------QQfdtlvgegggqmsggqkQRVAIARALI 608
Cdd:PRK13538 87 TEL---TALENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVPvrqlsagQQ-----------------RRVALARLWL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767920343 609 RNPKILLLDMATSALDNESEAMVQEVLSK-IQHGHTIISVAH 649
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
471-678 |
2.56e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 471 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRfyDPCE----------GMVTVDGHDIRSLNIQWLRDQIGIVEQ--E 538
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 539 PVlFSTTIAENIRYGR----------EDATMEDIVQAAKEANAynfimdlpqqfDTLVGEGGGQMSGGQKQRVAIARAL- 607
Cdd:PRK13547 94 PA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 608 --------IRNPKILLLDMATSALDNESE----AMVQEVLSKIQHGhtIISVAHRLS-TVRAADTIIGFEHGTAVERGTH 674
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLG--VLAIVHDPNlAARHADRIAMLADGAIVAHGAP 239
|
....
gi 767920343 675 EELL 678
Cdd:PRK13547 240 ADVL 243
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
454-677 |
2.87e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFhypSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL---RD 530
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEPVLFS-TTIAENIRYG-RE-----DATMEDIVQAAKEANAYNFIMDL-PQQFDtlvgegggqmsGGQKQRVA 602
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPlREhtqlpAPLLHSTVMMKLEAVGLRGAAKLmPSELS-----------GGMARRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADT--IIGFEHgtAVERGTHEEL 677
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHayIVADKK--IVAHGSAQAL 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
468-653 |
5.09e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 468 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQ-RFYDPC-EGMVTVDGhdiRSLNIQWLRdQIGIVEQEPVLFS-T 544
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPhL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 545 TIAENIRYGREDATMEDIVQAAKEANAYNFI--MDLPQQFDTLV-GEGGGQMSGGQKQRVAIARALIRNPKILLLDMATS 621
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIgNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190
....*....|....*....|....*....|...
gi 767920343 622 ALDNESE-AMVQEVLSKIQHGHTIISVAHRLST 653
Cdd:PLN03211 236 GLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
804-903 |
6.05e-08 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 55.33 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 804 PLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDd 883
Cdd:cd18780 16 PYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD- 94
|
90 100
....*....|....*....|
gi 767920343 884 lRNSPGALTTRLATDASQVQ 903
Cdd:cd18780 95 -VTRTGELLNRLSSDTQVLQ 113
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
767-902 |
6.26e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 56.65 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 767 QEEVEPAP-VRRILKFSAPEWPYMLVGSVG---AAVNGTVTPLY-AFLFSQILGTFSIPDkeeQRSQINGVCLLFVAmgc 841
Cdd:TIGR00958 140 QGQSETADlLFRLLGLSGRDWPWLISAFVFltlSSLGEMFIPFYtGRVIDTLGGDKGPPA---LASAIFFMCLLSIA--- 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 842 vSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQV 902
Cdd:TIGR00958 214 -SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTM 271
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
458-677 |
6.39e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.50 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 458 NVTFHYPSrPEVKILNDLNMVIKPGEMTALVGPSGAGKS-TALQLIQRFYDP--CEGMVTVDGHDIRSLN---IQWLR-D 530
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPekeLNKLRaE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 531 QIGIVEQEP----------------VLF-------STTIAENIRygredatMEDIV---QAAKEANAYnfimdlPQQFDt 584
Cdd:PRK09473 98 QISMIFQDPmtslnpymrvgeqlmeVLMlhkgmskAEAFEESVR-------MLDAVkmpEARKRMKMY------PHEFS- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 585 lvgegggqmsGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTII 661
Cdd:PRK09473 164 ----------GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVL 233
|
250
....*....|....*.
gi 767920343 662 GFEHGTAVERGTHEEL 677
Cdd:PRK09473 234 VMYAGRTMEYGNARDV 249
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
468-688 |
6.64e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.48 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 468 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQ----LIQrfydPCEGMVTVDGHDIRSLNIQWLRdQIGIV----EQ-- 537
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgILV----PTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 538 --EPVLFSTTIAENIrYGREDA----TMEDIVQaakeanaynfIMDLPQQFDTLVgegggqmsggqkqR---------VA 602
Cdd:COG4586 109 wdLPAIDSFRLLKAI-YRIPDAeykkRLDELVE----------LLDLGELLDTPV-------------RqlslgqrmrCE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 603 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 679
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
....*....
gi 767920343 680 RKGVYFTLV 688
Cdd:COG4586 245 RFGPYKTIV 253
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
180-394 |
9.78e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 54.80 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITGYIQIcFWVIAAARQIQ-KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIAdqMALFIQRM 258
Cdd:cd18543 46 LALGVAEAVLSFLRR-YLAGRLSLGVEhDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA--FGPFLLGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 259 TSTIC-GFLLGFFRGWKLTLVIISVSPLIGIGAAtigLSVSKFTDYELKAYAKAGVVA---DEVISSMRTVAAFGGEKRE 334
Cdd:cd18543 123 LLTLVvGLVVMLVLSPPLALVALASLPPLVLVAR---RFRRRYFPASRRAQDQAGDLAtvvEESVTGIRVVKAFGRERRE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 335 VERYEK--NLVFAQRwgIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18543 200 LDRFEAaaRRLRATR--LRAARLRARFWPLLEALPELGLAAVLALGGWLVAN-GSLTLGTLV 258
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
179-363 |
9.88e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 54.78 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 179 YAGIAVAVLITGYIQICFWVIA---AARQI-QKMrkfyFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALF 254
Cdd:cd18604 49 YALISLLSVLLGTLRYLLFFFGslrASRKLhERL----LHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 255 IQRMTSTICGFllgffrgwkltLVIISVSP---LIGIGAATIGLSVSKFtdY-----ELK---AYAKAGVVA--DEVISS 321
Cdd:cd18604 125 LESTLSLLVIL-----------IAIVVVSPaflLPAVVLAALYVYIGRL--YlrasrELKrleSVARSPILShfGETLAG 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767920343 322 MRTVAAFGGEKREVER-YEK---------NLVFAQRW-GIRKGIVMGFFTGFV 363
Cdd:cd18604 192 LVTIRAFGAEERFIEEmLRRidrysrafrYLWNLNRWlSVRIDLLGALFSFAT 244
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
789-904 |
1.01e-07 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 54.74 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 789 MLVGSVGAAVNGTVTPLYAFLFSQILGTFSIpdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 868
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFV---EKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 767920343 869 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQG 904
Cdd:cd18552 78 LFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQN 111
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
793-902 |
1.14e-07 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 54.44 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 793 SVGAAVNGTVtPlyaFLFSQILGTFS--IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGF 870
Cdd:cd18573 6 LVSSAVTMSV-P---FAIGKLIDVASkeSGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLF 81
|
90 100 110
....*....|....*....|....*....|..
gi 767920343 871 RAMLGQDIAWFDdlRNSPGALTTRLATDASQV 902
Cdd:cd18573 82 KSILRQDAAFFD--KNKTGELVSRLSSDTSVV 111
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
420-654 |
1.35e-07 |
|
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: 55.22 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 420 GRAAATSIFETIDRKPIIDCMSedGYKLD--------RIKGEI-EFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGP 490
Cdd:TIGR02633 217 GQHVATKDMSTMSEDDIITMMV--GREITslyphephEIGDVIlEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 491 SGAGKSTALQLIQRFYD-PCEGMVTVDGH--DIRSLnIQWLRDQI----------GIVEQEPVLFSTTIAENIRY---GR 554
Cdd:TIGR02633 295 VGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRNP-AQAIRAGIamvpedrkrhGIVPILGVGKNITLSVLKSFcfkMR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 555 EDATMED--IVQAAKEANAYNFIMDLP--------QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALD 624
Cdd:TIGR02633 374 IDAAAELqiIGSAIQRLKVKTASPFLPigrlsggnQQ------------------KAVLAKMLLTNPRVLILDEPTRGVD 435
|
250 260 270
....*....|....*....|....*....|.
gi 767920343 625 NESEAMVQEVLSKI-QHGHTIISVAHRLSTV 654
Cdd:TIGR02633 436 VGAKYEIYKLINQLaQEGVAIIVVSSELAEV 466
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
468-679 |
1.49e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 468 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRDQIGIVEQEPV---- 540
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasld 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 541 ---LFSTTIAENIRY-----GREDAT-----MEDIVQAAKEANAYnfimdlPQQFDtlvgegggqmsGGQKQRVAIARAL 607
Cdd:PRK10261 416 prqTVGDSIMEPLRVhgllpGKAAAArvawlLERVGLLPEHAWRY------PHEFS-----------GGQRQRICIARAL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 608 IRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLE 679
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
200-394 |
1.52e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 54.14 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 200 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSdDINKINDAIADQM-ALFIQRMTSTICGFLLgFFRGWKLTLV 278
Cdd:cd18782 69 TANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTAlTTLLDVLFSVIYIAVL-FSYSPLLTLV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 279 IISVSPLIGIgaatIGLSVSKFTDYELKAYAKAGVVAD----EVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGI 354
Cdd:cd18782 147 VLATVPLQLL----LTFLFGPILRRQIRRRAEASAKTQsylvESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTV 222
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767920343 355 VMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLV 394
Cdd:cd18782 223 LGTTSGSLSQFLNKLSSLLVLWVGAYLVL-RGELTLGQLI 261
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
472-678 |
1.82e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.31 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPCEGMVTVDGHDIRSLNIQ-------WLRDQigiveQEPVLF-- 542
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQ-----QSPPFAmp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 543 -----STTIAENIRYGREDATMEDIVQAAKeanaynfIMD-LPQQFDTLvgegggqmSGGQKQRVAIARALIR-----NP 611
Cdd:COG4138 86 vfqylALHQPAGASSEAVEQLLAQLAEALG-------LEDkLSRPLTQL--------SGGEWQRVRLAAVLLQvwptiNP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 612 --KILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:COG4138 151 egQLLLLDEPMNSLDVAQQAALDRLLRELcQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
467-624 |
2.70e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 467 PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI----QRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLF 542
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 543 STTIAENIRYG--------REDATMEDiVQAAKEANAYNFIMDLPQQFDTLV-GEGGGQMSGGQKQRVAIARALIRNPKI 613
Cdd:TIGR00956 152 HLTVGETLDFAarcktpqnRPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVgNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170
....*....|.
gi 767920343 614 LLLDMATSALD 624
Cdd:TIGR00956 231 QCWDNATRGLD 241
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
180-394 |
3.89e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 52.88 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVLITGYIQICFWVIAAARQIQKM----RKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA-LF 254
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLlydlRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVqLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 255 IQRMTSTICGFLLGFFRgWKLTLVIISVSPLIGIgaATIglsvsKFTDYELKAYAK-----AGVVAD--EVISSMRTVAA 327
Cdd:cd18546 122 VSLLTLVGIAVVLLVLD-PRLALVALAALPPLAL--ATR-----WFRRRSSRAYRRareriAAVNADlqETLAGIRVVQA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 328 FGGEKREVERY-EKNLVF--AQRWGIRkgiVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18546 194 FRRERRNAERFaELSDDYrdARLRAQR---LVAIYFPGVELLGNLATAAVLLVGAWRVAA-GTLTVGVLV 259
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
454-502 |
4.98e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 4.98e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLI 502
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
453-535 |
7.35e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 453 EIEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQI 532
Cdd:PRK10522 322 TLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
...
gi 767920343 533 GIV 535
Cdd:PRK10522 400 SAV 402
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
454-703 |
1.68e-06 |
|
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: 51.73 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRF--YDPCEGMVTVdgHDIRSLNIQWLRDQ 531
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIY--HVALCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 532 IGIVEQEPVLFST-------------TIAENIR-------------YGrEDATMEDIVQAAKEA-----NAYNFIMDLPQ 580
Cdd:TIGR03269 76 SKVGEPCPVCGGTlepeevdfwnlsdKLRRRIRkriaimlqrtfalYG-DDTVLDNVLEALEEIgyegkEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 581 --QFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSK--IQHGHTIISVAHRLSTV-R 655
Cdd:TIGR03269 155 mvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIeD 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767920343 656 AADTIIGFEHGTAVERGTHEELLErkgVYFTLVTLQSQGNQALNEEDI 703
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGEPI 279
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
181-394 |
1.70e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 51.01 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 181 GIAVAVLITGYIQICF---WVIAAAR---QIQKMRKFyFRRIMRMEIGWFDCNSVGELNTRFSDdinkiNDAIADqmaLF 254
Cdd:cd18779 45 GLGLAALVLTQLLAGLlrsHLLLRLRtrlDTQLTLGF-LEHLLRLPYRFFQQRSTGDLLMRLSS-----NATIRE---LL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 255 IQRMTSTIC--GFLLGFFrgwkltLVIISVSPL-----IGIGAATIGL------SVSKFTDYELKAYAKAGVVADEVISS 321
Cdd:cd18779 116 TSQTLSALLdgTLVLGYL------ALLFAQSPLlglvvLGLAALQVALllatrrRVRELMARELAAQAEAQSYLVEALSG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 322 MRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18779 190 IETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLD-GQLSLGTML 261
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
454-624 |
2.59e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.61 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDqIG 533
Cdd:PRK11650 4 LKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRD-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFS-TTIAENIRYGREDATM------EDIVQAAKeanaynfIMDL-------PQQFdtlvgegggqmSGGQKQ 599
Cdd:PRK11650 80 MVFQNYALYPhMSVRENMAYGLKIRGMpkaeieERVAEAAR-------ILELeplldrkPREL-----------SGGQRQ 141
|
170 180
....*....|....*....|....*
gi 767920343 600 RVAIARALIRNPKILLLDMATSALD 624
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
457-672 |
2.96e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 457 HNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL-------- 528
Cdd:PRK11701 10 RGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 529 -RDQIGIVEQEP-------VLFSTTIAENI------RYGREDATMEDIVQAAKEANAYnfIMDLPQQFdtlvgegggqmS 594
Cdd:PRK11701 87 lRTEWGFVHQHPrdglrmqVSAGGNIGERLmavgarHYGDIRATAGDWLERVEIDAAR--IDDLPTTF-----------S 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 595 GGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFEHGTAVER 671
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARlLAHRLLVMKQGRVVES 233
|
.
gi 767920343 672 G 672
Cdd:PRK11701 234 G 234
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
819-898 |
2.99e-06 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 50.08 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 819 IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATD 898
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTND 107
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
148-295 |
3.41e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 50.01 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 148 WTNSSLNQNMT----NGTRCGLLNIESEMIKFASY-YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIG 222
Cdd:cd18601 29 WANLEEKLNDTtdrvQGENSTNVDIEDLDRDFNLGiYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIR 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 223 WFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTsTICGFLlgffrgwkltLVIISVSPLIGIGAATIGL 295
Cdd:cd18601 109 FFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLL-QVVGVV----------LLAVVVNPWVLIPVIPLVI 170
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
470-624 |
6.82e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 470 KILNDLNMVIK---PGE-MTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH---DIRS-LNIQWLRDQIGIVEQEPVL 541
Cdd:PRK11144 8 QQLGDLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgICLPPEKRRIGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 542 FS-TTIAENIRYGReDATMedivqaakeanaynfimdlPQQFDTLVGEGGGQMSGG---------QKQRVAIARALIRNP 611
Cdd:PRK11144 88 FPhYKVRGNLRYGM-AKSM-------------------VAQFDKIVALLGIEPLLDrypgslsggEKQRVAIGRALLTAP 147
|
170
....*....|...
gi 767920343 612 KILLLDMATSALD 624
Cdd:PRK11144 148 ELLLMDEPLASLD 160
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
182-394 |
7.42e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 48.66 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 182 IAVAVLITGYIQICFwVIAAARQIQKMRKF--------YFRRIMRMEIGWFDCNSVGELNTRFSdDINKINDAIADQMAL 253
Cdd:cd18555 44 LGIGILILFLLYGLF-SFLRGYIIIKLQTKldkslmsdFFEHLLKLPYSFFENRSSGDLLFRAN-SNVYIRQILSNQVIS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 254 FIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIgaaTIGLS---VSKFTDYELKAYAKAGVVADEVISSMRTVAAFGG 330
Cdd:cd18555 122 LIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVL---LLLLTrkkIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGS 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 331 EKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18555 199 EKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVIN-GELTLGELI 261
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
457-649 |
8.98e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 457 HNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLiqrfydpcegMVTVD----GHDIRSLNIQwlrdqI 532
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRI----------MAGVDkefeGEARPAPGIK-----V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 533 GIVEQEPVLFST-TIAENI-------------------RYGREDATM----------EDIVQAAkeaNAYNF------IM 576
Cdd:PRK11819 73 GYLPQEPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFdalaaeqgelQEIIDAA---DAWDLdsqleiAM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 577 D---LPQQfDTLVGEGGGQMSGgqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQevlskiQHGH----TIISVAH 649
Cdd:PRK11819 150 DalrCPPW-DAKVTKLSGGERR----RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE------QFLHdypgTVVAVTH 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
454-677 |
1.48e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPcegmvTVDGHDIrslniqwLRDQIG 533
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP-----RSDASVV-------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFSTTIAENIRYGredatmedivqAAKEANAYNFIMD----------LPQQFDTLVGEGGGQMSGGQKQRVAI 603
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFG-----------SPFDPERYERAIDvtalqhdldlLPGGDLTEIGERGVNISGGQKQRVSM 751
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 604 ARALIRNPKILLLDMATSALDneseAMV-QEVLSKI----QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEEL 677
Cdd:PLN03130 752 ARAVYSNSDVYIFDDPLSALD----AHVgRQVFDKCikdeLRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
468-534 |
1.66e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 1.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 468 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI--QRFYDPCEGMVTVDGHDIRSLNIQwLRDQIGI 534
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGI 86
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
454-680 |
1.70e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFhYPSRPEVKilnDLNMVIKPGEMTALVGPSGAGKSTAlqliqrfydpCEGMVTVDGHDIRSLNIQWLRDQIG 533
Cdd:PRK10418 5 IELRNIAL-QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSLT----------CAAALGILPAGVRQTAGRVLLDGKP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQE-PVLFSTTIAENIR-----------YGRE----------DATMEDIVQAAKEANA------YNFIMDlpqqfdtl 585
Cdd:PRK10418 71 VAPCAlRGRKIATIMQNPRsafnplhtmhtHAREtclalgkpadDATLTAALEAVGLENAarvlklYPFEMS-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 586 vgegggqmsGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIG 662
Cdd:PRK10418 143 ---------GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVaRLADDVAV 213
|
250
....*....|....*...
gi 767920343 663 FEHGTAVERGTHEELLER 680
Cdd:PRK10418 214 MSHGRIVEQGDVETLFNA 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
465-651 |
2.21e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 465 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR-SLNIQWLRDQIGIVEQE-PVLF 542
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 543 STTIAENIRYGR---------EDATMEDIVQAAKEanaYNFIMDLPQQFDTLvgegggqmSGGQKQRVAIARALIRNPKI 613
Cdd:PRK10982 87 QRSVMDNMWLGRyptkgmfvdQDKMYRDTKAIFDE---LDIDIDPRAKVATL--------SVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767920343 614 LLLDMATSALdneSEAMVQEVLSKI----QHGHTIISVAHRL 651
Cdd:PRK10982 156 VIMDEPTSSL---TEKEVNHLFTIIrklkERGCGIVYISHKM 194
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
472-666 |
2.65e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 45.89 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI-QWLRDQIGIV-E---QEPVLFSTTI 546
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVpEdrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 547 AENIRygredatmedivqaakeanaynfimdLP-------QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMA 619
Cdd:cd03215 96 AENIA--------------------------LSsllsggnQQ------------------KVVLARWLARDPRVLILDEP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767920343 620 TSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHG 666
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
463-649 |
4.81e-05 |
|
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: 45.86 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 463 YPSRpeVKILNDLNMVIKPG-----EMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLR-DQIGIVe 536
Cdd:cd03237 3 YPTM--KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKaDYEGTV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 537 qepvlfsttiaenirygreDATMEDIVQAAKEANAYNF-IMDlPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILL 615
Cdd:cd03237 79 -------------------RDLLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 767920343 616 LDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 649
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFaeNNEKTAFVVEH 174
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
600-677 |
6.99e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 676
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHD 240
|
.
gi 767920343 677 L 677
Cdd:PRK11022 241 I 241
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
150-283 |
1.04e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 45.25 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 150 NSSLNQNMTNGTRCGLLNIE--SEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCN 227
Cdd:cd18599 33 GSGNTTNNVDNSTVDSGNISdnPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTT 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 228 SVGELNTRFSDDINKINDAIADQMALFIQRMtsticgfLLGFFrgwklTLVIISVS 283
Cdd:cd18599 113 PTGRILNRFSKDLDEVDVRLPFTLENFLQNV-------LLVVF-----SLIIIAIV 156
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
442-513 |
1.22e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 1.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 442 EDGYKLDRIKGEIEfhNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMV 513
Cdd:PRK15064 310 EQDKKLHRNALEVE--NLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
172-403 |
1.42e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 44.78 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 172 MIKFASYYAG-IAVAVLITgyiqicFWVIAAARQIQK-----MRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKIND 245
Cdd:cd18540 41 LTGFILLYLGlILIQALSV------FLFIRLAGKIEMgvsydLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 246 AIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIgigaatIGLSVsKFTDYELKAYAKA-----GVVAD--EV 318
Cdd:cd18540 115 IISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVL------AVVSI-YFQKKILKAYRKVrkinsRITGAfnEG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 319 ISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVqIFL 398
Cdd:cd18540 188 ITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVL-AGAITIGTLV-AFI 265
|
....*
gi 767920343 399 SVIVG 403
Cdd:cd18540 266 SYATQ 270
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
789-905 |
1.44e-04 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 44.73 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 789 MLVGSVGAAVnGTVTPLYAflfSQILGTFSipDKEEQRSQINGVCLLFVamgcVSLFTQFLQGYAFAKSGELLTKRLRKF 868
Cdd:cd18551 5 LLLSLLGTAA-SLAQPLLV---KNLIDALS--AGGSSGGLLALLVALFL----LQAVLSALSSYLLGRTGERVVLDLRRR 74
|
90 100 110
....*....|....*....|....*....|....*..
gi 767920343 869 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGL 905
Cdd:cd18551 75 LWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLREL 109
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
148-351 |
1.76e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 44.52 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 148 WTNSSLNQNMTNGTRCGLLNIESEMIKFASYYAGIAVAVLITGYIQ---ICFWVIAAARQI-QKMrkfyFRRIMRMEIGW 223
Cdd:cd18602 25 WTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTnlaGELAGLRAARRLhDRM----LRNIVRAPMRF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 224 FDCNSVGELNTRFSDDINKIndaiaDQ-MALFIQRMTSTICgFLLGFFrgwkltLVIISVSPLIGIGAATIGLS---VSK 299
Cdd:cd18602 101 FDTTPIGRILNRFSSDTNVI-----DQkLPTTLERLLRFLL-LCLSAI------IVNAIVTPYFLIALIPIIIVyyfLQK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 300 F---TDYELK---AYAKAGVVA--DEVISSMRTVAAFGGEKREVERYEK-----NLVF-----AQRW-GIR 351
Cdd:cd18602 169 FyraSSRELQrldNITKSPVFShfSETLGGLTTIRAFRQQARFTQQMLElidrnNTAFlflntANRWlGIR 239
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
148-347 |
1.82e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 44.44 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 148 WTNSSLNQNmtngtrcgLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCN 227
Cdd:cd18605 25 WVSHSNNSF--------FNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 228 SVGELNTRFSDDINKINDAIADQMALFIqRMTSTICGFLLGFFRGwkLTLVIISVSPLIGIGAatiglSVSKF---TDYE 304
Cdd:cd18605 97 PVGRILNRFSSDVYTIDDSLPFILNILL-AQLFGLLGYLVVICYQ--LPWLLLLLLPLAFIYY-----RIQRYyraTSRE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767920343 305 LK---AYAKAGVVA--DEVISSMRTVAAFGGEKREVERYEKNLVFAQR 347
Cdd:cd18605 169 LKrlnSVNLSPLYThfSETLKGLVTIRAFRKQERFLKEYLEKLENNQR 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
454-522 |
2.36e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 2.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 454 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI------QrfydpcEGMVTVDGHDIRS 522
Cdd:NF033858 2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagarkiQ------QGRVEVLGGDMAD 67
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
471-523 |
2.51e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 2.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 471 ILNDLNMVIKPGEMTALVGPSGAGKST--ALQLIQRFYDPCEGMVTVDGHDIRSL 523
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTlsATLAGREDYEVTGGTVEFKGKDLLEL 70
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
826-904 |
3.02e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 43.63 E-value: 3.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920343 826 RSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNspGALTTRLATDASQVQG 904
Cdd:cd18576 32 TASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV--GELTSRLSNDVTQIQD 108
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
433-754 |
3.04e-04 |
|
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: 45.00 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 433 RKPIIDCMSEDGYKLDRI-----KGEI-EFHNVTFHYP--SRPEVkilNDLNMVIKPGEMTALVGPSGAGKSTALQLIQR 504
Cdd:TIGR01257 1911 KEPIFDEDDDVAEERQRIisggnKTDIlRLNELTKVYSgtSSPAV---DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG 1987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 505 FYDPCEGMVTVDGHDIRSlNIQWLRDQIGIVEQEPVLfsttiaENIRYGREDATMEDIVQA--AKE----ANAYNFIMDL 578
Cdd:TIGR01257 1988 DTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGREHLYLYARLRGvpAEEiekvANWSIQSLGL 2060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 579 PQQFDTLVgeggGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMV-QEVLSKIQHGHTIISVAHRLSTVRAA 657
Cdd:TIGR01257 2061 SLYADRLA----GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEAL 2136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 658 DTIIGFE-HGTAVERGTHEELLERKGVYFtLVTLQsqgnqalneedIKdATEDDML-----ARTFSRGSYQDSLRasiRQ 731
Cdd:TIGR01257 2137 CTRLAIMvKGAFQCLGTIQHLKSKFGDGY-IVTMK-----------IK-SPKDDLLpdlnpVEQFFQGNFPGSVQ---RE 2200
|
330 340
....*....|....*....|....*...
gi 767920343 732 RSKSQLSYLVHEPPLA-----VVDHKST 754
Cdd:TIGR01257 2201 RHYNMLQFQVSSSSLArifqlLISHKDS 2228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
478-652 |
3.21e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.51 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 478 VIKPGEMTALVGPSGAGKSTALQLIQ--------RFYDPCEGMVTVD---GHDIRSLNIQWLRDQIGI------VEQEPV 540
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpqyVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 541 LFSTTIAENIRYGREDATMEDIVQAakeanaynfiMDLpqqfDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMAT 620
Cdd:cd03236 102 AVKGKVGELLKKKDERGKLDELVDQ----------LEL----RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|...
gi 767920343 621 SALD-NESEAMVQEVLSKIQHGHTIISVAHRLS 652
Cdd:cd03236 168 SYLDiKQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
472-667 |
3.43e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.31 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 472 LNDLNMVIKPGEMTALVGPSGAGKSTALQliqrfydpcEGMVTVDGHDIRSLNIQWLRDQIGIVEQepvlFSTTIAENIR 551
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRNKLIFIDQ----LQFLIDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 552 YgredatmedivqaakeanaynfiMDLPQQFDTLvgegggqmSGGQKQRVAIARALIRNPK--ILLLDMATSALDNESEA 629
Cdd:cd03238 78 Y-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 767920343 630 MVQEVLSK-IQHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
213-394 |
4.01e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 43.60 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 213 FRRIMRMEIGWFDCNSVGELNTRFsDDINKINDAIADQM-ALFIQRMTSTICGFLLgFFRGWKLTLVIISVSPL-IGIGA 290
Cdd:cd18567 82 FRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFvEALLDGLMAILTLVMM-FLYSPKLALIVLAAVALyALLRL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 291 ATIGlSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLC 370
Cdd:cd18567 160 ALYP-PLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLE 238
|
170 180
....*....|....*....|....
gi 767920343 371 YALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18567 239 NILVIYLGALLVLD-GEFTVGMLF 261
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
180-394 |
4.26e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 43.27 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 180 AGIAVAVL---ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELnTRFSDDINKINDAIADQMaLFIQ 256
Cdd:cd18783 46 IGVVIALLfegILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVL-TKHMQQIERIRQFLTGQL-FGTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 257 RMTSTICGFL-LGFFRGWKLTLVIISVSPLIgigAATIGLSVSKFTDYELKAY---AKAGVVADEVISSMRTVAAFGGEK 332
Cdd:cd18783 124 LDATSLLVFLpVLFFYSPTLALVVLAFSALI---ALIILAFLPPFRRRLQALYraeGERQAFLVETVHGIRTVKSLALEP 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920343 333 REVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 394
Cdd:cd18783 201 RQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFA-GSLTVGALI 261
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
457-522 |
6.37e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.14 E-value: 6.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 457 HNVTFhypSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRS 522
Cdd:PRK13543 15 HALAF---SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR 77
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
822-903 |
7.10e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 42.80 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 822 KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQ 901
Cdd:cd18542 31 GGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDT 108
|
..
gi 767920343 902 VQ 903
Cdd:cd18542 109 IR 110
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
454-513 |
9.52e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 9.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSRPevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMV 513
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
452-624 |
9.64e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 452 GEI--EFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdP--CEGMVTVDGH--DIRS--- 522
Cdd:PRK13549 256 GEVilEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFIDGKpvKIRNpqq 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 523 ---LNIQWL---RDQIGIVEQEPVLFSTTIAENIRY--------GREDATMEDIVQ--AAKEANAYNFIMDLP---QQfd 583
Cdd:PRK13549 335 aiaQGIAMVpedRKRDGIVPVMGVGKNITLAALDRFtggsriddAAELKTILESIQrlKVKTASPELAIARLSggnQQ-- 412
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767920343 584 tlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALD 624
Cdd:PRK13549 413 ----------------KAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
808-903 |
1.01e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 42.00 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 808 FLFSQILGTFSIPD----------KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQD 877
Cdd:cd18548 7 FKLLEVLLELLLPTlmadiidegiANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFS 86
|
90 100
....*....|....*....|....*.
gi 767920343 878 IAWFDDLrnSPGALTTRLATDASQVQ 903
Cdd:cd18548 87 FAEIDKF--GTSSLITRLTNDVTQVQ 110
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
459-518 |
1.35e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 459 VTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGH 518
Cdd:PLN03140 168 LGINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPslkVSGEITYNGY 230
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
207-419 |
1.64e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 41.64 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 207 KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLI 286
Cdd:cd18554 80 DIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 287 GIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEK-NLVFAQRWGIRKGIVMGFFTGfVWC 365
Cdd:cd18554 160 ILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKrNGHFLTRALKHTRWNAKTFSA-VNT 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767920343 366 LIFLCYALAFWYGSTLVLdEGEYTPGTLVQIF--LSVIVGAL-NLGNASPCL-EAFAT 419
Cdd:cd18554 239 ITDLAPLLVIGFAAYLVI-EGNLTVGTLVAFVgyMERMYSPLrRLVNSFTTLtQSFAS 295
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
468-571 |
1.68e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.91 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 468 EVKILN-----DLNMVIKPGeMTALVGPSGAGKSTALQLIQRFYDPcEGMVTVDGHDI-RSLNIQWLRDQIGIVeqepvl 541
Cdd:COG3593 5 KIKIKNfrsikDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGP-SSSRKFDEEDFyLGDDPDLPEIEIELT------ 76
|
90 100 110
....*....|....*....|....*....|
gi 767920343 542 FSTTIAENIRYGREDATMEDIVQAAKEANA 571
Cdd:COG3593 77 FGSLLSRLLRLLLKEEDKEELEEALEELNE 106
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
454-502 |
1.93e-03 |
|
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: 41.84 E-value: 1.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767920343 454 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLI 502
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMI 368
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
487-577 |
2.04e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 40.42 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 487 LVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIGIVEQEPvlfsttiAENIRYGREDAT--MEDIVQ 564
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELH----PHYRELQAADP-------KTASEYTQPDASrwVEKLLQ 84
|
90
....*....|...
gi 767920343 565 AAKEaNAYNFIMD 577
Cdd:pfam06414 85 HAIE-NGYNIILE 96
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
839-900 |
2.22e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 41.17 E-value: 2.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920343 839 MGCVSLFTQF---LQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDAS 900
Cdd:cd18590 42 MCLFSLGSSLsagLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDTT 104
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
420-617 |
2.50e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.54 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 420 GRAAATSIFETIDRKPIIDCM-----SEDGYKLDRIKGEI--EFHNVtfhypSRPEVkiLNDLNMVIKPGEMTALVGPSG 492
Cdd:COG1129 216 GRLVGTGPVAELTEDELVRLMvgrelEDLFPKRAAAPGEVvlEVEGL-----SVGGV--VRDVSFSVRAGEILGIAGLVG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 493 AGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlRDQI--------------GIVEQEPVLFSTTIAeN--------- 549
Cdd:COG1129 289 AGRTELARALFGADPADSGEIRLDGKPVRIRSP---RDAIragiayvpedrkgeGLVLDLSIRENITLA-Sldrlsrggl 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920343 550 IRYGREDATMEDIVQA--AKEANAYNFIMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLD 617
Cdd:COG1129 365 LDRRRERALAEEYIKRlrIKTPSPEQPVGNLSggnQQ------------------KVVLAKWLATDPKVLILD 419
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
601-667 |
3.10e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920343 601 VAIARALIRNPK---ILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRAADTIIGFEHGT 667
Cdd:PRK00635 1708 IKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLrTLVSLGHSVIYIDHDPALLKQADYLIEMGPGS 1778
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
454-652 |
3.14e-03 |
|
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: 41.27 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYPSrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhdirslniqwlRDQIG 533
Cdd:TIGR00954 452 IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 IVEQEPVLFSTTIAENIRY--GREDATMEDIVQAAKEAnaynfIMDLPQQFDTL--------VGEGGGQMSGGQKQRVAI 603
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIIYpdSSEDMKRRGLSDKDLEQ-----ILDNVQLTHILereggwsaVQDWMDVLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767920343 604 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIqhGHTIISVAHRLS 652
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
824-903 |
3.83e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 40.16 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 824 EQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQ 903
Cdd:cd18575 30 GNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQ 107
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
600-678 |
4.32e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.17 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 600 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 676
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLsQWADKINVLYCGQTVETAPSKE 245
|
..
gi 767920343 677 LL 678
Cdd:PRK15093 246 LV 247
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
458-521 |
4.81e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.55 E-value: 4.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920343 458 NVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR 521
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK 66
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
794-883 |
5.75e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 39.86 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 794 VGAAVNGTV--TPLYAFLFSQILGTfsipdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFR 871
Cdd:cd18565 22 IGVAIDAVFngEASFLPLVPASLGP------ADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYD 95
|
90
....*....|..
gi 767920343 872 AMLGQDIAWFDD 883
Cdd:cd18565 96 HVQRLDMAFFED 107
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
475-678 |
9.03e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 38.76 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 475 LNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPCEGMVTVDGHDIRSLNIQWLRDQIG-IVEQEPVLFSTTIAENIRYG 553
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 554 REDATMEDIVQAAKE--ANAYNFIMDLPQQFDTLvgegggqmSGGQKQRVAIARALIR-----NP--KILLLDMATSALD 624
Cdd:PRK03695 94 QPDKTRTEAVASALNevAEALGLDDKLGRSVNQL--------SGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767920343 625 NESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 678
Cdd:PRK03695 166 VAQQAALDRLLSELcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
454-660 |
9.94e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 454 IEFHNVTFHYpsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTvdghdIRSLNIQWLrdqig 533
Cdd:PRK13541 2 LSLHQLQFNI----EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNI----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920343 534 iveQEPvlFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQF--DTLVGEGGGQMSGGQKQRVAIARALIRNP 611
Cdd:PRK13541 68 ---AKP--YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFklHDLLDEKCYSLSSGMQKIVAIARLIACQS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767920343 612 KILLLDMATSALDNESEAMVQEVLS-KIQHGHTIISVAHRLSTVRAADTI 660
Cdd:PRK13541 143 DLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| |
