|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
448-1033 |
2.39e-170 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 511.25 E-value: 2.39e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 448 KKRNTVSIRRLAALNKPEVPVLLLGAIAAAGHGVLFPIFGLLLSKAIGMFYEPPNelRHDSRKWALVYVGLGCAGLLVVP 527
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD--LSALLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 528 VQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGF 607
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 608 TANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQG 687
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 688 VRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQVFKVFFAITITAMGVSQATSMAPDSNKAKDSAASIFRI 767
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 768 LDSKPKIDSSSDeGIALSLLIGEIELDHVSFKYPtrPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDS 847
Cdd:COG1132 318 LDEPPEIPDPPG-AVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 848 GRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASVGER 927
Cdd:COG1132 395 GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP-DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 928 GVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIA 1007
Cdd:COG1132 474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
570 580
....*....|....*....|....*.
gi 1562645982 1008 EKGSHDFLMKiTDGAYASLVALHSSS 1033
Cdd:COG1132 554 EQGTHEELLA-RGGLYARLYRLQFGE 578
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
791-1027 |
6.78e-136 |
|
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: 408.47 E-value: 6.78e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPK 950
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 951 ILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKiTDGAYASLV 1027
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLV 235
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
531-1029 |
6.49e-122 |
|
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: 384.82 E-value: 6.49e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 531 FFFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTAN 610
Cdd:TIGR02204 80 YLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITS 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 611 WKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRL 690
Cdd:TIGR02204 158 PKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 691 GVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQVFK-VFFAItITAMGVSQATSMAPDSNKAKDSAASIFRILD 769
Cdd:TIGR02204 238 IRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQfVFYAV-MVAGSIGTLSEVWGELQRAAGAAERLIELLQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 770 SKPKIDSSSDEGIALSLLIGEIELDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGR 849
Cdd:TIGR02204 317 AEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGR 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 850 VLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGV 929
Cdd:TIGR02204 397 ILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRP-DATDEEVEAAARAAHAHEFISALPEGYDTYLGERGV 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 930 QLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEK 1009
Cdd:TIGR02204 476 TLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQ 555
|
490 500
....*....|....*....|
gi 1562645982 1010 GSHDFLMKiTDGAYASLVAL 1029
Cdd:TIGR02204 556 GTHAELIA-KGGLYARLARL 574
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-343 |
7.33e-122 |
|
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: 374.50 E-value: 7.33e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 48 MIVGTISAVGNGLSKPLMTLVFGNLINTF-----GCTDPGHIVPMISKVSLKFVYLAIGTGAAALLQVACWMVTGERQAA 122
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 123 RIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPA 202
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK-NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 203 IVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFML 282
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 283 VIFCSYALAVWYGSKMIIKHGYNGGQVINVIFALMTGGMSLGQASPSLNAFASGKAAAYKI 343
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
442-1028 |
1.49e-121 |
|
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: 388.42 E-value: 1.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 442 RPKVDSKKRNTVSIRRLAALNKPEVPVLLLGAIAAaghgVLFPIFGLLLSKAIGMFYeppNE-LRHDSRKWaLVYVGLGC 520
Cdd:COG2274 131 TPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLAS----LLINLLALATPLFTQVVI---DRvLPNQDLST-LWVLAIGL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 521 AGLLVVP-----VQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLStDASTIKSLVGDALALIVQN 595
Cdd:COG2274 203 LLALLFEgllrlLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES--RSVGDLASRFR-DVESIREFLTGSLLTALLD 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 596 IATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKgfSADAKIMYEEASQVAN--DAIGSIRTVASFCSEKKVM 673
Cdd:COG2274 280 LLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLR--RLSREESEASAKRQSLlvETLRGIETIKALGAESRFR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 674 EAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQVFkVFFAITITAMG-VSQATSMAP 752
Cdd:COG2274 358 RRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLI-AFNILSGRFLApVAQLIGLLQ 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 753 DSNKAKDSAASIFRILDSKPKIDSSSDEgIALSLLIGEIELDHVSFKYPTRpDVQIFRDICLKMPSGKTVALVGESGSGK 832
Cdd:COG2274 437 RFQDAKIALERLDDILDLPPEREEGRSK-LSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 833 STVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNV 912
Cdd:COG2274 515 STLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDP-DATDEEIIEAARLAGLHDF 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 913 ISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTI 992
Cdd:COG2274 594 IEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI 673
|
570 580 590
....*....|....*....|....*....|....*.
gi 1562645982 993 KGADIIAVVKNGVIAEKGSHDFLMKiTDGAYASLVA 1028
Cdd:COG2274 674 RLADRIIVLDKGRIVEDGTHEELLA-RKGLYAELVQ 708
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
459-774 |
9.57e-121 |
|
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: 372.17 E-value: 9.57e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 459 AALNKPEVPVLLLGAIAAAGHGVLFPIFGLLLSKAIGMFYEP-PNELRHDSRKWALVYVGLGCAGLLVVPVQNFFFGVAG 537
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPdDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 538 GKLVERIRALSFQKVVHQQVSWFDDPANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVV 617
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 618 LAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSG 697
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 698 FGFSFFLMFCTNALIFYIGAILVKHGQATFEQVFKVFFAITITAMGVSQATSMAPDSNKAKDSAASIFRILDSKPKI 774
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
456-1026 |
1.90e-120 |
|
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: 380.99 E-value: 1.90e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 456 RRLAALNKPEVPVLLLGAIAAAGHGVLFPIFGLLLSKAIgmfyeppNELRHDSRKWALVYVGLGCAGLLVVP-----VQN 530
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLL-------DDGFGGRDRSVLWWVPLVVIGLAVLRgicsfVST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 531 FFFGVAGGKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTAN 610
Cdd:TIGR02203 76 YLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 611 WKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRL 690
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 691 GVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQvfkvfFAITITAMG-----VSQATSMAPDSNKAKDSAASIF 765
Cdd:TIGR02203 234 TSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-----FTAFITAMIalirpLKSLTNVNAPMQRGLAAAESLF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 766 RILDSKPKIDsssDEGIALSLLIGEIELDHVSFKYPTRpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDP 845
Cdd:TIGR02203 309 TLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 846 DSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPGDVTEEEIIAATTAANVHNVISSLPQGYDASVG 925
Cdd:TIGR02203 385 DSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 926 ERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGV 1005
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570 580
....*....|....*....|.
gi 1562645982 1006 IAEKGSHDFLMKiTDGAYASL 1026
Cdd:TIGR02203 545 IVERGTHNELLA-RNGLYAQL 564
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
533-1027 |
2.02e-114 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 369.44 E-value: 2.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 533 FGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWK 612
Cdd:TIGR00958 225 FNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 613 LMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGV 692
Cdd:TIGR00958 303 LTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKAL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 693 VSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQVfkVFFAITITAMG--VSQATSMAPDSNKAKDSAASIFRILDS 770
Cdd:TIGR00958 383 AYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNL--VSFLLYQEQLGeaVRVLSYVYSGMMQAVGASEKVFEYLDR 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 771 KPKIdsSSDEGIALSLLIGEIELDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRV 850
Cdd:TIGR00958 461 KPNI--PLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 851 LLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQ 930
Cdd:TIGR00958 539 LLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLT-DTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQ 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 931 LSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDalDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKG 1010
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMG 695
|
490
....*....|....*..
gi 1562645982 1011 SHDFLMKITDgAYASLV 1027
Cdd:TIGR00958 696 THKQLMEDQG-CYKHLV 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
791-1026 |
3.48e-113 |
|
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: 349.22 E-value: 3.48e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPK 950
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRP-GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 951 ILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKiTDGAYASL 1026
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA-QGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
765-1029 |
4.28e-109 |
|
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: 351.81 E-value: 4.28e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 765 FRILDSKPKIDSSSDegiALSLLI--GEIELDHVSFKYptRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERF 842
Cdd:COG5265 333 FDLLDQPPEVADAPD---APPLVVggGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 843 YDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDA 922
Cdd:COG5265 408 YDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP-DASEEEVEAAARAAQIHDFIESLPDGYDT 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 923 SVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVK 1002
Cdd:COG5265 487 RVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLE 566
|
250 260
....*....|....*....|....*..
gi 1562645982 1003 NGVIAEKGSHDFLMKiTDGAYASLVAL 1029
Cdd:COG5265 567 AGRIVERGTHAELLA-QGGLYAQMWAR 592
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
791-1026 |
4.56e-108 |
|
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: 335.74 E-value: 4.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPK 950
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRP-DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 951 ILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKiTDGAYASL 1026
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEM 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
538-1026 |
2.94e-101 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 330.06 E-value: 2.94e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 538 GKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVV 617
Cdd:PRK11176 94 GKVVMTMRRRLFGHMMGMPVSFFDK--QSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLIL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 618 LAVSPLILLQGTLQAKFLKGFSadaKIMYEEASQVANDA---IGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVS 694
Cdd:PRK11176 172 IVIAPIVSIAIRVVSKRFRNIS---KNMQNTMGQVTTSAeqmLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSAS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 695 GSGFGFSFFLMFCTNALIFYIgailvkhgqATFEQVFKVFFAITITAMGVSQATSMAP-------DSNKAKDSAA--SIF 765
Cdd:PRK11176 249 SISDPIIQLIASLALAFVLYA---------ASFPSVMDTLTAGTITVVFSSMIALMRPlksltnvNAQFQRGMAAcqTLF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 766 RILDSKPKIDSSSDEgiaLSLLIGEIELDHVSFKYPTRpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDP 845
Cdd:PRK11176 320 AILDLEQEKDEGKRV---IERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 846 DSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPGDVTEEEIIAATTAANVHNVISSLPQGYDASVG 925
Cdd:PRK11176 396 DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 926 ERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGV 1005
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGE 555
|
490 500
....*....|....*....|.
gi 1562645982 1006 IAEKGSHDFLMKiTDGAYASL 1026
Cdd:PRK11176 556 IVERGTHAELLA-QNGVYAQL 575
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
594-1027 |
7.53e-94 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 310.35 E-value: 7.53e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 594 QNIATIMAGLV---IGFTANWKL--MLVVLAVSPLILlqGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFC- 667
Cdd:PRK13657 136 EHLATLVALVVllpLALFMNWRLslVLVVLGIVYTLI--TTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNr 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 668 --SEKKVMEAYEKKCEG---PLKQGVRLGVVSGSGFGFSFFLMfctnalIFYIGAILVKHGQATFEQVfkVFFaITITAM 742
Cdd:PRK13657 214 ieAETQALRDIADNLLAaqmPVLSWWALASVLNRAASTITMLA------ILVLGAALVQKGQLRVGEV--VAF-VGFATL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 743 GVSQATSMAPDSNKAKDSAASI---FRILDSKPKIDSSSDeGIALSLLIGEIELDHVSFKYPTRPdvQIFRDICLKMPSG 819
Cdd:PRK13657 285 LIGRLDQVVAFINQVFMAAPKLeefFEVEDAVPDVRDPPG-AIDLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 820 KTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEE 899
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRP-DATDEE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 900 IIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVN 979
Cdd:PRK13657 441 MRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKG 520
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1562645982 980 RTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKiTDGAYASLV 1027
Cdd:PRK13657 521 RTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVA-RGGRFAALL 567
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
789-1018 |
1.60e-91 |
|
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: 291.44 E-value: 1.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYptRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQ 868
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKD 948
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRP-NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKI 1018
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
757-1017 |
1.31e-90 |
|
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: 300.91 E-value: 1.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 757 AKDSAASIFRILDSKPKIDSSSDEGIALSLLIgEIELDHVSFKYPTRPdvQIFRDICLKMPSGKTVALVGESGSGKSTVI 836
Cdd:COG4988 304 GIAAAEKIFALLDAPEPAAPAGTAPLPAAGPP-SIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 837 GLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSL 916
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRP-DASDEELEAALEAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 917 PQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGAD 996
Cdd:COG4988 460 PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQAD 539
|
250 260
....*....|....*....|.
gi 1562645982 997 IIAVVKNGVIAEKGSHDFLMK 1017
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLA 560
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
539-1029 |
2.93e-83 |
|
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: 280.88 E-value: 2.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 539 KLVERIRALSFQKVVHQqvswfdDPAN----SSGAIGARLSTDASTIKSLVGDALALIVqnIATIMAGLVIGFTA--NWK 612
Cdd:COG4987 85 RLLADLRVRLYRRLEPL------APAGlarlRSGDLLNRLVADVDALDNLYLRVLLPLL--VALLVILAAVAFLAffSPA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 613 LMLVVLAVspLILLQG---TLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVR 689
Cdd:COG4987 157 LALVLALG--LLLAGLllpLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 690 LGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFeqvfkVFFA-ITITAMGVSQATSMAPDS----NKAKDSAASI 764
Cdd:COG4987 235 LARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSG-----PLLAlLVLAALALFEALAPLPAAaqhlGRVRAAARRL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 765 FRILDSKPKIDSSSDEGIALSllIGEIELDHVSFKYPTRPDvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYD 844
Cdd:COG4987 310 NELLDAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 845 PDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASV 924
Cdd:COG4987 387 PQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP-DATDEELWAALERVGLGDWLAALPDGLDTWL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 925 GERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNG 1004
Cdd:COG4987 466 GEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDG 545
|
490 500
....*....|....*....|....*
gi 1562645982 1005 VIAEKGSHDFLMKiTDGAYASLVAL 1029
Cdd:COG4987 546 RIVEQGTHEELLA-QNGRYRQLYQR 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
791-1029 |
1.70e-82 |
|
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: 267.43 E-value: 1.70e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYptRPD-VQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQI 869
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLFNESIRANIAYGKPGdVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDP 949
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG-MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 950 KILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKiTDGAYASLVAL 1029
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLYQL 236
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
47-348 |
2.08e-82 |
|
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: 270.09 E-value: 2.08e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 47 LMIVGTISAVGNGLSKPLMTLVFGNLINTFGCTDPGHIVPMISKVSLKFVYLAIGTGAAALLQVACWMVTGERQAARIRG 126
Cdd:cd18578 10 LLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 127 KYMKAILRQDIGFFD-TETSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVI 205
Cdd:cd18578 90 LAFRAILRQDIAWFDdPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 206 AGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIF 285
Cdd:cd18578 170 AGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTF 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 286 CSYALAVWYGSKMIIKHGYNGGQVINVIFALMTGGMSLGQASPSLNAFASGKAAAYKIIGTHD 348
Cdd:cd18578 250 FAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLD 312
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
336-1029 |
1.46e-81 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 291.16 E-value: 1.46e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 336 GKAAAYKI-IGTHDELTRDPEGAYSQLIHLQEGSkvdngAQTSDPNRMDTSLDIDRTMLSSGSRRLSMRRSISRGSSGGR 414
Cdd:PTZ00265 698 NNAGSYIIeQGTHDALMKNKNGIYYTMINNQKVS-----SKKSSNNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKHENE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 415 HSFTVGFGIPGPIDVQENEVGHEDDHDRPKVDSKKRNTVSIR---RLAALNKPEVPVLLLGAIAAAGhgvLFPIFGLLLS 491
Cdd:PTZ00265 773 SASNKKSCKMSDENASENNAGGKLPFLRNLFKRKPKAPNNLRivyREIFSYKKDVTIIALSILVAGG---LYPVFALLYA 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 492 KAIGMFYEPPNeLRHDSRKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDDPANSSGAIG 571
Cdd:PTZ00265 850 KYVSTLFDFAN-LEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLS 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 572 ARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGF----------TANWKLMLVVLAVSPLILLQGTLQAKFLK----- 636
Cdd:PTZ00265 929 AHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFyfcpivaavlTGTYFIFMRVFAIRARLTANKDVEKKEINqpgtv 1008
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 637 -GFSADAKiMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYI 715
Cdd:PTZ00265 1009 fAYNSDDE-IFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWF 1087
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 716 GAILVKHGQATFEQVFKVFFAITITAMGVSQATSMAPDSNKAKDSAASIFRILDSKPKIDSSSDEGIAL---SLLIGEIE 792
Cdd:PTZ00265 1088 GSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIknkNDIKGKIE 1167
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 793 LDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYD---------------------------- 844
Cdd:PTZ00265 1168 IMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdee 1247
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 845 --------------------------PDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEE 898
Cdd:PTZ00265 1248 qnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATRE 1326
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 899 EIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQ----DALD 974
Cdd:PTZ00265 1327 DVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKD 1406
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 975 RvmVNRTTVVVAHRLSTIKGADIIAVVKN-----GVIAEKGSHDFLMKITDGAYASLVAL 1029
Cdd:PTZ00265 1407 K--ADKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLSVQDGVYKKYVKL 1464
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
787-1006 |
1.49e-80 |
|
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: 261.64 E-value: 1.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 787 LIGEIELDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLR 866
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAIL 946
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQ-SCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVI 1006
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
791-1004 |
1.57e-78 |
|
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: 253.84 E-value: 1.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNESIRANIaygkpgdvteeeiiaattaanvhnvisslpqgydasvgergvqLSGGQKQRIAIARAILKDPK 950
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 951 ILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNG 1004
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
584-1026 |
1.70e-77 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 268.53 E-value: 1.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 584 LVGDALALIVQNIATIMAGLVIGFTANwKLMLVVLAVSPLILL-----QGTLQAKFLKGFSADAkimyeEASQVANDAIG 658
Cdd:TIGR01846 252 LTGSALTVVLDLLFVVVFLAVMFFYSP-TLTGVVIGSLVCYALlsvfvGPILRKRVEDKFERSA-----AATSFLVESVT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 659 SIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQVFkvffAIT 738
Cdd:TIGR01846 326 GIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLV----AFN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 739 ITAMGVSQAT-SMAP---DSNKAKDSAASIFRILDSKpkIDSSSDEGIALSLLIGEIELDHVSFKYptRPDV-QIFRDIC 813
Cdd:TIGR01846 402 MLAGRVTQPVlRLAQlwqDFQQTGIALERLGDILNSP--TEPRSAGLAALPELRGAITFENIRFRY--APDSpEVLSNLN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 814 LKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPG 893
Cdd:TIGR01846 478 LDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 894 dVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDAL 973
Cdd:TIGR01846 558 -APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNM 636
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 974 DRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKiTDGAYASL 1026
Cdd:TIGR01846 637 REICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLA-LQGLYARL 688
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
469-764 |
3.49e-67 |
|
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: 227.74 E-value: 3.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 469 LLLGAIAAAGHGVLFPIFGLLLSKAIGMF------YEPPNELRHDSRKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVE 542
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 543 RIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSP 622
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 623 LILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSF 702
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 703 FLMFCTNALIFYIGAILVKHGQATFEQVFKVFFAITITAMGVSQATSMAPDSNKAKDSAASI 764
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-343 |
1.13e-66 |
|
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: 226.77 E-value: 1.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 48 MIVGTISAVGNGLSKPLMTLVFGNLINTFGCTDPGHIVPMISKVSLK---------------FVYLAIGTGA--AALLQV 110
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSSagpfekleeemtlyaYYYLIIGAIVliTAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 111 ACWMVTGERQAARIRGKYMKAILRQDIGFFDTETsTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGW 190
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVND-TGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 191 RLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQG 270
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 271 LVTGIGLGIFMLVIFCSYALAVWYGSKMIIKHGYNGGQVINVIFALMTGGMSLGQASPSLNAFASGKAAAYKI 343
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
789-1006 |
2.95e-66 |
|
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: 222.08 E-value: 2.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYPTRPDVQIfRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQ 868
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKD 948
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAP-LADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVI 1006
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
753-1001 |
6.15e-63 |
|
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: 223.32 E-value: 6.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 753 DSNKAKDSAASIFRILDSKPKIDSSSDEGIALSLLigEIELDHVSFKYPTRPDVqiFRDICLKMPSGKTVALVGESGSGK 832
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPAS--SLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 833 STVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNV 912
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARP-DASDAEIREALERAGLDEF 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 913 ISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTI 992
Cdd:TIGR02857 441 VAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALA 520
|
....*....
gi 1562645982 993 KGADIIAVV 1001
Cdd:TIGR02857 521 ALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
789-1011 |
2.84e-61 |
|
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: 208.12 E-value: 2.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYptRPDVQ-IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQ 867
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNESIRANIAygkP-GDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAIL 946
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD---PfGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
516-1034 |
1.48e-60 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 226.83 E-value: 1.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 516 VGLGCAGLLVVPVQNFFFGVAGGKLVERIRaLSFQKVVHQQVSWFDDpaNSSGAigaRLSTDA----STIKSLVGDALAL 591
Cdd:PTZ00265 104 VLIGIFQFILSFISSFCMDVVTTKILKTLK-LEFLKSVFYQDGQFHD--NNPGS---KLTSDLdfylEQVNAGIGTKFIT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 592 IVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKgFSADAKIMYEEAS-QVANDAIGSIRTVASFCSEK 670
Cdd:PTZ00265 178 IFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVK-INKKTSLLYNNNTmSIIEEALVGIRTVVSYCGEK 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 671 KVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGA-ILVK-----------HGQATFEQVFKVF---F 735
Cdd:PTZ00265 257 TILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTrIIISdlsnqqpnndfHGGSVISILLGVLismF 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 736 AITITAMGVSQATsmapdsnKAKDSAASIFRILDSKPKIDSSSDeGIALSLlIGEIELDHVSFKYPTRPDVQIFRDICLK 815
Cdd:PTZ00265 337 MLTIILPNITEYM-------KSLEATNSLYEIINRKPLVENNDD-GKKLKD-IKKIQFKNVRFHYDTRKDVEIYKDLNFT 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 816 MPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLL-DGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYG---- 890
Cdd:PTZ00265 408 LTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlysl 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 891 ------------------------------KPGD----------------------VTEEEIIAATTAANVHNVISSLPQ 918
Cdd:PTZ00265 488 kdlealsnyynedgndsqenknkrnscrakCAGDlndmsnttdsneliemrknyqtIKDSEVVDVSKKVLIHDFVSALPD 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 919 GYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAHRLSTIKGAD 996
Cdd:PTZ00265 568 KYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYAN 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 997 IIAVVKN-----------------------------------------------GVIAEKGSHDFLMKITDGAYASL--- 1026
Cdd:PTZ00265 648 TIFVLSNrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagSYIIEQGTHDALMKNKNGIYYTMinn 727
|
650
....*....|
gi 1562645982 1027 --VALHSSSN 1034
Cdd:PTZ00265 728 qkVSSKKSSN 737
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
528-1027 |
1.43e-58 |
|
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: 214.99 E-value: 1.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 528 VQNFFFGVAGGKLVERIrALSFQKVVHQ-QVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIG 606
Cdd:TIGR01193 215 IQIFLLNVLGQRLSIDI-ILSYIKHLFElPMSFFS--TRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 607 FTaNWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKimyeEASQVANDAI----GSIRTVASFCSEKKVMEAYEKKCEG 682
Cdd:TIGR01193 292 RQ-NMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAM----QANAVLNSSIiedlNGIETIKSLTSEAERYSKIDSEFGD 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 683 PLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQVfkvffaITITAMgVSQATSmaPDSN----KAK 758
Cdd:TIGR01193 367 YLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQL------ITFNAL-LSYFLT--PLENiinlQPK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 759 DSAASIFRI-LDSKPKIDS---SSDEGIALSLLIGEIELDHVSFKYPTrpDVQIFRDICLKMPSGKTVALVGESGSGKST 834
Cdd:TIGR01193 438 LQAARVANNrLNEVYLVDSefiNKKKRTELNNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKST 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 835 VIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPGDVTEEEIIAATTAANVHNVIS 914
Cdd:TIGR01193 516 LAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 915 SLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRvMVNRTTVVVAHRLSTIKG 994
Cdd:TIGR01193 596 NMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQ 674
|
490 500 510
....*....|....*....|....*....|...
gi 1562645982 995 ADIIAVVKNGVIAEKGSHDFLMKiTDGAYASLV 1027
Cdd:TIGR01193 675 SDKIIVLDHGKIIEQGSHDELLD-RNGFYASLI 706
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
760-1015 |
1.66e-58 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 211.49 E-value: 1.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 760 SAA--SIFRILDSKPKIDsssDEGIALSLLIGEIELDHVSFKYPTRpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIG 837
Cdd:PRK10789 284 SAAysRIRAMLAEAPVVK---DGSEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 838 LIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLP 917
Cdd:PRK10789 360 LIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRP-DATQQEIEHVARLASVHDDILRLP 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 918 QGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADI 997
Cdd:PRK10789 439 QGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASE 518
|
250
....*....|....*...
gi 1562645982 998 IAVVKNGVIAEKGSHDFL 1015
Cdd:PRK10789 519 ILVMQHGHIAQRGNHDQL 536
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
760-1026 |
1.68e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 211.61 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 760 SAASIFRILDSKPKIDSSSDEGIALSLliGEIELDHVSFKYPTRPDvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLI 839
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 840 ERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSlPQG 919
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEVLQQVGLEKLLED-DKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 920 YDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIA 999
Cdd:PRK11160 465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544
|
250 260
....*....|....*....|....*..
gi 1562645982 1000 VVKNGVIAEKGSHDFLMKiTDGAYASL 1026
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLA-QQGRYYQL 570
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
48-321 |
5.38e-57 |
|
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: 198.25 E-value: 5.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 48 MIVGTISAVGNGLSKPLMTLVFGNLINTFGCTDPGHIVPMIsKVSLKFVYLAIGTGAAALLQVACWMVTGERQAARIRGK 127
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALN-VYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 128 YMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAG 207
Cdd:pfam00664 80 LFKKILRQPMSFFDT-NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 208 AVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCS 287
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1562645982 288 YALAVWYGSKMIIKHGYNGGQVI--NVIFALMTGGM 321
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVafLSLFAQLFGPL 274
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
708-1028 |
8.02e-57 |
|
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: 209.43 E-value: 8.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 708 TNALIFYIGAILVKHGQATFEQVFKVFFAITITAMGVSQATSMAPDSNkakdSAASIFR----ILDSKPKIDS-SSDEGI 782
Cdd:TIGR03797 372 TSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISIL----AVIPLWErakpILEALPEVDEaKTDPGK 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 783 alslLIGEIELDHVSFKYptRPD-VQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK 861
Cdd:TIGR03797 448 ----LSGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 862 LNWLRQQIGLVGQEPVLFNESIRANIAYGKPgdVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAI 941
Cdd:TIGR03797 522 VQAVRRQLGVVLQNGRLMSGSIFENIAGGAP--LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLI 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRttVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKiTDG 1021
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA-REG 676
|
....*..
gi 1562645982 1022 AYASLVA 1028
Cdd:TIGR03797 677 LFAQLAR 683
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
512-1016 |
2.46e-56 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 205.72 E-value: 2.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 512 ALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALAL 591
Cdd:PRK10790 68 AAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFD--TQPVGQLISRVTNDTEVIRDLYVTVVAT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 592 IVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKF-------LKGFSADAKIMYEEasqVAN--DAIGSIRT 662
Cdd:PRK10790 146 VLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYstpivrrVRAYLADINDGFNE---VINgmSVIQQFRQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 663 VASFcsEKKVMEA----YEKKCEGPLKQGVRLGVVSGSGFGfsffLMFCTNALIF---YIGAILVKhgqatfeqvfkVFF 735
Cdd:PRK10790 223 QARF--GERMGEAsrshYMARMQTLRLDGFLLRPLLSLFSA----LILCGLLMLFgfsASGTIEVG-----------VLY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 736 AItITAMG-----VSQATSMAPDSNKAKDSAASIFRILDSkPKIDSSSDEgiaLSLLIGEIELDHVSFKYptRPDVQIFR 810
Cdd:PRK10790 286 AF-ISYLGrlnepLIELTTQQSMLQQAVVAGERVFELMDG-PRQQYGNDD---RPLQSGRIDIDNVSFAY--RDDNLVLQ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 811 DICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYG 890
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 891 KpgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQ 970
Cdd:PRK10790 439 R--DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQ 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1562645982 971 DALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLM 1016
Cdd:PRK10790 517 QALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
469-764 |
4.03e-54 |
|
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: 191.34 E-value: 4.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 469 LLLGAIAAAGHGVLFPIFGLLLSKAIGMF------------------YEPPNELRHDSRKWALVYVGLGCAGLLVVPVQN 530
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnssglnssAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 531 FFFGVAGGKLVERIRALSFQKVVHQQVSWFddPANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTAN 610
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 611 WKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRL 690
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 691 GVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQVFKVFFAITI-TAMGVSQATSMAPDSNkAKDSAASI 764
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIgAFSAGQQVPSIEAFAN-ARGAAYHI 312
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
711-1013 |
2.30e-53 |
|
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: 196.51 E-value: 2.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 711 LIFYIGAILVKHGQATFeqvfKVFFAITItAMG-----VSQATSMAPDSNKAKDSAASIFRILDSKPKidssSDEGIALS 785
Cdd:COG4618 255 AVLGLGAYLVIQGEITP----GAMIAASI-LMGralapIEQAIGGWKQFVSARQAYRRLNELLAAVPA----EPERMPLP 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 786 LLIGEIELDHVSFKYPTRpDVQIFRDICLKMPSGKTVALVGESGSGKST----VIGLIErfydPDSGRVLLDGVEIQkfk 861
Cdd:COG4618 326 RPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVWP----PTAGSVRLDGADLS--- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 862 lNWLRQQIG-LVG---QEPVLFNESIRANIAygKPGDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQ 937
Cdd:COG4618 398 -QWDREELGrHIGylpQDVELFDGTIAENIA--RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQ 474
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 938 RIAIARAILKDPKILLLDEATSALDAESERKVQDALDRV-MVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHD 1013
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRD 551
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
817-1028 |
5.90e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 195.83 E-value: 5.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 817 PSGKTVALVGESGSGKSTVIGLIERFYdPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKPgDVT 896
Cdd:PRK11174 374 PAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNP-DAS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 897 EEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRV 976
Cdd:PRK11174 452 DEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA 531
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 977 MVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKiTDGAYASLVA 1028
Cdd:PRK11174 532 SRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQ-AGGLFATLLA 582
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
715-989 |
1.32e-50 |
|
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: 187.57 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 715 IGAILVKHGQATFEQVFKVFFAITI-TAMGVSQATSMAPDS----NKAKDSAASIFRILDSKPKIDSSSDEGIALSLLIG 789
Cdd:TIGR02868 253 LGALWAGGPAVADGRLAPVTLAVLVlLPLAAFEAFAALPAAaqqlTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGK 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 790 -EIELDHVSFKYPTRPDVqiFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQ 868
Cdd:TIGR02868 333 pTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLFNESIRANIAYGKPgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKD 948
Cdd:TIGR02868 411 VSVCAQDAHLFDTTVRENLRLARP-DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLAD 489
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRL 989
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
755-1013 |
2.76e-48 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 181.01 E-value: 2.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 755 NKAKDSAASIFRILDSKPkidsSSDEGIALSLLIGEIELDHVSFKyPTRPDVQIFRDICLKMPSGKTVALVGESGSGKST 834
Cdd:TIGR01842 285 SGARQAYKRLNELLANYP----SRDPAMPLPEPEGHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKST 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 835 VIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIA-YGKpgDVTEEEIIAATTAANVHNVI 913
Cdd:TIGR01842 360 LARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIArFGE--NADPEKIIEAAKLAGVHELI 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 914 SSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNR-TTVVVAHRLSTI 992
Cdd:TIGR01842 438 LRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLL 517
|
250 260
....*....|....*....|.
gi 1562645982 993 KGADIIAVVKNGVIAEKGSHD 1013
Cdd:TIGR01842 518 GCVDKILVLQDGRIARFGERD 538
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
791-987 |
7.38e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.61 E-value: 7.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNESIRANIAYG---KPGDVTEEEIIAATTAANvhnvissLPQGY-DASVGErgvqLSGGQKQRIAIARAIL 946
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPfqlRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAH 987
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
469-742 |
2.13e-47 |
|
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: 170.52 E-value: 2.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 469 LLLGAIAAAGHGVLFPIFGLLLSKAIGMFYEPPNELRHDSRKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALS 548
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 549 FQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQG 628
Cdd:pfam00664 81 FKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 629 TLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCT 708
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1562645982 709 NALIFYIGAILVKHGQATFEQ--VFKVFFAITITAM 742
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
791-1011 |
3.94e-46 |
|
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: 165.43 E-value: 3.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYD-----PDSGRVLLDGVEI--QKFKLN 863
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 WLRQQIGLVGQEPVLFNESIRANIAYG------KPGDVTEEEIIAATTAAnvhnvisslpqGYDASVGER--GVQLSGGQ 935
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALRKA-----------ALWDEVKDRlhALGLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 936 KQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGP 223
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
51-343 |
4.51e-45 |
|
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: 164.66 E-value: 4.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 51 GTISAVGNGLSKPLMTLVFGNLINTFGCTDPGHivpMISKVSLKFVYLAIGTGAAALLQVACWMVTGERQAARIRGKYMK 130
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLD---VLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 131 AILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVM 210
Cdd:cd18557 78 SLLRQEIAFFD-KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 211 ATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYAL 290
Cdd:cd18557 157 GRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 291 AVWYGSKMIIKHGYNGGQVINVIFALMTGGMSLGQASPSLNAFASGKAAAYKI 343
Cdd:cd18557 237 VLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
791-1006 |
1.80e-44 |
|
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: 158.53 E-value: 1.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYP--TRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQ 868
Cdd:cd03246 1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLFNESIRANIaygkpgdvteeeiiaattaanvhnvisslpqgydasvgergvqLSGGQKQRIAIARAILKD 948
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRV-MVNRTTVVVAHRLSTIKGADIIAVVKNGVI 1006
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
791-1010 |
1.11e-43 |
|
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: 156.32 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKlNWLRQQIG 870
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNESIRANIaygkpgdvteeeiiaattaanvhnvisslpqgydasvgerGVQLSGGQKQRIAIARAILKDPK 950
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 951 ILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKG 1010
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
789-1011 |
1.66e-43 |
|
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: 157.19 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYptRPDV-QIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQ 867
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNESIRANI-AYGKpgdVTEEEIIAATtaanvhnvisslpqgydaSVGERGVQLSGGQKQRIAIARAIL 946
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDE---YSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
791-1011 |
3.49e-43 |
|
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: 157.11 E-value: 3.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPV--LFNESIRANIAYGkP---GdVTEEEIIAATTAAnvhnvissLpqgydASVG-----ERGV-QLSGGQKQRI 939
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFG-PenlG-LPREEIRERVEEA--------L-----ELVGlehlaDRPPhELSGGQKQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 940 AIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGT 217
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
51-324 |
2.73e-42 |
|
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: 156.64 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 51 GTISAVGNGLSKPLMTLVFGNLINTFGCTDPGHIVPMISKVSLKFVYLAI---GTGAAALLQVACWMVTGERQAARIRGK 127
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGvvlIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 128 YMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAG 207
Cdd:cd18780 81 LFSAIIAQEIAFFDV-TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 208 AVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCS 287
Cdd:cd18780 160 VIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLA 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 1562645982 288 YALAVWYGSKMIIKHGYNGGQVINVIFALMTGGMSLG 324
Cdd:cd18780 240 IVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFA 276
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
791-1008 |
1.20e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.50 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPT-RPDVQIFRDICLKMPSGKTVALVGESGSGKST---VIGLIERfydPDSGRVLLDGVEIQKFK---LN 863
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 WLR-QQIGLVGQEPVLFNE-SIRANIAY-----GKPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQK 936
Cdd:COG1136 82 RLRrRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 937 QRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRV--MVNRTTVVVAHRLSTIKGADIIAVVKNGVIAE 1008
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
791-1011 |
9.93e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 158.14 E-value: 9.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRP--DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK---LNWL 865
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 866 RQQIGLVGQEPVL-FNE--SIRANIAYG--KPGDVTEEEIiaattAANVHNVISSLpqGYDASVGER-GVQLSGGQKQRI 939
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlrLHGLLSRAER-----RERVAELLERV--GLPPDLADRyPHELSGGQRQRV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 940 AIARAILKDPKILLLDEATSALDAESERKVQDALDRV--MVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
792-1004 |
2.13e-40 |
|
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: 148.38 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 792 ELDHVSFKYPTRpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGL 871
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 872 VGQEP--VLFNESIRANIAYG-KPGDVTEEEIIAATTAANVHNVISSLPqgyDASVGergvQLSGGQKQRIAIARAILKD 948
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGlENLGLPEEEIEERVEEALELVGLEGLR---DRSPF----TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTIKG-ADIIAVVKNG 1004
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDG 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
809-959 |
4.14e-40 |
|
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: 145.10 E-value: 4.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 809 FRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNE-SIRANI 887
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 888 AYGkpgdVTEEEIIAATTAANVHNVISSLPQGYDAS--VGERGVQLSGGQKQRIAIARAILKDPKILLLDEATS 959
Cdd:pfam00005 81 RLG----LLLKGLSKREKDARAEEALEKLGLGDLADrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
791-1010 |
1.17e-39 |
|
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: 146.13 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIqkFKLNWLRQQIG 870
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLF-NESIRANIAYG-KPGDVTEEEIiaattAANVHNVISSLpqGYDASVGERGVQLSGGQKQRIAIARAILKD 948
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGlKLRGVPKAEI-----RARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRVMVNR--TTVVVAHRLS---TIkgADIIAVVKNGVIAEKG 1010
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEealAL--ADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
791-1010 |
1.90e-39 |
|
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: 146.11 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPD-VQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK---LNWLR 866
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEPVL-FN--ESIRANIA-----YGKPGDVTEEEIIAATTAANVHN---VISSLPQgydasvgergvQLSGGQ 935
Cdd:cd03257 82 KEIQMVFQDPMSsLNprMTIGEQIAeplriHGKLSKKEARKEAVLLLLVGVGLpeeVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 936 KQRIAIARAILKDPKILLLDEATSALDAESERKVQDALD--RVMVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKG 1010
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
791-1024 |
2.08e-39 |
|
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: 146.87 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRP-DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQI 869
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVL-FN--ESIRANIA-----YGKPGdvTEEEIIAAttAANVhnvisslpqGYDASVGERGV-QLSGGQKQRIA 940
Cdd:COG1124 82 QMVFQDPYAsLHprHTVDRILAeplriHGLPD--REERIAEL--LEQV---------GLPPSFLDRYPhQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNR--TTVVVAHRLSTI-KGADIIAVVKNGVIAEKGSHDFLMK 1017
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
....*..
gi 1562645982 1018 ITDGAYA 1024
Cdd:COG1124 229 GPKHPYT 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
791-1011 |
2.34e-39 |
|
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: 146.19 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRP-DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI---QKFKLNWLR 866
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEPVLFN-ESIRANIAY-----GKPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIA 940
Cdd:cd03258 82 RRIGMIFQHFNLLSsRTVFENVALpleiaGVPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALDRvmVNR----TTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRD--INRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
95-310 |
2.99e-39 |
|
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: 147.69 E-value: 2.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 95 FVYLAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGEMVGKFIQL 174
Cdd:cd18572 42 LLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD-ATKTGELTSRLTSDCQKVSDPLSTNLNVFLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 175 CSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQ 254
Cdd:cd18572 121 LVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 255 YNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYALAVWYGSKMIIKHGYNGGQVI 310
Cdd:cd18572 201 YERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLV 256
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
791-1006 |
3.40e-39 |
|
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: 144.94 E-value: 3.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPD-VQIFRDICLKMPSGKTVALVGESGSGKST---VIGLIERfydPDSGRVLLDGVEIQKFKLNWL- 865
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 866 ---RQQIGLVGQEPVLFNE-SIRANIAY-----GKPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQK 936
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 937 QRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRV--MVNRTTVVVAHRLSTIKGADIIAVVKNGVI 1006
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
791-1004 |
4.07e-39 |
|
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: 143.48 E-value: 4.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNW--LRQQ 868
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLF-NESIRANIAYGkpgdvteeeiiaattaanvhnvisslpqgydasvgergvqLSGGQKQRIAIARAILK 947
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 948 DPKILLLDEATSALDAESERKVQDALDRV--MVNRTTVVVAHRLS-TIKGADIIAVVKNG 1004
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
774-1030 |
1.27e-38 |
|
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: 144.67 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 774 IDSSSDEGiaLSLLIGEIELDHVSFKYPT--RPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVL 851
Cdd:cd03288 5 ISGSSNSG--LVGLGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 852 LDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANIAYGKpgDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQL 931
Cdd:cd03288 80 IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC--KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 932 SGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:cd03288 158 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDT 237
|
250
....*....|....*....
gi 1562645982 1012 HDFLMKITDGAYASLVALH 1030
Cdd:cd03288 238 PENLLAQEDGVFASLVRTD 256
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
791-1004 |
2.07e-38 |
|
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: 142.22 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQ--IFRDICLKMPSGKTVALVGESGSGKSTVIGLI--ErfYDPDSGRVLLDGveiqkfklnwlr 866
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 qQIGLVGQEPVLFNESIRANIAYGKPGDvtEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAIL 946
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGKPFD--EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 947 KDPKILLLDEATSALDAESERKV-QDALDRVMV-NRTTVVVAHRLSTIKGADIIAVVKNG 1004
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIfENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
791-1020 |
8.58e-38 |
|
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: 141.66 E-value: 8.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKST----VIGLIErfydPDSGRVLLDGVEIQKF---KLN 863
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVllklIIGLLR----PDSGEILVDGQDITGLsekELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 WLRQQIGLVGQEPVLFNE-SIRANIAYgkP----GDVTEEEIIAAttaanvhnVISSLpqgydASVGERGV------QLS 932
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVAF--PlrehTDLSEAEIREL--------VLEKL-----ELVGLPGAadkmpsELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 933 GGQKQRIAIARAILKDPKILLLDEATSALDAESE-------RKVQDALdrvmvNRTTVVVAHRLSTIKG-ADIIAVVKNG 1004
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSavideliRELRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADG 218
|
250
....*....|....*.
gi 1562645982 1005 VIAEKGSHDFLMKITD 1020
Cdd:COG1127 219 KIIAEGTPEELLASDD 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
791-1011 |
3.01e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.20 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWlRQQIG 870
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNE-SIRANI-----AYGKPGDVTEEEIIAATTAANvhnvissLPQGYDASVGergvQLSGGQKQRIAIARA 944
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIDELLELFG-------LTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 945 ILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
791-1011 |
3.05e-37 |
|
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: 140.38 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKfKLNWLRQQIG 870
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLF-NESIRANI-----AYGKPGDVTE---EEIIAATTaanvhnvissLPQGYDASVGErgvqLSGGQKQRIAI 941
Cdd:COG4555 78 VLPDERGLYdRLTVRENIryfaeLYGLFDEELKkriEELIELLG----------LEEFLDRRVGE----LSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGS 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
791-1020 |
4.09e-37 |
|
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: 139.56 E-value: 4.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK---LNWLRQ 867
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNE-SIRANIAYgkP----GDVTEEEIIAAttaanvhnVISSLpqgydASVGERGV------QLSGGQK 936
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAF--PlrehTRLSEEEIREI--------VLEKL-----EAVGLRGAedlypaELSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 937 QRIAIARAILKDPKILLLDEATSALD-------AESERKVQDALdrvmvNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAE 1008
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKEL-----GLTSIMVTHDLDTAFAiADRIAVLYDGKIVA 217
|
250
....*....|..
gi 1562645982 1009 KGSHDFLMKITD 1020
Cdd:cd03261 218 EGTPEELRASDD 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
791-1011 |
5.47e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 142.52 E-value: 5.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRP-DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLI---ERfydPDSGRVLLDGVEIQKFK---LN 863
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllER---PTSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 WLRQQIGLVGQEPVLFNE-SIRANIAY-----GKPGdvteEEIiaattAANVHNVIsslpqgydASVG--ERG----VQL 931
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALpleiaGVPK----AEI-----RKRVAELL--------ELVGlsDKAdaypSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 932 SGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRvmVNR----TTVVVAHRLSTIKG-ADIIAVVKNGVI 1006
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKD--INRelglTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 1562645982 1007 AEKGS 1011
Cdd:COG1135 220 VEQGP 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
789-1011 |
6.16e-37 |
|
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: 151.64 E-value: 6.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYptRPDVQ-IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQ 867
Cdd:TIGR00957 1283 GRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNESIRANIaygKP-GDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAIL 946
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNL---DPfSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGA 1502
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
791-987 |
6.62e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.84 E-value: 6.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRP-DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKfklnwLRQQI 869
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLFN-ESIRANIAYG-KPGDVTEEEIIAATTAAnvhnvissLpqgydASVGERGV------QLSGGQKQRIAI 941
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlELRGVPKAERRERAREL--------L-----ELVGLAGFedayphQLSGGMRQRVAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDALDRV-MVNRTTVV-VAH 987
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfVTH 197
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
791-1011 |
1.23e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.16 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIqkfklNWL---RQ 867
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLppeKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLF-NESIRANIAYG-KPGDVTEEEIIAATTAA--NVHnvISSLpqgydasvGERGV-QLSGGQKQRIAIA 942
Cdd:COG3842 78 NVGMVFQDYALFpHLTVAENVAFGlRMRGVPKAEIRARVAELleLVG--LEGL--------ADRYPhQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 943 RAILKDPKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAHRLS---TIkgADIIAVVKNGVIAEKGS 1011
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
791-1016 |
1.95e-36 |
|
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: 137.82 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYP-TRPDVQifrDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQI 869
Cdd:cd03295 1 IEFENVTKRYGgGKKAVN---NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLF-NESIRANIA-YGKPGDVTEEEII--AATTAANVHNVISSLPQGYDAsvgergvQLSGGQKQRIAIARAI 945
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENIAlVPKLLKWPKEKIRerADELLALVGLDPAEFADRYPH-------ELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 946 LKDPKILLLDEATSALDAESERKVQDALDRV--MVNRTTVVVAHRL-STIKGADIIAVVKNGVIAEKGSHDFLM 1016
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
26-357 |
2.97e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 145.69 E-value: 2.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 26 KKKQKVAFYKLFSFAdRLDVALMIVGTISAVGNGLSKPLMTLVFGNLINT-FGCTDPGHIVPMIskvsLKFVYLAIGTGA 104
Cdd:COG1132 2 SKSPRKLLRRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDAlLAGGDLSALLLLL----LLLLGLALLRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 105 AALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVI 184
Cdd:COG1132 77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDR-RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 185 AFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYN 264
Cdd:COG1132 156 LFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 265 TMVQQGLVTGIGLGIFMLVIFCSYALAVWYGSKMIIKHGYNGGQVINVIFALMTGGMSLGQASPSLNAFASGKAAAYKII 344
Cdd:COG1132 236 ANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIF 315
|
330
....*....|....*
gi 1562645982 345 GTHDE--LTRDPEGA 357
Cdd:COG1132 316 ELLDEppEIPDPPGA 330
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
791-986 |
3.55e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 136.72 E-value: 3.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK---LNWLRQ 867
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQE-PVLFNESIRANIAY-----GKPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAI 941
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDALDRvmVNR--TTVVVA 986
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEE--INRrgTTVLIA 193
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
792-1004 |
3.81e-36 |
|
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: 133.91 E-value: 3.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 792 ELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGL 871
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 872 VGQepvlfnesiraniaygkpgdvteeeiiaattaanvhnvisslpqgydasvgergvqLSGGQKQRIAIARAILKDPKI 951
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 952 LLLDEATSALDAESERKVQDALDRVMV-NRTTVVVAHRLSTI-KGADIIAVVKNG 1004
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
791-987 |
7.39e-36 |
|
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: 135.68 E-value: 7.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPT-RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKfklnwLRQQI 869
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLFN-ESIRANIAYG-KPGDVTEEEIIAATTAAnVHNVisslpqGYDASVGERGVQLSGGQKQRIAIARAILK 947
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlELQGVPKAEARERAEEL-LELV------GLSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1562645982 948 DPKILLLDEATSALDAESERKVQDALDRVMV-NRTTVV-VAH 987
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLlVTH 190
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
790-1011 |
2.22e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 138.36 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 790 EIELDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLI---ERfydPDSGRVLLDG------VEIQKf 860
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGrdlftnLPPRE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 861 klnwlRqQIGLVGQEPVLF-NESIRANIAYG-KPGDVTEEEIiaattAANVHNVI-----SSLPQGYDAsvgergvQLSG 933
Cdd:COG1118 75 -----R-RVGFVFQHYALFpHMTVAENIAFGlRVRPPSKAEI-----RARVEELLelvqlEGLADRYPS-------QLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 934 GQKQRIAIARAILKDPKILLLDEATSALDAeserKVQDALDRVM------VNRTTVVVAH------RLstikgADIIAVV 1001
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDA----KVRKELRRWLrrlhdeLGGTTVFVTHdqeealEL-----ADRVVVM 207
|
250
....*....|
gi 1562645982 1002 KNGVIAEKGS 1011
Cdd:COG1118 208 NQGRIEQVGT 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
791-1007 |
5.07e-35 |
|
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: 133.85 E-value: 5.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI---QKFKLNWLRQ 867
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNE-SIRANIAYGK----------PGDVTEEEIIAAttaanvhnvISSLPQ-GYDASVGERGVQLSGGQ 935
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSGRlgrrstwrslFGLFPKEEKQRA---------LAALERvGLLDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 936 KQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRV--MVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIA 1007
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
791-1006 |
9.41e-35 |
|
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: 130.60 E-value: 9.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwLRQQIG 870
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFnesiraniaygkpGDVTEEEIIaattaanvhnvisslpqgydasvgergvQLSGGQKQRIAIARAILKDPK 950
Cdd:cd03230 77 YLPEEPSLY-------------ENLTVRENL----------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 951 ILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTI-KGADIIAVVKNGVI 1006
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAeRLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
791-1011 |
1.20e-34 |
|
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: 133.25 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVL-FNESIRANIAYG---------KPGDVTEEEIIAATTAANvhnvISSLpqgydasvGERGV-QLSGGQKQRI 939
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgRPSAEDREAVEEALERTG----LEHL--------ADRPVdELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 940 AIARAILKDPKILLLDEATSALDAESERKVQDALDRV--MVNRTTVVVAHRLS-TIKGADIIAVVKNGVIAEKGS 1011
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
791-1011 |
1.55e-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: 132.43 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI--QKFKLNWLRQQ 868
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLF-NESIRANIAY------GKPGDVTEEeiIAATTAANVHnvissLPQGYDASVGergvQLSGGQKQRIAI 941
Cdd:COG1126 79 VGMVFQQFNLFpHLTVLENVTLapikvkKMSKAEAEE--RAMELLERVG-----LADKADAYPA----QLSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESerkVQDALDrVMVN-----RTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPEL---VGEVLD-VMRDlakegMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
67-327 |
2.32e-34 |
|
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: 133.38 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 67 LVFGNLINTFgctDPGHIVPMISKVSLKFVYLAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDtETST 146
Cdd:cd18576 17 LLAGQLIDAA---LGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFH-ERRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 147 GEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYA 226
Cdd:cd18576 93 GELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 227 EAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYALAVWYGSKMIIKHGYNG 306
Cdd:cd18576 173 EANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTA 252
|
250 260
....*....|....*....|..
gi 1562645982 307 GQVIN-VIFALMTGGmSLGQAS 327
Cdd:cd18576 253 GDLVAfLLYTLFIAG-SIGSLA 273
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
791-1011 |
4.23e-34 |
|
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: 138.11 E-value: 4.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpDVQIFRDICLKMPSGKTVALVGESGSGKST----VIGLIERFYDPdSGRVLLDGVEIQKFKLNWLR 866
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGRI-SGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEP--VLFNESIRANIA-----YGKPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRI 939
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAealenLGLSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 940 AIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNR--TTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGP 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
791-1006 |
1.70e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.79 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK---LNWLRQ 867
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNE-SIRANIAYGKPGDV----------TEEEIIAAttaanvhnvISSLpqgydASVG------ERGVQ 930
Cdd:COG3638 81 RIGMIFQQFNLVPRlSVLTNVLAGRLGRTstwrsllglfPPEDRERA---------LEAL-----ERVGladkayQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 931 LSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRvmVNR----TTVVVAHRLSTIKG-ADIIAVVKNGV 1005
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRR--IARedgiTVVVNLHQVDLARRyADRIIGLRDGR 224
|
.
gi 1562645982 1006 I 1006
Cdd:COG3638 225 V 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
810-1010 |
4.83e-33 |
|
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: 127.84 E-value: 4.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwlRQQIGLVGQEPVLF-NESIRANIA 888
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 889 YG-KPGDVTEEEIiaattAANVHNVISSLpqGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESER 967
Cdd:cd03299 94 YGlKKRKVDKKEI-----ERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1562645982 968 KVQDALDRVM-VNRTTVV-VAHRLSTIKG-ADIIAVVKNGVIAEKG 1010
Cdd:cd03299 167 KLREELKKIRkEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVG 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
790-1013 |
8.09e-33 |
|
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: 127.46 E-value: 8.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 790 EIELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwlRQQI 869
Cdd:cd03296 2 SIEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLFNE-SIRANIAYG---KPGDVTEEEiiaATTAANVHNVI-----SSLPQGYDAsvgergvQLSGGQKQRIA 940
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAFGlrvKPRSERPPE---AEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAHRLS-TIKGADIIAVVKNGVIAEKGSHD 1013
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPD 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
791-989 |
8.80e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.85 E-value: 8.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYD--PD---SGRVLLDGVEI--QKFKLN 863
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 WLRQQIGLVGQEPVLFNESIRANIAYG------KPGDVTEEEIIAATTAAN----VHNVISslpqgydasvgERGVQLSG 933
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESLRKAAlwdeVKDRLK-----------KSALGLSG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 934 GQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRL 989
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM 213
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
67-299 |
2.38e-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: 127.63 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 67 LVFGNLINTFgctDPGHIVPMISKVSLKFVYLAIG----TGAAA-LLQVACWMVTGERQAARIRGKYMKAILRQDIGFFD 141
Cdd:cd18573 17 FAIGKLIDVA---SKESGDIEIFGLSLKTFALALLgvfvVGAAAnFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 142 TeTSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRG 221
Cdd:cd18573 94 K-NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 222 QSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYALAVWYGSKMI 299
Cdd:cd18573 173 QDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLV 250
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
789-1027 |
2.76e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 136.79 E-value: 2.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYptRPDVQ-IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQ 867
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNESIRANI-AYGKPGDVteeEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAIL 946
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLdPFNEHNDA---DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKITDGAYASL 1026
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
.
gi 1562645982 1027 V 1027
Cdd:PLN03130 1471 V 1471
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
791-1011 |
4.87e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 128.38 E-value: 4.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPT-RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK---LNWLR 866
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEpvlFN----ESIRANIAY-----GKPgdvtEEEIiaattAANVHNV-----ISSLPQGYDAsvgergvQLS 932
Cdd:PRK11153 82 RQIGMIFQH---FNllssRTVFDNVALplelaGTP----KAEI-----KARVTELlelvgLSDKADRYPA-------QLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 933 GGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRvmVNR----TTVVVAHRLSTIKG-ADIIAVVKNGVIA 1007
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKD--INRelglTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
|
....
gi 1562645982 1008 EKGS 1011
Cdd:PRK11153 221 EQGT 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
791-987 |
7.13e-32 |
|
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: 123.79 E-value: 7.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI--QKFKLNWLRQQ 868
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLF-NESIRANIAY------GKPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAI 941
Cdd:cd03262 78 VGMVFQQFNLFpHLTVLENITLapikvkGMSKAEAEERALELLEKVGLADKADAYPA-----------QLSGGQQQRVAI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESerkVQDALDrVMVN-----RTTVVVAH 987
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPEL---VGEVLD-VMKDlaeegMTMVVVTH 193
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
789-1032 |
1.92e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 133.95 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYptRPDVQ-IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQ 867
Cdd:PLN03232 1233 GSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNESIRANI-AYGKPGDVteeEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAIL 946
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNIdPFSEHNDA---DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKITDGAYASL 1026
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRM 1467
|
....*.
gi 1562645982 1027 ValHSS 1032
Cdd:PLN03232 1468 V--HST 1471
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
48-343 |
2.76e-31 |
|
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: 124.59 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 48 MIVGTISAVGNGLSKPLMTLVFGNLINTFGctdPGHIVPMISKVSLKFVYLAIGTGAAALLQVACWMVTGERQAARIRGK 127
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI---PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 128 YMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAG 207
Cdd:cd07346 78 LFRHLQRLSLSFFD-RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 208 AVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCS 287
Cdd:cd07346 157 RYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 288 YALAVWYGSKMIIKHGYNGGQVINVIFALMTGGMSLGQASPSLNAFASGKAAAYKI 343
Cdd:cd07346 237 TALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
97-327 |
5.51e-31 |
|
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: 123.75 E-value: 5.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 97 YLAIGTGAAALLQVA----CWMVT--GERQAARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEMVGK 170
Cdd:cd18575 38 AFLLLLAVALVLALAsalrFYLVSwlGERVVADLRKAVFAHLLRLSPSFFET-TRTGEVLSRLTTDTTLIQTVVGSSLSI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 171 FIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQ 250
Cdd:cd18575 117 ALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDA 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 251 AIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYALAVWYGSKMIIKHGYNGGQVIN-VIFALMTGGmSLGQAS 327
Cdd:cd18575 197 ERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQfVFYAVLAAG-SVGALS 273
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
791-1015 |
6.01e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 6.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVI----GLIErfydPDSGRVLLDGVEIQKfklnwLR 866
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLkailGLLP----PTSGTVRLFGKPPRR-----AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQepvlfnesiRANIAYGKPgdVTEEEIIAATTAANVhnvisSLPQGYDAS-----------VG-----ERGV- 929
Cdd:COG1121 75 RRIGYVPQ---------RAEVDWDFP--ITVRDVVLMGRYGRR-----GLFRRPSRAdreavdealerVGledlaDRPIg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 930 QLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDR-VMVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIA 1007
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVA 218
|
....*...
gi 1562645982 1008 EKGSHDFL 1015
Cdd:COG1121 219 HGPPEEVL 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
791-1011 |
9.04e-31 |
|
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: 121.19 E-value: 9.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwlRQQIG 870
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNE-SIRANIAYGKPGDVTEEEIIAATTAANVHNVisslpqGYDASVGERGVQLSGGQKQRIAIARAILKDP 949
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLV------QLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 950 KILLLDEATSALDAESERKVQDALDRV--MVNRTTVVVAHRLS-TIKGADIIAVVKNGVIAEKGS 1011
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
791-1010 |
2.17e-30 |
|
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: 119.43 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLN---WLRQ 867
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQE-PVLFNESIRANIAY-----GKPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAI 941
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFalevtGVPPREIRKRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HrlstikGADIIAVVKNGVIA-EKG 1010
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtH------AKELVDTTRHRVIAlERG 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
792-1010 |
2.73e-30 |
|
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: 117.92 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 792 ELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGL 871
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 872 VGQepVLfnesIRANIAYGKPGDVTEeeiiaattaanvhnvisslpqgydasvgergvqLSGGQKQRIAIARAILKDPKI 951
Cdd:cd03214 78 VPQ--AL----ELLGLAHLADRPFNE---------------------------------LSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 952 LLLDEATSALDAESERKVQDALDRV--MVNRTTVVVAHRLS-TIKGADIIAVVKNGVIAEKG 1010
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
789-1011 |
4.53e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.87 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIqkfklNWLRQQ 868
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 ---IGLVGQEPVLF-NESIRANIAYG-KPGDVTEEEIiaattAANVHNV-----ISSL----PQgydasvgergvQLSGG 934
Cdd:COG3839 74 drnIAMVFQSYALYpHMTVYENIAFPlKLRKVPKAEI-----DRRVREAaellgLEDLldrkPK-----------QLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 935 QKQRIAIARAILKDPKILLLDEATSALDAE------SE-RKVQDALdrvmvNRTTVVVAHRLS---TIkgADIIAVVKNG 1004
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDG 210
|
....*..
gi 1562645982 1005 VIAEKGS 1011
Cdd:COG3839 211 RIQQVGT 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
791-1011 |
8.44e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 118.32 E-value: 8.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRP---DVQIfrdiclkmPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFklnwlrq 867
Cdd:COG3840 2 LRLDDLTYRYGDFPlrfDLTI--------AAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 qigLVGQEPV--LFNE-------SIRANIAYG-----KPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSG 933
Cdd:COG3840 67 ---PPAERPVsmLFQEnnlfphlTVAQNIGLGlrpglKLTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 934 GQKQRIAIARAILKDPKILLLDEATSALD----AESERKVQDALDRvmVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAE 1008
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAA 210
|
...
gi 1562645982 1009 KGS 1011
Cdd:COG3840 211 DGP 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
791-1011 |
8.60e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 8.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEP--VLFNESIRANIAYG------KPGDVteEEIIA-ATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAI 941
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGlenkkvPPKKM--KDIIDdLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDALD--RVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
95-324 |
9.54e-30 |
|
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: 120.11 E-value: 9.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 95 FVYLAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEMVGKFIQL 174
Cdd:cd18784 42 MGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDT-VKTGDITSRLTSDTTTMSDTVSLNLNIFLRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 175 CSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQ 254
Cdd:cd18784 121 LVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANR 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 255 YNQKLKVAYNTMVQQGLVTG---IGLGIFMLVIFcsyALAVWYGSKMIIKHGYNGGQVINVIFALMTGGMSLG 324
Cdd:cd18784 201 YSEKLKDTYKLKIKEALAYGgyvWSNELTELALT---VSTLYYGGHLVITGQISGGNLISFILYQLELGSCLE 270
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
810-1010 |
1.07e-29 |
|
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: 119.29 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQ----QIGLVGQEPVLF-NESIR 884
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 885 ANIAY-----GKPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAIARAILKDPKILLLDEATS 959
Cdd:cd03294 121 ENVAFglevqGVPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 960 ALDAESERKVQDALDRV--MVNRTTVVVAHRLS-TIKGADIIAVVKNGVIAEKG 1010
Cdd:cd03294 190 ALDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
474-726 |
1.37e-29 |
|
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: 119.66 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 474 IAAAGHGVLFPIF-GLLLSKAIGMFYEPPNELRHDSRKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKV 552
Cdd:cd18780 6 LVSSGTNLALPYFfGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 553 VHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQA 632
Cdd:cd18780 86 IAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 633 KFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALI 712
Cdd:cd18780 164 KYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLV 243
|
250
....*....|....
gi 1562645982 713 FYIGAILVKHGQAT 726
Cdd:cd18780 244 LWYGGRLVIDGELT 257
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
791-1010 |
1.70e-29 |
|
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: 116.97 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwlRQQIG 870
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLF-NESIRANIAYG-KPGDVTEEEIiaattAANVHNVISSLpqGYDASVGERGVQLSGGQKQRIAIARAILKD 948
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlKLRKVPKDEI-----DERVREVAELL--QIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAH-RLSTIKGADIIAVVKNGVIAEKG 1010
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
791-1000 |
6.56e-29 |
|
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: 114.88 E-value: 6.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKST----VIGLIErfydPDSGRVLLDGVEIQKFKLNWlR 866
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDAREDY-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEPVLFNE-SIRANIAY---GKPGDVTEEEIIAATTAANVhnvisslpQGY-DASVGergvQLSGGQKQRIAI 941
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRFwaaLYGLRADREAIDEALEAVGL--------AGLaDLPVR----QLSAGQKRRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTIKGADIIAV 1000
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
469-726 |
8.83e-29 |
|
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: 117.28 E-value: 8.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 469 LLLGAIAAAGHGVLFPIFGLLLSKAIGMFYeppnelRHDSRKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALS 548
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGD------LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 549 FQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQG 628
Cdd:cd18557 76 FSSLLRQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 629 TLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCT 708
Cdd:cd18557 154 KIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLS 233
|
250
....*....|....*...
gi 1562645982 709 NALIFYIGAILVKHGQAT 726
Cdd:cd18557 234 LLLVLWYGGYLVLSGQLT 251
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
792-1007 |
1.03e-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: 114.55 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 792 ELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKST----VIGLIErfydPDSGRVLLDGVEIQKFklnwlRQ 867
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTllkaILGLLK----PTSGSIRVFGKPLEKE-----RK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQepvlfnesiRANIAYGKPGDVteEEIIA-----------ATTAANVHNVISSLpqgydASVGERGV------Q 930
Cdd:cd03235 69 RIGYVPQ---------RRSIDRDFPISV--RDVVLmglyghkglfrRLSKADKAKVDEAL-----ERVGLSELadrqigE 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 931 LSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRV-MVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIA 1007
Cdd:cd03235 133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
791-1011 |
1.76e-28 |
|
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: 117.08 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRP-DVQIFRDICLKMPSGKTVALVGESGSGKST----VIGLIERFYDpDSGRVLLDGVEIQKFK---L 862
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLLPPPGI-TSGEILFDGEDLLKLSekeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 863 NWLR-QQIGLVGQEPVL-FN----------ESIRANiaygkpGDVTEEEIIAAttaanvhnVISSLpqgydASVG----E 926
Cdd:COG0444 81 RKIRgREIQMIFQDPMTsLNpvmtvgdqiaEPLRIH------GGLSKAEARER--------AIELL-----ERVGlpdpE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 927 RGV-----QLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNR-TTVV-VAHRLSTIKG-ADII 998
Cdd:COG0444 142 RRLdryphELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILfITHDLGVVAEiADRV 221
|
250
....*....|...
gi 1562645982 999 AVVKNGVIAEKGS 1011
Cdd:COG0444 222 AVMYAGRIVEEGP 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
791-1010 |
1.25e-27 |
|
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: 111.52 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpdvQIFRDICLKMPSGKTvALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwLRQQIG 870
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLF-NESIRANIAY-----GKPGDVTEEEIIAATTAANVHNVisslpqgYDASVGergvQLSGGQKQRIAIARA 944
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYiawlkGIPSKEVKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 945 ILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKG 1010
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
791-996 |
1.57e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 111.73 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNESIRANIA--YGKPGDVTEEEIIAATTAAnvhnviSSLPQG-YDASVGErgvqLSGGQKQRIAIARAILK 947
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLER------FALPDTiLTKNIAE----LSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 948 DPKILLLDEATSALDAESERKVQDALDRVMVNRTTVV--VAHRLSTIKGAD 996
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHAD 205
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
791-1011 |
3.37e-27 |
|
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: 112.14 E-value: 3.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNW-LRQQI 869
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVlfNESIRA----NIAYGkP---GdVTEEEIIAAttaanVHNVIsslpqgydASVG-----ERGVQ-LSGGQK 936
Cdd:TIGR04520 80 GMVFQNPD--NQFVGAtvedDVAFG-LenlG-VPREEMRKR-----VDEAL--------KLVGmedfrDREPHlLSGGQK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 937 QRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
791-1010 |
5.42e-27 |
|
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: 109.89 E-value: 5.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqifRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwlRQQIG 870
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNE-SIRANIAYGK-PG----DVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAIARA 944
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLsPGlkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 945 ILKDPKILLLDEATSALDAESERKVQDALDRVMVNR--TTVVVAHRLSTIKG-ADIIAVVKNGVIAEKG 1010
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
818-1010 |
7.40e-27 |
|
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: 109.31 E-value: 7.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 818 SGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI----QKFKLNWLRQQIGLVGQEPVLF-NESIRANIAYGKP 892
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 893 GDVTEEEIIAATTAANVHNVisslpqgydASVGERGV-QLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQD 971
Cdd:cd03297 102 RKRNREDRISVDELLDLLGL---------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1562645982 972 ALDRVM--VNRTTVVVAHRLSTI-KGADIIAVVKNGVIAEKG 1010
Cdd:cd03297 173 ELKQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
513-729 |
7.62e-27 |
|
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: 111.48 E-value: 7.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 513 LVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALI 592
Cdd:cd18572 40 LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVSDPLSTNLNVF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 593 VQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKV 672
Cdd:cd18572 118 LRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEERE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 673 MEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQ 729
Cdd:cd18572 198 ARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
808-1027 |
7.68e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 118.73 E-value: 7.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 808 IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANI 887
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 888 aygKP-GDVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILK-DPKILLLDEATSALDAES 965
Cdd:PTZ00243 1405 ---DPfLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPAL 1481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 966 ERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKITDGAYASLV 1027
Cdd:PTZ00243 1482 DRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
469-767 |
7.79e-27 |
|
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: 111.49 E-value: 7.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 469 LLLGAIAAAGHGVLFPIFGLLLSKAIGMFyePPNELRHDSRKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALS 548
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV--IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 549 FQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQG 628
Cdd:cd07346 79 FRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 629 TLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCT 708
Cdd:cd07346 157 RYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 709 NALIFYIGAILVKHGQATFEQVfkVFFaITITAMGVSQATSMAPDSNKAKDSAASIFRI 767
Cdd:cd07346 237 TALVLLYGGYLVLQGSLTIGEL--VAF-LAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
811-1011 |
1.52e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.52 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 811 DICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI--QKFKLNWLRQQIGLVGQEP--VLFNESIRAN 886
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 887 IAYG-KPGDVTEEEIiaattAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDA-- 963
Cdd:PRK13637 105 IAFGpINLGLSEEEI-----ENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkg 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 964 --ESERKVQDALDRvmVNRTTVVVAHRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13637 180 rdEILNKIKELHKE--YNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
804-1004 |
1.65e-26 |
|
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: 108.57 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 804 PDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVL----LDGVEIQKFKLNWLRQQIGLVGQEPVLF 879
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 880 NESIRANIAYGKPgdVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATS 959
Cdd:cd03290 92 NATVEENITFGSP--FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1562645982 960 ALDAE-SERKVQDALDRVMVN--RTTVVVAHRLSTIKGADIIAVVKNG 1004
Cdd:cd03290 170 ALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
802-964 |
1.88e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 107.95 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 802 TRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPD---SGRVLLDGVEIQKfkLNWLRQQIGLVGQEPVL 878
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA--LPAEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 879 F-NESIRANIAYGKPGDVTEEE----IIAATTAANVhnvisslpqgydASVGERGV-QLSGGQKQRIAIARAILKDPKIL 952
Cdd:COG4136 88 FpHLSVGENLAFALPPTIGRAQrrarVEQALEEAGL------------AGFADRDPaTLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|..
gi 1562645982 953 LLDEATSALDAE 964
Cdd:COG4136 156 LLDEPFSKLDAA 167
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
791-1011 |
2.02e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.35 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwlRQQIG 870
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLF-NESIRANIAYG-KPGDVTEEEIIAattaanvhNVISSLPQGYDASVGERGV-QLSGGQKQRIAIARAILK 947
Cdd:PRK09452 90 TVFQSYALFpHMTVFENVAFGlRMQKTPAAEITP--------RVMEALRMVQLEEFAQRKPhQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 948 DPKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAH-RLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQrkLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
791-1011 |
3.07e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.50 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDS---GRVLLDGVEIQKfKLNW-LR 866
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTA-KTVWdIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEP--VLFNESIRANIAYG-KPGDVTEEEIIAAttaanVHNVISSLpqGYDASVGERGVQLSGGQKQRIAIAR 943
Cdd:PRK13640 84 EKVGIVFQNPdnQFVGATVGDDVAFGlENRAVPRPEMIKI-----VRDVLADV--GMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 944 AILKDPKILLLDEATSALDAESERKVQDALDRVMV--NRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
793-1013 |
4.07e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.59 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 793 LDHVSFkyptrpdvQIFRdiclkmpsGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK---LNWLRQQI 869
Cdd:COG4608 34 VDGVSF--------DIRR--------GETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPvlfnesiraniaYG--KPGdVTEEEIIAAttAANVHNVISslPQGYDASVGE--RGV------------QLSG 933
Cdd:COG4608 98 QMVFQDP------------YAslNPR-MTVGDIIAE--PLRIHGLAS--KAERRERVAEllELVglrpehadryphEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 934 GQKQRIAIARAILKDPKILLLDEATSALDAESERKV-------QDALdrvmvNRTTVVVAHRLSTIKG-ADIIAVVKNGV 1005
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVlnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGK 235
|
....*...
gi 1562645982 1006 IAEKGSHD 1013
Cdd:COG4608 236 IVEIAPRD 243
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
791-1016 |
6.46e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.49 E-value: 6.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQ--KFKLNWLRQQ 868
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLFNE-SIRANIAYGkPGDV-----TEEEIIAATTAANVhnvisslpqGYDASVGERGVQLSGGQKQRIAIA 942
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFG-PLRVrgaskEEAEKQARELLAKV---------GLAERAHHYPSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 943 RAILKDPKILLLDEATSALDAESERKV----QDALDRVMvnrTTVVVAHRLSTIK--GADIIaVVKNGVIAEKGSHDFLM 1016
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVlkvmQDLAEEGM---TMVIVTHEIGFAEkvASRLI-FIDKGRIAEDGDPQVLI 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
789-988 |
1.01e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 113.36 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFkypTRPDVQ-IFRDICLKMPSGKTVALVGESGSGKSTVI-----------GLIERfydPDSGRVLLdgve 856
Cdd:COG4178 361 GALALEDLTL---RTPDGRpLLEDLSLSLKPGERLLITGPSGSGKSTLLraiaglwpygsGRIAR---PAGARVLF---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 857 iqkfklnwlrqqiglVGQEPVLFNESIRANIAY-GKPGDVTEEEIIAATTAANVHNVISSLPQGYDasvgeRGVQLSGGQ 935
Cdd:COG4178 431 ---------------LPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEEAD-----WDQVLSLGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 936 KQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHR 988
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
812-1033 |
1.55e-25 |
|
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: 114.66 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 812 ICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiqkfklnwlrqQIGLVGQEPVLFNESIRANIAYGK 891
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 892 PgdVTEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQD 971
Cdd:TIGR00957 724 A--LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 972 AL---DRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMKiTDGAYASLVALHSSS 1033
Cdd:TIGR00957 802 HVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ-RDGAFAEFLRTYAPD 865
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
45-343 |
1.66e-25 |
|
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: 107.52 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 45 VALMIVGTISAVGNGLSKPLMTlvfGNLINTFGcTDPGHIVPMISKVSLKFVYLAIGTGAAALLQVacwmvTGERQAARI 124
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLV---KNLIDALS-AGGSSGGLLALLVALFLLQAVLSALSSYLLGR-----TGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 125 RGKYMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGEmvgKFIQLCS---TFLGGFVIAFVKGWRLTVVLLATIP 201
Cdd:cd18551 72 RRRLWRRLLRLPVSFFD-RRRSGDLVSRVTNDTTLLRELITS---GLPQLVTgvlTVVGAVVLMFLLDWVLTLVTLAVVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 202 AIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFM 281
Cdd:cd18551 148 LAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMG 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 282 LVIFCSYALAVWYGSKMIIKHGYNGGQVINVIFALMTGGMSLGQASPSLNAFASGKAAAYKI 343
Cdd:cd18551 228 LAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
791-1010 |
1.68e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.14 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQIfRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPV-LFNESI-RANIAYG-----KPGDVTEEEIIAATTAANVHNVISSLPQGydasvgergvqLSGGQKQRIAIAR 943
Cdd:PRK13648 87 IVFQNPDnQFVGSIvKYDVAFGlenhaVPYDEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 944 AILKDPKILLLDEATSALDAESERKVQDALDRVMVNR--TTVVVAHRLSTIKGADIIAVVKNGVIAEKG 1010
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
98-326 |
2.29e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 112.89 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 98 LAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCST 177
Cdd:TIGR00958 210 LSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD-ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVM 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 178 FLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQ 257
Cdd:TIGR00958 289 LLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 258 KLK----------VAYNTMVqqgLVTGI-GLGIFMLVIfcsyalavWYGSKMIIKHGYNGGQVINviFALMTggMSLGQA 326
Cdd:TIGR00958 369 ALEetlqlnkrkaLAYAGYL---WTTSVlGMLIQVLVL--------YYGGQLVLTGKVSSGNLVS--FLLYQ--EQLGEA 433
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
800-1015 |
5.65e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 112.95 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 800 YPTRPDVqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVlldgveiqkfklnWLRQQIGLVGQEPVLF 879
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 880 NESIRANIAYgkpgdVTEEEiiaattAANVHNVI---------SSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPK 950
Cdd:PTZ00243 734 NATVRGNILF-----FDEED------AARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRD 802
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 951 ILLLDEATSALDAE-SERKVQDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSH-DFL 1015
Cdd:PTZ00243 803 VYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSaDFM 869
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
791-1007 |
5.70e-25 |
|
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: 102.12 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiqkfklnwlrqqig 870
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 lvgqEPVLFN---ESIRANIAYgkpgdvteeeiiaattaanVHnvisslpqgydasvgergvQLSGGQKQRIAIARAILK 947
Cdd:cd03216 62 ----KEVSFAsprDARRAGIAM-------------------VY-------------------QLSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 948 DPKILLLDEATSALDAESERKVQDALDRVMVNRTTVV-VAHRLSTIKG-ADIIAVVKNGVIA 1007
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
791-1010 |
1.83e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.33 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYP--TRPDVQifrDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQ 868
Cdd:PRK13635 6 IRVEHISFRYPdaATYALK---DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEP--VLFNESIRANIAY-----GKPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAI 941
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFgleniGVPREEMVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDALdRVMVNRTTVVV---AHRLSTIKGADIIAVVKNGVIAEKG 1010
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETV-RQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
67-343 |
3.00e-24 |
|
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: 104.16 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 67 LVFGNLIN---TFGCTDPGHIVPMISKVSLKFVYLAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDTe 143
Cdd:cd18574 17 LLLGDLVNvisRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDT- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 144 TSTGEIIGRMSGDtilIQE--------------AMGEMVGKFIQLcstflggFVIAFvkgwRLTVVLLATIPAIVIAGAV 209
Cdd:cd18574 96 HRTGELVNRLTAD---VQEfkssfkqcvsqglrSVTQTVGCVVSL-------YLISP----KLTLLLLVIVPVVVLVGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 210 MATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAynTMVQQGLvtGIGLGIFM----LVIF 285
Cdd:cd18574 162 YGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKA--AKLNEKL--GLGIGIFQglsnLALN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 286 CSYALAVWYGSKMIIKHGYNGGQVINVIFALMTGGMSLGQASPSLNAFASGKAAAYKI 343
Cdd:cd18574 238 GIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
811-1017 |
3.02e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 110.60 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 811 DICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLdgveiqkfklnwLRQQIGLVGQEPVLFNESIRANIAYG 890
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 891 KPGDVTEEEiiAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQ 970
Cdd:PLN03130 703 SPFDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1562645982 971 DA-LDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMK 1017
Cdd:PLN03130 781 DKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
784-992 |
3.25e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.19 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 784 LSLLIGEIELDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDS-----GRVLLDGVEI- 857
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 858 -QKFKLNWLRQQIGLVGQEPVLFNESIRANIAYG------KP----GDVTEEEIIAATTAANVHNVISslpqgydasvgE 926
Cdd:PRK14258 78 eRRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPkleiDDIVESALKDADLWDEIKHKIH-----------K 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 927 RGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALD--RVMVNRTTVVVAHRLSTI 992
Cdd:PRK14258 147 SALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
811-1025 |
3.77e-24 |
|
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: 105.19 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 811 DICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI----QKFKLNWLRQQIGLVGQEPVLFNE-SIRA 885
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 886 NIAYGKpgdvteEEIIAATTAANVHNVISSLpqGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAES 965
Cdd:TIGR02142 95 NLRYGM------KRARPSERRISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 966 ERKVQDALDRVM--VNRTTVVVAHRLSTI-KGADIIAVVKNGVIAEKGSHDFLMKITDGAYAS 1025
Cdd:TIGR02142 167 KYEILPYLERLHaeFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
791-987 |
4.14e-24 |
|
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: 102.13 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRP-DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLI---ERfydPDSGRVLLDGVEIqkFKLN--- 863
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDL--FALDeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 ---WLRQQIGLVGQepvlfnesiraniaygkpgdvtEEEIIAATTAanVHNVisSLP---QGYD----------ASVG-- 925
Cdd:COG4181 84 rarLRARHVGFVFQ----------------------SFQLLPTLTA--LENV--MLPlelAGRRdarararallERVGlg 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 926 ERG----VQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRvmVNR---TT-VVVAH 987
Cdd:COG4181 138 HRLdhypAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFE--LNRergTTlVLVTH 205
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
45-317 |
4.85e-24 |
|
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: 103.66 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 45 VALMIVGTISAVGN-GLSKPLMTLVFGNlintfgcTDPGhivpMISKVSLKFVYLAIGTGAAALLQVACWMVTGERQAAR 123
Cdd:cd18552 5 ILGMILVAATTAALaWLLKPLLDDIFVE-------KDLE----ALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 124 IRGKYMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAI 203
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFD-RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 204 VIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLV 283
Cdd:cd18552 153 ALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELL 232
|
250 260 270
....*....|....*....|....*....|....
gi 1562645982 284 IFCSYALAVWYGSKMIIKHGYNGGQVINVIFALM 317
Cdd:cd18552 233 GAIAIALVLWYGGYQVISGELTPGEFISFITALL 266
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
791-1013 |
5.34e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.78 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSfKYPTRpdVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKfkLNWLRQQIG 870
Cdd:PRK10851 3 IEIANIK-KSFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNE-SIRANIAYG--------KPgdvtEEEIIAATTAANVHNV-ISSLPQGYDAsvgergvQLSGGQKQRIA 940
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAFGltvlprreRP----NAAAIKAKVTQLLEMVqLAHLADRYPA-------QLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAH-RLSTIKGADIIAVVKNGVIAEKGSHD 1013
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHeeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
791-1010 |
5.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.89 E-value: 5.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYptRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEP--VLFNESIRANIAYGK-----PGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAIAR 943
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 944 AILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLS-TIKGADIIAVVKNG-VIAEKG 1010
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGrVLAEGD 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
766-1011 |
6.24e-24 |
|
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: 107.08 E-value: 6.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 766 RILDSKPKIDSSSDEGIALSLLigeiELDHVSFKYPT-----RPDVQIFR---DICLKMPSGKTVALVGESGSGKST--- 834
Cdd:COG4172 255 KLLAAEPRGDPRPVPPDAPPLL----EARDLKVWFPIkrglfRRTVGHVKavdGVSLTLRRGETLGLVGESGSGKSTlgl 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 835 -VIGLIerfydPDSGRVLLDGVEIQKFK---LNWLRQQIGLVGQEPV--LfneSIRANIaygkpgdvteEEIIA------ 902
Cdd:COG4172 331 aLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPFgsL---SPRMTV----------GQIIAeglrvh 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 903 --ATTAANVHN-VISSLPQ-GYDASVGERGV-QLSGGQKQRIAIARAILKDPKILLLDEATSALDaeseRKVQ----DAL 973
Cdd:COG4172 393 gpGLSAAERRArVAEALEEvGLDPAARHRYPhEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaqilDLL 468
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1562645982 974 DRVMVNR--TTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:COG4172 469 RDLQREHglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
805-1013 |
1.10e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 805 DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERF---YDPD---SGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVL 878
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 879 FNE-SIRANIAYG-KPGDVTEEEIIAATTAANVHNVisSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDE 956
Cdd:PRK14246 102 FPHlSIYDNIAYPlKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 957 ATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTI-KGADIIAVVKNGVIAEKGSHD 1013
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSN 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
791-1004 |
1.31e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.73 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEP--VLFNESIRANIAYG-KPGDVTEEEIIAattaaNVHNVISSLpqGYDASVGERGVQLSGGQKQRIAIARAILK 947
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGlENKGIPHEEMKE-----RVNEALELV--GMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 948 DPKILLLDEATSALDAESE----RKVQDALDRvmVNRTTVVVAHRLSTIKGADIIAVVKNG 1004
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
792-986 |
1.43e-23 |
|
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: 99.64 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 792 ELDHVSFKYPTRPDvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVeiqKFKLNWLRQQIGL 871
Cdd:cd03226 1 RIENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 872 VGQEP--VLFNESIRANIAYG-KPGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAIARAILKD 948
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGlKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSG 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA 986
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVI 182
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
791-976 |
1.48e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.09 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYP-TRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwlRqqi 869
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLFN-ESIRANIAYG---KPGDVTEEEIIAATTAANVhnvisslpqGYDAsVGERGV-QLSGGQKQRIAIARA 944
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGlrlRGVPKAERRARAEELLALV---------GLAD-FARRRIwQLSGGMRQRVGIARA 148
|
170 180 190
....*....|....*....|....*....|..
gi 1562645982 945 ILKDPKILLLDEATSALDAESERKVQDALDRV 976
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
790-1011 |
1.83e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 790 EIELDHVSFKY-PTRPDVQI-FRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK----LN 863
Cdd:PRK13634 2 DITFQKVEHRYqYKTPFERRaLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkkLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 WLRQQIGLVGQ--EPVLFNESIRANIAYGkPGD--VTEEEiiAATTAANVHNVIsslpqGYDASVGERG-VQLSGGQKQR 938
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFG-PMNfgVSEED--AKQKAREMIELV-----GLPEELLARSpFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 939 IAIARAILKDPKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAHRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGT 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
791-1015 |
2.37e-23 |
|
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: 99.50 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQIfRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKfKLNWLRQQIG 870
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNE-SIRANIAY-----GKPgdvtEEEIIaattaANVHNVIS--SLPQGYDASVGergvQLSGGQKQRIAIA 942
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLP----KSEIK-----EEVELLLRvlGLTDKANKRAR----TLSGGMKRKLSLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 943 RAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGSHDFL 1015
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
791-1011 |
2.99e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYP--TRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI-QKFK---LNW 864
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 865 LRQQIGLVGQ--EPVLFNESIRANIAYG-KPGDVTEEEIiaattAANVHNVISSLpqGYDASVGERG-VQLSGGQKQRIA 940
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpKNFKMNLDEV-----KNYAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALDRVMV--NRTTVVVAHRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTS 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
816-989 |
3.08e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.24 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 816 MPSGKTvALVGESGSGKSTVIGLIERFYD--PD---SGRVLLDGVEIQKFKLNW--LRQQIGLVGQEPVLFNESIRANIA 888
Cdd:PRK14239 29 YPNEIT-ALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPMSIYENVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 889 YG------KPGDVTEEEIIAATTAANVHNVISSlpQGYDASVGergvqLSGGQKQRIAIARAILKDPKILLLDEATSALD 962
Cdd:PRK14239 108 YGlrlkgiKDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
170 180
....*....|....*....|....*..
gi 1562645982 963 AESERKVQDALDRVMVNRTTVVVAHRL 989
Cdd:PRK14239 181 PISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
823-976 |
4.10e-23 |
|
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: 102.10 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 823 ALVGESGSGKSTVIGLI---ERfydPDSGRVLLDGVEIQKFKLN-WL---RQQIGLVGQEPVLFNE-SIRANIAYG-KPG 893
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVLQDSARGiFLpphRRRIGYVFQEARLFPHlSVRGNLLYGrKRA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 894 DvteeeiiAATTAANVHNVISSLpqgydasvG-----ERGV-QLSGGQKQRIAIARAILKDPKILLLDEATSALDAESER 967
Cdd:COG4148 106 P-------RAERRISFDEVVELL--------GighllDRRPaTLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
....*....
gi 1562645982 968 KVQDALDRV 976
Cdd:COG4148 171 EILPYLERL 179
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
789-1011 |
4.43e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.47 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYPTRP--DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI----QKFK- 861
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlKKIKe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 862 LNWLRQQIGLVGQEP--VLFNESIRANIAYGkPGDVTEEEIIAATTAANVHNVISsLPQGYdasVGERGVQLSGGQKQRI 939
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 940 AIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVN--RTTVVVAHRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
810-989 |
4.90e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.86 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKSTVI-------GLIERF-------------YDPDsgrvlLDGVEIqkfklnwlRQQI 869
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFrvegkvtfhgknlYAPD-----VDPVEV--------RRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLFNESIRANIAYGK-----PGDVTEEEIIAATTAANVHNVISSLPQGydasvgerGVQLSGGQKQRIAIARA 944
Cdd:PRK14243 94 GMVFQKPNPFPKSIYDNIAYGAringyKGDMDELVERSLRQAALWDEVKDKLKQS--------GLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1562645982 945 ILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRL 989
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
807-1010 |
7.06e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.05 E-value: 7.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 807 QIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI--------QKFKLNWLRQQIGLVGQEPVL 878
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 879 F-NESIRANIAYGkPGDVTEEEIIAATTAAnvhnvisslpQGYDASVGERGVQ------LSGGQKQRIAIARAILKDPKI 951
Cdd:PRK11264 97 FpHRTVLENIIEG-PVIVKGEPKEEATARA----------RELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 952 LLLDEATSALDAESERKVQDALdRVMV--NRTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKG 1010
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTI-RQLAqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
805-1010 |
9.50e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.83 E-value: 9.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 805 DVQIFRDICLKMPSGKTVALVGESGSGKSTVIG----LIERFYDPD-SGRVLLDGVEIQKFKLNWLRQQIGLVGQEP-VL 878
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 879 FNESIRANIAYG-------KPGDVTEEEIIAATTAANVHNVISSLpqgYDASVGergvQLSGGQKQRIAIARAILKDPKI 951
Cdd:PRK14247 95 PNLSIFENVALGlklnrlvKSKKELQERVRWALEKAQLWDEVKDR---LDAPAG----KLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 952 LLLDEATSALDAESERKVQDALDRVMVNRTTVVVAH------RLStikgaDIIAVVKNGVIAEKG 1010
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
791-1011 |
2.05e-22 |
|
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: 97.46 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSG---RVL---LDGVEIQKfklnw 864
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 865 LRQQIGLVG---QEPVLFNESIRANI---AYGKPG---DVTEEEIIAAttaanvHNVISSLpqGYDASVGERGVQLSGGQ 935
Cdd:COG1119 76 LRKRIGLVSpalQLRFPRDETVLDVVlsgFFDSIGlyrEPTDEQRERA------RELLELL--GLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 936 KQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVN--RTTVVVAHRLStikgaDIIAVVKNGVIAEKGS 1011
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVE-----EIPPGITHVLLLKDGR 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
810-1016 |
5.39e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.72 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQ----QIGLVGQEPVLF-NESIR 884
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 885 ANIAYGK-----PGDVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAIARAILKDPKILLLDEATS 959
Cdd:PRK10070 125 DNTAFGMelagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 960 ALDAESERKVQDALDRVMV--NRTTVVVAHRL-STIKGADIIAVVKNGVIAEKGSHDFLM 1016
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
789-992 |
9.29e-22 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 96.46 E-value: 9.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYpTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDsGRVLLDGVEIQKFKLNWLRQQ 868
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLFNESIRANI-AYGKPGDvteEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILK 947
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1562645982 948 DPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLSTI 992
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAM 200
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
791-1010 |
9.75e-22 |
|
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: 94.74 E-value: 9.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKY-PTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwLRQQI 869
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLFNE-SIRANIAY-----GKPGDvteeeiiAATtaANVHNVISSLpqGYDASVGERGVQLSGGQKQRIAIAR 943
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfaglyGLKGD-------ELT--ARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 944 AILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTIKG-ADIIAVVKNGVIAEKG 1010
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
811-1011 |
1.33e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 811 DICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLnwlrQQ--IGLVGQEPVLF-NESIRANI 887
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI----QQrdICMVFQSYALFpHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 888 AYG-KPGDVTEEEIiaattaanVHNVISSLPQGYDASVGERGV-QLSGGQKQRIAIARAILKDPKILLLDEATSALDAES 965
Cdd:PRK11432 100 GYGlKMLGVPKEER--------KQRVKEALELVDLAGFEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1562645982 966 ERKVQDALDRVM--VNRTTVVVAHRLS-TIKGADIIAVVKNGVIAEKGS 1011
Cdd:PRK11432 172 RRSMREKIRELQqqFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGS 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
791-1016 |
1.55e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.65 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKY---PTRPDVQIFRdiclkmpsGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwlRQ 867
Cdd:PRK10771 2 LKLTDITWLYhhlPMRFDLTVER--------GERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNE-SIRANIAYG-KPG---DVTEEEIIAATtAANV--HNVISSLPQgydasvgergvQLSGGQKQRIA 940
Cdd:PRK10771 72 PVSMLFQENNLFSHlTVAQNIGLGlNPGlklNAAQREKLHAI-ARQMgiEDLLARLPG-----------QLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNR--TTVVVAHRLSTikgADIIA----VVKNGVIAEKGSHDF 1014
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLED---AARIAprslVVADGRIAWDGPTDE 216
|
..
gi 1562645982 1015 LM 1016
Cdd:PRK10771 217 LL 218
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
98-286 |
2.23e-21 |
|
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: 95.48 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 98 LAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGE----MVGKFIQ 173
Cdd:cd18590 45 FSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE-KTKTGDLTSRLSTDTTLMSRSVALnanvLLRSLVK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 174 LCSTFlgGFVIAFvkGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIE 253
Cdd:cd18590 124 TLGML--GFMLSL--SWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEAC 199
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1562645982 254 QYNQKLKVAYNTMVQQGLVTGI--------GLGIFMLVIFC 286
Cdd:cd18590 200 RYSEALERTYNLKDRRDTVRAVyllvrrvlQLGVQVLMLYC 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
811-987 |
2.39e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.21 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 811 DICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLnwLRQQIGLVGQEPVLF-NESIRANIAY 889
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFpHMTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 890 GkpgdVTEEEIIAATTAANVHNVISSLPQGYDAsvGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKV 969
Cdd:PRK11607 115 G----LKQDKLPKAEIASRVNEMLGLVHMQEFA--KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
170 180
....*....|....*....|..
gi 1562645982 970 Q----DALDRVMVnrTTVVVAH 987
Cdd:PRK11607 189 QlevvDILERVGV--TCVMVTH 208
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
485-741 |
2.51e-21 |
|
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: 95.24 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 485 IFGLLLSKAIGMFYepPNELR-------HDSRKWALVYVGLGCAGLLVVP-----VQNFFFGVAGGKLVERIRALSFQKV 552
Cdd:cd18576 2 LILLLLSSAIGLVF--PLLAGqlidaalGGGDTASLNQIALLLLGLFLLQavfsfFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 553 VHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQA 632
Cdd:cd18576 80 QRLPLSFFHE--RRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 633 KFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALI 712
Cdd:cd18576 158 RRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAV 237
|
250 260 270
....*....|....*....|....*....|
gi 1562645982 713 FYIGAILVKHGQATFEQVFK-VFFAITITA 741
Cdd:cd18576 238 LWYGGRLVLAGELTAGDLVAfLLYTLFIAG 267
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
791-1017 |
2.53e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.82 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIG--LIERFYDPDSGRVLldgveiqkfklnwlRQQ 868
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISamLGELSHAETSSVVI--------------RGS 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLFNESIRANIAYGKpgDVTEEEIIAATTAANVHNVISSLPqGYDAS-VGERGVQLSGGQKQRIAIARAILK 947
Cdd:PLN03232 681 VAYVPQVSWIFNATVRENILFGS--DFESERYWRAIDVTALQHDLDLLP-GRDLTeIGERGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 948 DPKILLLDEATSALDAESERKVQDA-LDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGVIAEKGSHDFLMK 1017
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
791-1011 |
2.99e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.16 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEP--VLFNESIRANIAYGKPGD-VTEEEIIA----ATTAANVHNVISSLPqgydasvgergVQLSGGQKQRIAIAR 943
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQgIPREEMIKrvdeALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 944 AILKDPKILLLDEATSALD----AESERKVQDALDRVMVnrTTVVVAHRLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAA 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
791-976 |
3.16e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.38 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKfklnwLRQQIG 870
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-----PGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQ-EPVLFNESIRANIAYGKpgdvteeEIIAATTAANVHNVISSLPQGYDASVGERGV-QLSGGQKQRIAIARAILKD 948
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGL-------QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAAN 146
|
170 180
....*....|....*....|....*...
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRV 976
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
808-1005 |
4.83e-21 |
|
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: 99.98 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 808 IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiqkfklnwlrqQIGLVGQEPVLFNESIRANI 887
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 888 AYGKPGDvtEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESER 967
Cdd:TIGR01271 508 IFGLSYD--EYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190
....*....|....*....|....*....|....*....
gi 1562645982 968 KV-QDALDRVMVNRTTVVVAHRLSTIKGADIIAVVKNGV 1005
Cdd:TIGR01271 586 EIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
791-1010 |
4.92e-21 |
|
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: 92.28 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQifrDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWlrQQIG 870
Cdd:cd03268 1 LKTNDLTKTYGKKRVLD---DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNE-SIRANIAYGKPGDVTEEEIIaattaanvHNVISSLpqGYDASVGERGVQLSGGQKQRIAIARAILKDP 949
Cdd:cd03268 76 ALIEAPGFYPNlTARENLRLLARLLGIRKKRI--------DEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 950 KILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTI-KGADIIAVVKNGVIAEKG 1010
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
791-1004 |
5.57e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTrpdVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQkFK--LNWLRQQ 868
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRspRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLFNE-SIRANIAYG----KPGDVTEEEIIAATTAanvhnVISSLpqGYDASVGERGVQLSGGQKQRIAIAR 943
Cdd:COG1129 81 IAIIHQELNLVPNlSVAENIFLGreprRGGLIDWRAMRRRARE-----LLARL--GLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 944 AILKDPKILLLDEATSAL-DAESERkvqdaLDRVMvnR------TTVV-VAHRLSTIKG-ADIIAVVKNG 1004
Cdd:COG1129 154 ALSRDARVLILDEPTASLtEREVER-----LFRII--RrlkaqgVAIIyISHRLDEVFEiADRVTVLRDG 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
791-1011 |
1.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.27 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYP--TRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLN----W 864
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 865 LRQQIGLVGQ--EPVLFNESIRANIAYGkPGD--VTEEEiiAATTAANVHNVIsslpqGYDASVGERG-VQLSGGQKQRI 939
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG-PQNfgVSQEE--AEALAREKLALV-----GISESLFEKNpFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 940 AIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVV-VAHRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
801-1010 |
1.11e-20 |
|
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: 91.07 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 801 PTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLI--ERFYDPDSGRVLLDGveiQKFKLNWLRQQIGLVGQEPVL 878
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 879 F-NESIRANIAYgkpgdvteeeiiaattAANVhnvisslpqgydasvgeRGvqLSGGQKQRIAIARAILKDPKILLLDEA 957
Cdd:cd03213 94 HpTLTVRETLMF----------------AAKL-----------------RG--LSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 958 TSALDAESERKVQDALDR-VMVNRTTVVVAHRLST--IKGADIIAVVKNGVIAEKG 1010
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
818-1011 |
1.38e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.26 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 818 SGKTVALVGESGSGKSTV---IGLIERfydPDSGRVLLDGVEI-----QKFKLnwLRQQIGLVGQEPvlfnesiraniaY 889
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYYQGQDLlkadpEAQKL--LRQKIQIVFQNP------------Y 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 890 G------KPGDVTEEEII------AATTAANVHNVIsslpqgydASVGERGVQ-------LSGGQKQRIAIARAILKDPK 950
Cdd:PRK11308 103 GslnprkKVGQILEEPLLintslsAAERREKALAMM--------AKVGLRPEHydryphmFSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 951 ILLLDEATSALDAESERKVqdaLDRVM-----VNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:PRK11308 175 VVVADEPVSALDVSVQAQV---LNLMMdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
95-343 |
1.56e-20 |
|
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: 93.26 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 95 FVYLAIGTGAAALLQVACWMV-------TGERQAARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEM 167
Cdd:cd18542 38 LWLLALLILGVALLRGVFRYLqgylaekASQKVAYDLRNDLYDHLQRLSFSFHDK-ARTGDLMSRCTSDVDTIRRFLAFG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 168 VGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTG 247
Cdd:cd18542 117 LVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 248 EKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYALAVWYGSKMIIKHGYNGGQVinVIFALMTGGMS----- 322
Cdd:cd18542 197 EDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGEL--VAFISYLWMLIwpvrq 274
|
250 260
....*....|....*....|.
gi 1562645982 323 LGQAspsLNAFASGKAAAYKI 343
Cdd:cd18542 275 LGRL---INDMSRASASAERI 292
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
808-1004 |
1.62e-20 |
|
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: 93.00 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 808 IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiqkfklnwlrqQIGLVGQEPVLFNESIRANI 887
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 888 AYGKPGDvtEEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESER 967
Cdd:cd03291 119 IFGVSYD--EYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190
....*....|....*....|....*....|....*...
gi 1562645982 968 KVQDA-LDRVMVNRTTVVVAHRLSTIKGADIIAVVKNG 1004
Cdd:cd03291 197 EIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
793-965 |
2.06e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 793 LDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiqkfklnwlRQQIGLV 872
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 873 GQEPVLF-NESIRANI----------------AYGKPGDvTEEEIIAATTA-------------ANVHNVISSL---PQG 919
Cdd:COG0488 67 PQEPPLDdDLTVLDTVldgdaelraleaeleeLEAKLAE-PDEDLERLAELqeefealggweaeARAEEILSGLgfpEED 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1562645982 920 YDASVGErgvqLSGGQKQRIAIARAILKDPKILLLDEATSALDAES 965
Cdd:COG0488 146 LDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
795-1011 |
2.80e-20 |
|
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: 95.91 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 795 HVSFKYPTRpDVQIFRDICLKMPSGKTVALVGESGSGKS----TVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQ--- 867
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 -QIGLVGQEPV-----LFN------ESIRanIAYGKPGDVTEEEIIAATTAANVHNV---ISSLPQgydasvgergvQLS 932
Cdd:COG4172 92 nRIAMIFQEPMtslnpLHTigkqiaEVLR--LHRGLSGAAARARALELLERVGIPDPerrLDAYPH-----------QLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 933 GGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRvMVNRTTV----------VVAHRlstikgADIIAVVK 1002
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKD-LQRELGMalllithdlgVVRRF------ADRVAVMR 231
|
....*....
gi 1562645982 1003 NGVIAEKGS 1011
Cdd:COG4172 232 QGEIVEQGP 240
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
791-989 |
3.80e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.30 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVS--FKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKlNWLR-Q 867
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVL---FNESIRAN--IAYGK-------PGdVTEEEIiaattaANVHNVISSLPQGY----DASVGergvQL 931
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENlaLAYRRgkrrglrRG-LTKKRR------ELFRELLATLGLGLenrlDTKVG----LL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 932 SGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVmVNR---TTVVVAHRL 989
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNM 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
791-1013 |
3.90e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiQKFKLN------- 863
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAG---NHFDFSktpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 --WLRQQIGLVGQE----PVLfneSIRANI--AYGKPGDVTEEEiiaATTAANVHNVISSLPQGYDASvgerGVQLSGGQ 935
Cdd:PRK11124 77 irELRRNVGMVFQQynlwPHL---TVQQNLieAPCRVLGLSKDQ---ALARAEKLLERLRLKPYADRF----PLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 936 KQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVM-VNRTTVVVAHRLSTI-KGADIIAVVKNGVIAEKGSHD 1013
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAeTGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDAS 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-344 |
4.49e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 96.64 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 16 NNNGSQEKADK-KKQKVAFYKLFSFADRLDVALMIVGTISAVGNGLSKPLMTLVFGNLINTFGCTDpgHIVPMIskvsLK 94
Cdd:PTZ00265 29 NKKGTFELYKKiKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIMKNMNLGE--NVNDII----FS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 95 FVYLAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDTETSTgeiigRMSGDTILIQEAMGEMVG-KFIQ 173
Cdd:PTZ00265 103 LVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGS-----KLTSDLDFYLEQVNAGIGtKFIT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 174 L---CSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGaVMATIMSRMSSRGQSAYAE-AGSIVEQTVGSIRTVASFTGEK 249
Cdd:PTZ00265 178 IftyASAFLGLYIWSLFKNARLTLCITCVFPLIYICG-VICNKKVKINKKTSLLYNNnTMSIIEEALVGIRTVVSYCGEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 250 QAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYALAVWYGSKMII--------KHGYNGGQVINVIFALMTGGM 321
Cdd:PTZ00265 257 TILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSVISILLGVLISMF 336
|
330 340
....*....|....*....|....*.
gi 1562645982 322 SLGQASPSLNAFASGKAAA---YKII 344
Cdd:PTZ00265 337 MLTIILPNITEYMKSLEATnslYEII 362
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
790-1013 |
5.88e-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: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 790 EIELDHVSFKYPTrpdVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiQKFKLN------ 863
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG---HQFDFSqkpsek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 ---WLRQQIGLVGQEPVLFnesiraniaygkPGDVTEEEIIAA-------TTAANVHNVISSLPQGYDASVGER-GVQLS 932
Cdd:COG4161 76 airLLRQKVGMVFQQYNLW------------PHLTVMENLIEApckvlglSKEQAREKAMKLLARLRLTDKADRfPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 933 GGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRV-MVNRTTVVVAHRLSTI-KGADIIAVVKNGVIAEKG 1010
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELsQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQG 223
|
...
gi 1562645982 1011 SHD 1013
Cdd:COG4161 224 DAS 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
791-1011 |
7.73e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.14 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVlFNE--SIRANIAYGK-P---GDVTEE--EIIA-ATTAANvhnvISSLPQGY-DasvgergvQLSGGQKQRIA 940
Cdd:COG4604 79 ILRQENH-INSrlTVRELVAFGRfPyskGRLTAEdrEIIDeAIAYLD----LEDLADRYlD--------ELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALDRvMV---NRTTVVVAHRL---STIkgADIIAVVKNGVIAEKGS 1011
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRR-LAdelGKTVVIVLHDInfaSCY--ADHIVAMKDGRVVAQGT 219
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
469-743 |
1.17e-19 |
|
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: 90.56 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 469 LLLGAIAAAGHGVLFPIFGLLLSKAIgmfyeppNELRHDSRKWALVYVGLGCAGLLVVP-----VQNFFFGVAGGKLVER 543
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLL-------DDIFVEKDLEALLLVPLAIIGLFLLRglasyLQTYLMAYVGQRVVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 544 IRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPL 623
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 624 ILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFF 703
Cdd:cd18552 152 AALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMEL 231
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1562645982 704 LMFCTNALIFYIGAILVKHGQATFEQvfkvFFAItITAMG 743
Cdd:cd18552 232 LGAIAIALVLWYGGYQVISGELTPGE----FISF-ITALL 266
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
810-1008 |
1.52e-19 |
|
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: 89.03 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWL-RQQIGLVGQEPVLFNE-SIRANI 887
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 888 ----------AYGKPGDVTEEEIIAATTAANVHNVisSLPQGYDASVGErgvqLSGGQKQRIAIARAILKDPKILLLDEA 957
Cdd:cd03219 97 mvaaqartgsGLLLARARREEREARERAEELLERV--GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 958 TSALDAESERKVQDALDRVMV-NRTTVVVAHRLSTIKG-ADIIAVVKNG-VIAE 1008
Cdd:cd03219 171 AAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGrVIAE 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
791-1017 |
2.36e-19 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 89.09 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPT------RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK--- 861
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 862 LNWLRQQIGLVGQE-PVLFN--ESIRANIayGKP------GDVTEEEiiaATTAANVHNVisslpqGYDASVGER-GVQL 931
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNprMTVRQII--GEPlrhltsLDESEQK---ARIAELLDMV------GLRSEDADKlPRQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 932 SGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTT--VVVAHRLSTI-KGADIIAVVKNGVIAE 1008
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
250
....*....|.
gi 1562645982 1009 --KGSHDFLMK 1017
Cdd:TIGR02769 232 ecDVAQLLSFK 242
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
791-1010 |
2.54e-19 |
|
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: 87.97 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPT-------------------RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVL 851
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 852 LDGveiqkfKLNWLrqqIG--------LVGQEPVLFNESIraniaYGKPGDVT---EEEIIAattaanvhnvISSLPQGY 920
Cdd:cd03220 81 VRG------RVSSL---LGlgggfnpeLTGRENIYLNGRL-----LGLSRKEIdekIDEIIE----------FSELGDFI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 921 DASVGErgvqLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDAL-DRVMVNRTTVVVAHRLSTIKG-ADII 998
Cdd:cd03220 137 DLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRA 212
|
250
....*....|..
gi 1562645982 999 AVVKNGVIAEKG 1010
Cdd:cd03220 213 LVLEKGKIRFDG 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
810-1010 |
3.15e-19 |
|
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: 87.91 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQK--------FK----LNWL--RQQIGLVgqe 875
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrmvvFQnyslLPWLtvRENIALA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 876 pvlfNESIRANIAYGKPGDVTEEEI--IAATTAANvhnvisslpqgydasvgERGVQLSGGQKQRIAIARAILKDPKILL 953
Cdd:TIGR01184 79 ----VDRVLPDLSKSERRAIVEEHIalVGLTEAAD-----------------KRPGQLSGGMKQRVAIARALSIRPKVLL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 954 LDEATSALDAESERKVQDALDRVMV-NRTTVV-VAHRL-STIKGADIIAVVKNGVIAEKG 1010
Cdd:TIGR01184 138 LDEPFGALDALTRGNLQEELMQIWEeHRVTVLmVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
791-1016 |
5.70e-19 |
|
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: 86.72 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQK---FKLNwlRQ 867
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppHERA--RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNE-SIRANI---AYGKPGDVTEEEIiaattaANVHNVISSLPQGYDASVGergvQLSGGQKQRIAIAR 943
Cdd:cd03224 76 GIGYVPEGRRIFPElTVEENLllgAYARRRAKRKARL------ERVYELFPRLKERRKQLAG----TLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 944 AILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVV----AHRLSTIkgADIIAVVKNGVIAEKGSHDFLM 1016
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELL 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
794-962 |
6.84e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.82 E-value: 6.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 794 DHVSFKYPT------RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK---LNW 864
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 865 LRQQIGLVGQEPV-LFN--ESIRANIAygkpgdvteEEIIAATT---AANVHNVISSLPQ-GYDASVGER-GVQLSGGQK 936
Cdd:PRK10419 87 FRRDIQMVFQDSIsAVNprKTVREIIR---------EPLRHLLSldkAERLARASEMLRAvDLDDSVLDKrPPQLSGGQL 157
|
170 180
....*....|....*....|....*.
gi 1562645982 937 QRIAIARAILKDPKILLLDEATSALD 962
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
791-1011 |
7.42e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.74 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKF-KLNWLRQQI 869
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEP--VLFNESIRANIAYGkPGDVTEEEIiaattaanvhnvisSLPQGYDASVGERGVQ---------LSGGQKQR 938
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFG-PENLCLPPI--------------EIRKRVDRALAEIGLEkyrhrspktLSGGQGQC 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 939 IAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVN-RTTVVVAHRLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
531-744 |
7.49e-19 |
|
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: 88.31 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 531 FFFGVAGGKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTAN 610
Cdd:cd18575 58 YLVSWLGERVVADLRKAVFAHLLRLSPSFFET--TRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 611 WKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRL 690
Cdd:cd18575 136 PKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRR 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 691 GVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQVFK-VFFAItITAMGV 744
Cdd:cd18575 216 IRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQfVFYAV-LAAGSV 269
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
789-989 |
7.63e-19 |
|
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: 92.67 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYpTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDsGRVLLDGVEIQKFKLNWLRQQ 868
Cdd:TIGR01271 1216 GQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLFNESIRANI-AYGKPGDvteEEIIAATTAANVHNVISSLPQGYDASVGERGVQLSGGQKQRIAIARAILK 947
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLdPYEQWSD---EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILS 1370
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1562645982 948 DPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRL 989
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
793-1006 |
7.85e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.43 E-value: 7.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 793 LDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRvLLDGveiqKFKLNWLRQQIGLV 872
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAG----TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 873 GQEPVLFN-ESIRANIAYGKPGDVTEE--EIIAATTAANvhnvisslpqgydaSVGERGVQLSGGQKQRIAIARAILKDP 949
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGLKGQWRDAalQALAAVGLAD--------------RANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 950 KILLLDEATSALDAESERKVQDALDRVMVNR--TTVVVAHRLS-TIKGADIIAVVKNGVI 1006
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
809-984 |
9.70e-19 |
|
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: 86.33 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 809 FRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVL-------LDGVEIQKFKLNWLRQQ-IGLVGQepvlFN 880
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwVDLAQASPREILALRRRtIGYVSQ----FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 881 ESI-RaniaygkpgdVTEEEIIAAttaanvhnviSSLPQGYDASVG-ERGVQL------------------SGGQKQRIA 940
Cdd:COG4778 103 RVIpR----------VSALDVVAE----------PLLERGVDREEArARARELlarlnlperlwdlppatfSGGEQQRVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVV 984
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
791-962 |
9.99e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.44 E-value: 9.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQ--KFKLNWLRQQ 868
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEP--VLFNESIRANIAYGK-----PGDVTEEEIIAATTAANVhnvisslpQGYDASVGErgvQLSGGQKQRIAI 941
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPlnlglSKEEVEKRVKEALKAVGM--------EGFENKPPH---HLSGGQKKRVAI 148
|
170 180
....*....|....*....|.
gi 1562645982 942 ARAILKDPKILLLDEATSALD 962
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLD 169
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
790-1016 |
1.05e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 790 EIELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQI 869
Cdd:PRK11231 2 TLRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPvLFNE--SIRANIAYGKP------GDVTEEEiiaattaanVHNVISSLPQGYDASVGERGV-QLSGGQKQRIA 940
Cdd:PRK11231 79 ALLPQHH-LTPEgiTVRELVAYGRSpwlslwGRLSAED---------NARVNQAMEQTRINHLADRRLtDLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALDRVMVN-RTTVVVAHRLS-TIKGADIIAVVKNGVIAEKGSHDFLM 1016
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
791-1011 |
1.80e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYptRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEP--VLFNESIRANIAYGKPGDVTEEEIIAATTAANVHNVisslpqGYDASVGERGVQLSGGQKQRIAIARAILKD 948
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRVMVN--RTTVVVAHRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGT 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
791-1011 |
2.41e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 85.11 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwLRQQIG 870
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNE-SIRANIA-----YGKPGDVTEEEIIAATTAANVHNVISSLPQGYdasvgergvqlSGGQKQRIAIARA 944
Cdd:cd03265 77 IVFQDLSVDDElTGWENLYiharlYGVPGAERRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 945 ILKDPKILLLDEATSALDAESERKVQDALdRVMVNRTTVVV---------AHRLstikgADIIAVVKNGVIAEKGS 1011
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYI-EKLKEEFGMTIlltthymeeAEQL-----CDRVAIIDHGRIIAEGT 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
802-1010 |
3.34e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 802 TRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVL-FN 880
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 881 ESIRANIAYGKPGDVTEeeiIAATTAANVHNVISSLPQGYDASVGERGV-QLSGGQKQRIAIARAILKDPKILLLDEATS 959
Cdd:PRK09536 92 FDVRQVVEMGRTPHRSR---FDTWTETDRAAVERAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 960 ALDAESE-RKVQDALDRVMVNRTTVVVAHRLS-TIKGADIIAVVKNGVIAEKG 1010
Cdd:PRK09536 169 SLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
513-679 |
3.50e-18 |
|
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: 86.41 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 513 LVYVGLGCAGLLVV-PVQNF----FFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGD 587
Cdd:cd18573 40 LKTFALALLGVFVVgAAANFgrvyLLRIAGERIVARLRKRLFKSILRQDAAFFD--KNKTGELVSRLSSDTSVVGKSLTQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 588 ALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFC 667
Cdd:cd18573 118 NLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFA 197
|
170
....*....|..
gi 1562645982 668 SEKKVMEAYEKK 679
Cdd:cd18573 198 AERKEVERYAKK 209
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
805-1027 |
3.78e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.12 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 805 DVQIFRDICLKMPSGKTVALVGESGSGKST---VIGLIERfYDPDSGRVLLDGVEIqkfkLNWL-----RQQIGLVGQEP 876
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDI----LELSpderaRAGIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 877 VLF----NES-IRAniAYGKpgdVTEEEIIAATTAANVHNVISSLpqGYDASVGERGVQ--LSGGQKQRIAIARAILKDP 949
Cdd:COG0396 87 VEIpgvsVSNfLRT--ALNA---RRGEELSAREFLKLLKEKMKEL--GLDEDFLDRYVNegFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 950 KILLLDEATSALDAESERKVQDALDRVMV-NRTTVVVAH--R-LSTIKgADIIAVVKNGVIAEKGSHDFLMKITDGAYAS 1025
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRiLDYIK-PDFVHVLVDGRIVKSGGKELALELEEEGYDW 238
|
..
gi 1562645982 1026 LV 1027
Cdd:COG0396 239 LK 240
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
807-1010 |
5.05e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.89 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 807 QIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPD-----SGRVLLDGVEIQKFKLNWL--RQQIGLVGQEPVLF 879
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 880 -NESIRANIAYG-------KPGDVTEEEIIAATTAANVHNVISSLPQGYDAsvgergvQLSGGQKQRIAIARAILKDPKI 951
Cdd:PRK14267 98 pHLTIYDNVAIGvklnglvKSKKELDERVEWALKKAALWDEVKDRLNDYPS-------NLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 952 LLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHR-LSTIKGADIIAVVKNGVIAEKG 1010
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
811-1007 |
8.25e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.08 E-value: 8.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 811 DICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDG---VEI-QKFKLNWLRQQIGLVGQEPVLF-NESIRA 885
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAeKGICLPPEKRRIGYVFQDARLFpHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 886 NIAYGkpgdvteeeiIAATTAANVHNVISSLpqGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAES 965
Cdd:PRK11144 96 NLRYG----------MAKSMVAQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1562645982 966 ERKVQDALDRVM--VNRTTVVVAHRLSTI-KGADIIAVVKNG-VIA 1007
Cdd:PRK11144 164 KRELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGkVKA 209
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
797-1011 |
8.75e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 84.50 E-value: 8.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 797 SFKYPT----RPDVQIFRDICLKMPSGKTVALVGESGSGKSTV----IGLIErfydPDSGRVLLDGVEIQKFKLNWLRQQ 868
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLakmlAGIIE----PTSGEILINGHKLEYGDYKYRCKH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPvlfNESI--RANIaygkpGDVTEEEIIAAT--TAANVHN-VISSLPQgydasVGERGVQ-------LSGGQK 936
Cdd:COG4167 89 IRMIFQDP---NTSLnpRLNI-----GQILEEPLRLNTdlTAEEREErIFATLRL-----VGLLPEHanfyphmLSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 937 QRIAIARAILKDPKILLLDEATSALDAeSER--------KVQDALdrvmvNRTTVVVAHRLSTIKG-ADIIAVVKNGVIA 1007
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDM-SVRsqiinlmlELQEKL-----GISYIYVSQHLGIVKHiSDKVLVMHQGEVV 229
|
....
gi 1562645982 1008 EKGS 1011
Cdd:COG4167 230 EYGK 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
791-1006 |
1.62e-17 |
|
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: 82.33 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKlnwlRQQIG 870
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLF-NESIRANIAY-GKPGDVTEEEIiaattAANVHNVISSLPQGYDASvgERGVQLSGGQKQRIAIARAILKD 948
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQLKGLKKEEA-----RRRIDEWLERLELSEYAN--KRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRVMVNRTTVV-VAHRLSTI-KGADIIAVVKNGVI 1006
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVeELCDRVLLLNKGRA 206
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
804-1011 |
2.23e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.21 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 804 PDVQIFRDICLKMPSGKTVALVGESGSGKS----TVIGLIERFYDPDSGRVLLDGVEIQkfkLNWLR-QQIGLVGQEP-V 877
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRgRKIATIMQNPrS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 878 LFN--ESIRAN-----IAYGKPGDV-TEEEIIAATTAANVHNVISSLPqgydasvgergVQLSGGQKQRIAIARAILKDP 949
Cdd:PRK10418 91 AFNplHTMHTHaretcLALGKPADDaTLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 950 KILLLDEATSALDAESERKVQDALDRVMVNRT--TVVVAHRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGD 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
791-1011 |
2.71e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKY-PTRP-DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI----QKFKLNW 864
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 865 LRQQIGLVGQEP--VLFNESIRANIAYGKPG-DVTEEEiiAATTAANVHNVISSLPQGYDASVGErgvqLSGGQKQRIAI 941
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfGIPKEK--AEKIAAEKLEMVGLADEFWEKSPFE----LSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDALDRV-MVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
45-335 |
2.73e-17 |
|
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: 83.71 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 45 VALMIVGT-ISAVGNGLSKPLMTLVfgnlintfgctdpghIVPMISKVSLK-FVYLAIGTGAAALLQVACWMV------- 115
Cdd:cd18563 5 FLLMLLGTaLGLVPPYLTKILIDDV---------------LIQLGPGGNTSlLLLLVLGLAGAYVLSALLGILrgrllar 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 116 TGERQAARIRGKYMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVV 195
Cdd:cd18563 70 LGERITADLRRDLYEHLQRLSLSFFD-KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 196 LLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGI 275
Cdd:cd18563 149 VLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWAT 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 276 GLGIFMLVIFCSyALAVWYgskmiikhgYNGGQVINvifalmtGGMSLGqaspSLNAFAS 335
Cdd:cd18563 229 FFPLLTFLTSLG-TLIVWY---------FGGRQVLS-------GTMTLG----TLVAFLS 267
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
45-290 |
4.25e-17 |
|
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: 82.92 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 45 VALMIVGTISAVGNGLSKPLMTlvfGNLIN-TFGCTDPGHIVPMIskvslkFVYLAIGTGAAALLQVACWMVTGERQA-- 121
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLT---RRAIDgPIAHGDRSALWPLV------LLLLALGVAEAVLSFLRRYLAGRLSLGve 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 122 ARIRGKYMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGeMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIP 201
Cdd:cd18543 72 HDLRTDLFAHLQRLDGAFHD-RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 202 AIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQ--------YNQKLKVA-----YNTMVQ 268
Cdd:cd18543 150 PLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRfeaaarrlRATRLRAArlrarFWPLLE 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 1562645982 269 Q----GLVTGIGLGIFM----------LVIFCSYAL 290
Cdd:cd18543 230 AlpelGLAAVLALGGWLvangsltlgtLVAFSAYLT 265
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
791-1004 |
4.45e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.95 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKY-PTRP-DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQ----KFKLNW 864
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 865 LRQQIGLVGQ--EPVLFNESIRANIAYG-KPGDVTEEEiiaATTAAnvhnvISSLPQ-GYDASVGERG-VQLSGGQKQRI 939
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSEDE---AKEKA-----LKWLKKvGLSEDLISKSpFELSGGQMRRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 940 AIARAILKDPKILLLDEATSALDAESERKVQDA-LDRVMVNRTTVVVAHRLSTI-KGADIIAVVKNG 1004
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHG 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
798-1011 |
5.21e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.36 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 798 FKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVI----GL---------IERFY-----DPDSGRVLLDGVEIQK 859
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnGLikskygtiqVGDIYigdkkNNHELITNPYSKKIKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 860 FKLnwLRQQIGLVGQEP--VLFNESIRANIAYGkPGDVTEEEIIAATTAANVHNVIsslpqGYDASVGERG-VQLSGGQK 936
Cdd:PRK13631 111 FKE--LRRRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKM-----GLDDSYLERSpFGLSGGQK 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 937 QRIAIARAILKDPKILLLDEATSALDAESERK-VQDALDRVMVNRTTVVVAHRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
791-992 |
6.14e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYptRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK---LNWLRQ 867
Cdd:PRK10908 2 IRFEHVSKAY--LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEP-VLFNESIRANIAY-----GKPGDVTEEEIIAATTAANVHNVISSLPqgydasvgergVQLSGGQKQRIAI 941
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVAIpliiaGASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 942 ARAILKDPKILLLDEATSALD---AESERKVQDALDRVMVnrTTVVVAHRLSTI 992
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGV--TVLMATHDIGLI 200
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
468-956 |
6.46e-17 |
|
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: 85.23 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 468 VLLLGAIAA-AGHGVLfpifgLLLSKAIgmfyeppNELRHDSRKWALVYVGLgCAGLLVVPV----------QNFFFGVa 536
Cdd:COG4615 18 ALLLGLLSGlANAGLI-----ALINQAL-------NATGAALARLLLLFAGL-LVLLLLSRLasqllltrlgQHAVARL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 537 GGKLVERIRALSFQKVvhQQVSwfddpansSGAIGARLSTDASTIkSLVGDALALIVQNIATIMAGLVIGFTANWKLMLV 616
Cdd:COG4615 84 RLRLSRRILAAPLERL--ERIG--------AARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 617 VLAVSPL-ILLQGTLQAKFLKGFsadakimyEEASQVANDAIGSIRTVASFCSEKK---------VMEAYEKKCEGPLKQ 686
Cdd:COG4615 153 TLVLLGLgVAGYRLLVRRARRHL--------RRAREAEDRLFKHFRALLEGFKELKlnrrrrrafFDEDLQPTAERYRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 687 GVRLGVVSGSGFGFSFFLMFCTNALIFYIgaiLVKHGQATFEQVFKvfFAITIT-AMG-VSQATSMAPDSNKAKDSAASI 764
Cdd:COG4615 225 RIRADTIFALANNWGNLLFFALIGLILFL---LPALGWADPAVLSG--FVLVLLfLRGpLSQLVGALPTLSRANVALRKI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 765 FRI---LDSkPKIDSSSDEGIALSLLIGEIELDHVSFKYPTRPDVQIFR--DICLKMPSGKTVALVGESGSGKSTVIGLI 839
Cdd:COG4615 300 EELelaLAA-AEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 840 ERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNEsiraniAYGKPGDVTEEEI--------IAATTAANvHN 911
Cdd:COG4615 379 TGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPARArellerleLDHKVSVE-DG 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1562645982 912 VISSLpqgydasvgergvQLSGGQKQRIAIARAILKDPKILLLDE 956
Cdd:COG4615 452 RFSTT-------------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
807-958 |
8.67e-17 |
|
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: 80.65 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 807 QIFRDICLKMPSGKTVALVGESGSGKST----VIGLIerfyDPDSGRVLLDGVEIQKFKLNWL-RQQIGLV--GQE--PV 877
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTllktLMGLL----PVKSGSIRLDGEDITKLPPHERaRAGIAYVpqGREifPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 878 LfneSIRANIaygkpgdvteeEIIAATTAANVHNVISSLpqgYD------ASVGERGVQLSGGQKQRIAIARAILKDPKI 951
Cdd:TIGR03410 90 L---TVEENL-----------LTGLAALPRRSRKIPDEI---YElfpvlkEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
....*..
gi 1562645982 952 LLLDEAT 958
Cdd:TIGR03410 153 LLLDEPT 159
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
810-1008 |
9.41e-17 |
|
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: 81.24 E-value: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLnWLRQQIGLV--GQEPVLFNE-SIRAN 886
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIArtFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 887 IA---------------YGKPGDVTEEEIIAATTAAnvhnVISSLpqGYDASVGERGVQLSGGQKQRIAIARAILKDPKI 951
Cdd:COG0411 100 VLvaaharlgrgllaalLRLPRARREEREARERAEE----LLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 952 LLLDEATSALDAESERKVQDALDRV--MVNRTTVVVAHRLSTIKG-ADIIAVVKNG-VIAE 1008
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGrVIAE 234
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
512-680 |
9.47e-17 |
|
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: 81.97 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 512 ALVYVGLGCAGLLVVP-VQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALA 590
Cdd:cd18784 38 AIIIMGLLAIASSVAAgIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTVSLNLN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 591 LIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEK 670
Cdd:cd18784 116 IFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANED 195
|
170
....*....|
gi 1562645982 671 KVMEAYEKKC 680
Cdd:cd18784 196 GEANRYSEKL 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
766-970 |
1.00e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 766 RILDSKPKIDSSSDEGIALSLLigEIELDHVSFkyPTRPDV--------QIFRDICLKMPSGKTVALVGESGSGKSTViG 837
Cdd:PRK15134 255 KLLNSEPSGDPVPLPEPASPLL--DVEQLQVAF--PIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTT-G 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 838 LIERFYDPDSGRVLLDGVEIQKF---KLNWLRQQIGLVGQEPvlfNESI--RANIaygkpgdvteEEIIAA--------- 903
Cdd:PRK15134 330 LALLRLINSQGEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDP---NSSLnpRLNV----------LQIIEEglrvhqptl 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 904 TTAANVHNVISSLPQ-GYDASVGER-GVQLSGGQKQRIAIARAILKDPKILLLDEATSALDaeseRKVQ 970
Cdd:PRK15134 397 SAAQREQQVIAVMEEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQ 461
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
800-996 |
1.35e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 800 YPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiqKFKLNWLRQQIGLVGQEPVLF 879
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 880 NESI-----RANIAYGKPGDVTEEEIIAATTAANVHNVIsslpqgyDASVGErgvqLSGGQKQRIAIARAILKDPKILLL 954
Cdd:NF040873 75 RDLVamgrwARRGLWRRLTRDDRAAVDDALERVGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1562645982 955 DEATSALDAESERKVQDALDR-VMVNRTTVVVAHRLSTIKGAD 996
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRAD 186
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
793-1031 |
1.49e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.99 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 793 LDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLV 872
Cdd:PRK10575 14 LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 873 GQE-PVLFNESIRANIAYGK-P--------GDVTEEEIIAATTAANV----HNVISSlpqgydasvgergvqLSGGQKQR 938
Cdd:PRK10575 91 PQQlPAAEGMTVRELVAIGRyPwhgalgrfGAADREKVEEAISLVGLkplaHRLVDS---------------LSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 939 IAIARAILKDPKILLLDEATSALDAESERKVqdaldrvmvnrttVVVAHRLSTIKGADIIAVVkngviaekgsHDFLMKI 1018
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDV-------------LALVHRLSQERGLTVIAVL----------HDINMAA 212
|
250
....*....|...
gi 1562645982 1019 TDGAYasLVALHS 1031
Cdd:PRK10575 213 RYCDY--LVALRG 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
791-1021 |
1.55e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.96 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFkypTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKF---KLNWLRQ 867
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 868 QIGLVGQEPVLFNE-SIRANIAYGKPGDVTEEEIIAATTaanvhnVISSLpqgydASVGERGV------QLSGGQKQRIA 940
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPLREHTQLPAPLLHST------VMMKL-----EAVGLRGAaklmpsELSGGMARRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESER---KVQDALDRVMvNRTTVVVAHR----LSTIKGADIIAVVKngVIAEKGSHD 1013
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGvlvKLISELNSAL-GVTCVVVSHDvpevLSIADHAYIVADKK--IVAHGSAQA 230
|
250
....*....|....*....
gi 1562645982 1014 -----------FLMKITDG 1021
Cdd:PRK11831 231 lqanpdprvrqFLDGIADG 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
808-990 |
1.77e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 808 IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKF----KLNWLRQQIGLVGQEPVLF---- 879
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHLLpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 880 ---NESIRANIAYGKPGDVTEE--EIIAATtaanvhnvisslpqGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLL 954
Cdd:PRK11629 104 aleNVAMPLLIGKKKPAEINSRalEMLAAV--------------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1562645982 955 DEATSALDAESERKVQDALDRVMVNRTT--VVVAHRLS 990
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
808-1011 |
2.12e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 808 IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVlfnesirani 887
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAT---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 888 aygKPGDVTEEEIIA-------------------ATTAANVHNVISSLP-QGYDAsvgergvqLSGGQKQRIAIARAILK 947
Cdd:PRK10253 92 ---TPGDITVQELVArgryphqplftrwrkedeeAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 948 DPKILLLDEATSALDAESERKVQDALDRvmVNR----TTVVVAHRLS-TIKGADIIAVVKNGVIAEKGS 1011
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSE--LNRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQGA 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
774-1010 |
2.25e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.53 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 774 IDSSSDEGIALSLLIG---EIELDHVSFKYPTRpdvqifrdiclkmpsgKTVALVGESGSGKSTVIGLIERFYDP----- 845
Cdd:PRK14271 15 VDAAAPAMAAVNLTLGfagKTVLDQVSMGFPAR----------------AVTSLMGPTGSGKTTFLRTLNRMNDKvsgyr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 846 DSGRVLLDGVEIQKFK-LNWLRQQIGLVGQEPVLFNESIRANIAYG-KPGDVTEEEIIAATTAANVHNVisSLPQGYDAS 923
Cdd:PRK14271 79 YSGDVLLGGRSIFNYRdVLEFRRRVGMLFQRPNPFPMSIMDNVLAGvRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 924 VGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLS-TIKGADIIAVVK 1002
Cdd:PRK14271 157 LSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFF 236
|
....*...
gi 1562645982 1003 NGVIAEKG 1010
Cdd:PRK14271 237 DGRLVEEG 244
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
45-340 |
2.39e-16 |
|
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: 80.91 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 45 VALMIVGTISAVgnglskpLMTLVFGNLINTFGCTDPGHIVPMISKVSLKFVYLAIGTGAAALLQVAC--WMVT-GERQA 121
Cdd:cd18547 5 IILAIISTLLSV-------LGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQnrLMARvSQRTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 122 ARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIP 201
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFDT-HSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 202 AIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQ---YNQKLkvaYNTMVQQGLVTGIGLG 278
Cdd:cd18547 157 LSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEfdeINEEL---YKASFKAQFYSGLLMP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 279 IFMLVIFCSYALAVWYGSKMIIKHGYNGGQVinVIFALMTGGMS--LGQASPSLNAFASGKAAA 340
Cdd:cd18547 234 IMNFINNLGYVLVAVVGGLLVINGALTVGVI--QAFLQYSRQFSqpINQISQQINSLQSALAGA 295
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
791-1011 |
2.68e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.82 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG 870
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVL-FNESIRANIAYGK---PGDVTEEEIIAATTAANVhnvisslpqGYDASVGERGVQLSGGQKQRIAIARAIL 946
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRaphGLSRAEDDALVAAALAQV---------DLAHLAGRDYPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 947 ------KDPKILLLDEATSALD-AESERKVQDALDRVMVNRTTV-VVAHRLS-TIKGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAViVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
791-988 |
2.71e-16 |
|
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: 77.58 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVI-----------GLIERfydPDSGRVLLdgveiqk 859
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFralaglwpwgsGRIGM---PEGEDLLF------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 860 fklnwlrqqiglVGQEPVLFNESIRANIAYgkP-GDVteeeiiaattaanvhnvisslpqgydasvgergvqLSGGQKQR 938
Cdd:cd03223 69 ------------LPQRPYLPLGTLREQLIY--PwDDV-----------------------------------LSGGEQQR 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 939 IAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMvnrTTVV-VAHR 988
Cdd:cd03223 100 LAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG---ITVIsVGHR 147
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
791-1015 |
3.81e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.03 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQifrDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKfKLNWLRQQIG 870
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVN---GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNE-SIRAN-IAYGKPGDVTEEEIIAattaanvhnVISSLPQ--GYDASVGERGVQLSGGQKQRIAIARAIL 946
Cdd:PRK13536 118 VVPQFDNLDLEfTVRENlLVFGRYFGMSTREIEA---------VIPSLLEfaRLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVV-------AHRLstikgADIIAVVKNGV-IAEKGSHDFL 1015
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGRkIAEGRPHALI 260
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
98-339 |
4.48e-16 |
|
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: 80.15 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 98 LAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGEMVGKFIQlcST 177
Cdd:cd18541 49 LALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQ-KNRTGDLMARATNDLNAVRMALGPGILYLVD--AL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 178 FLGGFVIA--FVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQY 255
Cdd:cd18541 126 FLGVLVLVmmFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 256 NQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYALAVWYGSKMIIKHGYNGGQVI--NVIFALMTGGM-SLGQAspsLNA 332
Cdd:cd18541 206 DKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVafNSYLGMLIWPMmALGWV---INL 282
|
....*..
gi 1562645982 333 FASGKAA 339
Cdd:cd18541 283 IQRGAAS 289
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
791-962 |
4.60e-16 |
|
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: 78.74 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwLRQQIG 870
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH-KRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 L--VGQEPVLFNE-SIRANIA-----YGKPGDVTEEEIIAATTAANVHNVISSLpqgydasvgerGVQLSGGQKQRIAIA 942
Cdd:cd03218 77 IgyLPQEASIFRKlTVEENILavleiRGLSKKEREEKLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEIA 145
|
170 180
....*....|....*....|
gi 1562645982 943 RAILKDPKILLLDEATSALD 962
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVD 165
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
791-1013 |
4.96e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTrpdVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNwLRQQIG 870
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 --LVGQEPVLF-NESIRANIAYGKPG-DVTEEEIIAATTAANVHnvisslpQGYDASVGergvQLSGGQKQRIAIARAIL 946
Cdd:PRK15439 88 iyLVPQEPLLFpNLSVKENILFGLPKrQASMQKMKQLLAALGCQ-------LDLDSSAG----SLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 947 KDPKILLLDEATSALD-AESER---KVQDALDR-VMVnrttVVVAHRLSTIKG-ADIIAVVKNGVIAEKGSHD 1013
Cdd:PRK15439 157 RDSRILILDEPTASLTpAETERlfsRIRELLAQgVGI----VFISHKLPEIRQlADRISVMRDGTIALSGKTA 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
790-1015 |
5.46e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.13 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 790 EIELDHVSFKY----PTrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVI-----------GLIERFYD-------PDS 847
Cdd:PRK13651 2 QIKVKNIVKIFnkklPT--ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnalllpdtGTIEWIFKdeknkkkTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 848 GRVLLDGVEIQKFK------LNWLRQQIGLVGQ--EPVLFNESIRANIAYGKPG-DVTEEEiiAATTAANVHNVIsslpq 918
Cdd:PRK13651 80 KEKVLEKLVIQKTRfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSmGVSKEE--AKKRAAKYIELV----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 919 GYDASVGERG-VQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVN-RTTVVVAHRL-STIKGA 995
Cdd:PRK13651 153 GLDESYLQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWT 232
|
250 260
....*....|....*....|.
gi 1562645982 996 DIIAVVKNG-VIAEKGSHDFL 1015
Cdd:PRK13651 233 KRTIFFKDGkIIKDGDTYDIL 253
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
803-963 |
6.31e-16 |
|
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: 78.08 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 803 RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPD---SGRVLLDGVEIQKFKLnwlRQQIGLVGQEPVLF 879
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQF---QKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 880 NE-SIRANIAYGKP---GDVTEEEIIAATTAanvhnvISSLPQGYDASVGERGVQ-LSGGQKQRIAIARAILKDPKILLL 954
Cdd:cd03234 94 PGlTVRETLTYTAIlrlPRKSSDAIRKKRVE------DVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLIL 167
|
....*....
gi 1562645982 955 DEATSALDA 963
Cdd:cd03234 168 DEPTSGLDS 176
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
791-1010 |
7.48e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.14 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKY------------------PTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLL 852
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 853 DGVEIQKFKLNWLRQqIGLV-GQE-------PVLfnESIRANIA-YGKPGDVTEEEIIAATTAANVHNVIsslpqgyDAS 923
Cdd:cd03267 81 AGLVPWKRRKKFLRR-IGVVfGQKtqlwwdlPVI--DSFYLLAAiYDLPPARFKKRLDELSELLDLEELL-------DTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 924 VgeRgvQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVahrLSTIKGADIIAVVKN 1003
Cdd:cd03267 151 V--R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVL---LTSHYMKDIEALARR 223
|
....*..
gi 1562645982 1004 GVIAEKG 1010
Cdd:cd03267 224 VLVIDKG 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
791-1011 |
7.73e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.12 E-value: 7.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDG--VEIQKFKLNWLRQQ 868
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEP--VLFNESIRANIAYGKPG-DVTEEEIIAATTAANVHNVISSLPQGYDASvgergvqLSGGQKQRIAIARAI 945
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 946 LKDPKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAHRLSTIK-GADIIAVVKNGVIAEKGS 1011
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQkeLGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
814-1026 |
8.46e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.52 E-value: 8.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 814 LKMPSGKTVALVGESGSGKSTVI----GLIERFYDPDSgRVLLDGVEIQKF-----KLNWLRQQIGLVGQEPVLFNE-SI 883
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGS-HIELLGRTVQREgrlarDIRKSRANTGYIFQQFNLVNRlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 884 RANIAYGKPGDVT-EEEIIAATTAANVHNVISSLPQ-GYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSAL 961
Cdd:PRK09984 104 LENVLIGALGSTPfWRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 962 DAESERKVQDALDRVMVNR--TTVVVAHRLS-TIKGADIIAVVKNG-VIAEKGSHDFLMKITDGAYASL 1026
Cdd:PRK09984 184 DPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGhVFYDGSSQQFDNERFDHLYRSI 252
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
807-1016 |
1.65e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.70 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 807 QIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQ-------------KFKLNWLRQQIGLVG 873
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 874 QEPVLFNESIRANIAYGKPgdvteEEIIAATTAANVHNVISSLPQ-GYD-ASVGERGVQLSGGQKQRIAIARAILKDPKI 951
Cdd:PRK10619 99 QHFNLWSHMTVLENVMEAP-----IQVLGLSKQEARERAVKYLAKvGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 952 LLLDEATSALDAESERKVQDALDRVMVN-RTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGSHDFLM 1016
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
792-958 |
1.69e-15 |
|
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: 76.94 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 792 ELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKST----VIGLIerfyDPDSGRVLLDGVEIQKFKLNWL-R 866
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLL----PPRSGSIRFDGEDITGLPPHRIaR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEPVLFNE-SIRANI---AYGKPGDVTEEEIIAAttaanvhnVISSLPQgydasVGER----GVQLSGGQKQR 938
Cdd:COG0410 78 LGIGYVPEGRRIFPSlTVEENLllgAYARRDRAEVRADLER--------VYELFPR-----LKERrrqrAGTLSGGEQQM 144
|
170 180
....*....|....*....|
gi 1562645982 939 IAIARAILKDPKILLLDEAT 958
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPS 164
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
791-1011 |
1.94e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.04 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPT-------------------RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVL 851
Cdd:COG1134 5 IEVENVSKSYRLyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 852 LDGveiqkfKLNWLrqqIGL-VGqepvlFNESI--RANI-----AYGKPGDVTEE---EIIAattAANVHNVIsslpqgy 920
Cdd:COG1134 85 VNG------RVSAL---LELgAG-----FHPELtgRENIylngrLLGLSRKEIDEkfdEIVE---FAELGDFI------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 921 DASVGergvQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVV-VAHRLSTIKG-ADII 998
Cdd:COG1134 141 DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIfVSHSMGAVRRlCDRA 216
|
250
....*....|...
gi 1562645982 999 AVVKNGVIAEKGS 1011
Cdd:COG1134 217 IWLEKGRLVMDGD 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
820-1027 |
2.17e-15 |
|
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: 81.60 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 820 KTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKfKLNWLRQQIGLVGQEPVLFNE-SIRANIAY-----GKPG 893
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFyaqlkGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 894 DVTEEEIIAATTAANVHNvisslpqgydaSVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDAL 973
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 974 DRVMVNRTTVVVAHRL--STIKGaDIIAVVKNGVIAEKGSHDFLMK-ITDGAYASLV 1027
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMdeADLLG-DRIAIISQGRLYCSGTPLFLKNcFGTGFYLTLV 1160
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
791-987 |
2.47e-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: 74.02 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiqkfklnwlrqqig 870
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 lvgqepvlfnesiRANIAYgkpgdvteeeiiaattaanvhnvissLPQgydasvgergvqLSGGQKQRIAIARAILKDPK 950
Cdd:cd03221 62 -------------TVKIGY--------------------------FEQ------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*..
gi 1562645982 951 ILLLDEATSALDAESERKVQDALDRvmVNRTTVVVAH 987
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKE--YPGTVILVSH 125
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
98-310 |
2.71e-15 |
|
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: 77.51 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 98 LAIGTGAAALLQVAC---WMVTGERQAARIRGKYMKAILRQDIGFFDTEtSTGEIIGRMSGDTILIQEAMGEMVGKFIQL 174
Cdd:cd18589 42 MSLLTIASAVSEFVCdliYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN-QTGDIVSRVTTDTEDMSESLSENLSLLMWY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 175 CSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQ 254
Cdd:cd18589 121 LARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 255 YNQKLKVAYNTMVQQGLvtgiglgifmlvifcSYALAVWYG--SKMIIKHG--YNGGQVI 310
Cdd:cd18589 201 YRQRLQKTYRLNKKEAA---------------AYAVSMWTSsfSGLALKVGilYYGGQLV 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
791-1011 |
2.72e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.44 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQ---IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNW-LR 866
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEPvlfNESIRANI-----AYGkPGD--VTEEEIIA----ATTAANVHNVISSLPQgydasvgergvQLSGGQ 935
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVATIveedvAFG-PENlgIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 936 KQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRvmVNR----TTVVVAHRLSTIKGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKE--LNKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
468-726 |
5.03e-15 |
|
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: 76.70 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 468 VLLLGAIAAAGhGVLFPifgLLLSKAIGMFYEppnelRHDSRKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRAL 547
Cdd:cd18551 4 ALLLSLLGTAA-SLAQP---LLVKNLIDALSA-----GGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 548 SFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQ 627
Cdd:cd18551 75 LWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 628 GTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFC 707
Cdd:cd18551 153 ILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQL 232
|
250
....*....|....*....
gi 1562645982 708 TNALIFYIGAILVKHGQAT 726
Cdd:cd18551 233 ALLVVLGVGGARVASGALT 251
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
798-1011 |
5.66e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.20 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 798 FKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDG--VEIQKFKLNWLRQQIGLVGQE 875
Cdd:PRK13638 9 FRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 876 P--VLFNESIRANIAYG-KPGDVTEEEIiaattAANVHNVISSL-PQGYDasvgERGVQ-LSGGQKQRIAIARAILKDPK 950
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSlRNLGVPEAEI-----TRRVDEALTLVdAQHFR----HQPIQcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 951 ILLLDEATSALDAESERKVQDALDRVMVNRTTVVV-AHRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIyEISDAVYVLRQGQILTHGA 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
805-1010 |
7.97e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.38 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 805 DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVeiqkfKLNWL---RQQIGLVGQEPVLF-N 880
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-----RMNDVppaERGVGMVFQSYALYpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 881 ESIRANIAYG-KPGDVTEEEIiaattAANVHNVISSLPQGYdasVGERGVQ-LSGGQKQRIAIARAILKDPKILLLDEAT 958
Cdd:PRK11000 90 LSVAENMSFGlKLAGAKKEEI-----NQRVNQVAEVLQLAH---LLDRKPKaLSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 959 SALDAESERKVQDALDRV--MVNRTTVVVAH-RLSTIKGADIIAVVKNGVIAEKG 1010
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
88-321 |
1.58e-14 |
|
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: 75.51 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 88 ISKVSLKFVYLAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEamgeM 167
Cdd:cd18548 38 ILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID-KFGTSSLITRLTNDVTQVQN----F 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 168 VGKFIQLCS----TFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVA 243
Cdd:cd18548 113 VMMLLRMLVrapiMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 244 SFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYALAVWYGSKMIIKHGYNGGQVI-------NVIFAL 316
Cdd:cd18548 193 AFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVafinylmQILMSL 272
|
....*
gi 1562645982 317 MTGGM 321
Cdd:cd18548 273 MMLSM 277
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
811-1013 |
2.44e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 811 DICLKMPSGKTVALVGESGSGKST----VIGLIErfydPDSGRVLLDGVEIQKF-KLNWL--RQQIGLVGQEPvLFNESI 883
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMkDDEWRavRSDIQMIFQDP-LASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 884 RANIaygkpGDVTEE-------EIIAATTAANVH----------NVISSLPQgydasvgergvQLSGGQKQRIAIARAIL 946
Cdd:PRK15079 114 RMTI-----GEIIAEplrtyhpKLSRQEVKDRVKammlkvgllpNLINRYPH-----------EFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQD---ALDRVMvNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGSHD 1013
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNllqQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYD 247
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
789-956 |
2.65e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.52 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 789 GEIELDHVSFKYPTRPDVqifRDICLKMPSGKTVALVGESGSGKST----VIGLIErfydPDSGRVLLDGVEIQKFKLnW 864
Cdd:COG1137 2 MTLEAENLVKSYGKRTVV---KDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPM-H 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 865 LRQQ--IGLVGQEPVLFNE-SIRANIA-----YGKPGDVTEEEIIAATTAANVHNVISSlpqgydasvgeRGVQLSGGQK 936
Cdd:COG1137 74 KRARlgIGYLPQEASIFRKlTVEDNILavlelRKLSKKEREERLEELLEEFGITHLRKS-----------KAYSLSGGER 142
|
170 180
....*....|....*....|
gi 1562645982 937 QRIAIARAILKDPKILLLDE 956
Cdd:COG1137 143 RRVEIARALATNPKFILLDE 162
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
806-987 |
2.82e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.27 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 806 VQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGV------EIQKFKLNwlRQQIGLVGQEPVLF 879
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdEEARAKLR--AKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 880 -------NESIRAnIAYGKPGDVTEEEIIAATTAANVHNVISSLPqgydasvgergVQLSGGQKQRIAIARAILKDPKIL 952
Cdd:PRK10584 101 ptlnaleNVELPA-LLRGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1562645982 953 LLDEATSALDAESERKVQDALdrVMVNR----TTVVVAH 987
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLL--FSLNRehgtTLILVTH 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
791-1013 |
3.10e-14 |
|
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: 76.76 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERF--YDPDSGRVLLD--------GVEIQKF 860
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgYVERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 861 klnwlrqqiglVGQE-PVLFNESIRANIAYGKPGDVTEEEI---IAA----TTA-----ANVHNVISSLPQ-GYDASVG- 925
Cdd:TIGR03269 78 -----------VGEPcPVCGGTLEPEEVDFWNLSDKLRRRIrkrIAImlqrTFAlygddTVLDNVLEALEEiGYEGKEAv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 926 ERGVQL-----------------SGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNR--TTVVVA 986
Cdd:TIGR03269 147 GRAVDLiemvqlshrithiardlSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTS 226
|
250 260
....*....|....*....|....*...
gi 1562645982 987 HRLSTI-KGADIIAVVKNGVIAEKGSHD 1013
Cdd:TIGR03269 227 HWPEVIeDLSDKAIWLENGEIKEEGTPD 254
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
123-318 |
3.33e-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: 74.40 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 123 RIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSgDTILIQEAMGE-MVGKFIQLCsTFLGGFVIAFVKGWRLTVVLLATIP 201
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFET-RKTGEIISRFN-DANKIREAISStTISLFLDLL-MVIISGIILFFYNWKLFLITLLIIP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 202 AIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQK----LKVAYNTM----VQQGLVT 273
Cdd:cd18570 153 LYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKfsklLKKSFKLGklsnLQSSIKG 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1562645982 274 GIGLgIFMLVIFcsyalavWYGSKMIIKHGYNGGQVInVIFALMT 318
Cdd:cd18570 233 LISL-IGSLLIL-------WIGSYLVIKGQLSLGQLI-AFNALLG 268
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
807-1015 |
4.50e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.28 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 807 QIFRDICLKMPSGKTVALVGESGSGKS-TVIGLIERFYDPD----SGRVLLDGVEIQKFKLNWLRQ----QIGLVGQEP- 876
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 877 VLFN--ESIRANIA------YGKPGDVTEEEIIAATTAANVHNVISSL---PQgydasvgergvQLSGGQKQRIAIARAI 945
Cdd:PRK15134 103 VSLNplHTLEKQLYevlslhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPH-----------QLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 946 LKDPKILLLDEATSALDAESERKVQDALD--RVMVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGSHDFL 1015
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
791-1008 |
5.77e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLdGVEIqkfklnwlrqQIG 870
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNE--SIRANIAYGKPGDvTEEEIIAAT-----TAANVHNVISSlpqgydasvgergvqLSGGQKQRIAIAR 943
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGG-TEQEVRGYLgrflfSGDDAFKPVGV---------------LSGGEKARLALAK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 944 AILKDPKILLLDEATSALDAESERKVQDALDR----VmvnrttVVVAH-R--LSTIkgADIIAVVKNGVIAE 1008
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtV------LLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
510-726 |
6.14e-14 |
|
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: 73.62 E-value: 6.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 510 KWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDAL 589
Cdd:cd18542 40 LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDK--ARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 590 ALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGfsadakiMYEEASQ-------VANDAIGSIRT 662
Cdd:cd18542 118 VELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRP-------AFEEIREqegelntVLQENLTGVRV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 663 VASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQAT 726
Cdd:cd18542 191 VKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEIT 254
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
791-1008 |
6.25e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiQKFKLN----WLR 866
Cdd:COG3845 6 LELRGITKRFG---GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRsprdAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEPVLFNE-SIRANIAYGKPGdvTEEEIIAATTAAnvhNVISSLPQGY------DASVGergvQLSGGQKQRI 939
Cdd:COG3845 80 LGIGMVHQHFMLVPNlTVAENIVLGLEP--TKGGRLDRKAAR---ARIRELSERYgldvdpDAKVE----DLSVGEQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 940 AIARAILKDPKILLLDEATSAL-DAESErKVQDALdRVMVNR-TTVV-VAHRLSTIKG-ADIIAVVKNG-VIAE 1008
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLtPQEAD-ELFEIL-RRLAAEgKSIIfITHKLREVMAiADRVTVLRRGkVVGT 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
808-968 |
1.01e-13 |
|
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: 70.85 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 808 IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWlRQQIGLVGQEPVLFNE-SIRAN 886
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 887 IAYGKP-GDVTEEEIIAATTAANVhNVISSLPQGydasvgergvQLSGGQKQRIAIARAILKDPKILLLDEATSALDAES 965
Cdd:TIGR01189 94 LHFWAAiHGGAQRTIEDALAAVGL-TGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
...
gi 1562645982 966 ERK 968
Cdd:TIGR01189 163 VAL 165
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
793-971 |
1.76e-13 |
|
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: 74.59 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 793 LDHVSFKYPtrPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLL-DGVeiqkfklnwlrqQIGL 871
Cdd:TIGR03719 7 MNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGI------------KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 872 VGQEPVLFNE-SIRANI-------------------AYGKPGD-----VTE----EEIIAATTAANVHNVIS------SL 916
Cdd:TIGR03719 73 LPQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDAdfdklAAEqaelQEIIDAADAWDLDSQLEiamdalRC 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 917 PQGyDASVGErgvqLSGGQKQRIAIARAILKDPKILLLDEATSALDAES----ERKVQD 971
Cdd:TIGR03719 153 PPW-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
791-1011 |
1.77e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.45 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKfklnWLRQQIG 870
Cdd:COG4152 2 LELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLF-NESIRANIAY-----GKPGDVTEEEIIAATTAANvhnvissLPQGYDASVGErgvqLSGGQKQRIAIARA 944
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlarlkGLSKAEAKRRADEWLERLG-------LGDRANKKVEE----LSKGNQQKVQLIAA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 945 ILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTI-KGADIIAVVKNGVIAEKGS 1011
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGS 212
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
532-681 |
2.59e-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: 71.81 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 532 FFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANW 611
Cdd:cd18574 65 LLSVVGERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISP 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 612 KLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCE 681
Cdd:cd18574 143 KLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVE 212
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
468-678 |
3.39e-13 |
|
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: 71.26 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 468 VLLLGAIAAAghgVLFPifgLLLSKAIGMFYEPPNELRHDSRKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRAL 547
Cdd:cd18544 6 LLLLLATALE---LLGP---LLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 548 SFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQ 627
Cdd:cd18544 80 LFSHIQRLPLSFFDR--TPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 628 GTLQAKFLKgfsadaKIMYEEASQVA------NDAIGSIRTVASFCSEKKVMEAYEK 678
Cdd:cd18544 158 TYLFRKKSR------KAYREVREKLSrlnaflQESISGMSVIQLFNREKREFEEFDE 208
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
46-302 |
3.74e-13 |
|
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: 71.39 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 46 ALMIVGTISAVGNGLSKP-LMTLVFGNLINTFGCTDPGHIVPMISK--------VSLKFVYLAIGTGAAALLQVACWMVT 116
Cdd:cd18564 2 ALALLALLLETALRLLEPwPLKVVIDDVLGDKPLPGLLGLAPLLGPdplallllAAAALVGIALLRGLASYAGTYLTALV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 117 GERQAARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMgemVGKFIQLCS---TFLGGFVIAFVKGWRLT 193
Cdd:cd18564 82 GQRVVLDLRRDLFAHLQRLSLSFHDR-RRTGDLLSRLTGDVGAIQDLL---VSGVLPLLTnllTLVGMLGVMFWLDWQLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 194 VVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQ-------------KLK 260
Cdd:cd18564 158 LIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARenrkslraglraaRLQ 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1562645982 261 VAYNTMVQqgLVTGIGLgifmlvifcsyALAVWYGSKMIIKH 302
Cdd:cd18564 238 ALLSPVVD--VLVAVGT-----------ALVLWFGAWLVLAG 266
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
791-1012 |
4.03e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.60 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPT-RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWL---- 865
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 866 RQQIGLVGQEPVLF-------NESIRANIAyGKPGDVTEEEIIAATTAAnvhnvisslpqGYDASVGERGVQLSGGQKQR 938
Cdd:PRK10535 85 REHFGFIFQRYHLLshltaaqNVEVPAVYA-GLERKQRLLRAQELLQRL-----------GLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 939 IAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVN-RTTVVVAHRLSTIKGADIIAVVKNG-VIAEKGSH 1012
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGeIVRNPPAQ 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
802-967 |
5.14e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 802 TRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQkfkLNWLRQQIGLVGQ----EPV 877
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLGHrnamKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 878 LfneSIRANIA-----YGKPgdvtEEEIIAATTAANVHNVISsLPQGYdasvgergvqLSGGQKQRIAIARAILKDPKIL 952
Cdd:PRK13539 88 L---TVAENLEfwaafLGGE----ELDIAAALEAVGLAPLAH-LPFGY----------LSAGQKRRVALARLLVSNRPIW 149
|
170
....*....|....*
gi 1562645982 953 LLDEATSALDAESER 967
Cdd:PRK13539 150 ILDEPTAALDAAAVA 164
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
797-1011 |
5.86e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.20 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 797 SFKYPT----RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLV 872
Cdd:PRK15112 13 TFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 873 GQEPvlfNESIRANIAYGKPGDVTEEEIIAATTAANVHNVISSLPQgydasVGERGVQ-------LSGGQKQRIAIARAI 945
Cdd:PRK15112 93 FQDP---STSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQ-----VGLLPDHasyyphmLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 946 LKDPKILLLDEATSALDAESERKVQDALDRVMVNR--TTVVVAHRLSTIKG-ADIIAVVKNGVIAEKGS 1011
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
803-985 |
7.34e-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: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 803 RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIErFYDPD----SGRVLLDGVEIQKFKLN----WLRQQIGLVG- 873
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMRaisaYVQQDDLFIPt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 874 ---QEPVLFNESIRAniaygkPGDVTEEEIIAAttaanVHNVIS--SLPQGYDASVGERGVQ--LSGGQKQRIAIARAIL 946
Cdd:TIGR00955 114 ltvREHLMFQAHLRM------PRRVTKKEKRER-----VDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVV 985
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIIC 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
791-989 |
7.83e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKST----VIGLIErfydPDSGRVLLDgveiQKFKLNWLR 866
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTlvrvVLGLVA----PDEGVIKRN----GKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIGLVGQEPVLFNESIRAniaygKPGdVTEEEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQKQRIAIARAIL 946
Cdd:PRK09544 74 QKLYLDTTLPLTVNRFLRL-----RPG-TKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALD--RVMVNRTTVVVAHRL 989
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDL 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
792-1004 |
8.66e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 8.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 792 ELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEiQKFK--LNWLRQQI 869
Cdd:PRK11288 6 SFDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-MRFAstTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLFNE-SIRANIAYG----KPGDVTEEEIIAATTAANVHNVISSLPqgyDASVGErgvqLSGGQKQRIAIARA 944
Cdd:PRK11288 82 AIIYQELHLVPEmTVAENLYLGqlphKGGIVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 945 ILKDPKILLLDEATSALDA-ESER--KVQDAL---DRVMvnrttVVVAHRLSTI-KGADIIAVVKNG 1004
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSArEIEQlfRVIRELraeGRVI-----LYVSHRMEEIfALCDAITVFKDG 216
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
512-726 |
9.20e-13 |
|
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: 70.23 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 512 ALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALAL 591
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLVSGVLP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 592 IVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKK 671
Cdd:cd18564 135 LLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEH 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 672 VMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQAT 726
Cdd:cd18564 215 EERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLT 269
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
805-1018 |
9.50e-13 |
|
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: 68.32 E-value: 9.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 805 DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERF--YDPDSGRVLLDGVEIQKFKLN-WLRQQIGLVGQEPVlfne 881
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEeRARLGIFLAFQYPP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 882 siraniaygkpgdvteeEIIAATTAANVHNVisslpqgydasvgerGVQLSGGQKQRIAIARAILKDPKILLLDEATSAL 961
Cdd:cd03217 88 -----------------EIPGVKNADFLRYV---------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 962 DAESERKVQDALDRVM-VNRTTVVVAHR---LSTIKgADIIAVVKNGVIAEKGSHDFLMKI 1018
Cdd:cd03217 136 DIDALRLVAEVINKLReEGKSVLIITHYqrlLDYIK-PDRVHVLYDGRIVKSGDKELALEI 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
805-1004 |
1.69e-12 |
|
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: 71.01 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 805 DVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDS--GRVLLDGVEIQKFKL-NWLRQQIGLVGQEPVLFNE 881
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 882 -SIRANIAYGK----PGDVTEEeiiaATTAANVHNVISSLPqgYDASVGERGV-QLSGGQKQRIAIARAILKDPKILLLD 955
Cdd:TIGR02633 93 lSVAENIFLGNeitlPGGRMAY----NAMYLRAKNLLRELQ--LDADNVTRPVgDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 956 EATSAL-DAESERKVQDALDRVMVNRTTVVVAHRLSTIKG-ADIIAVVKNG 1004
Cdd:TIGR02633 167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
791-1015 |
1.73e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.45 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPDVQifrDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKfKLNWLRQQIG 870
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVD---GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQ----EPvlfNESIRANI-AYGKPGDVTeeeiiAATTAANVHNVI--SSLPQGYDASVGErgvqLSGGQKQRIAIAR 943
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLlVFGRYFGLS-----AAAARALVPPLLefAKLENKADAKVGE----LSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 944 AILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVV-------AHRLstikgADIIAVVKNG-VIAEKGSHDFL 1015
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGrKIAEGAPHALI 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
796-965 |
2.23e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 796 VSFKYPtrPDVQIFRDICLKMPSGKTVALVGESGSGKSTVI----GLierfyDPDS-GR-VLLDGVeiqkfklnwlrqQI 869
Cdd:PRK11819 12 VSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLrimaGV-----DKEFeGEaRPAPGI------------KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLfNES--IRANI-------------------AYGKPGDVTE---------EEIIAATTAANVHNVIS----- 914
Cdd:PRK11819 73 GYLPQEPQL-DPEktVRENVeegvaevkaaldrfneiyaAYAEPDADFDalaaeqgelQEIIDAADAWDLDSQLEiamda 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 915 -SLPQGyDASVGergvQLSGGQKQRIAIARAILKDPKILLLDEATSALDAES 965
Cdd:PRK11819 152 lRCPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
807-962 |
3.64e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 807 QIFRDICLKMPSGKTVALVGESGSGKST----VIGLIERfydpDSGRVLLDGVEIQKFKLNW-LRQQIGLVGQEPVLFNE 881
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 882 -----------SIRANIAYGKPGDVTEEEIiaatTAANVHNVISSLPQGydasvgergvqLSGGQKQRIAIARAILKDPK 950
Cdd:PRK10895 93 lsvydnlmavlQIRDDLSAEQREDRANELM----EEFHIEHLRDSMGQS-----------LSGGERRRVEIARALAANPK 157
|
170
....*....|..
gi 1562645982 951 ILLLDEATSALD 962
Cdd:PRK10895 158 FILLDEPFAGVD 169
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
98-303 |
3.64e-12 |
|
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: 68.28 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 98 LAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFdTETSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCST 177
Cdd:cd18550 48 VAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFF-TRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 178 FLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQT--VGSIRTVASFTGEKQAIEQY 255
Cdd:cd18550 127 LVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARF 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1562645982 256 NQKLKVAYNTMVQQGLVtGIGLGIFMLVIF-CSYALAVWYGSKMIIKHG 303
Cdd:cd18550 207 ARRSRELRDLGVRQALA-GRWFFAALGLFTaIGPALVYWVGGLLVIGGG 254
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
809-1010 |
3.94e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.64 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 809 FRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLL---DGVEIQKFKLN------WLRQQIGLVGQEP--- 876
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSeaerrrLLRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 877 VLFNESIRANIA----------YGKpgdvteeeiIAATTAANVHNV------ISSLPQGYdasvgergvqlSGGQKQRIA 940
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYGD---------IRATAGDWLERVeidaarIDDLPTTF-----------SGGMQQRLQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALdRVMVNR---TTVVVAHRLSTIKG-ADIIAVVKNGVIAEKG 1010
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLL-RGLVRElglAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
818-999 |
5.40e-12 |
|
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: 64.70 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 818 SGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGlvgqepvlfnesiraniaygkpgdvte 897
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 898 eeiiaattaanvhnvisslpqgydasVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVM 977
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180
....*....|....*....|....*...
gi 1562645982 978 V------NRTTVVVAHRLSTIKGADIIA 999
Cdd:smart00382 108 LlllkseKNLTVILTTNDEKDLGPALLR 135
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
808-965 |
7.41e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 808 IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQK----F--KLNWLRQQIG----LVGQEPV 877
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRqrdeYhqDLLYLGHQPGikteLTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 878 LFNESIRaniaygkpGDVTEEEIIAATTAANVhnvisslpQGY-DASVGergvQLSGGQKQRIAIARAILKDPKILLLDE 956
Cdd:PRK13538 96 RFYQRLH--------GPGDDEALWEALAQVGL--------AGFeDVPVR----QLSAGQQRRVALARLWLTRAPLWILDE 155
|
....*....
gi 1562645982 957 ATSALDAES 965
Cdd:PRK13538 156 PFTAIDKQG 164
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
503-726 |
7.98e-12 |
|
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: 67.15 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 503 ELRHDSRKWALVYVGLGCAGLLVVP-----VQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTD 577
Cdd:cd18563 32 QLGPGGNTSLLLLLVLGLAGAYVLSallgiLRGRLLARLGERITADLRRDLYEHLQRLSLSFFDK--RQTGSLMSRVTSD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 578 ASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLqGT------LQAKFLKGFSADAKImyeeaSQ 651
Cdd:cd18563 110 TDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVW-GSyffwkkIRRLFHRQWRRWSRL-----NS 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 652 VANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQAT 726
Cdd:cd18563 184 VLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMT 258
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
808-988 |
1.35e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 808 IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFY--DPDSGRVLLDGVEIqkfklnwlrqqiglvGQEPVLFnESIra 885
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GREASLI-DAI-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 886 niayGKPGDVTEeeiiaattAANV-HNVISSLPQGYDASVGErgvqLSGGQKQRIAIARAILKDPKILLLDEATSALDAE 964
Cdd:COG2401 107 ----GRKGDFKD--------AVELlNAVGLSDAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*...
gi 1562645982 965 S----ERKVQDALDRvmVNRTTVVVAHR 988
Cdd:COG2401 171 TakrvARNLQKLARR--AGITLVVATHH 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
791-1004 |
1.89e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTrpdVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKF--KLNWlRQQ 868
Cdd:PRK09700 6 ISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdhKLAA-QLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVLFNE-SIRANIAYGKPG----------DVTEEEIIAAttaanvhnvISSLPQGYDASVGERGVQLSGGQKQ 937
Cdd:PRK09700 82 IGIIYQELSVIDElTVLENLYIGRHLtkkvcgvniiDWREMRVRAA---------MMLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 938 RIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVV-VAHRLSTIKG-ADIIAVVKNG 1004
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
808-973 |
2.75e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.05 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 808 IFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIGLVGQEPVLFNESIRANI 887
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 888 AYGKPgDVTEEEIIAATTAANVhnvisslpQGY-DASVGergvQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESE 966
Cdd:cd03231 95 RFWHA-DHSDEQVEEALARVGL--------NGFeDRPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
....*..
gi 1562645982 967 RKVQDAL 973
Cdd:cd03231 162 ARFAEAM 168
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
810-1028 |
3.03e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.88 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKSTVI----GLIErfydPDSGRVLLDGVEIQKFKLNWLRQqIGLV-GQE-------PV 877
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIkmltGILV----PTSGEVRVLGYVPFKRRKEFARR-IGVVfGQRsqlwwdlPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 878 LfnESIRANIA-YGkpgdVTEEEIiaattAANVHNVISSLpqgydaSVGE------RgvQLSGGQKQRIAIARAILKDPK 950
Cdd:COG4586 114 I--DSFRLLKAiYR----IPDAEY-----KKRLDELVELL------DLGElldtpvR--QLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 951 ILLLDEATSALDAESERKVQDALDRvmVNR---TTVVVA-HRLstikgADIIAVVKNGVIAEKGShdflmKITDGAYASL 1026
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKE--YNRergTTILLTsHDM-----DDIEALCDRVIVIDHGR-----IIYDGSLEEL 242
|
..
gi 1562645982 1027 VA 1028
Cdd:COG4586 243 KE 244
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
791-980 |
3.23e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDhvsFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNWlRQQIG 870
Cdd:PRK13540 5 IELD---FDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEP-VLFNESIRANIAYGKPGDVTEEEIIAATTAANVHNVIsSLPQGYdasvgergvqLSGGQKQRIAIARAILKDP 949
Cdd:PRK13540 78 FVGHRSgINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKA 146
|
170 180 190
....*....|....*....|....*....|.
gi 1562645982 950 KILLLDEATSALDaesERKVQDALDRVMVNR 980
Cdd:PRK13540 147 KLWLLDEPLVALD---ELSLLTIITKIQEHR 174
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
809-1004 |
7.40e-11 |
|
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: 62.06 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 809 FRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFK-LNWLRQQIGLV----GQEPVLFNESI 883
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVpedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 884 RANIAygkpgdvteeeiiaattaanvhnvISSLpqgydasvgergvqLSGGQKQRIAIARAILKDPKILLLDEATSALD- 962
Cdd:cd03215 96 AENIA------------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDv 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1562645982 963 ---AESERKVQDALDRvmvNRTTVVVAHRLSTIKG-ADIIAVVKNG 1004
Cdd:cd03215 138 gakAEIYRLIRELADA---GKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
791-1006 |
8.11e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.86 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTrpDVQIFRDICLKMPSGKTVALVGESGSGKST----VIGLiERFydpDSGRVLLDGVEIqkfklNWLR 866
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERI---TSGEIWIGGRVV-----NELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 ---QQIGLVGQEPVLF-NESIRANIAYG-KPGDVTEEEIiaattAANVHNVISSLpqGYDASVGERGVQLSGGQKQRIAI 941
Cdd:PRK11650 73 padRDIAMVFQNYALYpHMSVRENMAYGlKIRGMPKAEI-----EERVAEAARIL--ELEPLLDRKPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 942 ARAILKDPKILLLDEATSALDAE------SE-RKVQDALdrvmvNRTTVVVAH-RLSTIKGADIIAVVKNGVI 1006
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKlrvqmrLEiQRLHRRL-----KTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
543-681 |
8.37e-11 |
|
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: 64.03 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 543 RIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSP 622
Cdd:cd18589 70 RLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLP 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 623 LILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCE 681
Cdd:cd18589 148 LLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQ 206
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
795-1011 |
8.59e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.75 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 795 HVSFKYPTrPDVQIFRDICLKMPSGKTVALVGESGSGKS----TVIGLIERfydpdSGRV----LLDGVEI---QKFKLN 863
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIggsaTFNGREIlnlPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 WLR-QQIGLVGQEP----------------VL-----------FNESIRaniaygkpgdvteeeIIAATTAANVHNVISS 915
Cdd:PRK09473 93 KLRaEQISMIFQDPmtslnpymrvgeqlmeVLmlhkgmskaeaFEESVR---------------MLDAVKMPEARKRMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 916 LPQgydasvgergvQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVM--VNRTTVVVAHRLSTIK 993
Cdd:PRK09473 158 YPH-----------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKreFNTAIIMITHDLGVVA 226
|
250
....*....|....*....
gi 1562645982 994 G-ADIIAVVKNGVIAEKGS 1011
Cdd:PRK09473 227 GiCDKVLVMYAGRTMEYGN 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
804-1004 |
9.42e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 804 PDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYdPD---SGRVLLDGVEIQKFKL-NWLRQQIGLVGQEPVLF 879
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 880 NE-SIRANIAYGK---PGDVTEEEIIAATTAANVHNVisslpqGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLD 955
Cdd:PRK13549 95 KElSVLENIFLGNeitPGGIMDYDAMYLRAQKLLAQL------KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 956 EATSALdAESERKVQDALDRVMVNR--TTVVVAHRLSTIKG-ADIIAVVKNG 1004
Cdd:PRK13549 169 EPTASL-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
809-1007 |
9.81e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 809 FRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFklnwLRQQ-IGLVGQE-------PVLFN 880
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNlVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 881 ESIRANiAYGKPG-----DVTEEEIIAATTAAnvhnviSSLPQGYDASVGErgvqLSGGQKQRIAIARAILKDPKILLLD 955
Cdd:PRK15056 99 DVVMMG-RYGHMGwlrraKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 956 EATSALDAESERKVQDALDRVMVN-RTTVVVAHRL-STIKGADIIAVVKNGVIA 1007
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLgSVTEFCDYTVMVKGTVLA 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
819-962 |
1.22e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 819 GKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKF---KLNWLRQQIGLVGQEPVLFNESiRANIAYG--KP- 892
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDP-RQTVGDSimEPl 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 893 ---GDVTEEEiiAATTAANVHNVISSLPQgydaSVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALD 962
Cdd:PRK10261 429 rvhGLLPGKA--AAARVAWLLERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
506-681 |
2.13e-10 |
|
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: 62.74 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 506 HDSRKWALVYVGLGCAGllvvpvQNFFFGVAGG-------KLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDA 578
Cdd:cd18590 32 HNAFTSAIGLMCLFSLG------SSLSAGLRGGlfmctlsRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 579 StiksLVGDALAL----IVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVAN 654
Cdd:cd18590 104 T----LMSRSVALnanvLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAR 179
|
170 180
....*....|....*....|....*..
gi 1562645982 655 DAIGSIRTVASFCSEKKVMEAYEKKCE 681
Cdd:cd18590 180 EAVSSIRTVRSFKAEEEEACRYSEALE 206
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
95-310 |
2.27e-10 |
|
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: 62.79 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 95 FVYLAIGTGAAAL--LQVACWMVTGERQAARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTiliqEAMGEM----V 168
Cdd:cd18544 45 LLYLGLLLLSFLLqyLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR-TPVGRLVTRVTNDT----EALNELftsgL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 169 GKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGE 248
Cdd:cd18544 120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNRE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 249 KQAIEQY---NQKLKVAYNTMVQQGLvtgiglgIFM-LVIFCSY---ALAVWYGSKMIIKHGYNGGQVI 310
Cdd:cd18544 200 KREFEEFdeiNQEYRKANLKSIKLFA-------LFRpLVELLSSlalALVLWYGGGQVLSGAVTLGVLY 261
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
45-302 |
4.66e-10 |
|
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: 61.71 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 45 VALMIVGTISAVGNGLSKPLMTlvfGNLINTFgctDPGHIVPMISKVSLKFVYLAIGTGAAALLQVACWMVTGERQAARI 124
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLI---KIAIDEY---IPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 125 RGKYMKAILRQDIGFFDtETSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIV 204
Cdd:cd18545 76 RQDLFSHLQKLSFSFFD-SRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 205 IAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIglgIFMLVI 284
Cdd:cd18545 155 LVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNAL---FWPLVE 231
|
250 260
....*....|....*....|.
gi 1562645982 285 FCS---YALAVWYGSKMIIKH 302
Cdd:cd18545 232 LISalgTALVYWYGGKLVLGG 252
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
791-1016 |
5.28e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKL-NWLRQQI 869
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLFNE-SIRANIAYGkpGDVTEEEiiaaTTAANVHNVISSLPQGYDASVgERGVQLSGGQKQRIAIARAILKD 948
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMG--GFFAERD----QFQERIKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRLS--TIKGADIIAVVKNGVIAEKGSHDFLM 1016
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
786-1010 |
5.58e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.28 E-value: 5.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 786 LLIGE--IELDHVSFKYPT--RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLL----DGVEI 857
Cdd:TIGR03269 273 VEVGEpiIKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 858 QKFKLNW---LRQQIGLVGQEPVLF-NESIRANIAYGKPGDVTEEeiiaattAANVHNVISSLPQGYDASVGERGV---- 929
Cdd:TIGR03269 353 TKPGPDGrgrAKRYIGILHQEYDLYpHRTVLDNLTEAIGLELPDE-------LARMKAVITLKMVGFDEEKAEEILdkyp 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 930 -QLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDAL--DRVMVNRTTVVVAHRLSTIKG-ADIIAVVKNGV 1005
Cdd:TIGR03269 426 dELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGK 505
|
....*
gi 1562645982 1006 IAEKG 1010
Cdd:TIGR03269 506 IVKIG 510
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
772-993 |
1.10e-09 |
|
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: 62.46 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 772 PKIDSSSDEGIALSLLIGE---------IELDHVSFKYPTRpDVQIfRDICLKMPSGKTVALVGESGSGKSTVIGLIERF 842
Cdd:TIGR00954 424 EEIESGREGGRNSNLVPGRgiveyqdngIKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 843 YDPDSGRVLLDGveiqkfklnwlRQQIGLVGQEPVLFNESIRANIAYG------KPGDVTEEEIIAATTAANVHNVISSl 916
Cdd:TIGR00954 502 WPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIYPdssedmKRRGLSDKDLEQILDNVQLTHILER- 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 917 PQGYDAsVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRvmVNRTTVVVAHRLSTIK 993
Cdd:TIGR00954 570 EGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK 643
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
132-301 |
1.51e-09 |
|
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: 60.54 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 132 ILRQDIGFFDtETSTGEIIGRMSGDTILIqeamGEMVGK-----FIQLCsTFLGGFVIAFVKGWRLTVVLLATIPAIVIA 206
Cdd:cd18549 85 LQKLSFSFFD-NNKTGQLMSRITNDLFDI----SELAHHgpedlFISII-TIIGSFIILLTINVPLTLIVFALLPLMIIF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 207 GAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQY---NQKLKVAYNTMVQQGLVTGIGLGIFMLV 283
Cdd:cd18549 159 TIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFdegNDRFLESKKKAYKAMAYFFSGMNFFTNL 238
|
170
....*....|....*...
gi 1562645982 284 IfcsYALAVWYGSKMIIK 301
Cdd:cd18549 239 L---NLVVLVAGGYFIIK 253
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
804-1009 |
1.51e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 804 PDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQkFKLNWLRQQ--IGLVGQEPVLFNE 881
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNGPKSSQEagIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 882 -SIRANIAYGKP-----GDVTEEEIIAATTA--ANVhnvisSLPQGYDASVGErgvqLSGGQKQRIAIARAILKDPKILL 953
Cdd:PRK10762 94 lTIAENIFLGREfvnrfGRIDWKKMYAEADKllARL-----NLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 954 LDEATSAL-DAESErkvqdALDRVM-----VNRTTVVVAHRLSTI-KGADIIAVVKNG-VIAEK 1009
Cdd:PRK10762 165 MDEPTDALtDTETE-----SLFRVIrelksQGRGIVYISHRLKEIfEICDDVTVFRDGqFIAER 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
803-962 |
1.83e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 803 RPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDG----------VEIQKFKLNWLRQ----Q 868
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHvrgaD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 869 IGLVGQEPVL-----------FNESIRANIAYGKPGDVTE-EEIIAATTAANVHNVISSLPQgydasvgergvQLSGGQK 936
Cdd:PRK10261 106 MAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEaKRMLDQVRIPEAQTILSRYPH-----------QLSGGMR 174
|
170 180
....*....|....*....|....*.
gi 1562645982 937 QRIAIARAILKDPKILLLDEATSALD 962
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALD 200
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
790-956 |
3.97e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 790 EIELDHVSFKYPTR-----PdvqifrdICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKLNW 864
Cdd:PRK10522 322 TLELRNVTFAYQDNgfsvgP-------INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 865 LRQQIGLVGQEPVLFNESIraniayGKPGDVTEEEIIAATTA--------ANVHNVISSLpqgydasvgergvQLSGGQK 936
Cdd:PRK10522 395 YRKLFSAVFTDFHLFDQLL------GPEGKPANPALVEKWLErlkmahklELEDGRISNL-------------KLSKGQK 455
|
170 180
....*....|....*....|
gi 1562645982 937 QRIAIARAILKDPKILLLDE 956
Cdd:PRK10522 456 KRLALLLALAEERDILLLDE 475
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
131-283 |
5.50e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 58.73 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 131 AILRQDIGFFDTEtSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVM 210
Cdd:cd18565 96 HVQRLDMAFFEDR-QTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 211 ATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGE-------KQAIEQYNQ------KLKVAYNTMVQqgLVTGIGL 277
Cdd:cd18565 175 QRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEdferervADASEEYRDanwraiRLRAAFFPVIR--LVAGAGF 252
|
....*.
gi 1562645982 278 GIFMLV 283
Cdd:cd18565 253 VATFVV 258
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
468-679 |
5.56e-09 |
|
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: 58.57 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 468 VLLLGAIAAAGhGVLFPIFgllLSKAIGMFYEPPNELRHDS----RKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVER 543
Cdd:cd18547 4 VIILAIISTLL-SVLGPYL---LGKAIDLIIEGLGGGGGVDfsglLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 544 IRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPL 623
Cdd:cd18547 80 LRKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 624 ILLQGTLQAKF-LKGFSADAKIMYEEASQVaNDAIGSIRTVASFCSEKKVMEAYEKK 679
Cdd:cd18547 158 SLLVTKFIAKRsQKYFRKQQKALGELNGYI-EEMISGQKVVKAFNREEEAIEEFDEI 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
804-969 |
6.81e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 804 PDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQ-KFKLNWLRQQIGLVGQEPVLFNE- 881
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 882 SIRANI---AYGKPGDVTEEEIIAATTAAnvhnVISSLpqGYDASVGERGVQLSGGQKQRIAIARAILKDPKILLLDEAT 958
Cdd:PRK10982 89 SVMDNMwlgRYPTKGMFVDQDKMYRDTKA----IFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170
....*....|.
gi 1562645982 959 SALdaeSERKV 969
Cdd:PRK10982 163 SSL---TEKEV 170
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
819-1017 |
7.10e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 819 GKTVALVGESGSGKSTVI----GLIerfydPDSGRVLLDGVEIQKFKLNWL-RQQIGLVGQEPVLFNESIRANIAYGKPG 893
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLarmaGLL-----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 894 DVTEEEIIAAttaanVHNVISSLpqGYDASVGERGVQLSGGQKQRIAIARAILK-------DPKILLLDEATSALD-AEs 965
Cdd:PRK03695 97 KTRTEAVASA-----LNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDvAQ- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 966 erkvQDALDRVMV-----NRTTVVVAHRLS-TIKGADIIAVVKNGVIAEKGSHDFLMK 1017
Cdd:PRK03695 169 ----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
812-1010 |
8.34e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 812 ICLKMPSGKTVALVGESGSGKS----TVIGLIERfydpdSGRVL-----LDGVEIQKFKLNWLRQqigLVGQE-PVLFNE 881
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDY-----PGRVMaekleFNGQDLQRISEKERRN---LVGAEvAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 882 SIRA-NIAYGKPGDVTEeeiiaattAANVHNvisslpQGYDASVGERGV--------------------QLSGGQKQRIA 940
Cdd:PRK11022 98 PMTSlNPCYTVGFQIME--------AIKVHQ------GGNKKTRRQRAIdllnqvgipdpasrldvyphQLSGGMSQRVM 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALDRVMV--NRTTVVVAHRLSTI-KGADIIAVVKNGVIAEKG 1010
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETG 236
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
819-987 |
9.09e-09 |
|
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: 57.42 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 819 GKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQkFKlnwlRQQIglvgqEPVlFNESIRANIAygkpgdvtee 898
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YK----PQYI-----KAD-YEGTVRDLLS---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 899 EIIAATTAANVHNVISSLPQGYDaSVGERGV-QLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVM 977
Cdd:cd03237 84 SITKDFYTHPYFKTEIAKPLQIE-QILDREVpELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170
....*....|..
gi 1562645982 978 VN--RTTVVVAH 987
Cdd:cd03237 163 ENneKTAFVVEH 174
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
809-958 |
1.08e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 809 FRDICLKMPSGKTVALVGESGSGKS----TVIGLierfYDPDSGRVLLDGVEIqKFK--LNWLRQQIGLV----GQEPVL 878
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTelarALFGA----DPADSGEIRLDGKPV-RIRspRDAIRAGIAYVpedrKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 879 FNESIRANIA------YGKPGDVTEEEIIAATTAAnvhnvISSL---PQGYDASVGergvQLSGGQKQRIAIARAILKDP 949
Cdd:COG1129 343 LDLSIRENITlasldrLSRGGLLDRRRERALAEEY-----IKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDP 413
|
....*....
gi 1562645982 950 KILLLDEAT 958
Cdd:COG1129 414 KVLILDEPT 422
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
797-986 |
1.48e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.73 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 797 SFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVI----GLIERFYDPdSGRVLLDGVEIQKFKlNWLRQQIGLV 872
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSV-EGDIHYNGIPYKEFA-EKYPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 873 GQEPVLFNEsiraniaygkpgdVTEEEIIAATTAANVHNVIsslpqgydasvgeRGVqlSGGQKQRIAIARAILKDPKIL 952
Cdd:cd03233 89 SEEDVHFPT-------------LTVRETLDFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1562645982 953 LLDEATSALDAESerkvqdALD-----RVMVN--RTTVVVA 986
Cdd:cd03233 141 CWDNSTRGLDSST------ALEilkciRTMADvlKTTTFVS 175
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
567-743 |
2.64e-08 |
|
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: 56.69 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 567 SGAIGARLStDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLqgtLQAKFLKGFS-ADAKIM 645
Cdd:cd18570 98 TGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYIL---IILLFNKPFKkKNREVM 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 646 YEEASQVAN--DAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHG 723
Cdd:cd18570 174 ESNAELNSYliESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKG 253
|
170 180
....*....|....*....|
gi 1562645982 724 QATFEQVFkVFFAITITAMG 743
Cdd:cd18570 254 QLSLGQLI-AFNALLGYFLG 272
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
512-726 |
2.82e-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: 56.34 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 512 ALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALAL 591
Cdd:cd18550 42 ALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGTLTS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 592 IVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVAND--AIGSIRTVASFCSE 669
Cdd:cd18550 120 VVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGRE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 670 KKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQAT 726
Cdd:cd18550 200 DDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLT 256
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
819-991 |
3.11e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.58 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 819 GKTVALVGESGSGKSTVIGLIERFYDPDS--GRVLLDGVEIQKFKLnwlrQQIGLVGQEPVLFNE-SIRANIAYGK---- 891
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL----KRTGFVTQDDILYPHlTVRETLVFCSllrl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 892 PGDVTEEEIIAATtaanvHNVISSL--PQGYDASVGE---RGVqlSGGQKQRIAIARAILKDPKILLLDEATSALDAESE 966
Cdd:PLN03211 170 PKSLTKQEKILVA-----ESVISELglTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180
....*....|....*....|....*.
gi 1562645982 967 -RKVQDALDRVMVNRTTVVVAHRLST 991
Cdd:PLN03211 243 yRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
798-986 |
4.16e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 798 FKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKST----VIGLIERFYDPDSGRVLLDGV---EIQKFKlnwlRQQIG 870
Cdd:TIGR00956 66 KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGItpeEIKKHY----RGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 LVGQEPVLFNE---------SIRANIAYGKPGDVTEEEIIAATTAanVHNVISSLPQGYDASVGE---RGVqlSGGQKQR 938
Cdd:TIGR00956 142 YNAETDVHFPHltvgetldfAARCKTPQNRPDGVSREEYAKHIAD--VYMATYGLSHTRNTKVGNdfvRGV--SGGERKR 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1562645982 939 IAIARAILKDPKILLLDEATSALDAESERKVQDALdRVMVN--RTTVVVA 986
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL-KTSANilDTTPLVA 266
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
784-1011 |
4.48e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 784 LSLLIGEIELDHVSFKyptrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERF--YDPDSGRVLLDGVEIQKFK 861
Cdd:CHL00131 3 KNKPILEIKNLHASVN-----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 862 LNwLRQQIG--LVGQEPVlfneSIraniaygkPGdVTEEEIIAAttAANVHNVISSLPQ-----------------GYDA 922
Cdd:CHL00131 78 PE-ERAHLGifLAFQYPI----EI--------PG-VSNADFLRL--AYNSKRKFQGLPEldplefleiineklklvGMDP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 923 SVGERGVQ--LSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVM-VNRTTVVVAH--RLSTIKGADI 997
Cdd:CHL00131 142 SFLSRNVNegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDY 221
|
250
....*....|....
gi 1562645982 998 IAVVKNGVIAEKGS 1011
Cdd:CHL00131 222 VHVMQNGKIIKTGD 235
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
510-726 |
4.49e-08 |
|
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: 55.88 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 510 KWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDAL 589
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQK--NRTGDLMARATNDLNAVRMALGPGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 590 ALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFCSE 669
Cdd:cd18541 119 LYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 670 KKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQAT 726
Cdd:cd18541 199 EAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTIT 255
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
791-1007 |
5.17e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDG-VEIQKFKLNWLRqqi 869
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAkVRMAVFSQHHVD--- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GL-VGQEPVLFnesiranIAYGKPGdVTEEEIIAATTAANVHNVISSLPQgydasvgergVQLSGGQKQRIAIARAILKD 948
Cdd:PLN03073 584 GLdLSSNPLLY-------MMRCFPG-VPEQKLRAHLGSFGVTGNLALQPM----------YTLSGGQKSRVAFAKITFKK 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 949 PKILLLDEATSALDAESERKVQDALdrVMVNRTTVVVAHRLSTIKGA-DIIAVVKNGVIA 1007
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISGSvDELWVVSEGKVT 703
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
791-974 |
5.95e-08 |
|
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: 56.48 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLL-DGVeiqkfklnwlrqQI 869
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEpvlfnesiRANIAygkPGDVTEEEIIAATTAANVHNV-ISSlpQGYDASVGERGV-------QLSGGQKQRIAI 941
Cdd:TIGR03719 388 AYVDQS--------RDALD---PNKTVWEEISGGLDIIKLGKReIPS--RAYVGRFNFKGSdqqkkvgQLSGGERNRVHL 454
|
170 180 190
....*....|....*....|....*....|...
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDALD 974
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
814-1004 |
6.08e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.00 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 814 LKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQKFKlnwlRQQIGLVG-----QEPVLFNESIrania 888
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP----GHQIARMGvvrtfQHVRLFREMT----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 889 ygkpgdVTEEEIIAATTAANVhNVISSL--PQGYDASVGE---RGVQ-----------------LSGGQKQRIAIARAIL 946
Cdd:PRK11300 97 ------VIENLLVAQHQQLKT-GLFSGLlkTPAFRRAESEaldRAATwlervgllehanrqagnLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562645982 947 KDPKILLLDEATSALDAESERKVQDALD--RVMVNRTTVVVAHRLSTIKG-ADIIAVVKNG 1004
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQG 230
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
463-626 |
7.89e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 55.18 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 463 KPEVPVLLLGAIAAAGHGVLFPifgLLLSKAIGMFYEPPNElrHDSRKWALVYVGLgcagLLVVPVQNFFFGVAGGKLVE 542
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFP---LLTKYAIDHFITPGTL--DGLTGFILLYLGL----ILIQALSVFLFIRLAGKIEM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 543 R----IRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVL 618
Cdd:cd18540 72 GvsydLRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVL 149
|
....*...
gi 1562645982 619 AVSPLILL 626
Cdd:cd18540 150 AVVPVLAV 157
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
511-727 |
1.06e-07 |
|
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: 54.78 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 511 WALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALA 590
Cdd:cd18545 42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDS--RPVGKILSRVINDVNSLSDLLSNGLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 591 LIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILlqgtLQAKFLKGFSADAKIMYEEASQVAN----DAIGSIRTVASF 666
Cdd:cd18545 120 NLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLV----LVVFLLRRRARKAWQRVRKKISNLNaylhESISGIRVIQSF 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 667 CSEKKVMEAYEKKCEGPLK---QGVRLGVVSGSGFGFSFFLmfcTNALIFYIGAILVKHGQATF 727
Cdd:cd18545 196 AREDENEEIFDELNRENRKanmRAVRLNALFWPLVELISAL---GTALVYWYGGKLVLGGAITV 256
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
511-678 |
1.19e-07 |
|
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: 54.41 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 511 WALVYVGLGCAGLLvvpvqnFFFG--VAGGKL---VE-RIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSL 584
Cdd:cd18543 41 LVLLLLALGVAEAV------LSFLrrYLAGRLslgVEhDLRTDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 585 VGDALaLIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVA 664
Cdd:cd18543 113 LAFGP-FLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVK 191
|
170
....*....|....
gi 1562645982 665 SFCSEKKVMEAYEK 678
Cdd:cd18543 192 AFGRERRELDRFEA 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
819-999 |
1.40e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 819 GKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDgveiqkfklnwLRqqiglvgqepvlfnesiranIAYgKPG----- 893
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------LK--------------------ISY-KPQyikpd 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 894 -DVTEEEIIAATTAA---NVHN--VIS--SLPQGYDASVGErgvqLSGGQKQRIAIARAILKDPKILLLDEATSALDAES 965
Cdd:PRK13409 413 yDGTVEDLLRSITDDlgsSYYKseIIKplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180 190
....*....|....*....|....*....|....*.
gi 1562645982 966 ERKVQDALDRVMVNR--TTVVVAHRLSTIkgaDIIA 999
Cdd:PRK13409 489 RLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
468-626 |
1.45e-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: 54.42 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 468 VLLLGAIAAAGhgVLFPifgLLLSKAI--GMfyeppneLRHDSRK-W--ALVYVGLGCAGLLVVPVQNFFFGVAGGKLVE 542
Cdd:cd18546 5 LLLVVVDTAAS--LAGP---LLVRYGIdsGV-------RAGDLGVlLlaAAAYLAVVLAGWVAQRAQTRLTGRTGERLLY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 543 RIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSP 622
Cdd:cd18546 73 DLRLRVFAHLQRLSLDFHER--ETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALP 150
|
....
gi 1562645982 623 LILL 626
Cdd:cd18546 151 PLAL 154
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
91-257 |
1.71e-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: 54.03 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 91 VSLKFVYLAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDTETStGEIIGRMSGDTiliqEAMGEMV-G 169
Cdd:cd18546 41 AAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETS-GRIMTRMTSDI----DALSELLqT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 170 KFIQLCS---TFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMAtimsRMSSRgqsAYAEA--------GSIVEqTVGS 238
Cdd:cd18546 116 GLVQLVVsllTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR----RRSSR---AYRRAreriaavnADLQE-TLAG 187
|
170
....*....|....*....
gi 1562645982 239 IRTVASFTGEKQAIEQYNQ 257
Cdd:cd18546 188 IRVVQAFRRERRNAERFAE 206
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
818-991 |
2.24e-07 |
|
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: 52.25 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 818 SGKTVALVGESGSGKSTV---------IGLIErfydpdsGRVLLDGveiQKFKLNWLRQqIGLVGQEPVLFNESirania 888
Cdd:cd03232 32 PGTLTALMGESGAGKTTLldvlagrktAGVIT-------GEILING---RPLDKNFQRS-TGYVEQQDVHSPNL------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 889 ygkpgdvteeeiiaattaanvhNVISSLpqgyDASVGERGvqLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERK 968
Cdd:cd03232 95 ----------------------TVREAL----RFSALLRG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|....
gi 1562645982 969 VQDALDRV-MVNRTTVVVAHRLST 991
Cdd:cd03232 147 IVRFLKKLaDSGQAILCTIHQPSA 170
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
810-998 |
3.28e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.00 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKSTVI------GLIERFY----DPDSGRVLlDGVEiqkfKLNWLRQqiglVGQEPV-- 877
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLHlkkeQPGNHDRI-EGLE----HIDKVIV----IDQSPIgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 878 -----------LFNEsIR-----------------------ANIAygkpgDVTEEEIIAA----TTAANVHNVISSLPQ- 918
Cdd:cd03271 83 tprsnpatytgVFDE-IRelfcevckgkrynretlevrykgKSIA-----DVLDMTVEEAleffENIPKIARKLQTLCDv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 919 --GYdASVGERGVQLSGGQKQRIAIARAILK---DPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTI 992
Cdd:cd03271 157 glGY-IKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVI 235
|
....*.
gi 1562645982 993 KGADII 998
Cdd:cd03271 236 KCADWI 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
819-999 |
3.50e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 819 GKTVALVGESGSGKSTVI----GLIErfydPDSGRVlldgveiqkfklnwlrqqiglvgqepvlfNESIRanIAYgKP-- 892
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAkilaGVLK----PDEGEV-----------------------------DEDLK--ISY-KPqy 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 893 ----GDVTEEEIIAATTAANV------HNVIS--SLPQGYDASVGErgvqLSGGQKQRIAIARAILKDPKILLLDEATSA 960
Cdd:COG1245 410 ispdYDGTVEEFLRSANTDDFgssyykTEIIKplGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1562645982 961 LDAESERKVQDALDRVMVNR--TTVVVAHRLSTIkgaDIIA 999
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS 523
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
511-669 |
4.81e-07 |
|
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: 52.95 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 511 WALVYVGLGCAGLLVVP--VQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDA 588
Cdd:cd18565 54 WLLGGLTVAAFLLESLFqyLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDDG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 589 LALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPLILL-----QGTLQAKFLKGFSADAKImyeeASQVANdAIGSIRTV 663
Cdd:cd18565 132 ANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAgtywfQRRIEPRYRAVREAVGDL----NARLEN-NLSGIAVI 206
|
....*.
gi 1562645982 664 ASFCSE 669
Cdd:cd18565 207 KAFTAE 212
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
470-681 |
5.98e-07 |
|
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: 52.45 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 470 LLGAIAAAGHGVLFPIF------GLLLSKAIGMFYeppnelrhdsrKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVER 543
Cdd:cd18549 8 LFCAVLIAALDLVFPLIvryiidDLLPSKNLRLIL-----------IIGAILLALYILRTLLNYFVTYWGHVMGARIETD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 544 IRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSPL 623
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDN--NKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 624 ILLQGTLQ-AKFLKGFSADAKIMYEEASQVaNDAIGSIRTVASFCSEKKVMEAYEKKCE 681
Cdd:cd18549 155 MIIFTIYFnKKMKKAFRRVREKIGEINAQL-EDSLSGIRVVKAFANEEYEIEKFDEGND 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
808-1015 |
6.51e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 808 IFRDICLKMPSGKTVALVGESGSGKSTVIG-LIERFYDPD-------SGRVLLDG---VEIQKFKLNWLRQQIGLVGQEP 876
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGaprgarvTGDVTLNGeplAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 877 VLFneSIRANIAYG------KPGDVTEE--EIIAATTAAnvhnvisslpQGYDASVGERGVQLSGGQKQRIAIARAILK- 947
Cdd:PRK13547 96 FAF--SAREIVLLGrypharRAGALTHRdgEIAWQALAL----------AGATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 948 --------DPKILLLDEATSALDAESERKVQDALDRVMV--NRTTVVVAHRLS-TIKGADIIAVVKNGVIAEKGS-HDFL 1015
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGApADVL 243
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
819-965 |
7.92e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 819 GKTVALVGESGSGKSTVI---------GLIErfydpdSGRVLLDGVEIQK-FKlnwlrQQIGLVGQ-----EPVLFNESI 883
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLnvlaervttGVIT------GGDRLVNGRPLDSsFQ-----RSIGYVQQqdlhlPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 884 RANIAYGKPGDVTEEEiiaatTAANVHNVISSLP-QGY-DASVGERGVQLSGGQKQRIAIARAILKDPKILL-LDEATSA 960
Cdd:TIGR00956 858 RFSAYLRQPKSVSKSE-----KMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
....*
gi 1562645982 961 LDAES 965
Cdd:TIGR00956 933 LDSQT 937
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
791-1013 |
8.43e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRPdvqIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVlldgveiqkfklNWlrqqig 870
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 lvgqepvlfneSIRANIAYgKPGDVTEEeiiaATTAANVHNVISSLPQGYDASVGERGV----------------QLSGG 934
Cdd:PRK15064 379 -----------SENANIGY-YAQDHAYD----FENDLTLFDWMSQWRQEGDDEQAVRGTlgrllfsqddikksvkVLSGG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 935 QKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDrvMVNRTTVVVAH------RLSTikgaDIIAVVKNGVIAE 1008
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSHdrefvsSLAT----RIIEITPDGVVDF 516
|
....*
gi 1562645982 1009 KGSHD 1013
Cdd:PRK15064 517 SGTYE 521
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
930-989 |
9.05e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 9.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 930 QLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVVVAHRL 989
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
818-1001 |
1.22e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 818 SGKTVALVGESGSGKSTVIGLIE--------RFYDPDSGRVLLD---GVEIQKFKLNWLRQQIGL------VGQEPVLFN 880
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpqyVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 881 ESIRANIaygKPGDVTE--EEIIAATTAANVHnvisslpqgydasvgERGV-QLSGGQKQRIAIARAILKDPKILLLDEA 957
Cdd:cd03236 105 GKVGELL---KKKDERGklDELVDQLELRHVL---------------DRNIdQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1562645982 958 TSALDAESERKVQDAL-DRVMVNRTTVVVAHRLSTIKG-ADIIAVV 1001
Cdd:cd03236 167 SSYLDIKQRLNAARLIrELAEDDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
929-1001 |
1.22e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 1.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 929 VQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVN--RTTVVVAHRLSTIKG-ADIIAVV 1001
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYlSDRIHVF 145
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
89-208 |
1.87e-06 |
|
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: 50.93 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 89 SKVSLKF---VYLAIGTGAAALLQVAC-WMVTGERQAAR-IRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEA 163
Cdd:cd18604 38 SEVSVLYylgIYALISLLSVLLGTLRYlLFFFGSLRASRkLHERLLHSVLRAPLRWLDT-TPVGRILNRFSKDIETIDSE 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1562645982 164 MGEMVGKFIQLCSTFLGGFVIAFVkgwrltVVLLATIPAIVIAGA 208
Cdd:cd18604 117 LADSLSSLLESTLSLLVILIAIVV------VSPAFLLPAVVLAAL 155
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
95-205 |
2.31e-06 |
|
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: 50.68 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 95 FVYLAIGTGAAALLQVACWMVTGERQAARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQE---AMGEMVGKF 171
Cdd:cd18602 56 YAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDT-TPIGRILNRFSSDTNVIDQklpTTLERLLRF 134
|
90 100 110
....*....|....*....|....*....|....*
gi 1562645982 172 IQLCstfLGGFVI-AFVKGWrltvVLLATIPAIVI 205
Cdd:cd18602 135 LLLC---LSAIIVnAIVTPY----FLIALIPIIIV 162
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
791-987 |
3.42e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPTRpdvQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRV-LLDGVEIQKF---KLNWLR 866
Cdd:PRK10636 313 LKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFaqhQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 867 QQIG----LVGQEPVLFNESIRANI-AYGKPGD-VTEEeiiaatTAanvhnvisslpqgydasvgergvQLSGGQKQRIA 940
Cdd:PRK10636 390 ADESplqhLARLAPQELEQKLRDYLgGFGFQGDkVTEE------TR-----------------------RFSGGEKARLV 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1562645982 941 IARAILKDPKILLLDEATSALDAESERKVQDALdrVMVNRTTVVVAH 987
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGALVVVSH 485
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
802-1004 |
3.63e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 802 TRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDS--GRVLLDGvEIQKFKLnwLRQ--QIGLV--GQE 875
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG-EVCRFKD--IRDseALGIViiHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 876 ----PVLfneSIRANIAYG----KPGDVTEEEIIAATTA--ANVhnvisSLPQGYDASVGERGVqlsgGQKQRIAIARAI 945
Cdd:NF040905 87 laliPYL---SIAENIFLGneraKRGVIDWNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 946 LKDPKILLLDEATSAL-DAESERkvqdALDRVMVNR----TTVVVAHRLSTI-KGADIIAVVKNG 1004
Cdd:NF040905 155 SKDVKLLILDEPTAALnEEDSAA----LLDLLLELKaqgiTSIIISHKLNEIrRVADSITVLRDG 215
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
132-301 |
4.07e-06 |
|
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: 49.84 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 132 ILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEMVGKFIQLCSTFLGGFVIAFVKGWRLTVVLLATIPAIVIAGAVMA 211
Cdd:cd18778 83 LQRLSLRYFDD-RQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 212 TIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYALA 291
Cdd:cd18778 162 KKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLV 241
|
170
....*....|
gi 1562645982 292 VWYGSKMIIK 301
Cdd:cd18778 242 LGFGGRLVLA 251
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
470-679 |
4.07e-06 |
|
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: 49.84 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 470 LLGAIAAAGHGVLFPifgLLLSKAIGMFYEPPNELrhdSRKWALVYVGLGCAGLlvvpvQNFFFG-------VAGGKLVE 542
Cdd:cd18778 5 LLCALLSTLLGLVPP---WLIRELVDLVTIGSKSL---GLLLGLALLLLGAYLL-----RALLNFlriylnhVAEQKVVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 543 RIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVSP 622
Cdd:cd18778 74 DLRSDLYDKLQRLSLRYFDD--RQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 623 LILLQGTLqakflkgFSADAKIMYEEASQVA-------NDAIGSIRTVASFcsekkVMEAYEKK 679
Cdd:cd18778 152 FLALGAWL-------YSKKVRPRYRKVREALgelnallQDNLSGIREIQAF-----GREEEEAK 203
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
95-205 |
4.87e-06 |
|
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: 49.42 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 95 FVYLAIGTGAAALLQVACWMVT---GERQAARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEMVGKF 171
Cdd:cd18580 42 GVYAALLVLASVLLVLLRWLLFvlaGLRASRRLHDKLLRSVLRAPMSFFDT-TPSGRILNRFSKDIGLIDEELPLALLDF 120
|
90 100 110
....*....|....*....|....*....|....
gi 1562645982 172 IQLCSTFLGGFVIAFVKGWrltVVLLATIPAIVI 205
Cdd:cd18580 121 LQSLFSVLGSLIVIAIVSP---YFLIVLPPLLVV 151
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
810-998 |
9.52e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.32 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKSTViglierfydpdsgrvLLDGVEIQKFKLnwLRQQIGLVGQEPVLFNESIRANIAY 889
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTL---------------VNEGLYASGKAR--LISFLPKFSRNKLIFIDQLQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 890 GkpgdvteeeiiaattaanvhnvISSLPQGYDASVgergvqLSGGQKQRIAIARAILKDPK--ILLLDEATSALDAESER 967
Cdd:cd03238 75 G----------------------LGYLTLGQKLST------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|..
gi 1562645982 968 KVQDALDRVMVNRTTV-VVAHRLSTIKGADII 998
Cdd:cd03238 127 QLLEVIKGLIDLGNTViLIEHNLDVLSSADWI 158
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
811-998 |
1.27e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 811 DICLK-MPSGKTVaLVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEI---QKFKLNWLRQQIGLVGQEPVLFNESIRAN 886
Cdd:PRK13541 18 DLSITfLPSAITY-IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniAKPYCTYIGHNLGLKLEMTVFENLKFWSE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 887 IaYGkpgdvTEEEIIAATTAANVHNVISslpqgydasvgERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESe 966
Cdd:PRK13541 97 I-YN-----SAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN- 158
|
170 180 190
....*....|....*....|....*....|....
gi 1562645982 967 RKVQDALDRVMVNRTTVVV--AHRLSTIKGADII 998
Cdd:PRK13541 159 RDLLNNLIVMKANSGGIVLlsSHLESSIKSAQIL 192
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
506-636 |
1.32e-05 |
|
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: 48.27 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 506 HDSRKWALVYVGLGCAG-LLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSL 584
Cdd:cd18580 35 SSSGYYLGVYAALLVLAsVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFD--TTPSGRILNRFSKDIGLIDEE 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 585 VGDALALIVQNIATIMAGLVIGFTANWkLMLVVLAvsPLILLQGTLQAKFLK 636
Cdd:cd18580 113 LPLALLDFLQSLFSVLGSLIVIAIVSP-YFLIVLP--PLLVVYYLLQRYYLR 161
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
819-962 |
1.62e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 819 GKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiqkfklNWlrqQIGLVGQE-PVLfnesIRANIAYGKPGDVTE 897
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------NW---QLAWVNQEtPAL----PQPALEYVIDGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 898 EEIIAATTAANVHN---VISSLPQGYDA----SVGERGVQL------------------SGGQKQRIAIARAILKDPKIL 952
Cdd:PRK10636 92 RQLEAQLHDANERNdghAIATIHGKLDAidawTIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSDLL 171
|
170
....*....|
gi 1562645982 953 LLDEATSALD 962
Cdd:PRK10636 172 LLDEPTNHLD 181
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
802-1008 |
2.28e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 802 TRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEIQ-KFKLNWLRQQIGLVGQ---EPV 877
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 878 LF-NESIRANIAY----------GKPG--DVTEEEIIAATTAANVHNVISSLPQgydaSVGErgvqLSGGQKQRIAIARA 944
Cdd:PRK09700 352 FFpNFSIAQNMAIsrslkdggykGAMGlfHEVDEQRTAENQRELLALKCHSVNQ----NITE----LSGGNQQKVLISKW 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 945 ILKDPKILLLDEATSALD--AESE-----RKVQDAldrvmvNRTTVVVAHRLSTIKGA-DIIAVVKNGVIAE 1008
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDvgAKAEiykvmRQLADD------GKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
514-626 |
2.51e-05 |
|
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: 47.47 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 514 VYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTIKSLVGDALALIV 593
Cdd:cd18606 40 IYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD--TTPLGRILNRFSKDTDVLDNELPDSLRMFL 117
|
90 100 110
....*....|....*....|....*....|....*...
gi 1562645982 594 QNIATIMAGLVigftanwkLMLVVL-----AVSPLILL 626
Cdd:cd18606 118 YTLSSIIGTFI--------LIIIYLpwfaiALPPLLVL 147
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
568-746 |
3.56e-05 |
|
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: 46.82 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 568 GAIGARLStDASTIKS-LVGDALALIVQNIATIMAgLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMY 646
Cdd:cd18782 99 GELSTRIS-ELDTIRGfLTGTALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEAS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 647 EEASQVANDAIGSIRTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQAT 726
Cdd:cd18782 177 AKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELT 256
|
170 180
....*....|....*....|
gi 1562645982 727 FEQvfkvFFAITITAMGVSQ 746
Cdd:cd18782 257 LGQ----LIAFRILSGYVTG 272
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
931-998 |
4.17e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 4.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 931 LSGGQKQRIAIARAILKD---PKILLLDEATSALDAESERKVQDALDRVMVNRTTVVV-AHRLSTIKGADII 998
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKTADYI 901
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
819-1013 |
4.67e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 819 GKTVALVGESGSGKSTVI---------GL--------IERFYDPDSGRVL---LDgVEIQKFKLnwLRQQIGLVGQEPVL 878
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLrymamhaidGIpkncqilhVEQEVVGDDTTALqcvLN-TDIERTQL--LEEEAQLVAQQREL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 879 FNESIRANIAYGKPGDVTEE-------------EIIAATTA-ANVHNVISSLPQGYDASVgERGVQLSGGQKQRIAIARA 944
Cdd:PLN03073 280 EFETETGKGKGANKDGVDKDavsqrleeiykrlELIDAYTAeARAASILAGLSFTPEMQV-KATKTFSGGWRMRIALARA 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1562645982 945 ILKDPKILLLDEATSALDAESERKVQDALdrVMVNRTTVVVAHR---LSTIKgADIIAVVKNGVIAEKGSHD 1013
Cdd:PLN03073 359 LFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHArefLNTVV-TDILHLHGQKLVTYKGDYD 427
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
796-1016 |
5.73e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.33 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 796 VSFKYPTRPdVQIFRDICLKMPSGKTVALVGESGSGKS----TVIGLIERFYDPDSGRVLLDGVEIQKFKLNWLRQQIG- 870
Cdd:PRK15093 11 IEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSPRERRKLVGh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 871 ---LVGQEP---VLFNESIRANIAYGKPGDVTEE--------------EIIAATTAANVHNVISSLPqgydasvgergVQ 930
Cdd:PRK15093 90 nvsMIFQEPqscLDPSERVGRQLMQNIPGWTYKGrwwqrfgwrkrraiELLHRVGIKDHKDAMRSFP-----------YE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 931 LSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVV--VAHRLSTI-KGADIIAVVKNGVIA 1007
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLsQWADKINVLYCGQTV 238
|
....*....
gi 1562645982 1008 EKGSHDFLM 1016
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
930-991 |
6.77e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 6.77e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 930 QLSGGQKQRIAIARAILKDPKILLLDEATSALD----AESERKVQDALDRvmvNRTTVVVAHRLST 991
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAI 274
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
931-965 |
8.03e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 8.03e-05
10 20 30
....*....|....*....|....*....|....*
gi 1562645982 931 LSGGQKQRIAIARAILKDPKILLLDEATSALDAES 965
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
788-962 |
8.23e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 788 IGEI--ELDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKS----TVIGlieRFYDPD-SGRVLLDGVEIQkf 860
Cdd:NF040905 253 IGEVvfEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTelamSVFG---RSYGRNiSGTVFKDGKEVD-- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 861 klnwlrqqIGLVGqepvlfnESIRANIAYgkpgdVTE----------EEIIAATTAANV-----HNVISS-----LPQGY 920
Cdd:NF040905 328 --------VSTVS-------DAIDAGLAY-----VTEdrkgyglnliDDIKRNITLANLgkvsrRGVIDEneeikVAEEY 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1562645982 921 DA-------SVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALD 962
Cdd:NF040905 388 RKkmniktpSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
584-741 |
1.09e-04 |
|
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: 45.24 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 584 LVGDALALIVqNIATIMAGLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAkimYEEASQVAN---DAIGSI 660
Cdd:cd18568 115 LTRSALTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREI---FQANAEQQSflvEALTGI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 661 RTVASFCSEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQV--FKVFFAIT 738
Cdd:cd18568 191 ATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLvaFNMLFGSV 270
|
...
gi 1562645982 739 ITA 741
Cdd:cd18568 271 INP 273
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
809-987 |
1.23e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 809 FRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGVEiqkfKLNWLRQ-QIG----------LVGQEPV 877
Cdd:PRK15064 17 FENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE----RLGKLRQdQFAfeeftvldtvIMGHTEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 878 LFNESIRANIaYGKPgDVTEEEIIAAttaANVHNVISSLpQGYDA--SVGE--RGV------------QLSGGQKQRIAI 941
Cdd:PRK15064 93 WEVKQERDRI-YALP-EMSEEDGMKV---ADLEVKFAEM-DGYTAeaRAGEllLGVgipeeqhyglmsEVAPGWKLRVLL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1562645982 942 ARAILKDPKILLLDEATSALDAESERKVQDAL-DRvmvNRTTVVVAH 987
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDINTIRWLEDVLnER---NSTMIIISH 210
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
921-990 |
1.46e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 1.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562645982 921 DASVGERGVQ-LSGGQKQRIAIARAILKDPKILLLDEATSALDAESE----RKVQDALDrvmVNRTTVVVAHRLS 990
Cdd:PLN03140 1009 DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAaivmRTVRNTVD---TGRTVVCTIHQPS 1080
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
123-219 |
1.67e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.48 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 123 RIRGKYMKAILRQDIGFFDTEtSTGEIIGRMSGDTILIQEAMGEMVGKFIQlCSTFLGGFVIA-FVKGWRLTVVLLATIP 201
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQ-PVGQLISRVTNDTEVIRDLYVTVVATVLR-SAALIGAMLVAmFSLDWRMALVAIMIFP 176
|
90
....*....|....*...
gi 1562645982 202 AIVIagaVMAtIMSRMSS 219
Cdd:PRK10790 177 AVLV---VMV-IYQRYST 190
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
45-301 |
1.98e-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: 44.39 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 45 VALMIVGTISAVGNGLSkPLMTlvfGNLINTFgctdpghIVPmisKVSLKFVYLAIGTGAAALLQVAC-WMVTgeRQAAR 123
Cdd:cd18540 5 ILLIILMLLVALLDAVF-PLLT---KYAIDHF-------ITP---GTLDGLTGFILLYLGLILIQALSvFLFI--RLAGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 124 IRGKYMKAiLRQD---------IGFFDTeTSTGEIIGRMSGDTiliqEAMGEMVG-KFIQLC---STFLGGFVIAFVKGW 190
Cdd:cd18540 69 IEMGVSYD-LRKKafehlqtlsFSYFDK-TPVGWIMARVTSDT----QRLGEIISwGLVDLVwgiTYMIGILIVMLILNW 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 191 RLTVVLLATIPAIVIAGAVMATIM-------SRMSSRGQSAYAEagSIVeqtvgSIRTVASFTGEKQAIEQYNQKLKVAY 263
Cdd:cd18540 143 KLALIVLAVVPVLAVVSIYFQKKIlkayrkvRKINSRITGAFNE--GIT-----GAKTTKTLVREEKNLREFKELTEEMR 215
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1562645982 264 NTMVQQGLVTgiglGIFM-LVIFCSY---ALAVWYGSKMIIK 301
Cdd:cd18540 216 RASVRAARLS----ALFLpIVLFLGSiatALVLWYGGILVLA 253
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
95-310 |
2.27e-04 |
|
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: 44.50 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 95 FVYLAIGTGAAALL---------QVACWmvTGERQAARIRGKYMKAILRQDIGFFDTETStGEIIGRM-SGDTILIQEAm 164
Cdd:cd18566 41 LQVLVIGVVIAILLesllrllrsYILAW--IGARFDHRLSNAAFEHLLSLPLSFFEREPS-GAHLERLnSLEQIREFLT- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 165 GEMVGKFIQLCSTFLGGFVIAFVKGWrLTVVLLATIPAIVIAGAVMATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVAS 244
Cdd:cd18566 117 GQALLALLDLPFVLIFLGLIWYLGGK-LVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562645982 245 FTGEKQAIEQYNQKLKVAYNTMVQQGLVTGIGLGIFMLVIFCSYALAVWYGSKMIIKHGYNGGQVI 310
Cdd:cd18566 196 MAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALI 261
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
788-962 |
2.43e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.82 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 788 IGE--IELDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPD-SGRVLLDGVEIQ-KFKLN 863
Cdd:TIGR02633 253 IGDviLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 864 WLRQQI----------GLVGQEPVLFNESIRANIAYGKPGDVTEEE----IIAATTAANVHNVISSLPQGydasvgergv 929
Cdd:TIGR02633 333 AIRAGIamvpedrkrhGIVPILGVGKNITLSVLKSFCFKMRIDAAAelqiIGSAIQRLKVKTASPFLPIG---------- 402
|
170 180 190
....*....|....*....|....*....|...
gi 1562645982 930 QLSGGQKQRIAIARAILKDPKILLLDEATSALD 962
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
132-319 |
2.79e-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: 350055 [Multi-domain] Cd Length: 294 Bit Score: 44.12 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 132 ILRQDIGFFDTETsTGEIIGRMSG-DTILiQEAMGEMVGKFIQLCSTFLGGFVIaFVKGWRLTVVLLATIPAIVIAGAVM 210
Cdd:cd18782 85 LLRLPLGFFDKRP-VGELSTRISElDTIR-GFLTGTALTTLLDVLFSVIYIAVL-FSYSPLLTLVVLATVPLQLLLTFLF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 211 ATIMSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAI----EQYNQKLKVAYNT----MVQQGLVTGIGLGIFML 282
Cdd:cd18782 162 GPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARwrwqNRYARSLGEGFKLtvlgTTSGSLSQFLNKLSSLL 241
|
170 180 190
....*....|....*....|....*....|....*..
gi 1562645982 283 VIfcsyalavWYGSKMIIKHGYNGGQVInvIFALMTG 319
Cdd:cd18782 242 VL--------WVGAYLVLRGELTLGQLI--AFRILSG 268
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
923-999 |
4.10e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 923 SVGERGVQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRTTVV-----------VAHRLST 991
Cdd:NF000106 137 AAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHELTV 216
|
....*...
gi 1562645982 992 IKGADIIA 999
Cdd:NF000106 217 IDRGRVIA 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
931-962 |
4.13e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 4.13e-04
10 20 30
....*....|....*....|....*....|..
gi 1562645982 931 LSGGQKQRIAIARAILKDPKILLLDEATSALD 962
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
788-962 |
5.19e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 788 IGEI--ELDHVSFKYPTRPDVQIFRDICLKMPSGKTVALVGESGSGKS-TVIGLIERFYDPDSGRVLLDGveiQKFKLNW 864
Cdd:PRK13549 255 IGEVilEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDG---KPVKIRN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 865 LRQQI--------------GLVGQEPVLFNESIRANIAYGKPG--DVTEEEIIAATTAANVHNVISSLpqgyDASVGerg 928
Cdd:PRK13549 332 PQQAIaqgiamvpedrkrdGIVPVMGVGKNITLAALDRFTGGSriDDAAELKTILESIQRLKVKTASP----ELAIA--- 404
|
170 180 190
....*....|....*....|....*....|....
gi 1562645982 929 vQLSGGQKQRIAIARAILKDPKILLLDEATSALD 962
Cdd:PRK13549 405 -RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
122-258 |
8.74e-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: 42.50 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 122 ARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMsgdtiliQEAmgEMVGKFI--QLCSTFLGGFV------IAFVKGWRLT 193
Cdd:cd18783 75 ARLALRTFDRLLSLPIDFFER-TPAGVLTKHM-------QQI--ERIRQFLtgQLFGTLLDATSllvflpVLFFYSPTLA 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 194 VVLLATipAIVIAGAVMATI--MSRMSSRGQSAYAEAGSIVEQTVGSIRTVASFTGEKQAIEQYNQK 258
Cdd:cd18783 145 LVVLAF--SALIALIILAFLppFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDER 209
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
791-986 |
1.18e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 791 IELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIerfydpdSG-RVLldgveiqkfklnwlrQQi 869
Cdd:NF033858 2 ARLEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGaRKI---------------QQ- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 glvGQEPVL--------FNESIRANIAY-----GK---PGDVTEEEI-----------------IAATTAAnvhnviSSL 916
Cdd:NF033858 56 ---GRVEVLggdmadarHRRAVCPRIAYmpqglGKnlyPTLSVFENLdffgrlfgqdaaerrrrIDELLRA------TGL 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562645982 917 pqgydASVGER--GvQLSGGQKQRIAIARAILKDPKILLLDEATSALDAESERKVQDALDRVMVNRT--TVVVA 986
Cdd:NF033858 127 -----APFADRpaG-KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVA 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
812-1007 |
1.37e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 812 ICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLDGveiqkfklnwlrqqiglvgqEPVLFN---ESIRANIA 888
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG--------------------KPIDIRsprDAIRAGIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 889 YGkPGDVTEEEIIA-ATTAANVHnvISS----------LPQGYDASVGERGVQ---------------LSGGQKQRIAIA 942
Cdd:PRK11288 332 LC-PEDRKAEGIIPvHSVADNIN--ISArrhhlragclINNRWEAENADRFIRslniktpsreqlimnLSGGNQQKAILG 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562645982 943 RAILKDPKILLLDEATSALDAESERKVQDAL-DRVMVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIA 1007
Cdd:PRK11288 409 RWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| DLIC |
pfam05783 |
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ... |
815-851 |
1.52e-03 |
|
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein light intermediate chain proteins. The light intermediate chains (LICs) of cytoplasmic dynein consist of multiple isoforms, which undergo post-translational modification to produce a large number of species. DLIC1 is known to be involved in assembly, organization, and function of centrosomes and mitotic spindles when bound to pericentrin. DLIC2 is a subunit of cytoplasmic dynein 2 that may play a role in maintaining Golgi organization by binding cytoplasmic dynein 2 to its Golgi-associated cargo.
Pssm-ID: 368612 Cd Length: 468 Bit Score: 42.14 E-value: 1.52e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1562645982 815 KMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVL 851
Cdd:pfam05783 21 KLPSGKNVLVLGEDGSGKTTLIAKLQGVEHPKKGRGL 57
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
794-962 |
1.63e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 794 DHVSFkyptrpdvQIFRdiclkmpsGKTVALVGESGSGKSTVI----GLIerfyDPDSGRVLLDGVEIQKFKLNwLRQQI 869
Cdd:NF033858 283 DHVSF--------RIRR--------GEIFGFLGSNGCGKSTTMkmltGLL----PASEGEAWLFGQPVDAGDIA-TRRRV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 GLVGQEPVLFNE-SIRANIA-----YGKPGDVTEEEIIAATTAANVHNVISSLPQGydasvgergvqLSGGQKQRIAIAR 943
Cdd:NF033858 342 GYMSQAFSLYGElTVRQNLElharlFHLPAAEIAARVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAV 410
|
170
....*....|....*....
gi 1562645982 944 AILKDPKILLLDEATSALD 962
Cdd:NF033858 411 AVIHKPELLILDEPTSGVD 429
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
810-1007 |
1.92e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 810 RDICLKMPSGKTVALVGESGSGKS----TVIGLIERfydpDSGRVLLDGVEIQKFKLNWL-----------RQQIGLVGQ 874
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTdiveTLFGIREK----SAGTITLHGKKINNHNANEAinhgfalvteeRRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 875 EPVLFNeSIRANI-AY-GKPGDVTEEEIIAATTAanvhnVISSL---PQGYDASVGergvQLSGGQKQRIAIARAILKDP 949
Cdd:PRK10982 341 LDIGFN-SLISNIrNYkNKVGLLDNSRMKSDTQW-----VIDSMrvkTPGHRTQIG----SLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 950 KILLLDEATSALDAESERKV-QDALDRVMVNRTTVVVAHRLSTIKG-ADIIAVVKNGVIA 1007
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVA 470
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
510-742 |
2.96e-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: 40.84 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 510 KWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDDpaNSSGAIGARLSTDASTIKSLVGDAL 589
Cdd:cd18548 40 RTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDK--FGTSSLITRLTNDVTQVQNFVMMLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 590 ALIVqnIATIMA--GLVIGFTANWKLMLVVLAVSPLILLQGTLQAKFLKGFSADAKIMYEEASQVANDAIGSIRTVASFC 667
Cdd:cd18548 118 RMLV--RAPIMLigAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 668 SEKKVMEAYEKKCEGPLKQGVRLGVVSGSGFGFSFFLMFCTNALIFYIGAILVKHGQATFEQV-------FKVFFAITIT 740
Cdd:cd18548 196 REDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMML 275
|
..
gi 1562645982 741 AM 742
Cdd:cd18548 276 SM 277
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
506-621 |
3.29e-03 |
|
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: 40.91 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 506 HDSRKWALVYVGLGCAGLLVVPVQNFFFgVAGGklverIRAlS---FQK----VVHQQVSWFDdpANSSGAIGARLSTDA 578
Cdd:cd18604 40 VSVLYYLGIYALISLLSVLLGTLRYLLF-FFGS-----LRA-SrklHERllhsVLRAPLRWLD--TTPVGRILNRFSKDI 110
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1562645982 579 STIKSLVGDALALIVQNIATIMAGLVIGFTANWKLMLVVLAVS 621
Cdd:cd18604 111 ETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLA 153
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
96-213 |
3.30e-03 |
|
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: 40.54 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 96 VYLAIGTGAAALL--QVACWMVTGERQAARIRGKYMKAILRQDIGFFDTeTSTGEIIGRMSGDTILIQEAMGEMVGKFIQ 173
Cdd:cd18606 40 IYAGLGVLQAIFLflFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDT-TPLGRILNRFSKDTDVLDNELPDSLRMFLY 118
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1562645982 174 LCSTFLGGFVIAFVkgwrltvvllaTIPAIVIAGAVMATI 213
Cdd:cd18606 119 TLSSIIGTFILIII-----------YLPWFAIALPPLLVL 147
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
792-964 |
3.55e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 792 ELDHVSFKYPtrpDVQIFRDICLKMPSGKTVALVGESGSGKSTVIGLIERFYDPDSGRVLLdG--VEIQKFklNWLRQQI 869
Cdd:PRK11147 321 EMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GtkLEVAYF--DQHRAEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 870 glvgqEPvlfNESIRANIAYGKpgdvteEEIiaaTTAANVHNVISSL------PQgydasvgeRGVQ----LSGGQKQRI 939
Cdd:PRK11147 395 -----DP---EKTVMDNLAEGK------QEV---MVNGRPRHVLGYLqdflfhPK--------RAMTpvkaLSGGERNRL 449
|
170 180
....*....|....*....|....*
gi 1562645982 940 AIARAILKDPKILLLDEATSALDAE 964
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
809-851 |
5.69e-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: 40.37 E-value: 5.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1562645982 809 FRDICLKMPSGKTVaLVGESGSGKSTVIGLIERFYDPDSGRVL 851
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSRKF 55
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
929-1002 |
6.99e-03 |
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ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.49 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 929 VQLSGGQKQRIAIA-----RAILKDPkILLLDEATSALDAESERKVQDALDRVMVNRTTVVVA-HRLSTIKGADIIAVVK 1002
Cdd:cd03227 76 LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVItHLPELAELADKLIHIK 154
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| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
502-634 |
7.27e-03 |
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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: 39.82 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 502 NELRHDSRKWALVYVGLGCAGLLVVPVQNFFFGVAGGKLVERIRALSFQKVVHQQVSWFDdpANSSGAIGARLSTDASTI 581
Cdd:cd18605 35 NFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFD--KTPVGRILNRFSSDVYTI 112
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1562645982 582 KslvgDALALIVQNIATIMAGL-----VIGFTANWklMLVVLAvsPLILLQGTLQAKF 634
Cdd:cd18605 113 D----DSLPFILNILLAQLFGLlgylvVICYQLPW--LLLLLL--PLAFIYYRIQRYY 162
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| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
96-205 |
7.43e-03 |
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Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, 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: 350047 [Multi-domain] Cd Length: 296 Bit Score: 39.77 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562645982 96 VYLAIGTGAAALLQVACWMVT-GERQAARIRGKYM-KAILRQDIGFFDTeTSTGEIIGRMSGDT----ILIQEAMGEMVG 169
Cdd:cd18603 46 VYGALGLGQAIFVFLGSLALAlGCVRASRNLHNKLlHNILRAPMSFFDT-TPLGRILNRFSKDIdtvdNTLPQNIRSFLN 124
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90 100 110
....*....|....*....|....*....|....*.
gi 1562645982 170 KFIQLCSTFlggFVIAFVKGWRLTVVllatIPAIVI 205
Cdd:cd18603 125 CLFQVISTL---VVISISTPIFLVVI----IPLAIL 153
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| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
930-975 |
9.76e-03 |
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SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.44 E-value: 9.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1562645982 930 QLSGGQKQRIA-------------IARAILKDPKILLLDEATSALDAESERKVQDALDR 975
Cdd:pfam13558 32 GLSGGEKQLLAylplaaalaaqygSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
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