|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
59-296 |
3.34e-152 |
|
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: 444.68 E-value: 3.34e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
361-677 |
2.76e-147 |
|
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: 435.34 E-value: 2.76e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 361 LKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEILGVFAILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSG 440
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 441 EYLTLRLRSMSFKAMLRQEIAFFDDHNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLV 520
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 521 IAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIG 600
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 601 FSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKKPDI 677
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-300 |
1.68e-133 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 409.55 E-value: 1.68e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 19 LQTLATARGAAYYLYQLITMDPPIDSySTEGKKLDNFQGNVQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGC 98
Cdd:COG1132 301 LNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 99 GKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHD 178
Cdd:COG1132 378 GKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 179 FIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLST 258
Cdd:COG1132 458 FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLST 537
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2119559688 259 IKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQSMKS 300
Cdd:COG1132 538 IRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-296 |
5.15e-117 |
|
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: 370.70 E-value: 5.15e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 3 FSVMIGAF--SLGNAMPHLQTLATARGAAYYLYQLitMDPPIDSYSTEGKK-LDNFQGNVQIRGVHFRYPSRpEAKILYG 79
Cdd:COG2274 417 FNILSGRFlaPVAQLIGLLQRFQDAKIALERLDDI--LDLPPEREEGRSKLsLPRLKGDIELENVSFRYPGD-SPPVLDN 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGH 159
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 160 LDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDA 239
Cdd:COG2274 574 PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN 653
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 240 LEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:COG2274 654 LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
59-292 |
1.06e-116 |
|
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: 353.07 E-value: 1.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQL 292
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-822 |
1.76e-114 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 380.14 E-value: 1.76e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 1 VFFSVMIGAFSLGNAMPHLQTLATARGAAYYLYQLITMDPPIDSySTEGKKLDNFQgNVQIRGVHFRYPSRPEAKILYGV 80
Cdd:PTZ00265 327 ILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 81 NLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI-DGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRY-- 157
Cdd:PTZ00265 405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYsl 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 158 ------------------------------------------------GHLDVTKE-------DIEQAAKMANAHDFIMD 182
Cdd:PTZ00265 485 yslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnELIEMRKNyqtikdsEVVDVSKKVLIHDFVSA 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 183 LPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIK 260
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIR 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 261 TADMI------------------------------------AGFKD-----------GVVAEQGTHNELM-SKQGIYQQL 292
Cdd:PTZ00265 645 YANTIfvlsnrergstvdvdiigedptkdnkennnknnkddNNNNNnnnnnkinnagSYIIEQGTHDALMkNKNGIYYTM 724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 293 VTLQSMKSADDNEIEDFNRDDTKRPSLRHQKSTIDmtPKKLAQDKKEEIKEEEKGEKEEEVDAS------------LGRI 360
Cdd:PTZ00265 725 INNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYD--PDEMNGNSKHENESASNKKSCKMSDENasennaggklpfLRNL 802
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 361 LKlNKSEAPF---------------IVMGCFASLVNGGAMPAFAVIFSEILGvfAILDEGEQERKIIQYVLMFVGVGVIS 425
Cdd:PTZ00265 803 FK-RKPKAPNnlrivyreifsykkdVTIIALSILVAGGLYPVFALLYAKYVS--TLFDFANLEANSNKYSLYILVIAIAM 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 426 LIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHNNSVGALTTRLATDASQVQGA-----------AGIKLGS 494
Cdd:PTZ00265 880 FISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGlvnnivifthfIVLFLVS 959
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 495 SLMA--FCSVVTGIVIGFVFswkITLLVIAFLPFVMIGGALEMQMMQGAAG-----KNKEALESAGKIAIESIENIRTVA 567
Cdd:PTZ00265 960 MVMSfyFCPIVAAVLTGTYF---IFMRVFAIRARLTANKDVEKKEINQPGTvfaynSDDEIFKDPSFLIQEAFYNMNTVI 1036
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 568 SLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAI 647
Cdd:PTZ00265 1037 IYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYA 1116
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 648 GNASAFAPDAAKAEQSAKEIFKLIDKKPDIDNESEKGEQLHT---FTANLSFANIIFRYPTRPDTTILKGLDLEVPQGQT 724
Cdd:PTZ00265 1117 GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKT 1196
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 725 VALVGSSGCGKSTTVQLTERFYDPAD------------------------------------------------------ 750
Cdd:PTZ00265 1197 TAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkns 1276
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 751 GIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGdnSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACKFAAIDEFIESLPN 1346
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
56-297 |
7.79e-114 |
|
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: 359.13 E-value: 7.79e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 56 QGNVQIRGVHFRYpsRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:COG5265 355 GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTL 295
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWAR 592
|
..
gi 2119559688 296 QS 297
Cdd:COG5265 593 QQ 594
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
59-296 |
8.32e-111 |
|
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: 338.05 E-value: 8.32e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
1-296 |
8.34e-106 |
|
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: 337.06 E-value: 8.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 1 VFFSVMIGAfSLGNAMPHLQTLATARGAAYYLYQLITMDPPIDSYSTEGKKLDNFQGNVQIRGVHFRYPSRPEAKILYGV 80
Cdd:TIGR02204 281 VFYAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 81 NLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHL 160
Cdd:TIGR02204 360 NLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRP 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 161 DVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDAL 240
Cdd:TIGR02204 440 DATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQAL 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 241 EKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:TIGR02204 520 ETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
57-287 |
1.39e-105 |
|
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: 324.18 E-value: 1.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 57 GNVQIRGVHFRYpsRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWREN 136
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 217 KILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQG 287
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
355-822 |
1.89e-104 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 333.67 E-value: 1.89e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 355 ASLGRILKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEIlgVFAILDEGEQERkIIQYVLMFVGVGVISLIAYFVQGY 434
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRI--IDALLAGGDLSA-LLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 435 MFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSW 514
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 515 KITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKA 594
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 595 HLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKK 674
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 675 PDIDnESEKGEQLHTFTANLSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVS 754
Cdd:COG1132 322 PEIP-DPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 755 LDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNsrEVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP--DATDEEVEEAAKAAQAHEFIEALPD 464
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
23-287 |
6.53e-100 |
|
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: 321.32 E-value: 6.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 23 ATARGAAYYLYQLITMDPPIDSYSTEGKKLDNfQGNVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKST 102
Cdd:COG4988 302 ANGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKST 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 103 IVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMD 182
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 183 LPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTA 262
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|....*
gi 2119559688 263 DMIAGFKDGVVAEQGTHNELMSKQG 287
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-296 |
5.07e-95 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 308.87 E-value: 5.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 1 VFFSVMIGAF----SLGNAMPHLQtlataRG--AAYYLYQLITMDPPIDsystEGK-KLDNFQGNVQIRGVHFRYPSRpE 73
Cdd:PRK11176 286 VVFSSMIALMrplkSLTNVNAQFQ-----RGmaACQTLFAILDLEQEKD----EGKrVIERAKGDIEFRNVTFTYPGK-E 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 74 AKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEE 153
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIAN 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NIRYGHLDV-TKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 232
Cdd:PRK11176 436 NIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 233 EGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:PRK11176 516 ERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-293 |
5.64e-95 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 312.43 E-value: 5.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 4 SVMIGAFSLGNAMPHLQT----LATARGAAYYLYQLITMDPPIDSysTEGKKLDNFQGNVQIRGVHFRYPSRPEAKILYG 79
Cdd:TIGR00958 422 SFLLYQEQLGEAVRVLSYvysgMMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKG 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGH 159
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 160 LDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDA 239
Cdd:TIGR00958 580 TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES 659
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 240 LEKAShgRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLV 293
Cdd:TIGR00958 660 RSRAS--RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-296 |
1.94e-94 |
|
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: 307.03 E-value: 1.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 1 VFFSVMIGAF----SLGNAMPHLQTLATArgaAYYLYQLITMDPPIDsysTEGKKLDNFQGNVQIRGVHFRYPSRpEAKI 76
Cdd:TIGR02203 275 AFITAMIALIrplkSLTNVNAPMQRGLAA---AESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIR 156
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 157 YGHL-DVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGI 235
Cdd:TIGR02203 428 YGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERL 507
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 236 VQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:TIGR02203 508 VQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
50-303 |
5.22e-94 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 306.50 E-value: 5.22e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 50 KKLDNFQGNVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN 129
Cdd:PRK13657 326 IDLGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIA 209
Cdd:PRK13657 404 RASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIY 289
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRF 563
|
250
....*....|....
gi 2119559688 290 QQLVTLQSMKSADD 303
Cdd:PRK13657 564 AALLRAQGMLQEDE 577
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
59-296 |
6.11e-93 |
|
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: 291.31 E-value: 6.11e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYpsRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENI 137
Cdd:cd03252 1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPK 217
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 218 ILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
38-297 |
1.30e-85 |
|
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: 287.02 E-value: 1.30e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 38 MDPPIDSYSTEGKKLDNFQGNVQIRGVHFRY-PSRPEakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEG 116
Cdd:TIGR01846 435 LNSPTEPRSAGLAALPELRGAITFENIRFRYaPDSPE--VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHG 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 117 QILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGA 196
Cdd:TIGR01846 513 QVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 197 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQ 276
Cdd:TIGR01846 593 NLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAES 672
|
250 260
....*....|....*....|.
gi 2119559688 277 GTHNELMSKQGIYQQLVTLQS 297
Cdd:TIGR01846 673 GRHEELLALQGLYARLWQQQS 693
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-295 |
2.64e-85 |
|
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: 282.43 E-value: 2.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 1 VFFSVMiGAF----SLGNAMPHLqtlATARGAAYYLYQLITMDPPIdSYSTEGKKLDNfQGNVQIRGVHFRYPSRPEAkI 76
Cdd:COG4987 278 LVLAAL-ALFealaPLPAAAQHL---GRVRAAARRLNELLDAPPAV-TEPAEPAPAPG-GPSLELEDVSFRYPGAGRP-V 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIR 156
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 157 YGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIV 236
Cdd:COG4987 431 LARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 237 QDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTL 295
Cdd:COG4987 511 LADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
59-271 |
1.03e-83 |
|
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: 264.25 E-value: 1.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIryghldvtkedieqaakmanahdfimdlpqkyetlvgergaqLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDG 271
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
53-265 |
2.51e-82 |
|
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: 262.79 E-value: 2.51e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 53 DNFQGNVQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKW 132
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 WRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARAL 212
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMI 265
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQI 218
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
371-667 |
2.47e-81 |
|
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: 263.18 E-value: 2.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIFSEILGVFA-----ILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTL 445
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 446 RLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLP 525
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKN--GAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 526 FVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQ 605
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 606 AVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEI 667
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
371-667 |
8.14e-78 |
|
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: 254.12 E-value: 8.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIFSEILGVFAILDE-----------------GEQERKIIQYVLMFVGVGVISLIAYFVQG 433
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMtnitgnssglnssagpfEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 434 YMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFS 513
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 514 WKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKK 593
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 594 AHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKA-FSAILFGGMAIGNASAFAPdAAKAEQSAKEI 667
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVfFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
41-293 |
8.08e-71 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 246.78 E-value: 8.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 41 PIDSYSTEGKKLdnfQGNVQIRGVHFRYpSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI 120
Cdd:TIGR03796 463 GSAATSEPPRRL---SGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILF 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 121 DGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSG 200
Cdd:TIGR03796 539 DGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSG 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 201 GQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKasHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHN 280
Cdd:TIGR03796 619 GQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHE 696
|
250
....*....|...
gi 2119559688 281 ELMSKQGIYQQLV 293
Cdd:TIGR03796 697 ELWAVGGAYARLI 709
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
51-303 |
4.02e-69 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 239.41 E-value: 4.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 51 KLDNFQGNVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINL 130
Cdd:TIGR01192 327 ELPNVKGAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIAR 210
Cdd:TIGR01192 405 ESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQ 290
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFY 564
|
250
....*....|...
gi 2119559688 291 QLVTLQSMKSADD 303
Cdd:TIGR01192 565 KLLRRSGLLTNQP 577
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-305 |
1.63e-68 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 237.30 E-value: 1.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 26 RGAAYY--LYQLITMDPPIDSYStegKKLDNFQGNVQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTI 103
Cdd:PRK10789 282 RGSAAYsrIRAMLAEAPVVKDGS---EPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 104 VQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDL 183
Cdd:PRK10789 358 LSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRL 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 184 PQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTAD 263
Cdd:PRK10789 438 PQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEAS 517
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2119559688 264 MIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQSMKSADDNE 305
Cdd:PRK10789 518 EILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALDDA 559
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
356-822 |
5.30e-68 |
|
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: 238.97 E-value: 5.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 356 SLGRILKLNKSEAPFIVMGCFASLVNGgampAFAVIFSeiLGVFAILDE---GEQERKIIQYVLMFVGVGVISLIAYFVQ 432
Cdd:COG2274 143 GLRWFLRLLRRYRRLLLQVLLASLLIN----LLALATP--LFTQVVIDRvlpNQDLSTLWVLAIGLLLALLFEGLLRLLR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 433 GYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLaTDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVF 512
Cdd:COG2274 217 SYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESR--SVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 513 SWKITLLVIAFLPFVMIGGALemqMMQGAAGKNKEALESAGKIA---IESIENIRTVASLTREDMFQKKFNHELQMPYNI 589
Cdd:COG2274 294 SPPLALVVLLLIPLYVLLGLL---FQPRLRRLSREESEASAKRQsllVETLRGIETIKALGAESRFRRRWENLLAKYLNA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 590 ALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDyVDVFKAFSaILFGGM--AIGNASAFAPDAAKAEQSAKEI 667
Cdd:COG2274 371 RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLT-LGQLIAFN-ILSGRFlaPVAQLIGLLQRFQDAKIALERL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 668 FKLIDKKPDIDnESEKGEQLHTFTANLSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD 747
Cdd:COG2274 449 DDILDLPPERE-EGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 748 PADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDnsREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG2274 527 PTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEAARLAGLHDFIEALPM 599
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
696-822 |
5.44e-68 |
|
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: 225.11 E-value: 5.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIV 775
Cdd:cd03249 3 FKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2119559688 776 SQEPVLFDRTIAENIAYGDNSRevTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPD 127
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-265 |
1.21e-67 |
|
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: 233.72 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 23 ATARGAAYYLYQLITMDPPIDSYSTEGKKLDNFQgnVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKST 102
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASS--LEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKST 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 103 IVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMD 182
Cdd:TIGR02857 364 LLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 183 LPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTA 262
Cdd:TIGR02857 444 LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
...
gi 2119559688 263 DMI 265
Cdd:TIGR02857 524 DRI 526
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
57-278 |
2.02e-67 |
|
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: 222.75 E-value: 2.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 57 GNVQIRGVHFRYpsRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGTTIEENiryghLD----VTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARA 211
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSN-----LDpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGT 278
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
57-274 |
4.87e-67 |
|
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: 221.69 E-value: 4.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 57 GNVQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWREN 136
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 217 KILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDG-VVA 274
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGrIVA 218
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
56-296 |
1.85e-63 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 225.99 E-value: 1.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 56 QGNVQIRGVHFRYpsRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWR 134
Cdd:TIGR03797 449 SGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGTTIEENIrYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVR 214
Cdd:TIGR03797 527 RQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVR 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRttIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVT 294
Cdd:TIGR03797 606 KPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
..
gi 2119559688 295 LQ 296
Cdd:TIGR03797 684 RQ 685
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-295 |
1.09e-62 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 230.30 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 33 YQLITMDPPIDSYSTEGKKLDN---FQGNVQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQR 109
Cdd:PTZ00265 1137 YPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMR 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 110 FYD------------------------------------------------------PEEGQILIDGVNLKDINLKWWRE 135
Cdd:PTZ00265 1217 FYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRN 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:PTZ00265 1297 LFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLRE 1376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 216 PKILLLDEATSALDTESEGIVQ----DALEKAShgRTTIVIAHRLSTIKTADMIAGFKD-----GVVAEQGTHNELMSKQ 286
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNSEKLIEktivDIKDKAD--KTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLSVQ 1454
|
330
....*....|
gi 2119559688 287 -GIYQQLVTL 295
Cdd:PTZ00265 1455 dGVYKKYVKL 1464
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-292 |
1.49e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 221.26 E-value: 1.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 23 ATARGAAYYLYQLitMDPPIDSYSTEGKKLDNFQGnVQIRGVHFRYPSrPEAKILYG-VNLQIKRGQTVALVGSSGCGKS 101
Cdd:PRK11174 315 AQAVGAAESLVTF--LETPLAHPQQGEKELASNDP-VTIEAEDLEILS-PDGKTLAGpLNFTLPAGQRIALVGPSGAGKT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 102 TIVQLLQRFYdPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIM 181
Cdd:PRK11174 391 SLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLP 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 182 DLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKT 261
Cdd:PRK11174 470 LLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQ 549
|
250 260 270
....*....|....*....|....*....|.
gi 2119559688 262 ADMIAGFKDGVVAEQGTHNELMSKQGIYQQL 292
Cdd:PRK11174 550 WDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
371-645 |
2.42e-62 |
|
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: 210.96 E-value: 2.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIFSEILGVFAILDEGEqERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSM 450
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPE-TQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 451 SFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIG 530
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 531 GALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFF 610
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 2119559688 611 AYAASFWLGAYLIKQSEVDY--VDVFKAFSAILFGGM 645
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVgdLVAFLSLFAQLFGPL 274
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
353-822 |
3.39e-62 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 223.06 E-value: 3.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 353 VDASLGRILKLNKSEAPFIVMG---CFASLVNGGAMPAFAVIFSEILGVfailDEGEQERKIIQYVLMFVGVGviSLIAY 429
Cdd:TIGR00958 145 TADLLFRLLGLSGRDWPWLISAfvfLTLSSLGEMFIPFYTGRVIDTLGG----DKGPPALASAIFFMCLLSIA--SSVSA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 430 FVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIG 509
Cdd:TIGR00958 219 GLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFM 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 510 FVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNI 589
Cdd:TIGR00958 297 LWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 590 ALKKAhLIGIGFSLSQAVM-FFAYAASFWLGAYLIKQSEVDYVDVFkafsAILFGGMAIGNA----SAFAPDAAKAEQSA 664
Cdd:TIGR00958 377 NKRKA-LAYAGYLWTTSVLgMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAvrvlSYVYSGMMQAVGAS 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 665 KEIFKLIDKKPDIDNEsekGEQLHTF-TANLSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTE 743
Cdd:TIGR00958 452 EKVFEYLDRKPNIPLT---GTLAPLNlEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 744 RFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNSREvtMDEIIDAARKANIHNFIASLPD 822
Cdd:TIGR00958 529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP--DEEIMAAAKAANAHDFIMEFPN 605
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
56-285 |
6.38e-61 |
|
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: 216.15 E-value: 6.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 56 QGNVQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDinlkWWRE 135
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ----WDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 ----NIGIVSQEPVLFGTTIEENI-RYGhlDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIAR 210
Cdd:COG4618 403 elgrHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEKA-SHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-292 |
1.86e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 206.60 E-value: 1.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 1 VFFSVMiGAFS----LGNAMPHL-QTLATARgaayYLYQLITMDPPIDSYSTEGKKLDnfQGNVQIRGVHFRYPSRPEaK 75
Cdd:PRK11160 283 FVFAAL-AAFEalmpVAGAFQHLgQVIASAR----RINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQ-P 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENI 155
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGHLDVTKEDIEQAAKMANAHDFIMDlPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGI 235
Cdd:PRK11160 435 LLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQ 513
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 236 VQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQL 292
Cdd:PRK11160 514 ILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
38-296 |
4.64e-55 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 200.33 E-value: 4.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 38 MDPPIDSYSTEGKKLDnfQGNVQIRGVHFRYpsRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQ 117
Cdd:PRK10790 322 MDGPRQQYGNDDRPLQ--SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 118 ILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHlDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQ 197
Cdd:PRK10790 398 IRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNN 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 198 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQG 277
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQG 556
|
250
....*....|....*....
gi 2119559688 278 THNELMSKQGIYQQLVTLQ 296
Cdd:PRK10790 557 THQQLLAAQGRYWQMYQLQ 575
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-256 |
1.85e-53 |
|
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: 194.50 E-value: 1.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 1 VFFSVMIGAFSLGNAMPH-LQTLATARGAAYYLYQLITMDPPIDSYSTEGKKLDNFQG-NVQIRGVHFRYPSRPEAkiLY 78
Cdd:TIGR02868 275 VLVLLPLAAFEAFAALPAaAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYG 158
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 159 HLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQD 238
Cdd:TIGR02868 433 RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLE 512
|
250
....*....|....*...
gi 2119559688 239 ALEKASHGRTTIVIAHRL 256
Cdd:TIGR02868 513 DLLAALSGRTVVLITHHL 530
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
379-822 |
1.69e-52 |
|
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: 192.62 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 379 LVNGGAMPAFAVIFSEILGVFA-ILDEG--EQERKIIQYV-LMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKA 454
Cdd:TIGR02203 17 VLAGVAMILVAATESTLAALLKpLLDDGfgGRDRSVLWWVpLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 455 MLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIggale 534
Cdd:TIGR02203 97 LLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSI----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 535 mqMMQGAAGK----NKEALESAGK---IAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAV 607
Cdd:TIGR02203 170 --LMRRVSKRlrriSKEIQNSMGQvttVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 608 MFFAYAASFWLGAYlikQSEVDYVDV--FKAF-SAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKKPDIDnesEKG 684
Cdd:TIGR02203 248 ASLALAVVLFIALF---QAQAGSLTAgdFTAFiTAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD---TGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 685 EQLHTFTANLSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN 764
Cdd:TIGR02203 322 RAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 765 LQWLRSQIGIVSQEPVLFDRTIAENIAYGDnSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:TIGR02203 401 LASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPL 457
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-294 |
8.06e-51 |
|
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: 190.34 E-value: 8.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 14 NAMPHLQT--LATARGAAYYLyqlitmdppIDSYSTEGKKLD---NFQGNVQIRGVHFRYPSrpEAKILYGVNLQIKRGQ 88
Cdd:TIGR01193 433 NLQPKLQAarVANNRLNEVYL---------VDSEFINKKKRTelnNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNS 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 89 TVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYG-HLDVTKEDI 167
Cdd:TIGR01193 502 KTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEI 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 168 EQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHgR 247
Cdd:TIGR01193 582 WAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-K 660
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2119559688 248 TTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVT 294
Cdd:TIGR01193 661 TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
60-254 |
4.42e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.00 E-value: 4.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVLFGTTIEENI----RYGHLDVTKEDIEQAAKMANAHDFIMDLPqkyetlvgerGAQLSGGQKQRIAIARALVRN 215
Cdd:COG4619 79 VPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKP----------VERLSGGERQRLALIRALLLQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAH 254
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-285 |
4.98e-50 |
|
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: 184.86 E-value: 4.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 24 TARGAAYYLYQLITMDPPIDsystEGKKLDNFQGNVQIRGVHFRYPSrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTI 103
Cdd:TIGR01842 286 GARQAYKRLNELLANYPSRD----PAMPLPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 104 VQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENI-RYGHlDVTKEDIEQAAKMANAHDFIMD 182
Cdd:TIGR01842 361 ARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 183 LPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKA-SHGRTTIVIAHRLSTIKT 261
Cdd:TIGR01842 440 LPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGC 519
|
250 260
....*....|....*....|....
gi 2119559688 262 ADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:TIGR01842 520 VDKILVLQDGRIARFGERDEVLAK 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
59-286 |
4.36e-49 |
|
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: 172.90 E-value: 4.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPV--LFGTTIEENIRYG--HLDVTKEDIEQAAKMANAhdfIMDLpqkyETLVGERGAQLSGGQKQRIAIARALVR 214
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpeNLGLPREEIRERVEEALE---LVGL----EHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA-HRLSTI-KTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
60-273 |
1.14e-48 |
|
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: 169.70 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:cd03246 2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVLFGTTIEENIryghldvtkedieqaakmanahdfimdlpqkyetlvgergaqLSGGQKQRIAIARALVRNPKIL 219
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 220 LLDEATSALDTESEGIVQDALEKAS-HGRTTIVIAHRLSTIKTADMIAGFKDGVV 273
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
79-226 |
1.98e-48 |
|
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: 168.21 E-value: 1.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLF-GTTIEENIRY 157
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 158 GHLDVTKEDIEQAAKMANAHDFiMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 226
Cdd:pfam00005 83 GLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
60-273 |
5.64e-47 |
|
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: 166.49 E-value: 5.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPEaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAhDFIMDLPQKYETlvgergAQLSGGQKQRIAIARALVRN 215
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALE-LVGLEGLRDRSP------FTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA-HRLstiktaDMIAGFKDGVV 273
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDL------DLLLELADRVI 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
378-822 |
6.06e-47 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 181.77 E-value: 6.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 378 SLVNGGAMPAFAVIFSEILgvfAILDEGEQERKIIqyvLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLR 457
Cdd:PTZ00265 69 ATISGGTLPFFVSVFGVIM---KNMNLGENVNDII---FSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 458 QEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLgSSLMAFCSVVTGIVIGFVF-SWKITLLVIAFLPFVMIGGALEMQ 536
Cdd:PTZ00265 143 QDGQFHD--NNPGSKLTSDLDFYLEQVNAGIGTKF-ITIFTYASAFLGLYIWSLFkNARLTLCITCVFPLIYICGVICNK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 537 MMQgaAGKNKEALESAGKIAI--ESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAA 614
Cdd:PTZ00265 220 KVK--INKKTSLLYNNNTMSIieEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 615 SFWLGAYLI------KQSEVDY--VDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKKPDIDNESEkGEQ 686
Cdd:PTZ00265 298 GFWYGTRIIisdlsnQQPNNDFhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDD-GKK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 687 LHTFTaNLSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADG-IVSLDGHNLKDLNL 765
Cdd:PTZ00265 377 LKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIINDSHNLKDINL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 766 QWLRSQIGIVSQEPVLFDRTIAENIAY------------------------GDNSREV--------------TMD----- 802
Cdd:PTZ00265 456 KWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRNScrakcagdlndmsnTTDsneli 535
|
490 500 510
....*....|....*....|....*....|..
gi 2119559688 803 ------------EIIDAARKANIHNFIASLPD 822
Cdd:PTZ00265 536 emrknyqtikdsEVVDVSKKVLIHDFVSALPD 567
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
59-284 |
6.48e-47 |
|
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: 175.09 E-value: 6.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRP--EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWW 133
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 RENIGIVSQEPV--LF-GTTIEENIRYG---HLDVTKEDIEQAAKMAnahdfiMD---LPqkyETLVGERGAQLSGGQKQ 204
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAEL------LErvgLP---PDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNE 281
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEE 491
|
...
gi 2119559688 282 LMS 284
Cdd:COG1123 492 VFA 494
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
59-282 |
1.51e-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: 165.82 E-value: 1.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD-----PEEGQILIDGVNL--KDINLK 131
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 132 WWRENIGIVSQEPVLFGTTIEENIRYG---HL----DVTKEDIEQAAKMANAHDFIMDLPQkyetlvgerGAQLSGGQKQ 204
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlHGiklkEELDERVEEALRKAALWDEVKDRLH---------ALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNEL 282
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
59-276 |
4.08e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.45 E-value: 4.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKST---IVQLLQRfydPEEGQILIDGVN---LKDINL- 130
Cdd:COG1136 5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDissLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEPVLFGT-TIEENI----RYGHLDVtKEDIEQAAKMANAhdfiMDLpqkyETLVGERGAQLSGGQKQR 205
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENValplLLAGVSR-KERRERARELLER----VGL----GDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQ 276
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
694-822 |
4.05e-45 |
|
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: 162.01 E-value: 4.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTtILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2119559688 774 IVSQEPVLFDRTIAENIAYGDnsREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPE 126
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
57-278 |
6.77e-45 |
|
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: 160.27 E-value: 6.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 57 GNVQIRGVHFRY-PSRPEakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:cd03369 5 GEIEVENLSVRYaPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGTTIEENI-RYGHLDvtKEDIEQAAKmanahdfimdlpqkyetlVGERGAQLSGGQKQRIAIARALVR 214
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGT 278
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
444-822 |
9.89e-45 |
|
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: 169.95 E-value: 9.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 444 TLR----LRSMSFKAMLRQEIAFFDDHNNsvGALTTRLATDASQVQG----------AAGIklgsslmafCSVVTGIVIG 509
Cdd:COG4987 83 TLRlladLRVRLYRRLEPLAPAGLARLRS--GDLLNRLVADVDALDNlylrvllpllVALL---------VILAAVAFLA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 510 FvFSWKITLLVIAFLpfVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLT---REDMFQKKFN---HEL 583
Cdd:COG4987 152 F-FSPALALVLALGL--LLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAaygALDRALARLDaaeARL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 584 QmpyNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVdvfkAFSAILFGGMAIGNASAFAPDAA----K 659
Cdd:COG4987 229 A---AAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGP----LLALLVLAALALFEALAPLPAAAqhlgR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 660 AEQSAKEIFKLIDKKPDIDnESEKGEQLHTFTAnLSFANIIFRYPTRPdTTILKGLDLEVPQGQTVALVGSSGCGKSTTV 739
Cdd:COG4987 302 VRAAARRLNELLDAPPAVT-EPAEPAPAPGGPS-LELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 740 QLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNsrEVTMDEIIDAARKANIHNFIAS 819
Cdd:COG4987 379 ALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAA 456
|
...
gi 2119559688 820 LPD 822
Cdd:COG4987 457 LPD 459
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
668-822 |
2.35e-44 |
|
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: 169.62 E-value: 2.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 668 FKLIDKKPDIdNESEKGEQLHTFTANLSFANIIFRYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD 747
Cdd:COG5265 333 FDLLDQPPEV-ADAPDAPPLVVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 748 PADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNsrEVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG5265 410 VTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP--DASEEEVEAAARAAQIHDFIESLPD 482
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
59-277 |
6.28e-44 |
|
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: 158.44 E-value: 6.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWR 134
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVL-------FGTTIEENIRYgHLDVTKEDIEQAAKMANAHDFIMDlpqkyETLVGERGAQLSGGQKQRIA 207
Cdd:cd03257 82 KEIQMVFQDPMSslnprmtIGEQIAEPLRI-HGKLSKKEARKEAVLLLLVGVGLP-----EEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 208 IARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQG 277
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
59-283 |
1.01e-43 |
|
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: 158.22 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWRE 135
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGT-TIEENIRYG---HLDVTKEDIEQAAKMANAhdfimdlpqkyetLVGERGA------QLSGGQKQR 205
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLEKLE-------------LVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVqDAL---EKASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNE 281
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVI-DELireLRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
..
gi 2119559688 282 LM 283
Cdd:COG1127 229 LL 230
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
59-284 |
2.31e-43 |
|
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: 157.66 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENI 137
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEP---------VlfGTTIEENIRYGHLDVTKEDIEQAAKmanahdfIMDLPqkyETLVGERGAQLSGGQKQRIAI 208
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLE-------QVGLP---PSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 209 ARALVRNPKILLLDEATSALDTesegIVQ----DALE--KASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNE 281
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDV----SVQaeilNLLKdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
...
gi 2119559688 282 LMS 284
Cdd:COG1124 226 LLA 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
59-277 |
3.50e-43 |
|
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: 155.76 E-value: 3.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDinLKWWRENIG 138
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG--VPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRYG--HLDVTKEDIEQAAKMANAHdfiMDLpqkyETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLEL---VGL----EGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQG 277
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
59-254 |
3.83e-43 |
|
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: 156.09 E-value: 3.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwrenI 137
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFG-TTIEENIRYGhLDVTKEDIEQAAkmANAHDFImdlpqkyeTLVGERGA------QLSGGQKQRIAIAR 210
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG-LELQGVPKAEAR--ERAEELL--------ELVGLSGFenayphQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAH 254
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
60-271 |
4.47e-43 |
|
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: 153.55 E-value: 4.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQepvlfgttieeniryghldvtkedieqaakmanahdfimdlpqkyetlvgergaqLSGGQKQRIAIARALVRNPKIL 219
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 220 LLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTA-DMIAGFKDG 271
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
59-278 |
4.76e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 156.31 E-value: 4.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL--KDINLKWWREN 136
Cdd:COG1126 2 IEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFG-TTIEENIRYGHLDVTKEDIEQAAKMAnahdfiMDLPQKyetlVG--ERG----AQLSGGQKQRIAIA 209
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPIKVKKMSKAEAEERA------MELLER----VGlaDKAdaypAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGT 278
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
59-286 |
7.52e-43 |
|
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: 156.36 E-value: 7.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVL-FGTTIEENI---RYGHLD----VTKED---IEQAAKMANAHDFImdlpqkyETLVGErgaqLSGGQKQRIA 207
Cdd:COG1120 79 YVPQEPPApFGLTVRELValgRYPHLGlfgrPSAEDreaVEEALERTGLEHLA-------DRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 208 IARALVRNPKILLLDEATSALDtesegI-----VQDALEK--ASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTH 279
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLD-----LahqleVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPP 222
|
....*..
gi 2119559688 280 NELMSKQ 286
Cdd:COG1120 223 EEVLTPE 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
59-271 |
7.67e-43 |
|
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: 153.50 E-value: 7.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKD--INLKWWREN 136
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLF-GTTIEENIRYGhldvtkedieqaakmanahdfimdlpqkyetlvgergaqLSGGQKQRIAIARALVRN 215
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIKT-ADMIAGFKDG 271
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
59-286 |
9.35e-43 |
|
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: 155.35 E-value: 9.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVN---LKDINLKWWRE 135
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGT-TIEENIRYG---HLDVTKEDIEQAAKManahdfimdlpqKYEtLVGERG------AQLSGGQKQR 205
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLE------------KLE-AVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNEL 282
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224
|
....
gi 2119559688 283 MSKQ 286
Cdd:cd03261 225 RASD 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
59-278 |
1.40e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 158.72 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDI-NLKWWRENI 137
Cdd:COG3842 6 LELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---RDVtGLPPEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFG-TTIEENIRYG--HLDVTKEDIEQ-AAKMANahdfIMDLPQKYETLVgergAQLSGGQKQRIAIARALV 213
Cdd:COG3842 80 GMVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRArVAELLE----LVGLEGLADRYP----HQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALeKASH---GRTTIVIAHRLS---TIktADMIAGFKDGVVAEQGT 278
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREEL-RRLQrelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
59-273 |
2.29e-42 |
|
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: 153.80 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWW---- 133
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 RENIGIVSQEPVLFGT-TIEENIRYGHL---DVTKEDIEQAAKMANahdfIMDLPQKYETLVgergAQLSGGQKQRIAIA 209
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLlagVPKKERRERAEELLE----RVGLGDRLNHYP----SELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRLSTIKTADMIAGFKDGVV 273
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
59-254 |
2.69e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.86 E-value: 2.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwrenI 137
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFG-TTIEENIRYGhLDVTKEDIEQAAKMAnahdfimdlpQKYETLVGERGA------QLSGGQKQRIAIAR 210
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALG-LELRGVPKAERRERA----------RELLELVGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAH 254
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
60-287 |
3.36e-42 |
|
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: 154.25 E-value: 3.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWwRENIGI 139
Cdd:COG4555 3 EVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVLF-GTTIEENIRY------GHLDVTKEDIEQAAKManahdfiMDLPQKYETLVGErgaqLSGGQKQRIAIARAL 212
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYfaelygLFDEELKKRIEELIEL-------LGLEEFLDRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMSKQG 287
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
59-277 |
4.18e-42 |
|
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: 151.31 E-value: 4.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINlKWWRENIG 138
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIryghldvtkedieqaakmanahdfimdlpqkyetlvgerGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQG 277
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
359-822 |
1.21e-41 |
|
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: 160.69 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 359 RILKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEILGvfAILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGR 438
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLA--GLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 439 SGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAGIKLGSslMAFCSVVTGIVIGFVF--SWKI 516
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGK--STGELATLLTEGVEALDGYFARYLPQ--LFLAALVPLLILVAVFplDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 517 TLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHE-----------LQM 585
Cdd:COG4988 161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEAsedfrkrtmkvLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 586 pyniALkkahligigfsLSQAVM-FFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILfggMAignASAFAP--------- 655
Cdd:COG4988 241 ----AF-----------LSSAVLeFFASLSIALVAVYIGFRLLGGSLTLFAALFVLL---LA---PEFFLPlrdlgsfyh 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 656 DAAKAEQSAKEIFKLIDKKPDidnESEKGEQLHTFTAN--LSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGC 733
Cdd:COG4988 300 ARANGIAAAEKIFALLDAPEP---AAPAGTAPLPAAGPpsIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 734 GKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDnsREVTMDEIIDAARKANI 813
Cdd:COG4988 375 GKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALEAAGL 452
|
....*....
gi 2119559688 814 HNFIASLPD 822
Cdd:COG4988 453 DEFVAALPD 461
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
694-822 |
2.16e-40 |
|
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: 148.53 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2119559688 774 IVSQEPVLFDRTIAENIAYGDNSreVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPD 125
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
59-285 |
3.36e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.29 E-value: 3.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRY-GHL-----DVTKEDIEQAAKManahdfiMDLPQKYETLVGergaQLSGGQKQRIAIARA 211
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfARLyglprKEARERIDELLEL-------FGLTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA-HRLSTI-KTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
57-289 |
5.39e-40 |
|
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: 160.11 E-value: 5.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 57 GNVQIRGVHFRYpsRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:TIGR00957 1283 GRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGTTIEENIR-YGHLdvTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVR 214
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIY 289
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
59-284 |
6.69e-40 |
|
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: 154.68 E-value: 6.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE---EGQILIDGVNLKDINLKWWRE 135
Cdd:COG1123 5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAHDFIMDLPQKYEtlvgergAQLSGGQKQRIAIARA 211
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
42-822 |
7.79e-40 |
|
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: 159.73 E-value: 7.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 42 IDSYSTEGKKLDNFQGN-VQIRGVHFRYpSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI 120
Cdd:TIGR00957 619 LEPDSIERRTIKPGEGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 121 DGvNLKDINLKWWRENIGIvsQEPVLFGTTIEENiRYghldvtKEDIEQAAKMAnahDFIMdLPQKYETLVGERGAQLSG 200
Cdd:TIGR00957 698 KG-SVAYVPQQAWIQNDSL--RENILFGKALNEK-YY------QQVLEACALLP---DLEI-LPSGDRTEIGEKGVNLSG 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 201 GQKQRIAIARALVRNPKILLLDEATSALDTE-SEGIVQDAL--EKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQG 277
Cdd:TIGR00957 764 GQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMG 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 278 THNELMSKQGIYQQLV----TLQSMKSADDNEIEDFNRDDTKRPSLRHQKSTIDMTPKKLAQDKKEEIKEEEKGEKEEEV 353
Cdd:TIGR00957 844 SYQELLQRDGAFAEFLrtyaPDEQQGHLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGS 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 354 DASL---------GRILKLNKSEAPFIVMGCFASLVNG-GAMPAFAVIF-------SEILGVF--------AILDEGEQE 408
Cdd:TIGR00957 924 SAELqkaeakeetWKLMEADKAQTGQVELSVYWDYMKAiGLFITFLSIFlfvcnhvSALASNYwlslwtddPMVNGTQNN 1003
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 409 RKIIQYVlmFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAA 488
Cdd:TIGR00957 1004 TSLRLSV--YGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMI 1079
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 489 GIKLGSSLMAFCSVVTGIVIgFVFSWKITLLVIafLPFVMIggALEMQMMQGAAGKNKEALESAGKIAIES-IENIRTVA 567
Cdd:TIGR00957 1080 PPVIKMFMGSLFNVIGALIV-ILLATPIAAVII--PPLGLL--YFFVQRFYVASSRQLKRLESVSRSPVYShFNETLLGV 1154
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 568 SLTREDMFQKKFNHELQM----------PYNIAlKKAHLIGIGFSLSQAVMF---FAYAASFWLGAYLIKQSeVDYVDVF 634
Cdd:TIGR00957 1155 SVIRAFEEQERFIHQSDLkvdenqkayyPSIVA-NRWLAVRLECVGNCIVLFaalFAVISRHSLSAGLVGLS-VSYSLQV 1232
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 635 KAFSAILFGGMAIGNASAFAPDAAKA-EQSAKEIFKLIDKKPDIDNESEKGEqlhtftanLSFANIIFRYptRPDTT-IL 712
Cdd:TIGR00957 1233 TFYLNWLVRMSSEMETNIVAVERLKEySETEKEAPWQIQETAPPSGWPPRGR--------VEFRNYCLRY--REDLDlVL 1302
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 713 KGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENI-A 791
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdP 1382
|
810 820 830
....*....|....*....|....*....|.
gi 2119559688 792 YGDNSREvtmdEIIDAARKANIHNFIASLPD 822
Cdd:TIGR00957 1383 FSQYSDE----EVWWALELAHLKTFVSALPD 1409
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
400-660 |
1.60e-39 |
|
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: 148.09 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 400 AILDEGEQERkIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHNnsVGALTTRLAT 479
Cdd:cd18557 25 TIIKGGDLDV-LNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHK--TGELTSRLSS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 480 DASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIES 559
Cdd:cd18557 102 DTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEES 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 560 IENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEvdyVDVFKAFSA 639
Cdd:cd18557 182 LSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQ---LTVGELTSF 258
|
250 260
....*....|....*....|....
gi 2119559688 640 ILFGGM---AIGNASAFAPDAAKA 660
Cdd:cd18557 259 ILYTIMvasSVGGLSSLLADIMKA 282
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
59-286 |
2.00e-39 |
|
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: 146.81 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDI-NLKWWRENI 137
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEP--VLFGTTIEENIRYG--HLDVTKEDI----EQAAKMANAHDFImdlpqKYETlvgergAQLSGGQKQRIAIA 209
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGleNLGVPREEMrkrvDEALKLVGMEDFR-----DREP------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 210 RALVRNPKILLLDEATSALDTES-EGIVQDALE-KASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
59-282 |
5.16e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.20 E-value: 5.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVN---LKDINLKWWRE 135
Cdd:COG3638 3 LELRNLSKRYPGGTPA--LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtaLRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFG-TTIEENIRYGHLD-----------VTKEDIEQAakmanahdfimdlpqkYETL--VG------ERG 195
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGRLGrtstwrsllglFPPEDRERA----------------LEALerVGladkayQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 196 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKAS--HGRTTIVIAHRLSTIKT-ADMIAGFKDGV 272
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAreDGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
250
....*....|
gi 2119559688 273 VAEQGTHNEL 282
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
59-285 |
6.09e-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: 144.26 E-value: 6.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWR 134
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGT-TIEENIRYGhLDVTKEDIEQAAKMANAHDFIMDLPQKYETlvgeRGAQLSGGQKQRIAIARALV 213
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALP-LEIAGVPKAEIEERVLELLELVGLEDKADA----YPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
696-822 |
9.35e-39 |
|
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: 143.77 E-value: 9.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIV 775
Cdd:cd03248 14 FQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLV 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2119559688 776 SQEPVLFDRTIAENIAYGDNSreVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03248 94 GQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELAS 138
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
59-271 |
1.45e-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: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPE--AKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwreN 136
Cdd:cd03250 1 ISVEDASFTWDSGEQetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGTTIEENIRYGH-------LDVTK-----EDIEQaakmanahdfimdLPQKYETLVGERGAQLSGGQKQ 204
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKpfdeeryEKVIKacalePDLEI-------------LPDGDLTEIGEKGINLSGGQKQ 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTE-SEGIVQDAL-EKASHGRTTIVIAHRLSTIKTADMIAGFKDG 271
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
401-822 |
1.88e-38 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 151.71 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 401 ILDEG--EQERKIIQYV-LMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRL 477
Cdd:PRK11176 51 LLDDGfgKADRSVLKWMpLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 478 ATDASQVQGAAG------IKLGSSLMAFCSVVtgivigFVFSWKITLLVIAFLPFVMIG-------------------GA 532
Cdd:PRK11176 129 TYDSEQVASSSSgalitvVREGASIIGLFIMM------FYYSWQLSLILIVIAPIVSIAirvvskrfrnisknmqntmGQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 533 LEM---QMMQGaagkNKEALESAGkiaiESIENIRtvasltredmFQKKFNHELQ--MPYNIALKKAHLIgIGFSLSQAV 607
Cdd:PRK11176 203 VTTsaeQMLKG----HKEVLIFGG----QEVETKR----------FDKVSNRMRQqgMKMVSASSISDPI-IQLIASLAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 608 MFFAYAASFwlgaYLIKQ--SEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSakeIFKLIDKKPDIDNESEKGE 685
Cdd:PRK11176 264 AFVLYAASF----PSVMDtlTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQT---LFAILDLEQEKDEGKRVIE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 686 QLhtfTANLSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNL 765
Cdd:PRK11176 337 RA---KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 766 QWLRSQIGIVSQEPVLFDRTIAENIAYGDN---SREvtmdEIIDAARKANIHNFIASLPD 822
Cdd:PRK11176 413 ASLRNQVALVSQNVHLFNDTIANNIAYARTeqySRE----QIEEAARMAYAMDFINKMDN 468
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
59-283 |
6.18e-38 |
|
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: 142.05 E-value: 6.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03295 1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRY--GHLDVTKEDIEQAAKMANAhdfIMDLPQkyETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALvpKLLKWPKEKIRERADELLA---LVGLDP--AEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRL-STIKTADMIAGFKDGVVAEQGTHNELM 283
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
59-253 |
8.44e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.96 E-value: 8.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLK---WWRE 135
Cdd:COG2884 2 IRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQE-PVLFGTTIEENIRYGhLDVTKEDIEQAAKMANAhdfIMD---LPQKYETLVgergAQLSGGQKQRIAIARA 211
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALP-LRVTGKSRKEIRRRVRE---VLDlvgLSDKAKALP----HELSGGEQQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2119559688 212 LVRNPKILLLDEATSALDTE-SEGIVqDALEKASHGRTTIVIA 253
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIA 193
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
59-278 |
1.04e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.06 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQ---LLQRfydPEEGQILIDGVNLKDIN---LK 131
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 132 WWRENIGIVSQEPVLFGT-TIEENIRYG--HLDVTKEDIEQ-AAKMANahdfimdlpqkyetLVG--ERG----AQLSGG 201
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALPleIAGVPKAEIRKrVAELLE--------------LVGlsDKAdaypSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 202 QKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGT 278
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
60-282 |
2.15e-37 |
|
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: 140.40 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGV---NLKDINLKWWREN 136
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFG-TTIEENIRYGHLD-----------VTKEDIEQAAKMANAhdfiMDLPQKYETlvgeRGAQLSGGQKQ 204
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGrrstwrslfglFPKEEKQRALAALER----VGLLDKAYQ----RADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKA--SHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNE 281
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAE 231
|
.
gi 2119559688 282 L 282
Cdd:cd03256 232 L 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
59-273 |
5.26e-37 |
|
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: 138.05 E-value: 5.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINLKWWREN 136
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFG-TTIEENIRYGHLDVTKEDIEQAAKMAnahdfiMDLPQKyetlVG------ERGAQLSGGQKQRIAIA 209
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIKVKGMSKAEAEERA------LELLEK----VGladkadAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEGIVQDALEKASH-GRTTIVIAHRLSTI-KTADMIAGFKDGVV 273
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
57-293 |
6.17e-37 |
|
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: 139.66 E-value: 6.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 57 GNVQIRGVHFRYPS--RPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWR 134
Cdd:cd03288 18 GEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGTTIEENIRyGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVR 214
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ-GIYQQLV 293
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
694-790 |
6.95e-37 |
|
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: 136.36 E-value: 6.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPdTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90
....*....|....*..
gi 2119559688 774 IVSQEPVLFDRTIAENI 790
Cdd:cd03228 80 YVPQDPFLFSGTIRENI 96
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
59-282 |
1.83e-36 |
|
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: 140.19 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDP---EEGQILIDGVNL-----KDIN 129
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklseKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LKWWREnIGIVSQEP---------VlfGTTIEENIRYgHLDVTKEDIEQAAK-------MANAHDFIMDLPQkyetlvge 193
Cdd:COG0444 82 KIRGRE-IQMIFQDPmtslnpvmtV--GDQIAEPLRI-HGGLSKAEARERAIellervgLPDPERRLDRYPH-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 194 rgaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTesegIVQ-DALE-----KASHGRTTIVIAHRLSTIK-TADMIA 266
Cdd:COG0444 150 ---ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVAeIADRVA 222
|
250
....*....|....*.
gi 2119559688 267 GFKDGVVAEQGTHNEL 282
Cdd:COG0444 223 VMYAGRIVEEGPVEEL 238
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
57-287 |
2.19e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 148.73 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 57 GNVQIRGVHFRYpsRPE-AKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGTTIEENiryghLDVTKE----DIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARA 211
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFN-----LDPFNEhndaDLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQG 287
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
77-285 |
2.81e-36 |
|
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: 137.08 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDI-NLKWWRENIGIVSQEPVLF-GTTIEEN 154
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDItNLPPEKRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 155 IRYG--HLDVTKEDIE----QAAKMAN-AHdfimdlpqkyetLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:cd03299 92 IAYGlkKRKVDKKEIErkvlEIAEMLGiDH------------LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 228 LDTESEGIVQDALEKASH--GRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:cd03299 160 LDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
692-822 |
4.74e-36 |
|
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: 136.20 E-value: 4.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 692 ANLSFANIIFRYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQ 771
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 772 IGIVSQEPVLFDRTIAENIAYGDNsrEVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRP--NATDEEVIEAAKEAGAHDFIMKLPN 127
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
59-277 |
6.23e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 136.71 E-value: 6.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD--PE---EGQILIDGVNL--KDINLK 131
Cdd:COG1117 12 IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 132 WWRENIGIVSQEPVLFGTTIEENIRYG---HLDVTKEDI----EQAAKMANAHDfimdlpqkyEtlVGER----GAQLSG 200
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlHGIKSKSELdeivEESLRKAALWD---------E--VKDRlkksALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 201 GQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKAShGRTTIVI-------AHRLStiktaDMIAGFKDGVV 273
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIvthnmqqAARVS-----DYTAFFYLGEL 231
|
....
gi 2119559688 274 AEQG 277
Cdd:COG1117 232 VEFG 235
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
374-623 |
6.39e-36 |
|
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: 137.77 E-value: 6.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 374 GCFASLVNGGAMPAFAVIFSEIL-GVFAILDEGEQE--RKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSM 450
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIdAVTNHSGSGGEEalRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 451 SFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIG 530
Cdd:cd18780 81 LFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 531 GALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFF 610
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250
....*....|...
gi 2119559688 611 AYAASFWLGAYLI 623
Cdd:cd18780 239 AIVLVLWYGGRLV 251
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
371-667 |
1.44e-35 |
|
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: 136.53 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIFSeilgvfAILDEGEQERK---IIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRL 447
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTK------LLIDDVIPAGDlslLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 448 RSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFV 527
Cdd:cd07346 75 RRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 528 MIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAV 607
Cdd:cd07346 153 VLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 608 MFFAYAASFWLGAYLIKQSEV---DYVdVFKAFSAILFGgmAIGNASAFAPDAAKAEQSAKEI 667
Cdd:cd07346 233 TALGTALVLLYGGYLVLQGSLtigELV-AFLAYLGMLFG--PIQRLANLYNQLQQALASLERI 292
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
59-286 |
1.68e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.83 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRenIG 138
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG---KPPRRARRR--IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVL---FGTTIEENI---RYGHL----DVTKED---IEQAAKMANAHDFImdlpqkyETLVGErgaqLSGGQKQR 205
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRglfrRPSRADreaVDEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEqGTHNELM 283
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVL 226
|
...
gi 2119559688 284 SKQ 286
Cdd:COG1121 227 TPE 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
59-229 |
5.83e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 136.74 E-value: 5.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDIN-LKWWRENI 137
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVTdLPPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFGT-TIEENIRYGhL---DVTKEDIEQ----AAKManahdfiMDLpqkyETLVGERGAQLSGGQKQRIAIA 209
Cdd:COG3839 78 AMVFQSYALYPHmTVYENIAFP-LklrKVPKAEIDRrvreAAEL-------LGL----EDLLDRKPKQLSGGQRQRVALG 145
|
170 180
....*....|....*....|
gi 2119559688 210 RALVRNPKILLLDEATSALD 229
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLD 165
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
59-273 |
1.35e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 129.83 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRYghldvtkedieqaakmanahdfimdlpqkyetlvgergaqlSGGQKQRIAIARALVRNPK 217
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 218 ILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVV 273
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
57-287 |
2.91e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 142.04 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 57 GNVQIRGVHFRYpsRPE-AKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:PLN03232 1233 GSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGTTIEENIR--YGHLDVtkeDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNIDpfSEHNDA---DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQG 287
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
59-282 |
3.44e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 134.12 E-value: 3.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLkDINLKWWRENIG 138
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFG-TTIEENIRYG--HLDVTKEDIEqaakmANAHDFI--MDLpqkyETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:COG1118 79 FVFQHYALFPhMTVAENIAFGlrVRPPSKAEIR-----ARVEELLelVQL----EGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 214 RNPKILLLDEATSALDTEsegiVQDALEK---ASH---GRTTIVIAH------RLstiktADMIAGFKDGVVAEQGTHNE 281
Cdd:COG1118 150 VEPEVLLLDEPFGALDAK----VRKELRRwlrRLHdelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDE 220
|
.
gi 2119559688 282 L 282
Cdd:COG1118 221 V 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
80-283 |
3.66e-34 |
|
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: 132.00 E-value: 3.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE----NIGIVSQEPVLF-GTTIEEN 154
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 155 IRYGhLDVT----KEDIEQAAK---MANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:cd03294 123 VAFG-LEVQgvprAEREERAAEaleLVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 228 LDTESEGIVQDALEK--ASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELM 283
Cdd:cd03294 191 LDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
59-292 |
3.95e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 132.16 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEP--VLFGTTIEENIRYG------HLDVTKEDIEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAIAR 210
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 211 ALVRNPKILLLDEATSALDTESE----GIVQDAleKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
....*.
gi 2119559688 287 GIYQQL 292
Cdd:PRK13650 232 NDLLQL 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
52-283 |
5.04e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.65 E-value: 5.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 52 LDNFQGNVQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLK 131
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 132 WWRENIGIVSQEP--VLFGTTIEENIRYG------HLDVTKEDIEQAAKMANAHDFIMDLPQKyetlvgergaqLSGGQK 203
Cdd:PRK13632 80 EIRKKIGIIFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 204 QRIAIARALVRNPKILLLDEATSALD----TESEGIVQDALEKAShgRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTH 279
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRK--KTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
....
gi 2119559688 280 NELM 283
Cdd:PRK13632 227 KEIL 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
60-277 |
1.50e-33 |
|
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: 127.17 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSqepvlfgttieeniryghldvtkedieQAAKMANAHDFImdlpqkyetlvgERG-AQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03214 78 VP---------------------------QALELLGLAHLA------------DRPfNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 219 LLLDEATSALD--TESE--GIVQDalEKASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQG 277
Cdd:cd03214 119 LLLDEPTSHLDiaHQIEllELLRR--LARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
79-285 |
1.79e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 131.78 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWRENIGIVSQEP---------Vl 146
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPyaslnprmtV- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 fGTTIEENIRYgHLDVTKEDIEQAAKmanahdFIMDlpqkyetLVGERGA-------QLSGGQKQRIAIARALVRNPKIL 219
Cdd:COG4608 115 -GDIIAEPLRI-HGLASKAERRERVA------ELLE-------LVGLRPEhadryphEFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 220 LLDEATSALDTeSegiVQdA-----LE--KASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:COG4608 180 VCDEPVSALDV-S---IQ-AqvlnlLEdlQDELGLTYLFISHDLSVVRhISDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
60-254 |
2.11e-33 |
|
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: 127.76 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYpsRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRENIGI 139
Cdd:cd03226 1 RIENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIARALVRN 215
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH 254
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
75-277 |
4.06e-33 |
|
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: 127.03 E-value: 4.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIK---RGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKD----INLKWWRENIGIVSQEPVLF 147
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 -GTTIEENIRYG-HLDVTKEDIEQAAKMANAhdfiMDLPQkyetLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 225
Cdd:cd03297 88 pHLNVRENLAFGlKRKRNREDRISVDELLDL----LGLDH----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 226 SALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQG 277
Cdd:cd03297 160 SALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
358-822 |
7.76e-33 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 134.70 E-value: 7.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 358 GRILKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEILGVFAILDEgeqerkIIQYVLMFVGVGVISLIAY-FVqgymf 436
Cdd:PRK13657 8 ARVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGD------IFPLLAAWAGFGLFNIIAGvLV----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 437 GRSGEYLTLRLR----SMSFKAMLRQEIAFfddH--NNSVGALTTRL-ATDAsqvqgAAGIKLG---SSLMAFCSVVTGI 506
Cdd:PRK13657 77 ARHADRLAHRRRlavlTEYFERIIQLPLAW---HsqRGSGRALHTLLrGTDA-----LFGLWLEfmrEHLATLVALVVLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 507 VIGFVFSWKITLLVIAF-LPFVMIGgALEMQM---MQGAAGKNKEALESAgkiAIESIENIRTVASLTR---EDMFQKKF 579
Cdd:PRK13657 149 PLALFMNWRLSLVLVVLgIVYTLIT-TLVMRKtkdGQAAVEEHYHDLFAH---VSDAIGNVSVVQSYNRieaETQALRDI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 580 NHEL---QMPyniALKKAHLIGIgfsLSQAVMFFAYAASFWLGAYLIKQSEVDYVDV--FKAFSAILFGgmAIGNASAFA 654
Cdd:PRK13657 225 ADNLlaaQMP---VLSWWALASV---LNRAASTITMLAILVLGAALVQKGQLRVGEVvaFVGFATLLIG--RLDQVVAFI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 655 PDAAKAEQSAKEIFKLIDKKPDIdNESEKGEQLHTFTANLSFANIIFRYPTRPDTtiLKGLDLEVPQGQTVALVGSSGCG 734
Cdd:PRK13657 297 NQVFMAAPKLEEFFEVEDAVPDV-RDPPGAIDLGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 735 KSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGdnsRE-VTMDEIIDAARKANI 813
Cdd:PRK13657 374 KSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG---RPdATDEEMRAAAERAQA 450
|
....*....
gi 2119559688 814 HNFIASLPD 822
Cdd:PRK13657 451 HDFIERKPD 459
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
694-822 |
1.71e-32 |
|
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: 126.06 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYptRPDTT-ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQI 772
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2119559688 773 GIVSQEPVLFDRTIAENIAYGDNSreVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPE 126
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
59-821 |
1.89e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 136.26 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQ-LLQRFYDPEEGQILIDGvnlkdinlkwwreNI 137
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-------------SV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFGTTIEENIRYGHlDVTKEDIEQAAKM-ANAHDFIMdLPQKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:PLN03232 682 AYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVtALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 217 KILLLDEATSALDTESEGIVQDALEKAS-HGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLvtl 295
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL--- 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 296 qsMKSAddNEIEDFNRDDTKRPSLRHQ--KSTIDMTPKKLA--QDKKEEIKEEEKGEKEEEVDASLGRILKLNKSEAP-F 370
Cdd:PLN03232 837 --MENA--GKMDATQEVNTNDENILKLgpTVTIDVSERNLGstKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGlW 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVnggAMPAFAVIFSEILGVFAILDEGEQERK---IIQYVLMfvGVGVISLIayFVQGYMFGRSGEYLTLRL 447
Cdd:PLN03232 913 VVMILLVCYL---TTEVLRVSSSTWLSIWTDQSTPKSYSPgfyIVVYALL--GFGQVAVT--FTNSFWLISSSLHAAKRL 985
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 448 RSMSFKAMLRQEIAFFddHNNSVGALTTRLATDASQVQGAAGIKLGSSL-MAFCSVVTGIVIGFVFS---WKITLLVIAF 523
Cdd:PLN03232 986 HDAMLNSILRAPMLFF--HTNPTGRVINRFSKDIGDIDRNVANLMNMFMnQLWQLLSTFALIGTVSTislWAIMPLLILF 1063
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 524 LPFVMIGGALEMQMMQGAAGKNKEALESAGKiAIESIENIRTVASLTREDMFQKKFnhelqMPYNIALKKAHLIGIGF-- 601
Cdd:PLN03232 1064 YAAYLYYQSTSREVRRLDSVTRSPIYAQFGE-ALNGLSSIRAYKAYDRMAKINGKS-----MDNNIRFTLANTSSNRWlt 1137
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 602 --SLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIgnASAFAPDAAKAEQSAKEIFKL---ID---K 673
Cdd:PLN03232 1138 irLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITTL--LSGVLRQASKAENSLNSVERVgnyIDlpsE 1215
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 674 KPDIDnESEKGEQLHTFTANLSFANIIFRYptRPD-TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGI 752
Cdd:PLN03232 1216 ATAII-ENNRPVSGWPSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGR 1292
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 753 VSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIaygDNSREVTMDEIIDAARKANIHNFIASLP 821
Cdd:PLN03232 1293 IMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNP 1358
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
60-274 |
3.65e-32 |
|
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: 124.18 E-value: 3.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDInlkwwRENIGI 139
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVL---FGTTIEENI---RYGHL-------DVTKEDIEQAAKMANAHDFImdlpqkyETLVGErgaqLSGGQKQRI 206
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmgLYGHKglfrrlsKADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 207 AIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVA 274
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
59-253 |
4.15e-32 |
|
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: 124.06 E-value: 4.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGV---NLKDINLKWWRE 135
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGT-TIEENIRYGhLDVTKEDIEQAAKMANAHDFIMDLPQKYETLvgerGAQLSGGQKQRIAIARALVR 214
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVN 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA 253
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
59-229 |
5.18e-32 |
|
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: 124.66 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLkdINLKWWRENIG 138
Cdd:cd03300 1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRYGhLDVTKEDI-EQAAKMANAHDFImdlpqKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFG-LRLKKLPKaEIKERVAEALDLV-----QLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170
....*....|...
gi 2119559688 217 KILLLDEATSALD 229
Cdd:cd03300 150 KVLLLDEPLGALD 162
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
59-298 |
5.66e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.32 E-value: 5.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRY-PSRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL--KDINLKWWR 134
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMAnahdfiMDLPQ-KYETLVGERGAQLSGGQKQRIAIA 209
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEgivQDALEKAS-----HGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNElm 283
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGR---DEILNKIKelhkeYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE-- 231
|
250
....*....|....*
gi 2119559688 284 skqgIYQQLVTLQSM 298
Cdd:PRK13637 232 ----VFKEVETLESI 242
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
59-284 |
6.03e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 6.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLkwW--REN 136
Cdd:PRK13635 6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETV--WdvRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEP--VLFGTTIEENIRYG--HLDVTKED----IEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAI 208
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGleNIGVPREEmverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 209 ARALVRNPKILLLDEATSALDTESEgivQDALE-----KASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELM 283
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
.
gi 2119559688 284 S 284
Cdd:PRK13635 229 K 229
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
413-627 |
7.77e-32 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 126.09 E-value: 7.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 413 QYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDhnNSVGALTTRLATDASQVQGAAGIKL 492
Cdd:cd18573 42 TFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDK--NKTGELVSRLSSDTSVVGKSLTQNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 493 GSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTRE 572
Cdd:cd18573 120 SDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 573 DMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSE 627
Cdd:cd18573 200 RKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGE 254
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
411-654 |
1.13e-30 |
|
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: 122.21 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 411 IIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFddHNNSVGALTTRLATDASQVQGAagi 490
Cdd:cd18576 35 LNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFF--HERRVGELTSRLSNDVTQIQDT--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 491 kLGSSLMAFCS----VVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTV 566
Cdd:cd18576 110 -LTTTLAEFLRqiltLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 567 ASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFkAFsaILFGGMA 646
Cdd:cd18576 189 KAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLV-AF--LLYTLFI 265
|
....*...
gi 2119559688 647 IGNASAFA 654
Cdd:cd18576 266 AGSIGSLA 273
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
59-790 |
2.15e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 129.47 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGK-STIVQLLQRFYDPEEGQILIDGvnlkdinlkwwreNI 137
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG-------------TV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFGTTIEENIRYGhLDVTKEDIEQAAKMAN-AHDFIMdLPQKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTAlQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 217 KILLLDEATSALDTESEGIVQDA-LEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLV-T 294
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMeN 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 295 LQSMKSADDNEIEdFNRDDT-------KRPSLRHQKSTIDMTPKKlaqdkKEEIKEEEKGEKEEEVDAslgRILKLNKSE 367
Cdd:PLN03130 840 AGKMEEYVEENGE-EEDDQTsskpvanGNANNLKKDSSSKKKSKE-----GKSVLIKQEERETGVVSW---KVLERYKNA 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 368 --APFIVMGCFASLVnggAMPAFAVIFSEILGVFAilDEGE-QERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLT 444
Cdd:PLN03130 911 lgGAWVVMILFLCYV---LTEVFRVSSSTWLSEWT--DQGTpKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAA 985
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 445 LRLRSMSFKAMLRQEIAFFddHNNSVGALTTRLATDASQ----VQGAAGIKLGSslmAFCSVVTGIVIGFVFS---WKIT 517
Cdd:PLN03130 986 KRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKDLGDidrnVAVFVNMFLGQ---IFQLLSTFVLIGIVSTislWAIM 1060
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 518 LLVIAFLpfvmiGGALEMQmmqgaagknkealesagkiaiESIENIRTVASLTREDMFqKKFNHELQMPYNIALKKAH-- 595
Cdd:PLN03130 1061 PLLVLFY-----GAYLYYQ---------------------STAREVKRLDSITRSPVY-AQFGEALNGLSTIRAYKAYdr 1113
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 596 LIGI-GFSLSQAVMF--FAYAASFWLGaylIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPD---------------- 656
Cdd:PLN03130 1114 MAEInGRSMDNNIRFtlVNMSSNRWLA---IRLETLGGLMIWLTASFAVMQNGRAENQAAFASTmglllsyalnitsllt 1190
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 657 -----AAKAEQSakeiFKLIDKKPD-IDNESEKGEQLHT--------FTANLSFANIIFRYptRPD-TTILKGLDLEVPQ 721
Cdd:PLN03130 1191 avlrlASLAENS----LNAVERVGTyIDLPSEAPLVIENnrpppgwpSSGSIKFEDVVLRY--RPElPPVLHGLSFEISP 1264
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 722 GQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENI 790
Cdd:PLN03130 1265 SEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
59-278 |
3.05e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 123.52 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIG 138
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRYGhL---DVTKEDIE----QAAKMAnahdfimdlpqKYETLVGERGAQLSGGQKQRIAIAR 210
Cdd:PRK09452 90 TVFQSYALFpHMTVFENVAFG-LrmqKTPAAEITprvmEALRMV-----------QLEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALeKASH---GRTTIVIAH-RLSTIKTADMIAGFKDGVVAEQGT 278
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNEL-KALQrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
59-277 |
3.49e-30 |
|
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: 118.51 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIG 138
Cdd:cd03301 1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRYG------HLDVTKEDIEQAAKMAnahdfimdlpqKYETLVGERGAQLSGGQKQRIAIARA 211
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAELL-----------QIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAH-RLSTIKTADMIAGFKDGVVAEQG 277
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
369-822 |
3.64e-30 |
|
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: 125.86 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 369 PFIVMGCFASLVNGGAMPAFAVIFSEIL-GVFAildEGEQERKIIQYVLMFVGVGVI-SLIAYFvQGYMFGRSGEYLTLR 446
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVdGLIS---AGEPLAELLPALGALALVLLLrALLGWL-QERAAARAAAAVKSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 447 LRSMSFKAMLRQEIAffDDHNNSVGALTTRLATDASQVQG-AAGIKLGSSLMAFCSVVTGIVIgFVFSWKITLLVIAFLP 525
Cdd:TIGR02857 79 LRERLLEAVAALGPR--WLQGRPSGELATLALEGVEALDGyFARYLPQLVLAVIVPLAILAAV-FPQDWISGLILLLTAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 526 FVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQmpyniALKKAHL--IGIGFsL 603
Cdd:TIGR02857 156 LIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSE-----EYRERTMrvLRIAF-L 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 604 SQAVMFFAYAASfwlgaylikqseVDYVDVFKAFSaILFGGMAIGNA--------SAFAP---------DAAKAEQSAKE 666
Cdd:TIGR02857 230 SSAVLELFATLS------------VALVAVYIGFR-LLAGDLDLATGlfvlllapEFYLPlrqlgaqyhARADGVAAAEA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 667 IFKLIDKKPDIdnESEKGEQLHTFTANLSFANIIFRYPTRpdTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFY 746
Cdd:TIGR02857 297 LFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 747 DPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDnsREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:TIGR02857 373 DPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALPQ 446
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
59-278 |
5.66e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 121.83 E-value: 5.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAKI-LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVN---LKDINLKWWR 134
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQE-PVLFGTTIEENIRY-----GhldVTKEDIEqaAKMANAHDF--IMDLPQKYEtlvgergAQLSGGQKQRI 206
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALplelaG---TPKAEIK--ARVTELLELvgLSDKADRYP-------AQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 207 AIARALVRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGT 278
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKrICDRVAVIDAGRLVEQGT 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
59-283 |
5.78e-30 |
|
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: 119.03 E-value: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQ---IL---IDGVNLKDInlkw 132
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFgerRGGEDVWEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 wRENIGIVS---QEPVLFGTTIEENI---------RYGHldVTKEDIEQAAKMANAhdfiMDLpqkyETLVGERGAQLSG 200
Cdd:COG1119 77 -RKRIGLVSpalQLRFPRDETVLDVVlsgffdsigLYRE--PTDEQRERARELLEL----LGL----AHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 201 GQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIV-IAHRLStiktaDMIAGF------KDGV 272
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIthvlllKDGR 220
|
250
....*....|.
gi 2119559688 273 VAEQGTHNELM 283
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
59-254 |
6.73e-30 |
|
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: 117.58 E-value: 6.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWwRENIG 138
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRY----GHLDVTKEDIEQAAKmanahdfIMDLpQKYETLvgeRGAQLSGGQKQRIAIARALV 213
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALE-------AVGL-AGLADL---PVRQLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAH 254
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTH 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
79-284 |
1.01e-29 |
|
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: 124.41 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKST----IVQLLqrfydPEEGQILIDGVNLKDIN---LKWWRENIGIVSQEPvlFGT-- 149
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 ---TIEENIRYG----HLDVTKEDIEQAAKMAnahdfiMD---LP----QKYEtlvgergAQLSGGQKQRIAIARALVRN 215
Cdd:COG4172 377 prmTVGQIIAEGlrvhGPGLSAAERRARVAEA------LEevgLDpaarHRYP-------HEFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 216 PKILLLDEATSALDTesegIVQ----DALEK--ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMS 284
Cdd:COG4172 444 PKLLVLDEPTSALDV----SVQaqilDLLRDlqREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
73-284 |
1.08e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 118.27 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKD--INLKWWRENIGIVSQEPVLF-GT 149
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGMVFQQFYLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVtkedieQAAKMANAHDFIMDLPQKyetlVG--ERG----AQLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:PRK09493 93 TALENVMFGPLRV------RGASKEEAEKQARELLAK----VGlaERAhhypSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 224 ATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
59-282 |
2.66e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.82 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDInLKWWREN 136
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGT-TIEENIRYGHLDVT------KEDIEQAAKMANAHDFIMDLpqkyETLVGErgaqLSGGQKQRIAIA 209
Cdd:COG1129 81 IAIIHQELNLVPNlSVAENIFLGREPRRgglidwRAMRRRARELLARLGLDIDP----DTPVGD----LSVAQQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 210 RALVRNPKILLLDEATSAL-DTESE---GIVQDaLekASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNEL 282
Cdd:COG1129 153 RALSRDARVLILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
58-284 |
4.73e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.01 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 58 NVQIRGVHFRYPSRP-EAkilygvNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwREN 136
Cdd:COG3840 1 MLRLDDLTYRYGDFPlRF------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFG-TTIEENIRYG-----HLDVT-KEDIEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAIA 209
Cdd:COG3840 73 VSMLFQENNLFPhLTVAQNIGLGlrpglKLTAEqRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 210 RALVRNPKILLLDEATSALD----TESEGIVQDALekASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMS 284
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDpalrQEMLDLVDELC--RERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
59-282 |
5.32e-29 |
|
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: 115.90 E-value: 5.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIG 138
Cdd:cd03296 3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFG-TTIEENIRYGhLDVTK--EDIEQAAKMANAHDfIMDLPQkYETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFG-LRVKPrsERPPEAEIRAKVHE-LLKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNEL 282
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
59-274 |
5.91e-29 |
|
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: 113.29 E-value: 5.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwrenig 138
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 ivsqEPVLFGTTIEEniryghldvtkedieQAAKMANAHdfimdlpqkyetlvgergaQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03216 62 ----KEVSFASPRDA---------------RRAGIAMVY-------------------QLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVA 274
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
398-628 |
9.67e-29 |
|
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: 116.87 E-value: 9.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 398 VFAILDEGEQErKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDhnNSVGALTTRL 477
Cdd:cd18572 23 IDAVVADGSRE-AFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDA--TKTGELTSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 478 ATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAI 557
Cdd:cd18572 100 TSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 558 ESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEV 628
Cdd:cd18572 180 EALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
80-229 |
1.80e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.51 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIGIVSQEPVLF-GTTIEENIRYG 158
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGENVGYG 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 159 --HLDVTKEDIEQAAKMANAhdfIMDLPQKYETLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK11432 103 lkMLGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
69-278 |
2.41e-28 |
|
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: 112.64 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 69 PSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL--QRFYDPEEGQILIDGVNLKdinLKWWRENIGIVSQEPVL 146
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 FGT-TIEENIRYghldvtkedieqAAKManahdfimdlpqkyetlvgeRGaqLSGGQKQRIAIARALVRNPKILLLDEAT 225
Cdd:cd03213 94 HPTlTVRETLMF------------AAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 226 SALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTiktaDMIAGFKDGVVAEQGT 278
Cdd:cd03213 140 SGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQGR 189
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
59-277 |
7.01e-28 |
|
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: 111.90 E-value: 7.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTvALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRYGHL--DVTKEDIEQAAKMANAHdfiMDLPQKYETLVGergaQLSGGQKQRIAIARALVRN 215
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYIAWlkGIPSKEVKARVDEVLEL---VNLGDRAKKKIG----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQG 277
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
59-286 |
7.23e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 113.33 E-value: 7.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD--PE---EGQILIDGVNL-----KDI 128
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIysprtDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 129 NLkwwRENIGIVSQEPVLFGTTIEENIRYG-------HLDVTKEDIEQAAKMANAHDFIMDlpQKYETLVGergaqLSGG 201
Cdd:PRK14239 83 DL---RKEIGMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 202 QKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG-TH 279
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNdTK 232
|
....*..
gi 2119559688 280 NELMSKQ 286
Cdd:PRK14239 233 QMFMNPK 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
59-286 |
9.91e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.31 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEP--VLFGTTIEENIRYG---HL---DVTKEDIEQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIAR 210
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGlenHAvpyDEMHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
60-263 |
1.14e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 111.73 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:PRK10247 9 QLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVLFGTTIEENIRYGHLdVTKEDIEQAAKMANAHDFimDLPqkyETLVGERGAQLSGGQKQRIAIARALVRNPKIL 219
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPWQ-IRNQQPDPAIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2119559688 220 LLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKTAD 263
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRyvREQNIAVLWVTHDKDEINHAD 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
59-282 |
2.31e-27 |
|
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: 110.67 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRY------GHLDVTKEDIEQAAKManahdfiMDLPQKYETLVGergaQLSGGQKQRIAIARA 211
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkgLPKSEIKEEVELLLRV-------LGLTDKANKRAR----TLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAH------RLstiktADMIAGFKDGVVAEQGTHNEL 282
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeAL-----CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
60-284 |
2.46e-27 |
|
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: 110.60 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLK-----DINlkwwR 134
Cdd:cd03224 2 EVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpphERA----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGT-TIEENIRYGHLDVTKEDIEQAAkmanahDFIMDL-PQKYETLvGERGAQLSGGQKQRIAIARAL 212
Cdd:cd03224 75 AGIGYVPEGRRIFPElTVEENLLLGAYARRRAKRKARL------ERVYELfPRLKERR-KQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 213 VRNPKILLLDEATSALdteSEGIVQ---DALEK-ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:cd03224 148 MSRPKLLLLDEPSEGL---APKIVEeifEAIRElRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
59-254 |
2.55e-27 |
|
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: 110.99 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN----LKWW 133
Cdd:COG4181 9 IELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 RENIGIVSQEPVLFGT-TIEENI-----RYGHldvtKEDIEQAAKMANAhdfiMDLpqkyetlvGERG----AQLSGGQK 203
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVmlpleLAGR----RDARARARALLER----VGL--------GHRLdhypAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 204 QRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAH 254
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTH 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
80-254 |
2.89e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 114.55 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDInlKWWRENIGIVSQEPVLF-GTTIEENIRYG 158
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFpHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 159 hldvTKEDIEQAAKMANAHDFIMDLPQKYEtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQ- 237
Cdd:PRK11607 116 ----LKQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQl 190
|
170 180
....*....|....*....|
gi 2119559688 238 ---DALEKAshGRTTIVIAH 254
Cdd:PRK11607 191 evvDILERV--GVTCVMVTH 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
59-292 |
3.93e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.82 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEE---GQILIDGVNLKDINLKWWRE 135
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEP--VLFGTTIEENIRYG--HLDVTKED----IEQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIA 207
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEmikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 208 IARALVRNPKILLLDEATSALDTESE----GIVQDALEKasHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELM 283
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKeqilKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
....*....
gi 2119559688 284 SKQGIYQQL 292
Cdd:PRK13640 232 SKVEMLKEI 240
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
59-271 |
4.39e-27 |
|
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: 109.73 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWW----R 134
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGTTIEENIRYGHlDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVR 214
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 215 NPKILLLDEATSALDTE-SEGIVQDALEK--ASHGRTTIVIAHRLSTIKTADMIAGFKDG 271
Cdd:cd03290 158 NTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
60-257 |
8.57e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.55 E-value: 8.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPS------RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---L 130
Cdd:PRK10419 5 NVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEPV-------LFGTTIEENIRygHLdvtkEDIEQAAKMANAHDFI--MDLPqkyETLVGERGAQLSGG 201
Cdd:PRK10419 85 KAFRRDIQMVFQDSIsavnprkTVREIIREPLR--HL----LSLDKAERLARASEMLraVDLD---DSVLDKRPPQLSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 202 QKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTT--IVIAHRLS 257
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLR 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
76-284 |
8.59e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.84 E-value: 8.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQI-----LIDG---VNLKDINLKWWRENIGIVSQEPVLF 147
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTarsLSQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 -GTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKyETLVGERgaqLSGGQKQRIAIARALVRNPKILLLDEATS 226
Cdd:PRK11264 98 pHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK-ETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 227 ALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK11264 174 ALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
59-286 |
8.71e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.09 E-value: 8.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINLKWWREN 136
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAHDFIMDLPQKYETLvgergaqLSGGQKQRIAIARAL 212
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 213 VRNPKILLLDEATSALDTE--SEgIVQDALEKASHGRTTIVIA-HRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
59-284 |
1.47e-26 |
|
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: 109.89 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPS------RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN--- 129
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LKWWRENIGIVSQE-PVLFG--TTIEENIR--YGHLDVTKEDiEQAAKMANAHDfIMDLPqkyETLVGERGAQLSGGQKQ 204
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNprMTVRQIIGepLRHLTSLDES-EQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNE 281
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQ 237
|
...
gi 2119559688 282 LMS 284
Cdd:TIGR02769 238 LLS 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
61-285 |
1.54e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.49 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 61 IRGVHFRY-PSRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI------DGVNLKDinLKW 132
Cdd:PRK13634 5 FQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKK--LKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 WRENIGIVSQ--EPVLFGTTIEENIRYGHLD--VTKEDIEQAAKMANAhdfIMDLPqkyETLVGERGAQLSGGQKQRIAI 208
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLP---EELLARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 209 ARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-284 |
1.64e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 109.74 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE-----EGQILIDGVNL--KDINLK 131
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 132 WWRENIGIVSQEPVLFGTTIEENIRYG------HLDVTKEDI-EQAAKMANAHDFIMDLPQKyetlvgeRGAQLSGGQKQ 204
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTES----EGIVQDALEKAShgRTTIVIAHRLSTI-KTADMIAGFKD-----GVVA 274
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSLRLRSE--LTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLV 235
|
250
....*....|
gi 2119559688 275 EQGTHNELMS 284
Cdd:PRK14258 236 EFGLTKKIFN 245
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
59-291 |
2.12e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:PRK13647 5 IEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEP--VLFGTTIEENIRYG--HLDVTKEDI----EQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIAR 210
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVerrvEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA-HRLS-TIKTADMIAGFKDGVVAEQGThNELMSKQGI 288
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDEDI 230
|
...
gi 2119559688 289 YQQ 291
Cdd:PRK13647 231 VEQ 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
80-284 |
3.26e-26 |
|
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: 110.97 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKD----INLKWWRENIGIVSQEPVLFG-TTIEEN 154
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 155 IRYGHLDVTKEDIEQAakmanaHDFIMDLpQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEG 234
Cdd:TIGR02142 96 LRYGMKRARPSERRIS------FERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 235 IVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:TIGR02142 169 EILPYLERlhAEFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
80-232 |
5.04e-26 |
|
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: 110.58 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQL---LQRfydPEEGQILIDGVNLKD----INLKWWRENIGIVSQEPVLFGT-TI 151
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRYGH----LDVTKEDIEQAAKManahdfiMDLpqkyETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:COG4148 95 RGNLLYGRkrapRAERRISFDEVVEL-------LGI----GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
....*
gi 2119559688 228 LDTES 232
Cdd:COG4148 164 LDLAR 168
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
59-284 |
6.01e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.24 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN--LKWWREN 136
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAHdfimdlpqkyetlVGERGAQ------LSGGQKQRI 206
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEALKA-------------VGMEGFEnkpphhLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 207 AIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA-HRLSTIKT-ADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
59-279 |
8.21e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.02 E-value: 8.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--------VNLKDINL 130
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 kwWRENIGIVSQE----PVLfgtTIEENIRYGHLDVTKEDIEQAAKMANAH-------DFIMDLPQkyetlvgergaQLS 199
Cdd:PRK11124 80 --LRRNVGMVFQQynlwPHL---TVQQNLIEAPCRVLGLSKDQALARAEKLlerlrlkPYADRFPL-----------HLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 200 GGQKQRIAIARALVRNPKILLLDEATSALDTE-SEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG 277
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIVEQG 223
|
..
gi 2119559688 278 TH 279
Cdd:PRK11124 224 DA 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
82-277 |
9.46e-26 |
|
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: 105.65 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 82 LQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIGIVSQEPVLFG-TTIEENIRYG-- 158
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLGls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 159 -HLDVTKEDiEQAAKMANAHdfiMDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQ 237
Cdd:cd03298 97 pGLKLTAED-RQAIEVALAR---VGLAGLEKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2119559688 238 DALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG 277
Cdd:cd03298 169 DLVLDlhAETKMTVLMVTHQPEDAkRLAQRVVFLDNGRIAAQG 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
663-791 |
1.81e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.84 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 663 SAKEIFKLIDKKPDIDNESEKGEQLHTftANLSFANIIFRYPTRPDTtILKGLDLEVPQGQTVALVGSSGCGKSTTVQLT 742
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2119559688 743 ERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIA 791
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLL 435
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
58-286 |
2.10e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.87 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 58 NVQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--------VNLKDIN 129
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LkwWRENIGIVSQE----PVLfgtTIEENIRYGHLDVTKEDIEQAAKMANAH-------DFIMDLPQkyetlvgergaQL 198
Cdd:COG4161 79 L--LRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLlarlrltDKADRFPL-----------HL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 199 SGGQKQRIAIARALVRNPKILLLDEATSALDTE-SEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQ 276
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQ 222
|
250
....*....|
gi 2119559688 277 GTHNELMSKQ 286
Cdd:COG4161 223 GDASHFTQPQ 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
61-273 |
2.10e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 106.30 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 61 IRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDInlkwwRENIGIV 140
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 141 SQEPVLFG-TTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAIARALVRNPKIL 219
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 220 LLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLS-TIKTADMIAGFKDGVV 273
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
423-822 |
2.67e-25 |
|
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: 111.38 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 423 VISLIAYFVQGY-------MFGRSGEYLTLRLRSMSFKAMLRQeiAFFDDHNNSVGALTtrlatDASQVQGAAGiklGSS 495
Cdd:COG4618 64 LLALGLYAVMGLldavrsrILVRVGARLDRRLGPRVFDAAFRA--ALRGGGGAAAQALR-----DLDTLRQFLT---GPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 496 LMAFC----SVVTgIVIGFVFSWKITLLVIAFLpFVMIGGALEMQMMqgaagkNKEALESAGKIAIESIE-------NIR 564
Cdd:COG4618 134 LFALFdlpwAPIF-LAVLFLFHPLLGLLALVGA-LVLVALALLNERL------TRKPLKEANEAAIRANAfaeaalrNAE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 565 TVASL-TREDMFQK--KFNHELQMPYNIALKKAHLIGigfSLSQAVMFFAYAASFWLGAYLIKQSEvdyvdvfkafsaiL 641
Cdd:COG4618 206 VIEAMgMLPALRRRwqRANARALALQARASDRAGGFS---ALSKFLRLLLQSAVLGLGAYLVIQGE-------------I 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 642 FGGMAIGnAS-----AFAP-DAA--------KAEQSAKEIFKLIDKKPdidnESEKGEQLHTFTANLSFANIIFRYPTRp 707
Cdd:COG4618 270 TPGAMIA-ASilmgrALAPiEQAiggwkqfvSARQAYRRLNELLAAVP----AEPERMPLPRPKGRLSVENLTVVPPGS- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIA 787
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIA 423
|
410 420 430
....*....|....*....|....*....|....*..
gi 2119559688 788 ENIAygdnsR--EVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG4618 424 ENIA-----RfgDADPEKVVAAAKLAGVHEMILRLPD 455
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
67-790 |
3.77e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 112.56 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 67 RYPSRPEaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQIlidgvnlkdinlkWWRENIGIVSQEPVL 146
Cdd:PTZ00243 667 FFELEPK-VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 FGTTIEENIryghLDVTKEDIEQAAKMANAHDFIMDLPQ---KYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:PTZ00243 733 MNATVRGNI----LFFDEEDAARLADAVRVSQLEADLAQlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 224 ATSALDTE-SEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMsKQGIYQQLVTlQSMKSAD 302
Cdd:PTZ00243 809 PLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATLAA-ELKENKD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 303 DNEiEDFNRDDTKRPSLRHQKSTIDMTPKKlaqdkkeeIKEEEKGEKEEEVDASLGRILKLNKSEAPFIVMGCFASLVN- 381
Cdd:PTZ00243 887 SKE-GDADAEVAEVDAAPGGAVDHEPPVAK--------QEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRf 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 382 -GGAMPAFAVI----FSEILGVFAIL-----DEGEQERKIIQYVLMFVGVGVISLIAY---FVQGYMFGRSGEYLTLR-- 446
Cdd:PTZ00243 958 cGGLHAAGFVLatfaVTELVTVSSGVwlsmwSTRSFKLSAATYLYVYLGIVLLGTFSVplrFFLSYEAMRRGSRNMHRdl 1037
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 447 LRSMSfkamlRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIgfvfswkitllVIAFLPF 526
Cdd:PTZ00243 1038 LRSVS-----RGTMSFFD--TTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILV-----------TSASQPF 1099
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 527 VMIG----GALEMQMMQGAAGKNKEA--LESAGKIAI-----ESIENIRTVASLTREDMFQKKFNHELQMPY-------- 587
Cdd:PTZ00243 1100 VLVAlvpcGYLYYRLMQFYNSANREIrrIKSVAKSPVftlleEALQGSATITAYGKAHLVMQEALRRLDVVYscsylenv 1179
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 588 -------------NIALKKAHLIGIG-------------FSLSQAVMFFAYAASFWLG----------------AYLIKQ 625
Cdd:PTZ00243 1180 anrwlgvrveflsNIVVTVIALIGVIgtmlratsqeiglVSLSLTMAMQTTATLNWLVrqvatveadmnsverlLYYTDE 1259
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 626 SEVDYVDVFKAFSAILFG--GMAIGNASAFAPDAAKAEQSAKeifklidkkpdidnesekgeqlHTFTA-NLSFANIIFR 702
Cdd:PTZ00243 1260 VPHEDMPELDEEVDALERrtGMAADVTGTVVIEPASPTSAAP----------------------HPVQAgSLVFEGVQMR 1317
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 703 Y----PtrpdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQE 778
Cdd:PTZ00243 1318 YreglP-----LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQD 1392
|
810
....*....|..
gi 2119559688 779 PVLFDRTIAENI 790
Cdd:PTZ00243 1393 PVLFDGTVRQNV 1404
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
59-289 |
3.83e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 107.36 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSR-----PEA--KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN-- 129
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkPERlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 -LKWWRENIGIVSQEPV-------LFGTTIEENIRYgHLDVTK-EDIEQAAKManahdfiMdlpqkyeTLVGERGAQ--- 197
Cdd:PRK11308 86 aQKLLRQKIQIVFQNPYgslnprkKVGQILEEPLLI-NTSLSAaERREKALAM-------M-------AKVGLRPEHydr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 198 ----LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIV-------QDALekashGRTTIVIAHRLSTIK-TAD-- 263
Cdd:PRK11308 151 yphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEhIADev 225
|
250 260
....*....|....*....|....*.
gi 2119559688 264 MIAGFkdGVVAEQGthnelmSKQGIY 289
Cdd:PRK11308 226 MVMYL--GRCVEKG------TKEQIF 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
64-285 |
5.89e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 64 VHFRYPSRPEAKILYG---VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKW-WRENIGI 139
Cdd:PRK13633 10 VSYKYESNEESTEKLAlddVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEP--VLFGTTIEENIRYG--HLDVTKEDI----EQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIARA 211
Cdd:PRK13633 90 VFQNPdnQIVATIVEEDVAFGpeNLGIPPEEIrervDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKAS--HGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNkkYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
73-297 |
1.11e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.83 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL----KDINLKWWRENIGIVSQ--EPVL 146
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQIRKKVGLVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 FGTTIEENIRYG--HLDVTKEDIEQAAKMAnahdfiMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PRK13649 99 FEETVLKDVAFGpqNFGVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 225 TSALDTESEGIVQDALEKASHGRTTIVIAHRLstiktADMIAGFKDGV-VAEQGTHNELMSKQGIYQQLVTLQS 297
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHL-----MDDVANYADFVyVLEKGKLVLSGKPKDIFQDVDFLEE 241
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
73-256 |
1.56e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDI-NLKWWR--ENIGIVSQEPVLfGT 149
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG---KDVtKLPEYKraKYIGRVFQDPMM-GT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 ----TIEENI--------RYG-HLDVTKEDI----EQAAKMAnahdfiMDLPQKYETLVGergaQLSGGQKQRIAIARAL 212
Cdd:COG1101 94 apsmTIEENLalayrrgkRRGlRRGLTKKRRelfrELLATLG------LGLENRLDTKVG----LLSGGQRQALSLLMAT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRL 256
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
79-268 |
2.06e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 103.32 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD-----PEEGQILIDGVNL--KDINLKWWRENIGIVSQEPVLFGTTI 151
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRYG--------HLDvtkEDIEQAAKMANAHDFIMDLpqkyetlVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:PRK14243 108 YDNIAYGaringykgDMD---ELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2119559688 224 ATSALDTESEGIVQDALEKASHGRTTIVIAHRL-STIKTADMIAGF 268
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFF 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
54-286 |
2.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.32 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 54 NFQGNVQIRGVHFRYPSRP--EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG----VNLKD 127
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 128 IN-LKWWRENIGIVSQEP--VLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFImDLPQKYetlVGERGAQLSGGQKQ 204
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNE 281
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFE 237
|
....*
gi 2119559688 282 LMSKQ 286
Cdd:PRK13645 238 IFSNQ 242
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
60-229 |
2.28e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.40 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLK----DinlkwwR 134
Cdd:COG4525 5 TVRHVSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgaD------R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 eniGIVSQEPVLFG-TTIEENIRYGhLDVTKedIEQAAKMANAHDFImdlpqkyeTLVGERGA------QLSGGQKQRIA 207
Cdd:COG4525 79 ---GVVFQKDALLPwLNVLDNVAFG-LRLRG--VPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVG 144
|
170 180
....*....|....*....|..
gi 2119559688 208 IARALVRNPKILLLDEATSALD 229
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALD 166
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
59-284 |
3.13e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.14 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN-LKWWRENI 137
Cdd:PRK13644 2 IRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAHDFImdlpQKYETlvgERGAQLSGGQKQRIAIARALV 213
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEIGL----EKYRH---RSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEKA-SHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
56-254 |
3.17e-24 |
|
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: 101.74 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 56 QGNVQIRGVHfrypsrpeakilyGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILID----GVNLKD---- 127
Cdd:COG4778 19 QGGKRLPVLD-------------GVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQaspr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 128 --INLKwwRENIGIVSQepvlFGTTIEeniRYGHLDVTKED-IEQAAKMANAHDFIMDLPQKYEtlVGERGAQL-----S 199
Cdd:COG4778 86 eiLALR--RRTIGYVSQ----FLRVIP---RVSALDVVAEPlLERGVDREEARARARELLARLN--LPERLWDLppatfS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 200 GGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIV-IAH 254
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
387-623 |
3.20e-24 |
|
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: 103.67 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 387 AFAVIFSeILGVFA----------ILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAML 456
Cdd:cd18551 2 ILALLLS-LLGTAAslaqpllvknLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 457 RQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQ 536
Cdd:cd18551 81 RLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 537 MMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASF 616
Cdd:cd18551 159 RIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVL 238
|
....*..
gi 2119559688 617 WLGAYLI 623
Cdd:cd18551 239 GVGGARV 245
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
81-229 |
4.34e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.58 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 81 NLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIGIVSQEPVLFG-TTIEENIRYG- 158
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 159 ----HLDVT-KEDIEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK10771 97 npglKLNAAqREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
73-285 |
5.37e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.94 E-value: 5.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL----KDINLKWWRENIGIVSQ--EPVL 146
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPVRKRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 FGTTIEENIRYGHLDVtKEDIEQAAkmANAHDFIMDLpqKYETLVGERGA-QLSGGQKQRIAIARALVRNPKILLLDEAT 225
Cdd:PRK13646 99 FEDTVEREIIFGPKNF-KMNLDEVK--NYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 226 SALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
57-293 |
6.38e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 108.71 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 57 GNVQIRGVHFRY----PSrpeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKW 132
Cdd:PTZ00243 1307 GSLVFEGVQMRYreglPL-----VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 WRENIGIVSQEPVLFGTTIEENIRyGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARAL 212
Cdd:PTZ00243 1382 LRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 213 V-RNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNEL-MSKQGIYQ 290
Cdd:PTZ00243 1461 LkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFH 1540
|
...
gi 2119559688 291 QLV 293
Cdd:PTZ00243 1541 SMV 1543
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
59-284 |
6.80e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.48 E-value: 6.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEP--VLFGTTIEENIRYG--HLDVTKED----IEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAIAR 210
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGmeNQGIPREEmikrVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
60-225 |
7.38e-24 |
|
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: 101.21 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLkdINLKWW---REN 136
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI--TGLPPHriaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGT-TIEENIR---YGHLDvtKEDIEQAAkmanahDFIMDL-PQKYETLvGERGAQLSGGQKQRIAIARA 211
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLLlgaYARRD--RAEVRADL------ERVYELfPRLKERR-RQRAGTLSGGEQQMLAIGRA 150
|
170
....*....|....
gi 2119559688 212 LVRNPKILLLDEAT 225
Cdd:COG0410 151 LMSRPKLLLLDEPS 164
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
59-283 |
9.97e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.93 E-value: 9.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEP-----------VLFGttieeniRY----GHLdvTKEDieqAAKMANAHDFiMDLpqkyETLVGERGAQLSGGQK 203
Cdd:COG4604 79 ILRQENhinsrltvrelVAFG-------RFpyskGRL--TAED---REIIDEAIAY-LDL----EDLADRYLDELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 204 QRIAIARALVRNPKILLLDEATSALDTE-SEGIVQdALEKAS--HGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTH 279
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKhSVQMMK-LLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKDGRVVAQGTP 220
|
....
gi 2119559688 280 NELM 283
Cdd:COG4604 221 EEII 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
81-284 |
1.18e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.34 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 81 NLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE----NIGIVSQEPVLF-GTTIEENI 155
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGhldVTKEDIEQAAKMANAHDFIMDLpqKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGI 235
Cdd:PRK10070 128 AFG---MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 236 VQDALEK--ASHGRTTIVIAHRL-STIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK10070 203 MQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
693-822 |
1.34e-23 |
|
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: 99.97 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 693 NLSFANIIFRYPTRPDTTiLKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQI 772
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPA-LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2119559688 773 GIVSQEPVLFDRTIAENIAYGDnsREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPN 128
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
59-277 |
1.73e-23 |
|
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: 99.21 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRenIG 138
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRYGH--LDVTKEDIEQAAKMANAHDFimdlpqkyetlVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:cd03268 76 ALIEAPGFYPNlTARENLRLLArlLGIRKKRIDEVLDVVGLKDS-----------AKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 216 PKILLLDEATSALDTesEGI--VQDAL-EKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG 277
Cdd:cd03268 145 PDLLILDEPTNGLDP--DGIkeLRELIlSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
57-294 |
2.27e-23 |
|
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: 100.70 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 57 GNVQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDpEEGQILIDGVNLKDINLKWWREN 136
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGTTIEENIR-YGHLdvTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVT 294
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
63-260 |
2.84e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 101.71 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 63 GVHF------RYPSRPEA--KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWR 134
Cdd:PRK15079 15 KVHFdikdgkQWFWQPPKtlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 E---NIGIVSQEPV-------LFGTTIEENIRYGHLDVTKEDIEQAAKManahdfIMD----LPQkyetLVGERGAQLSG 200
Cdd:PRK15079 95 AvrsDIQMIFQDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKA------MMLkvglLPN----LINRYPHEFSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 201 GQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIK 260
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlqREMGLSLIFIAHDLAVVK 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
415-821 |
3.89e-23 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 104.41 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 415 VLMFVGVG-----VISLIAYFVQGYMFGRSGEyLTLRLRSMSFKAMLRQEIAFFDDHNNsvGALTTRLATDASQVQGAAG 489
Cdd:PRK10789 35 ILMWIGTMvliavVVYLLRYVWRVLLFGASYQ-LAVELREDFYRQLSRQHPEFYLRHRT--GDLMARATNDVDRVVFAAG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 490 ---IKLGSSLMAFCSVVtgIVIGFVFSWKITLLVIAFLPFVMI-----GGALEMQMMQGAAgknkeALESAGKIAIESIE 561
Cdd:PRK10789 112 egvLTLVDSLVMGCAVL--IVMSTQISWQLTLLALLPMPVMAImikryGDQLHERFKLAQA-----AFSSLNDRTQESLT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 562 NIRTVASLTREDMFQKKFNhelQMPYNIALKKAHL------------IGIGFSlsqavMFFAYAASFWLgaylikqsevd 629
Cdd:PRK10789 185 SIRMIKAFGLEDRQSALFA---ADAEDTGKKNMRVaridarfdptiyIAIGMA-----NLLAIGGGSWM----------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 630 yvdvfkafsaILFGGMAIGNASAFA--------PDAAKA-------EQSA--KEIFKLIDKKPDIDNESEK-GEQLHTFT 691
Cdd:PRK10789 246 ----------VVNGSLTLGQLTSFVmylglmiwPMLALAwmfniveRGSAaySRIRAMLAEAPVVKDGSEPvPEGRGELD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 692 ANLSfaniIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQ 771
Cdd:PRK10789 316 VNIR----QFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2119559688 772 IGIVSQEPVLFDRTIAENIAYGdnSREVTMDEIIDAARKANIHNFIASLP 821
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNIALG--RPDATQQEIEHVARLASVHDDILRLP 438
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
61-232 |
4.17e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.99 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 61 IRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDgvnlkdinlKWWRenIGIV 140
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 141 SQEPVLF-GTTIEENIRYGH--LDVTKEDIEQA-AKMANAHDFIM---------------DLPQKYETLVGERG------ 195
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDaeLRALEAELEELeAKLAEPDEDLErlaelqeefealggwEAEARAEEILSGLGfpeedl 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2119559688 196 ----AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 232
Cdd:COG0488 147 drpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
396-620 |
4.45e-23 |
|
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: 100.25 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 396 LGVFAILDEG---EQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGA 472
Cdd:cd18575 17 QGLRLLIDQGfaaGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 473 LTTRLATDASQVQGAagikLGSSL-MAFCSVVT---GIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEA 548
Cdd:cd18575 95 VLSRLTTDTTLIQTV----VGSSLsIALRNLLLligGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDR 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 549 LESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGA 620
Cdd:cd18575 171 LADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGA 242
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
471-822 |
5.01e-23 |
|
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: 103.98 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 471 GALTTRLATDASQVQGA---AGIKLGSSLMAFCSVVTGIvigFVFSWKITLLVIAFLpfvMIGGALeMQMMQGAAGKNKE 547
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLyvrVIVPAGVALVVGAAAVAAI---AVLSVPAALILAAGL---LLAGFV-APLVSLRAARAAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 548 ALE--SAGKIAIESIENIRTVASLT---REDMFQKKF---NHELQmpyNIALKKAHLIGIGFSLSQAVMFFAYAASFWLG 619
Cdd:TIGR02868 183 QALarLRGELAAQLTDALDGAAELVasgALPAALAQVeeaDRELT---RAERRAAAATALGAALTLLAAGLAVLGALWAG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 620 AYLIKQSEVDYVdvfkAFSAILFGGMAIGNASAFAPDAA----KAEQSAKEIFKLIDKKPDI-DNESEKGEQLHTFTANL 694
Cdd:TIGR02868 260 GPAVADGRLAPV----TLAVLVLLPLAAFEAFAALPAAAqqltRVRAAAERIVEVLDAAGPVaEGSAPAAGAVGLGKPTL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 695 SFANIIFRYPTRPDttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGI 774
Cdd:TIGR02868 336 ELRDLSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2119559688 775 VSQEPVLFDRTIAENIAYGdnSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:TIGR02868 414 CAQDAHLFDTTVRENLRLA--RPDATDEELWAALERVGLADWLRALPD 459
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
712-822 |
5.08e-23 |
|
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: 95.79 E-value: 5.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDR-TIAENI 790
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 2119559688 791 AYG----DNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:pfam00005 81 RLGlllkGLSKREKDARAEEALEKLGLGDLADRPVG 116
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
64-284 |
6.66e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.89 E-value: 6.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 64 VHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDI-------------NL 130
Cdd:PRK10619 11 LHKRYG---EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEPVLFG-TTIEENIRYGHLDV----TKEDIEQAAKMANAHDFIMDLPQKYEtlvgergAQLSGGQKQR 205
Cdd:PRK10619 88 RLLRTRLTMVFQHFNLWShMTVLENVMEAPIQVlglsKQEARERAVKYLAKVGIDERAQGKYP-------VHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNELM 283
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLF 240
|
.
gi 2119559688 284 S 284
Cdd:PRK10619 241 G 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
79-278 |
9.08e-23 |
|
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: 103.23 E-value: 9.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKS----TIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE----NIGIVSQEPV----- 145
Cdd:COG4172 28 GVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMtslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 146 LFgtTIE----ENIRYgHLDVTKED-------------IEQAAKMANA--HdfimdlpqkyetlvgergaQLSGGQKQRI 206
Cdd:COG4172 108 LH--TIGkqiaEVLRL-HRGLSGAAararalellervgIPDPERRLDAypH-------------------QLSGGQRQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 207 AIARALVRNPKILLLDEATSALDTesegIVQ----DALE--KASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGT 278
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDV----TVQaqilDLLKdlQRELGMALLLITHDLGVVrRFADRVAVMRQGEIVEQGP 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
694-790 |
9.20e-23 |
|
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: 96.23 E-value: 9.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwLRSQIG 773
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90
....*....|....*..
gi 2119559688 774 IVSQEPVLFDRTIAENI 790
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL 95
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
79-257 |
1.19e-22 |
|
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: 97.51 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDinlkwWREN----IGIVS--QEPVLFGT-TI 151
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-----LPPHeiarLGIGRtfQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRYGHLDVTKEDI-------EQAAKMANAHDFI--MDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLD 222
Cdd:cd03219 93 LENVMVAAQARTGSGLllararrEEREARERAEELLerVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 2119559688 223 EATSAL-DTESEGIVQDALEKASHGRTTIVIAHRLS 257
Cdd:cd03219 169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMD 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
59-265 |
1.51e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.03 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKD----INLKw 132
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaIALG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 wrenIGIVSQEPVLFGT-TIEENIRYGH--LDVTKEDIEQAAKManahdfIMDLPQKY------ETLVGergaQLSGGQK 203
Cdd:COG3845 82 ----IGMVHQHFMLVPNlTVAENIVLGLepTKGGRLDRKAARAR------IRELSERYgldvdpDAKVE----DLSVGEQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 204 QRIAIARALVRNPKILLLDEATSALdTESEgiVQ---DALEK-ASHGRTTIVIAHRLSTIKT-ADMI 265
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVL-TPQE--ADelfEILRRlAAEGKSIIFITHKLREVMAiADRV 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
693-822 |
1.62e-22 |
|
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: 96.79 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 693 NLSFANIIFRYptRPDT-TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQ 771
Cdd:cd03244 2 DIEFKNVSLRY--RPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 772 IGIVSQEPVLFDRTIAENIaygDNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPG 127
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
56-285 |
2.02e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.29 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 56 QGNVQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD--PE---EGQILIDGVNLKDINL 130
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEPVLFGT-TIEENIRYG----HLDVTKEDIEQAAKMAnahdfiMDLPQKYETL---VGERGAQLSGGQ 202
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWA------LEKAQLWDEVkdrLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 203 KQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAH-RLSTIKTADMIAGFKDGVVAEQGTHNE 281
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
....
gi 2119559688 282 LMSK 285
Cdd:PRK14247 232 VFTN 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
61-229 |
2.05e-22 |
|
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: 96.84 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 61 IRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINL-KWWRENIGI 139
Cdd:cd03218 3 AENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVLF-GTTIEENIRyGHLDVTKEDIEQAAKMANA--HDFimdlpqKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:cd03218 80 LPQEASIFrKLTVEENIL-AVLEIRGLSKKEREEKLEEllEEF------HITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170
....*....|...
gi 2119559688 217 KILLLDEATSALD 229
Cdd:cd03218 153 KFLLLDEPFAGVD 165
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
59-277 |
2.63e-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: 95.90 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRY-PSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENI 137
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFG-TTIEENIRY-GHLdvtkedieQAAKMANAHDFIMDLPQKY--ETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYfAGL--------YGLKGDELTARLEELADRLgmEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQG 277
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
75-298 |
3.99e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.62 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVL-FGTTIEE 153
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NIRYG---HLD----VTKED---IEQAakMANAHdfimdlpqkYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:PRK11231 96 LVAYGrspWLSlwgrLSAEDnarVNQA--MEQTR---------INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 224 ATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELMSkQGIYQQLVTLQSM 298
Cdd:PRK11231 165 PTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMT-PGLLRTVFDVEAE 240
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-256 |
5.21e-22 |
|
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: 102.30 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 16 MPHLQTLATARGAAYYLYQLITMDPPidsystEGKKLDNFQGNVQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGS 95
Cdd:TIGR01271 1181 LPQEEPRPSGGGGKYQLSTVLVIENP------HAQKCWPSGGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGR 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 96 SGCGKSTIVQLLQRFYDpEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRyGHLDVTKEDIEQAAKMAN 175
Cdd:TIGR01271 1254 TGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVG 1331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 176 AHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHR 255
Cdd:TIGR01271 1332 LKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHR 1411
|
.
gi 2119559688 256 L 256
Cdd:TIGR01271 1412 V 1412
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
58-282 |
5.91e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.56 E-value: 5.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 58 NVQIRGVhfrYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENI 137
Cdd:PRK11000 3 SVTLRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLF-GTTIEENIRYGhLDVTKEDIEQAAKMANAHDFIMDLpqkyETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:PRK11000 78 GMVFQSYALYpHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 217 KILLLDEATSALDTESEgiVQDALEKAS-H---GRTTIVIAH-RLSTIKTADMIAGFKDGVVAEQGTHNEL 282
Cdd:PRK11000 153 SVFLLDEPLSNLDAALR--VQMRIEISRlHkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
56-255 |
7.91e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.27 E-value: 7.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 56 QGNVQIRGVHFRYPS-RPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI-DGvnlkdinlkww 133
Cdd:COG4178 360 DGALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAG----------- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 rENIGIVSQEPVLFGTTIEENIRY--GHLDVTKEDIEQAAKMANAHDFIMDLPQkyetlVGERGAQLSGGQKQRIAIARA 211
Cdd:COG4178 426 -ARVLFLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERLDE-----EADWDQVLSLGEQQRLAFARL 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHR 255
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
73-290 |
8.95e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.23 E-value: 8.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGV---------------NLKDI-NLKWWREN 136
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknnhelitnpYSKKIkNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDieqAAKMANAHDFIMDLpqKYETLvgERGA-QLSGGQKQRIAIARA 211
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGpvALGVKKSE---AKKLAKFYLNKMGL--DDSYL--ERSPfGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 212 LVRNPKILLLDEATSALDTESEG-IVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMSKQGIY 289
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
.
gi 2119559688 290 Q 290
Cdd:PRK13631 271 N 271
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
76-231 |
1.09e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.09 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE---EGQILIDGVNLKDINLKwwRENIGIVSQEPVLFG-TTI 151
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRYGhL--DVTKED----IEQAAKMANAHDFimdlpqkyetlvGERG-AQLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:COG4136 94 GENLAFA-LppTIGRAQrrarVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRALLAEPRALLLDEP 160
|
....*..
gi 2119559688 225 TSALDTE 231
Cdd:COG4136 161 FSKLDAA 167
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
708-807 |
1.30e-21 |
|
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: 94.17 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD-----PADGIVSLDGHNLKDLNLQ--WLRSQIGIVSQEPV 780
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlELRRRVGMVFQKPN 91
|
90 100
....*....|....*....|....*..
gi 2119559688 781 LFDRTIAENIAYGDNSREVTMDEIIDA 807
Cdd:cd03260 92 PFPGSIYDNVAYGLRLHGIKLKEELDE 118
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
371-642 |
1.31e-21 |
|
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: 95.95 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIfseILGVFAILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSM 450
Cdd:cd18552 1 LALAILGMILVAATTAALAWL---LKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 451 SFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIG 530
Cdd:cd18552 78 LFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 531 GALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFF 610
Cdd:cd18552 156 IRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAI 235
|
250 260 270
....*....|....*....|....*....|..
gi 2119559688 611 AYAASFWLGAYLIKQSEVDyVDVFKAFSAILF 642
Cdd:cd18552 236 AIALVLWYGGYQVISGELT-PGEFISFITALL 266
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
60-254 |
1.34e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWwreniGI 139
Cdd:PRK11248 3 QISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQ-EPVLFGTTIEENIRYGhldVTKEDIEQAAKMANAHDFImdlpqkyeTLVGERGA------QLSGGQKQRIAIARAL 212
Cdd:PRK11248 75 VFQnEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQML--------KKVGLEGAekryiwQLSGGQRQRVGIARAL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAH 254
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
77-254 |
1.37e-21 |
|
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: 94.45 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG-----------VNLKDINLKWWRenigivsqepv 145
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitepgpdrmVVFQNYSLLPWL----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 146 lfgtTIEENIrYGHLDVTKEDIEQAAKMANAHDFImdlpqkyeTLVG------ERGAQLSGGQKQRIAIARALVRNPKIL 219
Cdd:TIGR01184 70 ----TVRENI-ALAVDRVLPDLSKSERRAIVEEHI--------ALVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVL 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 2119559688 220 LLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAH 254
Cdd:TIGR01184 137 LLDEPFGALDALTRGNLQEELMQiwEEHRVTVLMVTH 173
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
75-271 |
2.06e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.85 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYdPE---EGQILIDGVNLKDINLK-WWRENIGIVSQEPVLF-GT 149
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVkEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLpqKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALd 229
Cdd:PRK13549 98 SVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2119559688 230 TESE-----GIVQDAlekASHGRTTIVIAHRLSTIKT-ADMIAGFKDG 271
Cdd:PRK13549 175 TESEtavllDIIRDL---KAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
76-286 |
2.83e-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: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwreNIGIVSQEPVLFGTTIEENI 155
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGhLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD--TESE 233
Cdd:TIGR01271 508 IFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTEKE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 234 gIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:TIGR01271 587 -IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
58-229 |
4.51e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 58 NVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNlkdiNLKWWRE 135
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVN----ELEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLF-GTTIEENIRYGhLD---VTKEDIEQ----AAKmanahdfIMDLpqkyETLVGERGAQLSGGQKQRIA 207
Cdd:PRK11650 77 DIAMVFQNYALYpHMSVRENMAYG-LKirgMPKAEIEErvaeAAR-------ILEL----EPLLDRKPRELSGGQRQRVA 144
|
170 180
....*....|....*....|..
gi 2119559688 208 IARALVRNPKILLLDEATSALD 229
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLD 166
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
60-278 |
7.10e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.91 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDinlkWWRE---- 135
Cdd:PRK13548 4 EARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD----WSPAelar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVL-FGTTIEENI---RYGHLDVTKED---IEQAakMANAhdfimDLpqkyETLVGERGAQLSGGQKQRIAI 208
Cdd:PRK13548 77 RRAVLPQHSSLsFPFTVEEVVamgRAPHGLSRAEDdalVAAA--LAQV-----DL----AHLAGRDYPQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 209 ARALVR------NPKILLLDEATSALD-TESEGIVQDALEKA-SHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGT 278
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
68-285 |
8.46e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 8.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 68 YPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEP--V 145
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 146 LFGTTIEENIRYGHLDV------TKEDIEQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIARALVRNPKIL 219
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLgldeetVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 220 LLDEATSALDTESEGIVQDALEKAS--HGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPetYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
71-254 |
9.60e-21 |
|
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: 91.56 E-value: 9.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 71 RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL---QRFYDPEEGQILIDGVNLKDinlKWWRENIGIVSQEPVLF 147
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 -GTTIEENIRY-GHLDVTKEdieQAAKMANAHDFIMDLPQKYETLVG-ERGAQLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:cd03234 94 pGLTVRETLTYtAILRLPRK---SSDAIRKKRVEDVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|.
gi 2119559688 225 TSALDTESE-GIVQDALEKASHGRTTIVIAH 254
Cdd:cd03234 171 TSGLDSFTAlNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
73-282 |
1.02e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.61 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQI--------------LIDGVNLKDI---------- 128
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKEKVLEKLViqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 129 NLKWWRENIGIVSQ--EPVLFGTTIEENIRYG--HLDVTKEDIEQ-AAKMANahdfIMDLPQKYEtlvgERGA-QLSGGQ 202
Cdd:PRK13651 99 KIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEEAKKrAAKYIE----LVGLDESYL----QRSPfELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 203 KQRIAIARALVRNPKILLLDEATSALDTESegiVQDALEKASH----GRTTIVIAHRL-STIKTADMIAGFKDG-VVAEQ 276
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEIFDNlnkqGKTIILVTHDLdNVLEWTKRTIFFKDGkIIKDG 247
|
....*.
gi 2119559688 277 GTHNEL 282
Cdd:PRK13651 248 DTYDIL 253
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
76-277 |
1.03e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.60 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE-----EGQILIDGVNL--KDINLKWWRENIGIVSQEPVLF- 147
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 GTTIEENI----RYGHLDVTKEDI----EQAAKMANAHDFIMDLPQKYEtlvgergAQLSGGQKQRIAIARALVRNPKIL 219
Cdd:PRK14267 99 HLTIYDNVaigvKLNGLVKSKKELdervEWALKKAALWDEVKDRLNDYP-------SNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 220 LLDEATSALDTESEGIVQDALEKASHGRTTIVIAHR-LSTIKTADMIAGFKDGVVAEQG 277
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
74-286 |
1.08e-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: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 74 AKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwreNIGIVSQEPVLFGTTIEE 153
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NIRYGhLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD--TE 231
Cdd:cd03291 117 NIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 232 SEgIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:cd03291 196 KE-IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
60-223 |
1.38e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKST----IVQLLQrfydPEEGQILIDGvnlKDI-NLKWW- 133
Cdd:COG1137 5 EAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDG---EDItHLPMHk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 --RENIGIVSQEPVLF-GTTIEENIRyGHLDVTKEDIEQAAkmanahdfimdlpQKYETLVGE---------RGAQLSGG 201
Cdd:COG1137 75 raRLGIGYLPQEASIFrKLTVEDNIL-AVLELRKLSKKERE-------------ERLEELLEEfgithlrksKAYSLSGG 140
|
170 180
....*....|....*....|..
gi 2119559688 202 QKQRIAIARALVRNPKILLLDE 223
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDE 162
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
79-282 |
1.54e-20 |
|
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: 90.89 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL----KDInlkwwRENIGIVSQEPVL-FGTTIEE 153
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrepREV-----RRRIGIVFQDLSVdDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NIR-----YGHL-DVTKEDIEQAAKManahdfiMDLPQKYETLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:cd03265 93 NLYiharlYGVPgAERRERIDELLDF-------VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 228 LDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNEL 282
Cdd:cd03265 162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
60-235 |
1.78e-20 |
|
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: 91.05 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLkdinLKW-----WR 134
Cdd:TIGR03410 2 EVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI----TKLppherAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGT-TIEENIRYGhLDVtkedieQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:TIGR03410 75 AGIAYVPQGREIFPRlTVEENLLTG-LAA------LPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180
....*....|....*....|..
gi 2119559688 214 RNPKILLLDEATsaldtesEGI 235
Cdd:TIGR03410 148 TRPKLLLLDEPT-------EGI 162
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
60-283 |
2.18e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.77 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:PRK10575 13 ALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQE-PVLFGTTIEENI------------RYGHLDvtKEDIEQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRI 206
Cdd:PRK10575 90 LPQQlPAAEGMTVRELVaigrypwhgalgRFGAAD--REKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 207 AIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAhRLSTIKTA----DMIAGFKDGVVAEQGTHNEL 282
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAEL 235
|
.
gi 2119559688 283 M 283
Cdd:PRK10575 236 M 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
76-284 |
2.90e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.26 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRF---YDPE---EGQILIDGVNLKDINLKWWRENIGIVSQEPVLF-G 148
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 228
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 229 DTESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
60-281 |
3.30e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.56 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN----LKWWR 134
Cdd:PRK10535 6 ELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQE-PVLFGTTIEENIRyghLDVTKEDIEQAAKMANAHDFIMDLpqKYETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:PRK10535 86 EHFGFIFQRyHLLSHLTAAQNVE---VPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTADMIAGFKDG-VVAEQGTHNE 281
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGeIVRNPPAQEK 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
63-297 |
3.59e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.22 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 63 GVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINLKWWRENIGIV 140
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 141 SQEP--VLFGTTIEENIRYG--HLDVTKEDI----EQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIARAL 212
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSlrNLGVPEAEItrrvDEALTLVDAQHFRHQPIQ-----------CLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG------THNELMS 284
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAME 231
|
250
....*....|....
gi 2119559688 285 KQGIYQQ-LVTLQS 297
Cdd:PRK13638 232 QAGLTQPwLVKLHT 245
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
694-811 |
5.35e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 90.53 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRP-DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDlnlqwLRSQI 772
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2119559688 773 GIVSQEPVLFD-RTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERAREL 122
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
80-299 |
5.48e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.67 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPvlfGTTIEENIRYGH 159
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP---NTSLNPRLNIGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 160 -LDV-----TKEDIEQAAKMANahdfimdlpqkyETL--VGERGAQ-------LSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:COG4167 109 iLEEplrlnTDLTAEEREERIF------------ATLrlVGLLPEHanfyphmLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 225 TSALDTESEG-IVQDALE-KASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNELMS--KQGIYQQLVTLQSMK 299
Cdd:COG4167 177 LAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKhISDKVLVMHQGEVVEYGKTAEVFAnpQHEVTKRLIESHFGE 256
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
694-811 |
6.04e-20 |
|
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: 89.31 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2119559688 774 IVSQEPV--LFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEA 118
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
67-263 |
7.03e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.06 E-value: 7.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 67 RYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwRENIGIVSQ---E 143
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 144 PVLFGTTIEENI---RYGHLD----VTKEDIEQAAKMANAhdfiMDLpqkyETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:NF040873 67 PDSLPLTVRDLVamgRWARRGlwrrLTRDDRAAVDDALER----VGL----ADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2119559688 217 KILLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTIKTAD 263
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
75-231 |
8.19e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.07 E-value: 8.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRE-NIGIVSQEPVLF-GTTIE 152
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSRLHARDrKVGFVFQHYALFrHMTVF 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 153 ENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQkYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 231
Cdd:PRK10851 93 DNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQ-LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
79-257 |
1.00e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 89.71 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDIN-LK-WWRENIGIVS--QEPVLFGT-TIEE 153
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG---RDITgLPpHRIARLGIARtfQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NIRYGHLDVTKEDIEQA--------AKMANAHDFIMD------LPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKIL 219
Cdd:COG0411 99 NVLVAAHARLGRGLLAAllrlprarREEREARERAEEllervgLADRADEPAGN----LSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2119559688 220 LLDEATSAL-DTESEGIVQ--DALeKASHGRTTIVIAHRLS 257
Cdd:COG0411 175 LLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMD 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
59-285 |
1.07e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRY-PSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL----KDINLKW 132
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFAsRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 WRENIGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEqaaKMANAHDFIMDLPQKYETlvgERGAQLSGGQKQRIAI 208
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGpqNFGIPKEKAE---KIAAEKLEMVGLADEFWE---KSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 209 ARALVRNPKILLLDEATSALDTESEGIVQDALEKASH-GRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
59-277 |
1.86e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.50 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRY-PSRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG----VNLKDINLKW 132
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 WRENIGIVSQ--EPVLFGTTIEENIRYGHLDV---TKEDIEQAAKMANAhdfiMDLPqkyETLVGERGAQLSGGQKQRIA 207
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFgfsEDEAKEKALKWLKK----VGLS---EDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 208 IARALVRNPKILLLDEATSALDTES-EGIVQDALEKASHGRTTIVIAHRLstiktaDMIAGFKDGV-VAEQG 277
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNM------DDVAEYADDVlVLEHG 221
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
410-623 |
2.07e-19 |
|
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: 89.29 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 410 KIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAG 489
Cdd:cd18784 34 KFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTVS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 490 IKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASL 569
Cdd:cd18784 112 LNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSF 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 570 TREDMFQKKFNHELQMPYNIALKKAHLIGiGFSLSQAVMFFAYAAS-FWLGAYLI 623
Cdd:cd18784 192 ANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELALTVStLYYGGHLV 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
73-277 |
2.96e-19 |
|
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: 86.95 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINlkwwRENIGIVSQEPVLF-GTTI 151
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRY-GHL-DVTKEDIEqaakmANAHDFI--MDLPQKYEtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:cd03269 88 IDQLVYlAQLkGLKKEEAR-----RRIDEWLerLELSEYAN----KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 228 LDTESEGIVQDAL-EKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG 277
Cdd:cd03269 159 LDPVNVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
76-254 |
3.03e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.53 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN----LKWWRENIGIVSQEPVLFGT-T 150
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAKLRAKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIRYGHLdVTKEDIEQAAKMANAHDFIMDLPQKYETLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 230
Cdd:PRK10584 105 ALENVELPAL-LRGESSRQSRNGAKALLEQLGLGKRLDHL----PAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180
....*....|....*....|....*.
gi 2119559688 231 ESEGIVQDALEKAS--HGRTTIVIAH 254
Cdd:PRK10584 180 QTGDKIADLLFSLNreHGTTLILVTH 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
694-811 |
4.19e-19 |
|
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: 86.76 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPT-RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNlqwlrSQI 772
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2119559688 773 GIVSQEPVLFD-RTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL 115
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
70-265 |
5.42e-19 |
|
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: 84.90 E-value: 5.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 70 SRPEAKILYG-VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDgvnlkdinlkwWRENIGIVSQEPVLFG 148
Cdd:cd03223 9 ATPDGRVLLKdLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-----------EGEDLLFLPQRPYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYGHLDVtkedieqaakmanahdfimdlpqkyetlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 228
Cdd:cd03223 78 GTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180 190
....*....|....*....|....*....|....*..
gi 2119559688 229 DTESEGIVQDALEKasHGRTTIVIAHRLSTIKTADMI 265
Cdd:cd03223 123 DEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRV 157
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
80-302 |
7.14e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.35 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFG-TTIEENI--- 155
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQELVarg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGHLDV----TKEDIEQAAKMANAHDFIMDLPQKYETlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 231
Cdd:PRK10253 106 RYPHQPLftrwRKEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 232 SEgivQDALEKASH-----GRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELMSKQGIyQQLVTLQSMKSAD 302
Cdd:PRK10253 178 HQ---IDLLELLSElnrekGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAELI-ERIYGLRCMIIDD 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-295 |
9.37e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 9.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 31 YLYQLITMDP-----PIDSYSTEGKKLDNFQGNVQIRGVHFRYpSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQ 105
Cdd:PRK15134 252 YTQKLLNSEPsgdpvPLPEPASPLLDVEQLQVAFPIRKGILKR-TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 106 LLQRFYdPEEGQILIDGVNLKDINLKW---WRENIGIVSQEP---------VLfgTTIEENIRYGHLDVTKEDIEQAAKM 173
Cdd:PRK15134 331 ALLRLI-NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 174 AnAHDFIMD--LPQKYEtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTT 249
Cdd:PRK15134 408 V-MEEVGLDpeTRHRYP-------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSlqQKHQLAY 479
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2119559688 250 IVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMS--KQGIYQQLVTL 295
Cdd:PRK15134 480 LFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAapQQEYTRQLLAL 528
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
387-627 |
1.51e-18 |
|
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: 87.08 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 387 AFAVIFSEILGVF--AILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFd 464
Cdd:cd18541 13 LLQLLIPRIIGRAidALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 465 dHNNSVGALTTRLATDASQVQGAAGIKLgssLMAFCSVVTGI-VIGFVF--SWKITLLVIAFLPFVMIGGALEMQMMQGA 541
Cdd:cd18541 92 -QKNRTGDLMARATNDLNAVRMALGPGI---LYLVDALFLGVlVLVMMFtiSPKLTLIALLPLPLLALLVYRLGKKIHKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 542 AGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAY 621
Cdd:cd18541 168 FRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGR 247
|
....*.
gi 2119559688 622 LIKQSE 627
Cdd:cd18541 248 LVIRGT 253
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
70-253 |
1.71e-18 |
|
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: 84.47 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGT 149
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVTKEDIEQAAKMANAHDFiMDLPqkyetlvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*
gi 2119559688 230 TESEGIVQDALekASH-GRTTIVIA 253
Cdd:cd03231 158 KAGVARFAEAM--AGHcARGGMVVL 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
694-791 |
1.84e-18 |
|
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: 85.43 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90
....*....|....*....
gi 2119559688 774 IVSQEPVLF-DRTIAENIA 791
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIA 97
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
60-285 |
2.14e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.50 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRypsrPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL--QRFYDPEEGQILIDGVNLKDinlkwW--- 133
Cdd:COG0396 2 EIKNLHVS----VEGKeILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILE-----Lspd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 ---RENIGIVSQEPVLF-GTTIEENIR--YGHLDVTKEDIEQAAKMANAHDFIMDLPQKYetlvGERG--AQLSGGQKQR 205
Cdd:COG0396 73 eraRAGIFLAFQYPVEIpGVSVSNFLRtaLNARRGEELSAREFLKLLKEKMKELGLDEDF----LDRYvnEGFSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH--RLSTIKTADMIAGFKDGVVAEQGTHnEL 282
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-EL 227
|
...
gi 2119559688 283 MSK 285
Cdd:COG0396 228 ALE 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
60-277 |
3.34e-18 |
|
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: 83.73 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFrypSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE--EGQILIDGVNLKDINL-KWWREN 136
Cdd:cd03217 2 EIKDLHV---SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPeERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLF-GTTIEENIRYghldvtkedieqaakmanahdfimdlpqkyetlVGErgaQLSGGQKQRIAIARALVRN 215
Cdd:cd03217 79 IFLAFQYPPEIpGVKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH--RLSTIKTADMIAGFKDGVVAEQG 277
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
694-811 |
4.35e-18 |
|
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: 88.42 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRP--DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWL 768
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2119559688 769 RSQIGIVSQEPV--LFDR-TIAENIAYG-DNSREVTMDEIIDAARKA 811
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPlRLHGLLSRAERRERVAEL 387
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
59-254 |
5.21e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 81.34 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDgvnlkdinlkwwrenig 138
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 ivsqepvlfgttieENIRYGHLDvtkedieqaakmanahdfimdlpqkyetlvgergaQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03221 61 --------------STVKIGYFE-----------------------------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*...
gi 2119559688 219 LLLDEATSALDTESegivQDALEKA--SHGRTTIVIAH 254
Cdd:cd03221 92 LLLDEPTNHLDLES----IEALEEAlkEYPGTVILVSH 125
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
694-790 |
9.44e-18 |
|
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: 81.49 E-value: 9.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90
....*....|....*..
gi 2119559688 774 IVSQEPVLFDRTIAENI 790
Cdd:cd03246 80 YLPQDDELFSGSIAENI 96
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
388-623 |
1.26e-17 |
|
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: 84.02 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 388 FAVIFSEILGVFA------ILDE---GEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQ 458
Cdd:cd18542 6 LALLLATALNLLIpllirrIIDSvigGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 459 EIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMM 538
Cdd:cd18542 86 SFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 539 QGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWL 618
Cdd:cd18542 164 RPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWV 243
|
....*
gi 2119559688 619 GAYLI 623
Cdd:cd18542 244 GGYLV 248
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
77-259 |
1.35e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.62 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVN---LKDINLKWWRENIGIVSQEP-VLFGTTIE 152
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 153 ENIRYGHL--DVTKEDIEQAAKMANAHDFIMDLPQKYETlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 230
Cdd:PRK10908 98 DNVAIPLIiaGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190
....*....|....*....|....*....|
gi 2119559688 231 E-SEGIVQDALEKASHGRTTIVIAHRLSTI 259
Cdd:PRK10908 171 AlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
411-628 |
1.35e-17 |
|
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: 83.98 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 411 IIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQV-----Q 485
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALnelftS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 486 GAAGIkLGSSLMafcsvVTGIVIG-FVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEAL-ESAGKIAiESIENI 563
Cdd:cd18544 118 GLVTL-IGDLLL-----LIGILIAmFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLsRLNAFLQ-ESISGM 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 564 RTVASLTREDMFQKKFNHelqmpYNIALKKAHLIGI-GFSLSQAVMFFAYAAS----FWLGAYLIKQSEV 628
Cdd:cd18544 191 SVIQLFNREKREFEEFDE-----INQEYRKANLKSIkLFALFRPLVELLSSLAlalvLWYGGGQVLSGAV 255
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
59-286 |
1.55e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.66 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWRE 135
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLF-GTTIEENIRY---GHLDVTKEDIEQAAKManahdfimdlpqKYETlVGERGA------QLSGGQKQR 205
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYplrEHTQLPAPLLHSTVMM------------KLEA-VGLRGAaklmpsELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHR----LSTIKTADMIAGFKdgVVAEqGTH 279
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVADKK--IVAH-GSA 228
|
....*..
gi 2119559688 280 NELMSKQ 286
Cdd:PRK11831 229 QALQANP 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
72-271 |
1.81e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.38 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 72 PEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYdPE---EGQILIDG--VNLKDINLKwwrENIGIV--SQE- 143
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevCRFKDIRDS---EALGIViiHQEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 144 ---PVLfgtTIEENIRYGHldvtkediEQAAKManahdfIMDLPQKY----------------ETLVGERGAqlsgGQKQ 204
Cdd:NF040905 88 aliPYL---SIAENIFLGN--------ERAKRG------VIDWNETNrrarellakvgldespDTLVTDIGV----GKQQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 205 RIAIARALVRNPKILLLDEATSAL-DTESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDG 271
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDG 215
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
370-784 |
1.98e-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: 86.39 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 370 FIVMGCFASLVNGGAMpafAVIFSEILGVFAILDegeqerkiiQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRS 449
Cdd:COG4615 18 ALLLGLLSGLANAGLI---ALINQALNATGAALA---------RLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 450 MSFKAMLRQEIAFFDdhnnSVGA--LTTRLATDASQVQGAAgiklgSSLMAFCSVVTGIVIGFVF----SWKITLLVIAF 523
Cdd:COG4615 86 RLSRRILAAPLERLE----RIGAarLLAALTEDVRTISQAF-----VRLPELLQSVALVLGCLAYlawlSPPLFLLTLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 524 LPFVMIGGALEMQMMQ---GAAGKNKEALesagkiaiesIENIRTVA---------SLTREDMFQKKFNH--ELQMPYNI 589
Cdd:COG4615 157 LGLGVAGYRLLVRRARrhlRRAREAEDRL----------FKHFRALLegfkelklnRRRRRAFFDEDLQPtaERYRDLRI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 590 alkKAHLI-GIGFSLSQAVMFFAYAASFWLGAYLikqSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIF 668
Cdd:COG4615 227 ---RADTIfALANNWGNLLFFALIGLILFLLPAL---GWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 669 KL---IDKKPDIDNESEKGEQLHTFTAnLSFANIIFRYPTRPDTT--ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTE 743
Cdd:COG4615 301 ELelaLAAAEPAAADAAAPPAPADFQT-LELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLT 379
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2119559688 744 RFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDR 784
Cdd:COG4615 380 GLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR 420
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
705-811 |
1.99e-17 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 81.80 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 705 TRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVLFD- 783
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
|
90 100
....*....|....*....|....*...
gi 2119559688 784 RTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVREL 114
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
72-271 |
3.13e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.73 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 72 PEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE-NIGIVSQE----PVL 146
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAaGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 fgtTIEENIRYGHLD-----VTKEDIEQAAKMANAH---DFIMDLPQKYetlvgergaqLSGGQKQRIAIARALVRNPKI 218
Cdd:PRK11288 95 ---TVAENLYLGQLPhkggiVNRRLLNYEAREQLEHlgvDIDPDTPLKY----------LSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 219 LLLDEATSALDT-ESEGI--VQDALEkaSHGRTTIVIAHRLSTI-KTADMIAGFKDG 271
Cdd:PRK11288 162 IAFDEPTSSLSArEIEQLfrVIRELR--AEGRVILYVSHRMEEIfALCDAITVFKDG 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
59-282 |
4.01e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.85 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINlkwwRENIG 138
Cdd:COG4152 2 LELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRY-GHL-DVTKEDIEQAAKmanahDFI--MDLPQKYETLVGErgaqLSGGQKQRIAIARALV 213
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlARLkGLSKAEAKRRAD-----EWLerLGLGDRANKKVEE----LSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNEL 282
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
60-271 |
4.86e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHfryPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWREN--- 136
Cdd:PRK10762 6 QLKGID---KAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 -IGIVSQEPVLFGT-TIEENIRYGHLDVTKEDIEQAAKM-ANAHDFIMDLPQKY--ETLVGErgaqLSGGQKQRIAIARA 211
Cdd:PRK10762 80 gIGIIHQELNLIPQlTIAENIFLGREFVNRFGRIDWKKMyAEADKLLARLNLRFssDKLVGE----LSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 212 LVRNPKILLLDEATSAL-DTESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDG 271
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDG 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
71-257 |
4.93e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 71 RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQrFYDPE----EGQILIDGvnlKDINLKWWRENIGIVSQEPVL 146
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 FGT-TIEENIRY-GHLDVtKEDIEQAAKMANAHDFI--MDLPQKYETLVGERGAQ--LSGGQKQRIAIARALVRNPKILL 220
Cdd:TIGR00955 111 IPTlTVREHLMFqAHLRM-PRRVTKKEKRERVDEVLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 2119559688 221 LDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLS 257
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPS 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
80-229 |
7.17e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.00 E-value: 7.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL----KDINLKWWRENIGIVSQEPVLF-GTTIEEN 154
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHYKVRGN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 155 IRYGhldvtkedieQAAKMANAHDFIMDLpQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK11144 97 LRYG----------MAKSMVAQFDKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
75-228 |
7.78e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.69 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINlKW-----WRENIGIVSQEPVLFG- 148
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG---KDIT-DWqtakiMREAVAIVPEGRRVFSr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYGHLDVTKEDIEQaaKMANAHDFimdLPQKYETLVgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 228
Cdd:PRK11614 95 MTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
76-284 |
8.09e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.68 E-value: 8.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDP-----EEGQILIDG---VNLKDInlKWWRENIGIVSQEPVLF 147
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGrsiFNYRDV--LEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 GTTIEENIRYG---HLDVTKEDIEQAAKmanAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PRK14271 114 PMSIMDNVLAGvraHKLVPRKEFRGVAQ---ARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 225 TSALDTESEGIVQDALEKASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
77-271 |
9.10e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 9.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWREN-IGIVSQE-PVLFGTTIEEN 154
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 155 IRYGHLDVTKE------DIEQAAKMANAHDFIMDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 228
Cdd:PRK09700 101 LYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2119559688 229 -DTESEGIVQDALEKASHGRTTIVIAHRLSTIK-TADMIAGFKDG 271
Cdd:PRK09700 177 tNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRrICDRYTVMKDG 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-234 |
1.00e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 33 YQLITM-DPPIDSYSTEGKKLDNFQGNVQIRGVHFRYPSRP--------EAKILYGVNLQIKRGQTVALVGSSGCGKSTI 103
Cdd:PRK10261 287 FPLISLeHPAKQEPPIEQDTVVDGEPILQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTT 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 104 VQLLQRFYDPEEGQILIDGV---NLKDINLKWWRENIGIVSQEPV-------LFGTTIEENIRYGHLDVTKEDIEQAAKM 173
Cdd:PRK10261 367 GRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYasldprqTVGDSIMEPLRVHGLLPGKAAAARVAWL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 174 ANAHDFIMDLPQKYEtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEG 234
Cdd:PRK10261 447 LERVGLLPEHAWRYP-------HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
708-813 |
1.08e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.85 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD--P---ADGIVSLDGHNL--KDLNLQWLRSQIGIVSQEPV 780
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPN 102
|
90 100 110
....*....|....*....|....*....|....*....
gi 2119559688 781 LFDRTIAENIAYG-----DNSREVtMDEIIDAA-RKANI 813
Cdd:COG1117 103 PFPKSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAAL 140
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
59-275 |
1.20e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIdGVNLKdinlkwwrenIG 138
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF--GTTIEENIRYGHLDVTKEDIEQAAKmanahDFimdL--PQKYETLVGErgaqLSGGQKQRIAIARALVR 214
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLG-----RF---LfsGDDAFKPVGV----LSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKAShGrTTIVIAH-R--LSTIktADMIAGFKDGVVAE 275
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
694-811 |
1.22e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.45 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIG 773
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2119559688 774 IVSQEPVLF-DRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:COG3842 81 MVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAEL 119
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
59-254 |
1.40e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVL---FgtTIEEN-IRYG-HLDVTKEDIEqaAKMANAHDFimdlpQKYETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:PRK13536 118 VVPQFDNLdleF--TVRENlLVFGrYFGMSTREIE--AVIPSLLEF-----ARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH 254
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTH 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
695-811 |
1.41e-16 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 79.05 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 695 SFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGI 774
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 2119559688 775 VSQEP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEA 118
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
708-792 |
2.52e-16 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 79.25 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQIGIVSQEPVLFD- 783
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIGMLFQGGALFDs 96
|
....*....
gi 2119559688 784 RTIAENIAY 792
Cdd:COG1127 97 LTVFENVAF 105
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
62-277 |
2.83e-16 |
|
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: 78.73 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 62 RGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdiNLKWWRE-NIGIv 140
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLGlGGGF- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 141 sqEPVLfgtTIEENIRYGH--LDVTKEDIEQaaKMANAHDFiMDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03220 96 --NPEL---TGRENIYLNGrlLGLSRKEIDE--KIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 219 LLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQG 277
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
76-278 |
3.09e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN----LKWWRENIGIVSQ-EPVLFGTT 150
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAELRNQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIRYGHL---DVTKEDIEQAAKMANAhdfiMDLPQKyetlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:PRK11629 104 ALENVAMPLLigkKKPAEINSRALEMLAA----VGLEHR----ANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 228 LDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGT 278
Cdd:PRK11629 176 LDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
59-282 |
3.76e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN-LKWWRENI 137
Cdd:PRK15439 12 LCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFGT-TIEENIRYG---HLDvTKEDIEQAAKMANAHdfiMDLPQKYETL-VGERgaqlsggqkQRIAIARAL 212
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGlpkRQA-SMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 213 VRNPKILLLDEATSALD-TESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNEL 282
Cdd:PRK15439 156 MRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
694-809 |
3.89e-16 |
|
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: 77.84 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYptRPD-TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQI 772
Cdd:cd03369 7 IEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 2119559688 773 GIVSQEPVLFDRTIAENIaygDNSREVTMDEIIDAAR 809
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR 118
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
695-777 |
5.46e-16 |
|
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: 76.13 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 695 SFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGI 774
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
...
gi 2119559688 775 VSQ 777
Cdd:cd00267 78 VPQ 80
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
70-273 |
6.25e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.66 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVL-FG 148
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYG---HL-------DVTKEDIEQAAKMANAHDFImDLPQkyetlvgergAQLSGGQKQRIAIARALVRNPKI 218
Cdd:PRK09536 92 FDVRQVVEMGrtpHRsrfdtwtETDRAAVERAMERTGVAQFA-DRPV----------TSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 219 LLLDEATSALDTESE----GIVQDALEKashGRTTIVIAHRLstiktaDMIAGFKDGVV 273
Cdd:PRK09536 161 LLLDEPTASLDINHQvrtlELVRRLVDD---GKTAVAAIHDL------DLAARYCDELV 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
70-253 |
7.35e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 76.63 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWwRENIGIVSQEPVLFGT 149
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 -TIEENIRYGH--LDVTKEDIEQAAKMANAHDFiMDLPqkyetlvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATS 226
Cdd:TIGR01189 88 lSALENLHFWAaiHGGAQRTIEDALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*...
gi 2119559688 227 ALDTESEGIVQDALekASH-GRTTIVIA 253
Cdd:TIGR01189 157 ALDKAGVALLAGLL--RAHlARGGIVLL 182
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
401-667 |
7.53e-16 |
|
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: 78.98 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 401 ILDEGEQER---KIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRL 477
Cdd:cd18548 25 IIDEGIANGdlsYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKF--GTSSLITRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 478 ATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAI 557
Cdd:cd18548 103 TNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 558 ESIENIRTVASLTREDMFQKKF---NHELqmpYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVF 634
Cdd:cd18548 183 ENLTGIRVIRAFNREDYEEERFdkaNDDL---TDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLV 259
|
250 260 270
....*....|....*....|....*....|....*..
gi 2119559688 635 kAFSA----ILFGGMAIGNASAFAPdaaKAEQSAKEI 667
Cdd:cd18548 260 -AFINylmqILMSLMMLSMVFVMLP---RASASAKRI 292
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
694-793 |
7.76e-16 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 76.07 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQW--LRSQ 771
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100
....*....|....*....|...
gi 2119559688 772 IGIVSQEPVLFDR-TIAENIAYG 793
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG 100
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
75-285 |
1.03e-15 |
|
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: 81.00 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRF--YDPEEGQIL--------------------------------- 119
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 120 IDGVNLKDINLKWWRENIGIVSQEP-VLFGT-TIEENIRYGHLDV---TKEDIEQAA---KMANAHDFIMDLPQkyetlv 191
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTfALYGDdTVLDNVLEALEEIgyeGKEAVGRAVdliEMVQLSHRITHIAR------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 192 gergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKA--SHGRTTIVIAHRLSTI-KTADMIAGF 268
Cdd:TIGR03269 168 -----DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIeDLSDKAIWL 242
|
250
....*....|....*..
gi 2119559688 269 KDGVVAEQGTHNELMSK 285
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV 259
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
694-793 |
1.10e-15 |
|
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: 77.78 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100
....*....|....*....|.
gi 2119559688 774 IVSQEPVL-FDRTIAENIAYG 793
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALG 99
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
66-284 |
1.17e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 66 FRYPS----RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVS 141
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 142 QEPvlfGTTIEENIRYGH-LDV-----TKEDIEQAAKmanahdfimdlpQKYETL--VGERGAQ-------LSGGQKQRI 206
Cdd:PRK15112 94 QDP---STSLNPRQRISQiLDFplrlnTDLEPEQREK------------QIIETLrqVGLLPDHasyyphmLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 207 AIARALVRNPKILLLDEATSALD-TESEGIVQDALE-KASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNELM 283
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVL 238
|
.
gi 2119559688 284 S 284
Cdd:PRK15112 239 A 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
75-271 |
1.19e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.64 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYdPE---EGQILIDGVNLKDINLK-WWRENIGIVSQEPVLF-GT 149
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL- 228
Cdd:TIGR02633 94 SVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLt 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2119559688 229 DTESEGIVQDALEKASHGRTTIVIAHRLSTIKT-ADMIAGFKDG 271
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
75-258 |
1.23e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 76.13 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL-QRFYDPE-EGQILIDGvNLKDINLkwwRENIGIVSQEPVLFGT-TI 151
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILING-RPLDKNF---QRSTGYVEQQDVHSPNlTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRYghldvtkedieqAAKManahdfimdlpqkyetlvgeRGaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 231
Cdd:cd03232 97 REALRF------------SALL--------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180
....*....|....*....|....*...
gi 2119559688 232 SEGIVQDALEK-ASHGRTTIVIAHRLST 258
Cdd:cd03232 143 AAYNIVRFLKKlADSGQAILCTIHQPSA 170
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
388-628 |
1.40e-15 |
|
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: 78.29 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 388 FAVIFSEILGVF------AILDEGEQERKI---IQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQ 458
Cdd:cd18550 6 LLILLSALLGLLpplllrEIIDDALPQGDLgllVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 459 EIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMM 538
Cdd:cd18550 86 SLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 539 QGAAGKNKEALESAGKIAIE--SIENIRTVASLTREDMFQKKFNHELQMPYNIALkKAHLIGIGFSLS-QAVMFFAYAAS 615
Cdd:cd18550 164 RKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGV-RQALAGRWFFAAlGLFTAIGPALV 242
|
250
....*....|...
gi 2119559688 616 FWLGAYLIKQSEV 628
Cdd:cd18550 243 YWVGGLLVIGGGL 255
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
75-278 |
1.44e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.36 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD----PEEGQILI------DGVNLKDINLKwwRENIGIVSQEP 144
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLgrtvqrEGRLARDIRKS--RANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 VLFGT-TIEENIRYGHLDVT--------------KEDIEQA-AKMANAHdfimdlpqkyetLVGERGAQLSGGQKQRIAI 208
Cdd:PRK09984 96 NLVNRlSVLENVLIGALGSTpfwrtcfswftreqKQRALQAlTRVGMVH------------FAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 209 ARALVRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGT 278
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
67-278 |
1.55e-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: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 67 RYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwrenigIVSqePVL 146
Cdd:COG1134 32 RRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----------------RVS--ALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 -FGT------TIEENIRYG--HLDVTKEDIEqaAKMANAHDF--I---MDLPQKYetlvgergaqLSGGQKQRIAIARAL 212
Cdd:COG1134 94 eLGAgfhpelTGRENIYLNgrLLGLSRKEID--EKFDEIVEFaeLgdfIDQPVKT----------YSSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 213 VRNPKILLLDEATSALDTE----SEGIVQdalEKASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGT 278
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
401-617 |
1.65e-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: 77.90 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 401 ILDEGEQERKIIQYVLMFVgVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATD 480
Cdd:cd18589 26 IMNKDAPEAFTAAITVMSL-LTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 481 ASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESI 560
Cdd:cd18589 103 TEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETF 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 561 ENIRTVASLTREDMFQKKFNHELQMPYNIALKKAhligigfslsqavmfFAYAASFW 617
Cdd:cd18589 183 SAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEA---------------AAYAVSMW 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
694-811 |
1.75e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 80.33 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPA---DGIVSLDGHNLKDLNLQWLRS 770
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2119559688 771 QIGIVSQEP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLEL 126
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
410-653 |
2.56e-15 |
|
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: 77.44 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 410 KIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAG 489
Cdd:cd18547 43 GLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTH--SHGDIMSRVTNDVDNISQALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 490 IKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEAL-ESAGKIAiESIENIRTVAS 568
Cdd:cd18547 121 QSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALgELNGYIE-EMISGQKVVKA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 569 LTREDMFQKKF---NHELqmpYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLikqsevdyvdvfkafsaILFGGM 645
Cdd:cd18547 200 FNREEEAIEEFdeiNEEL---YKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLL-----------------VINGAL 259
|
....*...
gi 2119559688 646 AIGNASAF 653
Cdd:cd18547 260 TVGVIQAF 267
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
708-792 |
2.59e-15 |
|
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: 76.00 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQIGIVSQEPVLFDR 784
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGMLFQSGALFDS 91
|
....*....
gi 2119559688 785 -TIAENIAY 792
Cdd:cd03261 92 lTVFENVAF 100
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
691-817 |
2.73e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.95 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 691 TANLSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRS 770
Cdd:PRK13632 5 SVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 771 QIGIVSQEPvlfDR-----TIAENIAYGDNSREVT---MDEII-DAARKANIHNFI 817
Cdd:PRK13632 84 KIGIIFQNP---DNqfigaTVEDDIAFGLENKKVPpkkMKDIIdDLAKKVGMEDYL 136
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
694-792 |
3.09e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.47 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRS 770
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100
....*....|....*....|...
gi 2119559688 771 QIGIVSQE-PVLFDRTIAENIAY 792
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVAL 102
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
426-607 |
3.20e-15 |
|
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: 77.20 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 426 LIAYFVQG-------YMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHNNsvGALTTRLATDASQVQGAAGIKLGSSLMA 498
Cdd:cd18574 49 LGLYLLQSlltfayiSLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRT--GELVNRLTADVQEFKSSFKQCVSQGLRS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 499 FCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKK 578
Cdd:cd18574 127 VTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELEL 206
|
170 180
....*....|....*....|....*....
gi 2119559688 579 FNHELQmpynIALKKAHLIGIGFSLSQAV 607
Cdd:cd18574 207 YEEEVE----KAAKLNEKLGLGIGIFQGL 231
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
387-623 |
4.07e-15 |
|
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: 76.72 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 387 AFAVIFSEILGVFAIL---------DE---GEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKA 454
Cdd:cd18570 5 ILILLLSLLITLLGIAgsfffqiliDDiipSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 455 MLRQEIAFFDdhNNSVGALTTRLaTDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALE 534
Cdd:cd18570 85 LLKLPLSFFE--TRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 535 MQMMQgaaGKNKEALESAGK---IAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFA 611
Cdd:cd18570 162 NKPFK---KKNREVMESNAElnsYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIG 238
|
250
....*....|..
gi 2119559688 612 YAASFWLGAYLI 623
Cdd:cd18570 239 SLLILWIGSYLV 250
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
707-822 |
1.62e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 707 PDTTILKG-LDLEVPQGQTVALVGSSGCGKSTTVQLTERFYdPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRT 785
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110
....*....|....*....|....*....|....*..
gi 2119559688 786 IAENIAYGDNsrEVTMDEIIDAARKANIHNFIASLPD 822
Cdd:PRK11174 439 LRDNVLLGNP--DASDEQLQQALENAWVSEFLPLLPQ 473
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
80-278 |
1.65e-14 |
|
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: 78.13 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDI--NLKWWRENIGIVSQEPVLFG--TTIEENI 155
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIetNLDAVRQSLGMCPQHNILFHhlTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGHLDVTKEDIEQAAKMANAHDfiMDLPQKYEtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGI 235
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLED--TGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2119559688 236 VQDALEKASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGT 278
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
694-779 |
1.66e-14 |
|
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: 73.69 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDT-TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLR 769
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90
....*....|
gi 2119559688 770 SQIGIVSQEP 779
Cdd:cd03257 82 KEIQMVFQDP 91
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
693-822 |
1.85e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.07 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 693 NLSFAniifrYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQI 772
Cdd:PRK10790 345 NVSFA-----Y--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGV 417
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2119559688 773 GIVSQEPVLFDRTIAENIAYGdnsREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPD 464
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
698-792 |
1.91e-14 |
|
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: 72.05 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwLRSQIGIVSQ 777
Cdd:cd03230 5 NLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLPE 80
|
90
....*....|....*.
gi 2119559688 778 EPVLFDR-TIAENIAY 792
Cdd:cd03230 81 EPSLYENlTVRENLKL 96
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
71-253 |
2.12e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.60 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 71 RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRENIGIVSQ----EPVL 146
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 fgtTIEENIRY--GHLDVTKEDIEQAAKMANAHDfIMDLPQKYetlvgergaqLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PRK13539 89 ---TVAENLEFwaAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|
gi 2119559688 225 TSALDTESEGIVQDALekASH-GRTTIVIA 253
Cdd:PRK13539 155 TAALDAAAVALFAELI--RAHlAQGGIVIA 182
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
696-792 |
2.40e-14 |
|
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: 72.83 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQI 772
Cdd:cd03292 3 FINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100
....*....|....*....|.
gi 2119559688 773 GIVSQE-PVLFDRTIAENIAY 792
Cdd:cd03292 81 GVVFQDfRLLPDRNVYENVAF 101
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
415-623 |
3.23e-14 |
|
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: 74.47 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 415 VLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGA---AGIK 491
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRR--RTGDLLSRLTGDVGAIQDLlvsGVLP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 492 LGSSLmafCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAgknKEALESAGKIAI---ESIENIRTVAS 568
Cdd:cd18564 135 LLTNL---LTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEAS---REQRRREGALASvaqESLSAIRVVQA 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 569 LTREDMFQKKFNHELQMPYNIALkKAHLIGIGFS-LSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18564 209 FGREEHEERRFARENRKSLRAGL-RAARLQALLSpVVDVLVAVGTALVLWFGAWLV 263
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-223 |
4.45e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 12 LGNAMPHLQTLATARGAAYYLYQLiTMDPPIDSYSTeGKKLDNFQgNVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVA 91
Cdd:PRK10522 279 LLSAVGALPTLLSAQVAFNKLNKL-ALAPYKAEFPR-PQAFPDWQ-TLELRNVTFAYQDNGFS--VGPINLTIKRGELLF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 92 LVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIE-ENIRYGHLDVTK--EDIE 168
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGpEGKPANPALVEKwlERLK 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 169 QAAKMANAHDFIMDLpqkyetlvgergaQLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:PRK10522 434 MAHKLELEDGRISNL-------------KLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
694-811 |
5.07e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.20 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2119559688 774 IVSQEP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEA 124
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
712-811 |
5.16e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD-----PADGIVSLDGHNL--KDLNLQWLRSQIGIVSQEPVLFDR 784
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110
....*....|....*....|....*....|
gi 2119559688 785 TIAENIAYGD--NSREVTMDEIIDAA-RKA 811
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVERSlRQA 135
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
60-223 |
8.54e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 74.83 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPEAK--ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENI 137
Cdd:COG4615 329 ELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFGTTIeeniryghldvtkeDIEQAAKMANAHDFI--MDLPQKyetlVG-ERGA----QLSGGQKQRIAIAR 210
Cdd:COG4615 409 SAVFSDFHLFDRLL--------------GLDGEADPARARELLerLELDHK----VSvEDGRfsttDLSQGQRKRLALLV 470
|
170
....*....|...
gi 2119559688 211 ALVRNPKILLLDE 223
Cdd:COG4615 471 ALLEDRPILVFDE 483
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
65-259 |
1.14e-13 |
|
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: 71.21 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 65 HFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinLKWWRENIGIVSQEP 144
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-------LVPWKRRKKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 VLFGTTIE-----------------ENIRYGHLdvtKEDIEQAAKMANAHDfIMDLPQKyetlvgergaQLSGGQKQRIA 207
Cdd:cd03267 98 VVFGQKTQlwwdlpvidsfyllaaiYDLPPARF---KKRLDELSELLDLEE-LLDTPVR----------QLSLGQRMRAE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 208 IARALVRNPKILLLDEATSALDTESEGIVQDAL--EKASHGRTTIVIAHRLSTI 259
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkeYNRERGTTVLLTSHYMKDI 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
79-284 |
1.14e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKS-TIVQLLQRFYDPE----EGQILIDGVNL---KDINLKWWREN-IGIVSQEPVLFGT 149
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaSEQTLRGVRGNkIAMIFQEPMVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 ---TIEENIrYG----HLDVTKE-------------DIEQAAKMANahdfimDLPQkyetlvgergaQLSGGQKQRIAIA 209
Cdd:PRK15134 107 plhTLEKQL-YEvlslHRGMRREaargeilncldrvGIRQAAKRLT------DYPH-----------QLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
698-811 |
1.19e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.08 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQ 777
Cdd:PRK13647 9 DLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 2119559688 778 EP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK13647 87 DPddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEA 122
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
59-284 |
1.43e-13 |
|
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: 74.07 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPS--RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQI-------LIDGVNLKDIN 129
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LKWWRENIGIVSQEPVLFG-TTIEENIRYG-HLDVTKEdieqAAKMANAHDFIMD--LPQKYETLVGERGAQLSGGQKQR 205
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLTEAiGLELPDE----LARMKAVITLKMVgfDEEKAEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNEL 282
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEI 515
|
..
gi 2119559688 283 MS 284
Cdd:TIGR03269 516 VE 517
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
75-229 |
1.49e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.08 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINL----KWWRENIGIVSQEPVLFGT- 149
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD---EDISLlplhARARRGIGYLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIrYGHLDVtKEDIEQAAKMANAHDFIMDLpqKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK10895 94 SVYDNL-MAVLQI-RDDLSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
59-254 |
1.71e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQ----EPVLfgtTIEENI----RYGHLDVTkediEQAAKMANAHDFiMDLPQKYETLVGErgaqLSGGQKQRIAIAR 210
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLlvfgRYFGLSAA----AARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH 254
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTH 196
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
433-624 |
2.58e-13 |
|
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: 71.22 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 433 GYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDhnNSVGALTTRLATDASQVqgAAGIKLGSSLMAFCSVVTGIVIGFVF 512
Cdd:cd18590 57 GGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDTTLM--SRSVALNANVLLRSLVKTLGMLGFML 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 513 --SWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIA 590
Cdd:cd18590 133 slSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLK 212
|
170 180 190
....*....|....*....|....*....|....
gi 2119559688 591 LKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIK 624
Cdd:cd18590 213 DRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQ 246
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
52-255 |
2.72e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 52 LDNFqgNVQIRGVHFRypsrpeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFY--DPEEGQILIDgvnlkdiN 129
Cdd:COG2401 31 LEAF--GVELRVVERY--------VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP-------D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LKWWRENIGIvsqepvlfgttieENIryGHLDVTKEDIE--QAAKMANAHDFImdlpQKYetlvgergAQLSGGQKQRIA 207
Cdd:COG2401 94 NQFGREASLI-------------DAI--GRKGDFKDAVEllNAVGLSDAVLWL----RRF--------KELSTGQKFRFR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2119559688 208 IARALVRNPKILLLDEATSALDTESEGIVQDALEKAS--HGRTTIVIAHR 255
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArrAGITLVVATHH 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
698-811 |
3.35e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.45 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTRpdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD-----PADGIVSLDGHNL--KDLNLQWLRS 770
Cdd:PRK14258 12 NLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLNRLRR 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2119559688 771 QIGIVSQEPVLFDRTIAENIAYGDN----SREVTMDEIIDAARKA 811
Cdd:PRK14258 89 QVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKD 133
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
694-822 |
3.42e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 69.69 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPT-RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLT---ERfydPADGIVSLDGHNLKDLN---LQ 766
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 767 WLRSQ-IGIVSQEPVLFDR-TIAENIA----YGDNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS 143
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
84-332 |
3.46e-13 |
|
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: 70.13 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 84 IKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNlkdinlkwwrenigiVSQEPVLFGTTIEENIRYGHLDVT 163
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------VSYKPQYIKADYEGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 164 KEdieqaakMANAHDFIMDL--PQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE 241
Cdd:cd03237 87 KD-------FYTHPYFKTEIakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 242 K--ASHGRTTIVIAHrlsTIKTADMIAgfkDGVVAEQGthnelmsKQGIYQQLVTLQSMKSADDNEIED----FNRD-DT 314
Cdd:cd03237 160 RfaENNEKTAFVVEH---DIIMIDYLA---DRLIVFEG-------EPSVNGVANPPQSLRSGMNRFLKNlditFRRDpET 226
|
250
....*....|....*...
gi 2119559688 315 KRPSLRHQKSTIDMTPKK 332
Cdd:cd03237 227 GRPRINKLGSVKDREQKE 244
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
86-268 |
3.69e-13 |
|
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: 67.78 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 86 RGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIdgvnlkdINLKWWRENIGIvsqepvlfgttieeniryghldvtke 165
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLD-------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 166 dieqaakmanahdfimdlpQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE---- 241
Cdd:smart00382 48 -------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190
....*....|....*....|....*....|
gi 2119559688 242 ---KASHGRTTIVIAHRLSTIKTADMIAGF 268
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
70-254 |
4.45e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDI------NLKWWRENIGIvsqE 143
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 144 PVLfgtTIEENIRY---GHLDVTKEDIEQAAKMANAHDFiMDLPqkyetlvgerGAQLSGGQKQRIAIARALVRNPKILL 220
Cdd:PRK13538 87 TEL---TALENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 2119559688 221 LDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH 254
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
692-793 |
5.04e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 71.26 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 692 ANLSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhnlKDLNlqWLRSQ 771
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVT--DLPPK 73
|
90 100
....*....|....*....|....*.
gi 2119559688 772 ---IGIVSQEPVLFDR-TIAENIAYG 793
Cdd:COG3839 74 drnIAMVFQSYALYPHmTVYENIAFP 99
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
702-792 |
5.58e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.88 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 702 RYPTRP-DTTILKGLDLEVPQGQTVALVGSSGCGKST---TVQLTERfydPADGIVSLDGHNLKDLN---LQWLRSQIGI 774
Cdd:COG1135 10 TFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSereLRAARRKIGM 86
|
90
....*....|....*....
gi 2119559688 775 VSQEPVLFD-RTIAENIAY 792
Cdd:COG1135 87 IFQHFNLLSsRTVAENVAL 105
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
77-278 |
5.96e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKdinlKWWREN-IGIVSQE-------PVLfg 148
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVAYVPQSeevdwsfPVL-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 ttIEENI---RYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEAT 225
Cdd:PRK15056 97 --VEDVVmmgRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 226 SALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTIKTadmiagFKDGVVAEQGT 278
Cdd:PRK15056 171 TGVDVKTEARIISLLrELRDEGKTMLVSTHNLGSVTE------FCDYTVMVKGT 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
79-271 |
6.70e-13 |
|
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: 67.84 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRENI--GIV------SQEPVLFGTT 150
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIraGIAyvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIryghldvtkedieqaakmanahdfimdlpqkyeTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 230
Cdd:cd03215 95 VAENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2119559688 231 ES-EGIVQDALEKASHGRTTIVIahrlST-----IKTADMIAGFKDG 271
Cdd:cd03215 138 GAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEG 180
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
694-793 |
1.51e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 69.79 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQL---TERfydPADGIVSLDGHNLkDLNLQWLRS 770
Cdd:COG1118 3 IEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDL-FTNLPPRER 75
|
90 100
....*....|....*....|....
gi 2119559688 771 QIGIVSQEPVLF-DRTIAENIAYG 793
Cdd:COG1118 76 RVGFVFQHYALFpHMTVAENIAFG 99
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
714-779 |
1.74e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 69.38 E-value: 1.74e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 714 GLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQIGIVSQEP 779
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP 104
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
71-229 |
2.32e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 71 RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG----------VNLKDINLKWWRE----N 136
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHvrgaD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVL-------FGTTIEENIRYgHLDVTKED-IEQAAKMANAhdfiMDLPQKyETLVGERGAQLSGGQKQRIAI 208
Cdd:PRK10261 106 MAMIFQEPMTslnpvftVGEQIAESIRL-HQGASREEaMVEAKRMLDQ----VRIPEA-QTILSRYPHQLSGGMRQRVMI 179
|
170 180
....*....|....*....|.
gi 2119559688 209 ARALVRNPKILLLDEATSALD 229
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALD 200
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
76-259 |
2.38e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.91 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDP---EEGQILIDGVNLKdinlKWWRENIGIVSQEPVLFGT-TI 151
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD----SSFQRSIGYVQQQDLHLPTsTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRY-GHLDVTKEdIEQAAKMANAhDFIMDL--PQKY-ETLVGERGAQLSGGQKQRIAIARALVRNPKILL-LDEATS 226
Cdd:TIGR00956 854 RESLRFsAYLRQPKS-VSKSEKMEYV-EEVIKLleMESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 931
|
170 180 190
....*....|....*....|....*....|....
gi 2119559688 227 ALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTI 259
Cdd:TIGR00956 932 GLDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
698-777 |
3.39e-12 |
|
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: 65.53 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTRpdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQ 777
Cdd:cd03214 4 NLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
694-779 |
3.57e-12 |
|
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: 67.14 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRP-DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQI 772
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
....*..
gi 2119559688 773 GIVSQEP 779
Cdd:COG1124 82 QMVFQDP 88
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
398-581 |
4.06e-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: 67.92 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 398 VFAILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRL 477
Cdd:cd18563 29 VLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKR--QTGSLMSRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 478 ATDASQVQ-----GAAGIkLGSSLMAfcsVVTGIVIgFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESA 552
Cdd:cd18563 107 TSDTDRLQdflsdGLPDF-LTNILMI---IGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRL 181
|
170 180
....*....|....*....|....*....
gi 2119559688 553 GKIAIESIENIRTVASLTREDMFQKKFNH 581
Cdd:cd18563 182 NSVLNDTLPGIRVVKAFGQEKREIKRFDE 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
60-292 |
4.78e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.87 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINL--------- 130
Cdd:PRK11701 8 SVRGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEP-------VLFGTTIEENI------RYGHLDVTK----EDIEQAAkmanahDFIMDLPQKYetlvge 193
Cdd:PRK11701 85 RLLRTEWGFVHQHPrdglrmqVSAGGNIGERLmavgarHYGDIRATAgdwlERVEIDA------ARIDDLPTTF------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 194 rgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIK-TADMIAGFKD 270
Cdd:PRK11701 153 -----SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvRELGLAVVIVTHDLAVARlLAHRLLVMKQ 227
|
250 260
....*....|....*....|...
gi 2119559688 271 GVVAEQG-THNELMSKQGIYQQL 292
Cdd:PRK11701 228 GRVVESGlTDQVLDDPQHPYTQL 250
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
75-229 |
4.88e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILidgvnlKDINLKwwrenIGIVSQEPVLFGT---TI 151
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLR-----IGYVPQKLYLDTTlplTV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 152 EENIRYgHLDVTKEDIEQAAKMANAHDFIMDLPQKyetlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK09544 87 NRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
69-229 |
7.90e-12 |
|
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: 65.36 E-value: 7.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 69 PSRPEAKILYGVNLQIKRGQTVALVGSSGCGKST----IVQLLQRFYDPEeGQILIDGVNLKDINLKWWRENIgIVSQEP 144
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKYPGEII-YVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 VLFGT-TIEENIRYghldvtkedieqAAKMaNAHDFImdlpqkyetlvgeRGaqLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:cd03233 93 VHFPTlTVRETLDF------------ALRC-KGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDN 144
|
....*.
gi 2119559688 224 ATSALD 229
Cdd:cd03233 145 STRGLD 150
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
696-793 |
1.00e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 65.82 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIV 775
Cdd:cd03296 5 VRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFV 79
|
90
....*....|....*....
gi 2119559688 776 SQEPVLFDR-TIAENIAYG 793
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFG 98
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
70-271 |
1.23e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRE----NIGIVSQE-P 144
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFKSSKEalenGISMVHQElN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 VLFGTTIEENIRYGHLDVTKEDIEQaAKMANAHDFIMDL------PQkyetlvgERGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:PRK10982 84 LVLQRSVMDNMWLGRYPTKGMFVDQ-DKMYRDTKAIFDEldididPR-------AKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 219 LLLDEATSALdTESE-----GIVQDALEKashGRTTIVIAHRLSTI-KTADMIAGFKDG 271
Cdd:PRK10982 156 VIMDEPTSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIfQLCDEITILRDG 210
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
415-637 |
1.61e-11 |
|
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: 65.93 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 415 VLMFVGVGVISLIAYFVQ--GYMFGRSGEYltlRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKL 492
Cdd:cd18549 46 AILLALYILRTLLNYFVTywGHVMGARIET---DMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDISELAHHGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 493 GSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEalesagKIA-----IE-SIENIRTV 566
Cdd:cd18549 121 EDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVRE------KIGeinaqLEdSLSGIRVV 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 567 ASLTREDMFQKKFNHElqmpyNIALKKA-----HLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFkAF 637
Cdd:cd18549 195 KAFANEEYEIEKFDEG-----NDRFLESkkkayKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLV-AF 264
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
698-804 |
1.61e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 65.87 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN--LQWLRSQIGIV 775
Cdd:PRK13639 6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRKTVGIV 83
|
90 100 110
....*....|....*....|....*....|.
gi 2119559688 776 SQEP--VLFDRTIAENIAYGDNSREVTMDEI 804
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGPLNLGLSKEEV 114
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
73-258 |
1.69e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQ-RFYDPE-EGQILIDGVNLKDINLKwwreNIGIVSQEPVLF-GT 149
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYpHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLP-QKYE-TLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVISELGlTKCEnTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190
....*....|....*....|....*....|....*
gi 2119559688 225 TSALD-TESEGIVQDALEKASHGRTTIVIAHRLST 258
Cdd:PLN03211 234 TSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
705-822 |
2.14e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.04 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 705 TRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDP---ADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVL 781
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2119559688 782 FDR-TIAENIAYG---DNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG4136 88 FPHlSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA 132
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
357-623 |
2.32e-11 |
|
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: 65.67 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 357 LGRILKLnkseAPFIVMG-CFASLVNGgaMPAFAVIFSEILGvfaILDEGEQerkIIQYVLMFVGVGVISLIAYFVQGYM 435
Cdd:cd18565 10 LNRLFDL----APPLLIGvAIDAVFNG--EASFLPLVPASLG---PADPRGQ---LWLLGGLTVAAFLLESLFQYLSGVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 436 FGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWK 515
Cdd:cd18565 78 WRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 516 ITLLVIAFLPFVMIGGALEMQMMQgaaGKNKEALESAGKIA--IE-SIENIRTVASLTREDmFQKKFNHELQMPYNIALK 592
Cdd:cd18565 156 LALVALLPVPLIIAGTYWFQRRIE---PRYRAVREAVGDLNarLEnNLSGIAVIKAFTAED-FERERVADASEEYRDANW 231
|
250 260 270
....*....|....*....|....*....|..
gi 2119559688 593 KAHLIGIGFS-LSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18565 232 RAIRLRAAFFpVIRLVAGAGFVATFVVGGYWV 263
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
702-779 |
2.60e-11 |
|
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: 65.46 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 702 RYPTRPDT-TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDP---ADGIVSLDGHNLKDLN---LQWLR-SQIG 773
Cdd:COG0444 10 YFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLRKIRgREIQ 89
|
....*.
gi 2119559688 774 IVSQEP 779
Cdd:COG0444 90 MIFQDP 95
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
693-811 |
2.61e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.07 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 693 NLSFaniIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL--KDLNLQWLRS 770
Cdd:PRK13637 7 NLTH---IYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRK 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2119559688 771 QIGIVSQEP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK13637 84 KVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRA 126
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
708-804 |
2.82e-11 |
|
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: 64.18 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLkdLNLQWLRSQIGIVSQEPVLFDR-TI 786
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPHlTV 89
|
90
....*....|....*...
gi 2119559688 787 AENIAYGDNSREVTMDEI 804
Cdd:cd03300 90 FENIAFGLRLKKLPKAEI 107
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
694-791 |
3.04e-11 |
|
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: 63.66 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTT-ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWL---- 768
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100
....*....|....*....|....
gi 2119559688 769 RSQIGIVSQEP-VLFDRTIAENIA 791
Cdd:cd03255 81 RRHIGFVFQSFnLLPDLTALENVE 104
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
708-811 |
3.07e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVLFDR-TI 786
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPHmSL 95
|
90 100
....*....|....*....|....*
gi 2119559688 787 AENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK11432 96 GENVGYGLKMLGVPKEERKQRVKEA 120
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
75-285 |
3.44e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.31 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPeEGQILIDGVNLKDINL---------KWWRENIGIVSQEP- 144
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTADRFRWNGIDLlklsprerrKIIGREIAMIFQEPs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 ------VLFGTTIEENI---RY-GHL-DVTKEDIEQAAKMANA-----HDFIMD-LPQkyetlvgergaQLSGGQKQRIA 207
Cdd:COG4170 100 scldpsAKIGDQLIEAIpswTFkGKWwQRFKWRKKRAIELLHRvgikdHKDIMNsYPH-----------ELTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 208 IARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARlnQLQGTSILLISHDLESIsQWADTITVLYCGQTVESGPTEQILK 248
|
.
gi 2119559688 285 K 285
Cdd:COG4170 249 S 249
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
79-278 |
3.52e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.24 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLK-----DINLKwwreniGIVS--QEPVLFGT-T 150
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpghQIARM------GVVRtfQHVRLFREmT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENI---RYGHLDVT---------------KEDIEQAAKMANAhdfiMDLpqkyeTLVGERGA-QLSGGQKQRIAIARA 211
Cdd:PRK11300 97 VIENLlvaQHQQLKTGlfsgllktpafrraeSEALDRAATWLER----VGL-----LEHANRQAgNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 212 LVRNPKILLLDEATSALD-TESEGIVQ--DALEKaSHGRTTIVIAHRLStiktadMIAGFKDGV-VAEQGT 278
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNpKETKELDEliAELRN-EHNVTVLLIEHDMK------LVMGISDRIyVVNQGT 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
59-282 |
3.60e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFrYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDP----EEGQILIDGVNLKDINLKwwR 134
Cdd:PRK10418 5 IELRNIAL-QAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEP-------------------VLFGTTIEENIRYGHLDVTKEDIEQAAKManaHDFimdlpqkyetlvgerg 195
Cdd:PRK10418 79 RKIATIMQNPrsafnplhtmhtharetclALGKPADDATLTAALEAVGLENAARVLKL---YPF---------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 196 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGV 272
Cdd:PRK10418 140 -EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGR 218
|
250
....*....|
gi 2119559688 273 VAEQGTHNEL 282
Cdd:PRK10418 219 IVEQGDVETL 228
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
409-641 |
4.14e-11 |
|
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: 64.81 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 409 RKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAa 488
Cdd:cd18543 36 SALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRW--QSGQLLSRATSDLSLVQRF- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 489 gikLGSSLMAFCSVVT---GIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAgknKEALESAGKIAI---ESIEN 562
Cdd:cd18543 113 ---LAFGPFLLGNLLTlvvGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLATvveESVTG 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 563 IRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDyVDVFKAFSAIL 641
Cdd:cd18543 187 IRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLT-LGTLVAFSAYL 264
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
37-260 |
5.50e-11 |
|
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: 66.31 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 37 TMDPPIDSYSTEGKKLDNFQGNVQIR----GVHFRYPS--RPEAKILYG-VNLQIKRGQTVALVGSSGCGKSTIVQLLQ- 108
Cdd:TIGR00954 421 PRVEEIESGREGGRNSNLVPGRGIVEyqdnGIKFENIPlvTPNGDVLIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGe 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 109 -------RFYDPEEGQILIdgvnlkdinlkwwrenigiVSQEP----------VLFGTTIEENIRYGHLDvtkEDIEQaa 171
Cdd:TIGR00954 501 lwpvyggRLTKPAKGKLFY-------------------VPQRPymtlgtlrdqIIYPDSSEDMKRRGLSD---KDLEQ-- 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 172 kmanahdfIMDLPQKYETLVGERGAQ--------LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKA 243
Cdd:TIGR00954 557 --------ILDNVQLTHILEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF 628
|
250
....*....|....*..
gi 2119559688 244 shGRTTIVIAHRLSTIK 260
Cdd:TIGR00954 629 --GITLFSVSHRKSLWK 643
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
64-263 |
7.15e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 7.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 64 VHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIGIVSQE 143
Cdd:PRK13540 7 LDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 144 ----PVLfgtTIEENIRYG-HLDVTKEDIEQAAKMANAHDFImDLPqkyetlvgerGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:PRK13540 83 sginPYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLI-DYP----------CGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2119559688 219 LLLDEATSALDTES-EGIVQDALEKASHGRTTIVIAHRLSTIKTAD 263
Cdd:PRK13540 149 WLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
700-779 |
7.61e-11 |
|
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: 65.48 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 700 IFRyPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTT----VQLTerfydPADGIVSLDGHNLKDLN---LQWLRSQI 772
Cdd:COG4172 291 LFR-RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRM 364
|
....*..
gi 2119559688 773 GIVSQEP 779
Cdd:COG4172 365 QVVFQDP 371
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
694-778 |
7.87e-11 |
|
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: 63.18 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRyptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGI-VSLDGHNLKDLNLQWLRSQI 772
Cdd:COG1119 4 LELRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
....*.
gi 2119559688 773 GIVSQE 778
Cdd:COG1119 81 GLVSPA 86
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
58-321 |
9.13e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 58 NVQIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILID---GVNL------KDI 128
Cdd:PRK10938 3 SLQISQGTFRLS---DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshITRLsfeqlqKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 129 NLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDvtKEDIEQAAKMANahdfIMDLpqkyetlVGERGAQLSGGQKQRIAI 208
Cdd:PRK10938 80 SDEWQRNNTDMLSPGEDDTGRTTAEIIQDEVKD--PARCEQLAQQFG----ITAL-------LDRRFKYLSTGETRKTLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 209 ARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIV-IAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSkQ 286
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ-Q 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2119559688 287 GIYQQLV---TLQSMK--SADDNEIEDFNRDDTKRPSLRH 321
Cdd:PRK10938 226 ALVAQLAhseQLEGVQlpEPDEPSARHALPANEPRIVLNN 265
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
698-804 |
9.33e-11 |
|
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: 62.27 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQ 777
Cdd:cd03301 5 NVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQ 79
|
90 100
....*....|....*....|....*...
gi 2119559688 778 EPVLFDR-TIAENIAYGDNSREVTMDEI 804
Cdd:cd03301 80 NYALYPHmTVYDNIAFGLKLRKVPKDEI 107
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
79-225 |
1.08e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINlKWWRENIGIVS----QEPVLFGTTIE 152
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPR-DAIRAGIAYVPedrkGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 153 ENI---------RYGHLDVTKEDieqaakmANAHDFIMDL---PQKYETLVGergaQLSGGQKQRIAIARALVRNPKILL 220
Cdd:COG1129 349 ENItlasldrlsRGGLLDRRRER-------ALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
....*
gi 2119559688 221 LDEAT 225
Cdd:COG1129 418 LDEPT 422
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
711-821 |
1.12e-10 |
|
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: 63.00 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 711 ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENI 790
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110
....*....|....*....|....*....|.
gi 2119559688 791 aygDNSREVTMDEIIDAARKANIHNFIASLP 821
Cdd:cd03288 116 ---DPECKCTDDRLWEALEIAQLKNMVKSLP 143
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
694-816 |
1.28e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.11 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTTiLKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:PRK13635 6 IRVEHISFRYPDAATYA-LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 774 IVSQEPvlfDR-----TIAENIAYGDNSREVTMDEII----DAARKANIHNF 816
Cdd:PRK13635 85 MVFQNP---DNqfvgaTVQDDVAFGLENIGVPREEMVervdQALRQVGMEDF 133
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
411-639 |
1.79e-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: 62.87 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 411 IIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGI 490
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 491 KLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPfVMIGGALEMQMMQGAAGKNKEAlesagKIAI------ESIENIR 564
Cdd:cd18545 117 GLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLP-LLVLVVFLLRRRARKAWQRVRK-----KISNlnaylhESISGIR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 565 TVASLTREDMFQKKFNhELqmpyNIALKKAHL--IGIGFSLSQAVMF---FAYAASFWLGAYLIKQSEVDyVDVFKAFSA 639
Cdd:cd18545 191 VIQSFAREDENEEIFD-EL----NRENRKANMraVRLNALFWPLVELisaLGTALVYWYGGKLVLGGAIT-VGVLVAFIG 264
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
708-793 |
3.15e-10 |
|
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: 60.62 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL--KDLNLQWLRSQIGIVSQEPVLF-DR 784
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFpHL 91
|
....*....
gi 2119559688 785 TIAENIAYG 793
Cdd:cd03262 92 TVLENITLA 100
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
698-794 |
3.62e-10 |
|
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: 60.35 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhnlKDLNLQWLRSQIGIVSQ 777
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90
....*....|....*....
gi 2119559688 778 EP--VLFDRTIAENIAYGD 794
Cdd:cd03226 79 DVdyQLFTDSVREELLLGL 97
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
77-284 |
3.92e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTivqLLQRFYD--PEEGQILIDGVNLKDINL-KWWRENIGIVSQEPVLFGTTIee 153
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAaELARHRAYLSQQQTPPFAMPV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 nirYGHLDVTKEDIEQAAKMANAHDFIMDLPQ---KYETLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLDE 223
Cdd:PRK03695 87 ---FQYLTLHQPDKTRTEAVASALNEVAEALGlddKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 224 ATSALDTESEGIVqDAL--EKASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK03695 160 PMNSLDVAQQAAL-DRLlsELCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
708-793 |
4.35e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.18 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVL-FDRTI 786
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITV 93
|
....*..
gi 2119559688 787 AENIAYG 793
Cdd:PRK11231 94 RELVAYG 100
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
70-290 |
4.58e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQ-RFYDPEE-------GQILIDGVNLKDIN---LKWWRENIG 138
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDaprLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQ--------EPVLFGttieeniRYGHLDV-------TKEDIEQAAKMANAhdfimdlpqkyETLVGERGAQLSGGQK 203
Cdd:PRK13547 90 QAAQpafafsarEIVLLG-------RYPHARRagalthrDGEIAWQALALAGA-----------TALVGRDVTTLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 204 QRIAIARAL---------VRNPKILLLDEATSALDTESEGIVQDALEKASH----GRTTIVIAHRLSTiKTADMIAGFKD 270
Cdd:PRK13547 152 ARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAA-RHADRIAMLAD 230
|
250 260
....*....|....*....|
gi 2119559688 271 GVVAEQGTHNELMSKQGIYQ 290
Cdd:PRK13547 231 GAIVAHGAPADVLTPAHIAR 250
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
708-804 |
5.47e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.89 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVLFDR-TI 786
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPHmTV 103
|
90
....*....|....*...
gi 2119559688 787 AENIAYGDNSREVTMDEI 804
Cdd:PRK09452 104 FENVAFGLRMQKTPAAEI 121
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
80-229 |
5.87e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINLkwwRENIGIVSQEPVLFGT-TIEENIR 156
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIAT---RRRVGYMSQAFSLYGElTVRQNLE 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 157 -YGHL-DVTKEDIEQA-AKMAnaHDFimDLpqkyETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:NF033858 362 lHARLfHLPAAEIAARvAEML--ERF--DL----ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
712-813 |
9.15e-10 |
|
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: 59.66 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVLF-DRTIAENI 790
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100
....*....|....*....|....*..
gi 2119559688 791 AYG----DNSREVTMDEIIDAARKANI 813
Cdd:cd03299 93 AYGlkkrKVDKKEIERKVLEIAEMLGI 119
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
415-623 |
1.00e-09 |
|
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: 60.58 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 415 VLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGS 494
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 495 SLMAFCSVVTGIVIGFVFSWKITLLVIAFLPfVMIGGALEMQMMQGAAgkNKEALESAGKIA---IESIENIRTVASLTR 571
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALP-PLALATRWFRRRSSRA--YRRARERIAAVNadlQETLAGIRVVQAFRR 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 572 EDMFQKKFNHElqmpyNIALKKAH-----LIGIGFSLSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18546 197 ERRNAERFAEL-----SDDYRDARlraqrLVAIYFPGVELLGNLATAAVLLVGAWRV 248
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
83-266 |
1.01e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.11 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 83 QIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQIlidgvnlkDINLKwwrenigiVSQEP----VLFGTTIEENIRyg 158
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLK--------ISYKPqyisPDYDGTVEEFLR-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 159 hlDVTKEDIEqaAKMANaHDFI--MDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIV 236
Cdd:COG1245 424 --SANTDDFG--SSYYK-TEIIkpLGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
170 180 190
....*....|....*....|....*....|..
gi 2119559688 237 QDALEK--ASHGRTTIVIAHRLSTIktaDMIA 266
Cdd:COG1245 495 AKAIRRfaENRGKTAMVVDHDIYLI---DYIS 523
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
58-284 |
1.11e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.91 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 58 NVQIRGVHF---RYPSRPEAKILYGVNlqikRGQTVALVGSSGCGKS----TIVQLLQRFYDPEEGQILIDGVNLKDINL 130
Cdd:PRK11022 5 NVDKLSVHFgdeSAPFRAVDRISYSVK----QGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIG----IVSQEPVlfgTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPqkyeTLVG-----ER----GAQ 197
Cdd:PRK11022 81 KERRNLVGaevaMIFQDPM---TSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLL----NQVGipdpaSRldvyPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 198 LSGGQKQRIAIARALVRNPKILLLDEATSALD-TESEGIVQDALE-KASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVA 274
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVV 233
|
250
....*....|
gi 2119559688 275 EQGTHNELMS 284
Cdd:PRK11022 234 ETGKAHDIFR 243
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
48-288 |
1.16e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 48 EGKKLdnFQGNVQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQIlidgvnlkd 127
Cdd:PRK15064 311 QDKKL--HRNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 128 inlKWwREN--IGIVSQEPVL-FGTTI---------------EENIR--YGHLDVTKEDIEQAAKManahdfimdlpqky 187
Cdd:PRK15064 377 ---KW-SENanIGYYAQDHAYdFENDLtlfdwmsqwrqegddEQAVRgtLGRLLFSQDDIKKSVKV-------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 188 etlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-------ASHGRTTI-VIAHRLSTI 259
Cdd:PRK15064 439 ----------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKyegtlifVSHDREFVsSLATRIIEI 508
|
250 260
....*....|....*....|....*....
gi 2119559688 260 KTadmiagfkDGVVAEQGTHNELMSKQGI 288
Cdd:PRK15064 509 TP--------DGVVDFSGTYEEYLRSQGI 529
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
60-232 |
1.29e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQrfydpeegqilidGVNlKDINLKWWRE---N 136
Cdd:TIGR03719 6 TMNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KDFNGEARPQpgiK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGT-TIEENIRYG---HLDVTKEDIEQAAKMA-----------------------NAHDF------IMD- 182
Cdd:TIGR03719 70 VGYLPQEPQLDPTkTVRENVEEGvaeIKDALDRFNEISAKYAepdadfdklaaeqaelqeiidaaDAWDLdsqleiAMDa 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 183 --LPQKyETLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 232
Cdd:TIGR03719 150 lrCPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
83-266 |
1.38e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 83 QIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQIlidgvnlkDINLKwwrenigiVSQEPvlfgTTIEENIryghlDV 162
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELK--------ISYKP----QYIKPDY-----DG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 163 TKED-IEQAAKMANA----HDFI--MDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGI 235
Cdd:PRK13409 416 TVEDlLRSITDDLGSsyykSEIIkpLQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|...
gi 2119559688 236 VQDALEK--ASHGRTTIVIAHRLSTIktaDMIA 266
Cdd:PRK13409 492 VAKAIRRiaEEREATALVVDHDIYMI---DYIS 521
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
698-811 |
1.59e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.75 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQ 777
Cdd:PRK13650 9 NLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 2119559688 778 EP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK13650 89 NPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEA 124
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
709-779 |
2.60e-09 |
|
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: 60.47 E-value: 2.60e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 709 TTILKGLDLEVPQGQTVALVGSSGCGKSTT----VQLTERFYDPADGIVSLDGHNLKDLNLQWLR----SQIGIVSQEP 779
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEP 101
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
715-807 |
4.83e-09 |
|
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: 57.30 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 715 LDLEVPqGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKD----LNLQWLRSQIGIVSQEPVLFDR-TIAEN 789
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlNVREN 95
|
90 100
....*....|....*....|...
gi 2119559688 790 IAYG-----DNSREVTMDEIIDA 807
Cdd:cd03297 96 LAFGlkrkrNREDRISVDELLDL 118
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
712-808 |
5.69e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD-----PADGIVSLDGHNLKDLNLQW--LRSQIGIVSQEPVLFDR 784
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPM 100
|
90 100
....*....|....*....|....
gi 2119559688 785 TIAENIAYGDNSREVTMDEIIDAA 808
Cdd:PRK14239 101 SIYENVVYGLRLKGIKDKQVLDEA 124
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
708-806 |
6.31e-09 |
|
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: 57.06 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNL-QWLRSQIGIVSQEPVLFDR-T 785
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFPElT 91
|
90 100
....*....|....*....|....*.
gi 2119559688 786 IAENI-----AYGDNSREVTMDEIID 806
Cdd:cd03224 92 VEENLllgayARRRAKRKARLERVYE 117
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-268 |
7.87e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 57.38 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 78 YGVN------LQIKR-GQTVALVGSSGCGKSTIVQLLQ--------RFYDPEEGQILID---GVNLKDINLKWWRENIGI 139
Cdd:cd03236 10 YGPNsfklhrLPVPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 ------VSQEPVLFGTTIEENIRYGHLDVTKEDIEQAakmanahdfiMDLpqkyETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:cd03236 90 ivkpqyVDLIPKAVKGKVGELLKKKDERGKLDELVDQ----------LEL----RHVLDRNIDQLSGGELQRVAIAAALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTIktaDMIAGF 268
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIrELAEDDNYVLVVEHDLAVL---DYLSDY 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
694-764 |
8.54e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.39 E-value: 8.54e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 694 LSFANIIFRYPT------RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN 764
Cdd:PRK10419 4 LNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
405-645 |
1.10e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 57.16 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 405 GEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQV 484
Cdd:cd18778 33 SKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDR--QTGDLMSRVINDVANV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 485 QG--AAGIKLGSSlmafcSVVTGIVIG---FVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIES 559
Cdd:cd18778 111 ERliADGIPQGIT-----NVLTLVGVAiilFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 560 IENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLsqaVMFFA---YAASFWLGAYLIKQSEVDYVDVFkA 636
Cdd:cd18778 186 LSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPL---MEFLTslgTVLVLGFGGRLVLAGELTIGDLV-A 261
|
....*....
gi 2119559688 637 FsaILFGGM 645
Cdd:cd18778 262 F--LLYLGL 268
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
694-793 |
1.46e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 55.55 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTT--ILKGLDLEVPQGQTVALVGSSGCGKSTTVQ--LTErfYDPADGIVSLDGHnlkdlnlqwlr 769
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSalLGE--LEKLSGSVSVPGS----------- 67
|
90 100
....*....|....*....|....
gi 2119559688 770 sqIGIVSQEPVLFDRTIAENIAYG 793
Cdd:cd03250 68 --IAYVSQEPWIQNGTIRENILFG 89
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
708-793 |
1.53e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.39 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD-----PADGIVSLDGHNL--KDLNLQWLRSQIGIVSQEPV 780
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPN 95
|
90
....*....|....
gi 2119559688 781 LFDR-TIAENIAYG 793
Cdd:PRK14267 96 PFPHlTIYDNVAIG 109
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
696-791 |
1.57e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.12 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPT-RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQ 771
Cdd:PRK11153 4 LKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQ 83
|
90 100
....*....|....*....|.
gi 2119559688 772 IGIVSQE-PVLFDRTIAENIA 791
Cdd:PRK11153 84 IGMIFQHfNLLSSRTVFDNVA 104
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
710-793 |
1.67e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.53 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 710 TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVL-FDRTIAE 788
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQE 100
|
....*
gi 2119559688 789 NIAYG 793
Cdd:PRK10253 101 LVARG 105
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
150-282 |
1.97e-08 |
|
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: 58.10 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEenIRYGH------LDVTKEDieqaakmanAHDFIMDLP---QKYETLV---------GERGAQLSGGQKQRIAIARA 211
Cdd:TIGR00630 775 TLE--VKYKGkniadvLDMTVEE---------AYEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKE 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 212 LVR---NPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTADMI------AGFKDGVVAEQGTHNE 281
Cdd:TIGR00630 844 LSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEE 923
|
.
gi 2119559688 282 L 282
Cdd:TIGR00630 924 V 924
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
708-792 |
2.18e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.49 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIA 787
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
....*
gi 2119559688 788 ENIAY 792
Cdd:PRK10247 99 DNLIF 103
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
81-272 |
2.20e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.66 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 81 NLQIKRGQTVALVGSSGCGKS----TIVQLLQRfydpeEGQI----LIDG---VNLKDINLKWWR-ENIGIVSQEPVlfg 148
Cdd:PRK09473 36 NFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIggsaTFNGreiLNLPEKELNKLRaEQISMIFQDPM--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYG---------HLDVTK-EDIEQ------AAKMANAHDFIMDLPQKYetlvgergaqlSGGQKQRIAIARAL 212
Cdd:PRK09473 108 TSLNPYMRVGeqlmevlmlHKGMSKaEAFEEsvrmldAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLStiktadMIAGFKDGV 272
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLG------VVAGICDKV 232
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
44-231 |
2.43e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 44 SYSTEGKKL-DNFQGNVQirgvhfrypsrpeakilygvnlqikRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIdG 122
Cdd:PRK11147 326 NYQIDGKQLvKDFSAQVQ-------------------------RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-G 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 123 VNLKDINLKWWRENIgivsqEPvlfGTTIEENIRYGHLDVTKEDIEQAAkMANAHDFIMDlPQKYETLVgergAQLSGGQ 202
Cdd:PRK11147 380 TKLEVAYFDQHRAEL-----DP---EKTVMDNLAEGKQEVMVNGRPRHV-LGYLQDFLFH-PKRAMTPV----KALSGGE 445
|
170 180
....*....|....*....|....*....
gi 2119559688 203 KQRIAIARALVRNPKILLLDEATSALDTE 231
Cdd:PRK11147 446 RNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
414-623 |
2.48e-08 |
|
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: 56.44 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 414 YVLMfVGVGVISL---IAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLAtDASQVQGAAGi 490
Cdd:cd18566 42 QVLV-IGVVIAILlesLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLT- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 491 klGSSLMAFCS---VVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVA 567
Cdd:cd18566 117 --GQALLALLDlpfVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 568 SLTREDMFQKKFNhELQMPYNIA-LKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18566 195 AMAMEPQMLRRYE-RLQANAAYAgFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLV 250
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
716-806 |
3.03e-08 |
|
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: 56.65 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 716 DLEVPQGQTVALVGSSGCGKSTTVQL---TERfydPADGIVSLDGHNLKD-LNLQWL---RSQIGIVSQEPVLFD-RTIA 787
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLQDsARGIFLpphRRRIGYVFQEARLFPhLSVR 95
|
90 100
....*....|....*....|....
gi 2119559688 788 ENIAYG-----DNSREVTMDEIID 806
Cdd:COG4148 96 GNLLYGrkrapRAERRISFDEVVE 119
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
701-822 |
3.08e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.01 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 701 FRYPTrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL--KDLNLQWLRSQIGIVSQE 778
Cdd:PRK13636 13 YNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMVFQD 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2119559688 779 P--VLFDRTIAENIAYGDNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:PRK13636 91 PdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKD 136
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
60-232 |
3.25e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQrfydpeegqilidGVNlKDINLKWWRE---N 136
Cdd:PRK11819 8 TMNRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KEFEGEARPApgiK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGT-TIEENIRYGHLDVTK-----EDI------------EQAAKMA---------NAHDF------IMD- 182
Cdd:PRK11819 72 VGYLPQEPQLDPEkTVRENVEEGVAEVKAaldrfNEIyaayaepdadfdALAAEQGelqeiidaaDAWDLdsqleiAMDa 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 183 --LPQKyETLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 232
Cdd:PRK11819 152 lrCPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
702-741 |
3.27e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.45 E-value: 3.27e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2119559688 702 RYPTRpdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQL 741
Cdd:PRK11247 21 RYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRL 57
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
712-810 |
3.63e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.52 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL----KDLNLQWLRSQIGIVSQ--EPVLFDRT 785
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQIRKKVGLVFQfpESQLFEET 102
|
90 100
....*....|....*....|....*
gi 2119559688 786 IAENIAYGDNSREVTMDEIIDAARK 810
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEALARE 127
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
414-627 |
3.76e-08 |
|
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: 55.68 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 414 YVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLatdaSQVQGAAGIKLG 493
Cdd:cd18782 44 IGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPVGELSTRI----SELDTIRGFLTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 494 SSLMAFCSVVTG---IVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQgaaGKNKEALESAGKIA---IESIENIRTVA 567
Cdd:cd18782 118 TALTTLLDVLFSviyIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILR---RQIRRRAEASAKTQsylVESLTGIQTVK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 568 SLTREDMFQKKFNHELqmpynialkkAHLIGIGFSLSQAVMFFAYAASF----------WLGAYLIKQSE 627
Cdd:cd18782 195 AQNAELKARWRWQNRY----------ARSLGEGFKLTVLGTTSGSLSQFlnklssllvlWVGAYLVLRGE 254
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
712-808 |
3.97e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.56 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDG----HNLKDLNLQWLRSQIGIVSQ--EPVLFDRT 785
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRPVRKRIGMVFQfpESQLFEDT 102
|
90 100
....*....|....*....|...
gi 2119559688 786 IAENIAYGDNSREVTMDEIIDAA 808
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYA 125
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
698-804 |
4.09e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.61 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhNLKdlnlqwlrsqIGIVSQ 777
Cdd:COG0488 3 NLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLPQ 68
|
90 100
....*....|....*....|....*...
gi 2119559688 778 EPVLFD-RTIAENIAYGDNSREVTMDEI 804
Cdd:COG0488 69 EPPLDDdLTVLDTVLDGDAELRALEAEL 96
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
706-808 |
5.14e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 706 RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVL-FDR 784
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100
....*....|....*....|....*..
gi 2119559688 785 TIAENIAYG---DNSREVTMDEIIDAA 808
Cdd:PRK13548 92 TVEEVVAMGrapHGLSRAEDDALVAAA 118
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
712-811 |
5.28e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.41 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL----KDLNLQWLRSQIGIVSQ--EPVLFDRT 785
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLRKKVGIVFQfpEHQLFEET 102
|
90 100
....*....|....*....|....*.
gi 2119559688 786 IAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK13634 103 VEKDICFGPMNFGVSEEDAKQKAREM 128
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
694-821 |
5.54e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.19 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTtILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDP---ADGIVSLDGHNLKDLNLQWLRS 770
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 771 QIGIVSQEP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA----NIHNFIASLP 821
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVladvGMLDYIDSEP 141
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
712-791 |
5.57e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.11 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHN---LKDLNLQWLRSQIGIVSQE-PVLFDRTIA 787
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDhHLLMDRTVY 97
|
....
gi 2119559688 788 ENIA 791
Cdd:PRK10908 98 DNVA 101
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
712-757 |
6.31e-08 |
|
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: 54.39 E-value: 6.31e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDG 757
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG 46
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
702-792 |
6.32e-08 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 54.05 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 702 RYPTRPdTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDlNLQWLRSQIGIVSQEPVL 781
Cdd:cd03263 9 TYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDAL 86
|
90
....*....|..
gi 2119559688 782 FDR-TIAENIAY 792
Cdd:cd03263 87 FDElTVREHLRF 98
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
82-232 |
6.64e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 82 LQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDgvnlKDInlkwwrenigIVS---QEP--VLFGTT---IEE 153
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDL----------IVArlqQDPprNVEGTVydfVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NI--------RYGHL------DVTKEDIEQAAKM------ANAHDF---IMDLPQKYETLVGERGAQLSGGQKQRIAIAR 210
Cdd:PRK11147 90 GIeeqaeylkRYHDIshlvetDPSEKNLNELAKLqeqldhHNLWQLenrINEVLAQLGLDPDAALSSLSGGWLRKAALGR 169
|
170 180
....*....|....*....|..
gi 2119559688 211 ALVRNPKILLLDEATSALDTES 232
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIET 191
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
73-246 |
7.35e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL--QRFYDPEEGQILIDGVNLKDINLKwWRENIGI--VSQEPV-LF 147
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGIflAFQYPIeIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 GTTIEENIRyghLDVTKEDIEQAAKMANAHDFIMDLPQKYEtLVGERGAQL--------SGGQKQRIAIARALVRNPKIL 219
Cdd:CHL00131 98 GVSNADFLR---LAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELA 173
|
170 180
....*....|....*....|....*..
gi 2119559688 220 LLDEATSALDTesegivqDALEKASHG 246
Cdd:CHL00131 174 ILDETDSGLDI-------DALKIIAEG 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
76-259 |
7.71e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL----QRFYDPEEGQILIDGVNLKDInLKWWRENIGIVSQEPVLFGT-T 150
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFPHlT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEE-----------NIRYghLDVTKEdiEQAAKMANAHDFIMDLPQKYETLVGE---RGaqLSGGQKQRIAIARALVRNP 216
Cdd:TIGR00956 155 VGEtldfaarcktpQNRP--DGVSRE--EYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGA 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2119559688 217 KILLLDEATSALDTESegivqdALEKASHGRTTIVIAHRLSTI 259
Cdd:TIGR00956 229 KIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
694-810 |
7.76e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.84 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrPDTTI-LKGLD---LEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGH----NLKDLNL 765
Cdd:PRK13641 3 IKFENVDYIYS--PGTPMeKKGLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2119559688 766 QWLRSQIGIVSQ--EPVLFDRTIAENIAYGDNSREVTMDEIIDAARK 810
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALK 127
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
75-257 |
1.14e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL--QRFYDPEEGQILIDGVNLKD---INLKWWRENIGIVSQEpvlfgT 149
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQetfARISGYCEQNDIHSPQ-----V 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHL-----DVTKED-------IEQAAKMANAHDFIMDLPqkyetlvGERGaqLSGGQKQRIAIARALVRNPK 217
Cdd:PLN03140 969 TVRESLIYSAFlrlpkEVSKEEkmmfvdeVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPS 1039
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2119559688 218 ILLLDEATSALDTESEGIVQDALEKA-SHGRTTIVIAHRLS 257
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIVMRTVRNTvDTGRTVVCTIHQPS 1080
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
73-262 |
1.20e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWRENIGIVSQepvlfgT 149
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLE------M 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVTKEDIEQAAkmanAHDFimdlpqKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK13541 86 TVFENLKFWSEIYNSAETLYAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
170 180 190
....*....|....*....|....*....|....
gi 2119559688 230 TESEGIVQDALE-KASHGRTTIVIAHRLSTIKTA 262
Cdd:PRK13541 156 KENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
77-265 |
1.34e-07 |
|
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: 52.33 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQllqrfydpeegqilidgvnlkdinlkwwrenigivsqepvlfgTTIEENIR 156
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------------------------------------EGLYASGK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 157 YGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLvGERGAQLSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEG 234
Cdd:cd03238 48 ARLISFLPKFSRNKLIFIDQLQFLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|..
gi 2119559688 235 IVQDALEK-ASHGRTTIVIAHRLSTIKTADMI 265
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWI 158
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
60-229 |
1.37e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.83 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 60 QIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE-EGQILIDGvnlKDINLKWWRENI- 137
Cdd:TIGR02633 259 EARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFING---KPVDIRNPAQAIr 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 -------------GIVSQEPVLFGTTIEENIRY---GHLDVTKED--IEQAAKMANAHDFIMDLPQkyetlvgergAQLS 199
Cdd:TIGR02633 336 agiamvpedrkrhGIVPILGVGKNITLSVLKSFcfkMRIDAAAELqiIGSAIQRLKVKTASPFLPI----------GRLS 405
|
170 180 190
....*....|....*....|....*....|
gi 2119559688 200 GGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
80-281 |
1.40e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRENI--GIV------SQEPVLFGTTI 151
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIraGIMlcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENI---------RYGHLdvtkedIEQAAKMANAHDFIMDLPQKY---ETLVGergaQLSGGQKQRIAIARALVRNPKIL 219
Cdd:PRK11288 349 ADNInisarrhhlRAGCL------INNRWEAENADRFIRSLNIKTpsrEQLIM----NLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 220 LLDEATSALD--TESEgIVQDALEKASHGRTTIVIAHRL-STIKTADMIAGFKDGVVAEQGTHNE 281
Cdd:PRK11288 419 LLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
77-278 |
1.45e-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: 53.39 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQ-----LLQRFYDPEEGQILidgvNLKDInlkWWRENIG---IVSQEPVlfG 148
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypALARRLHLKKEQPG----NHDRI---EGLEHIDkviVIDQSPI--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEEN------------------------------IRYGH------LDVTKEDieqaakmanAHDFIMDLPQ---KYET 189
Cdd:cd03271 82 RTPRSNpatytgvfdeirelfcevckgkrynretleVRYKGksiadvLDMTVEE---------ALEFFENIPKiarKLQT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 190 LV---------GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRL 256
Cdd:cd03271 153 LCdvglgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNL 232
|
250 260
....*....|....*....|....*...
gi 2119559688 257 STIKTADMI------AGFKDGVVAEQGT 278
Cdd:cd03271 233 DVIKCADWIidlgpeGGDGGGQVVASGT 260
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
69-229 |
1.72e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 69 PSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE-EGQILIDGvnlKDINLKWWRENI---------- 137
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDG---KPVKIRNPQQAIaqgiamvped 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 ----GIVSQEPVLFGTTIEENIRYGHLDVtkedIEQAAKMANAHDFIMDLPQKYETLVgERGAQLSGGQKQRIAIARALV 213
Cdd:PRK13549 347 rkrdGIVPVMGVGKNITLAALDRFTGGSR----IDDAAELKTILESIQRLKVKTASPE-LAIARLSGGNQQKAVLAKCLL 421
|
170
....*....|....*.
gi 2119559688 214 RNPKILLLDEATSALD 229
Cdd:PRK13549 422 LNPKILILDEPTRGID 437
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
79-259 |
1.88e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.94 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLkdinlkwWRE------NIGIVsqepvlFG---- 148
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP-------FKRrkefarRIGVV------FGqrsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 -----TTIEEniryghLDVTKE--DIEQAAKMANAHDF--IMDLPQKYETLVgeRgaQLSGGQKQRIAIARALVRNPKIL 219
Cdd:COG4586 107 lwwdlPAIDS------FRLLKAiyRIPDAEYKKRLDELveLLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2119559688 220 LLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI 259
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDI 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
78-266 |
2.13e-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: 54.41 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 78 YGVN---L----QIKRGQTVALVGSSGCGKSTIVQLLQrfydpeeGQIlidgvnlkdinlkwwRENIGIVSQEPvlfgtT 150
Cdd:COG1245 83 YGENgfrLyglpVPKKGKVTGILGPNGIGKSTALKILS-------GEL---------------KPNLGDYDEEP-----S 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIRY-------GHL-DVTKEDIEQAAKmanahdfimdlPQ------KY------ETL--VGERGA------------ 196
Cdd:COG1245 136 WDEVLKRfrgtelqDYFkKLANGEIKVAHK-----------PQyvdlipKVfkgtvrELLekVDERGKldelaeklglen 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 197 -------QLSGGQKQRIAIARALVRNPKILLLDEATSALD----TESEGIVQDALEKashGRTTIVIAHRLSTIktaDMI 265
Cdd:COG1245 205 ildrdisELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAIL---DYL 278
|
.
gi 2119559688 266 A 266
Cdd:COG1245 279 A 279
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
694-764 |
2.14e-07 |
|
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: 53.27 E-value: 2.14e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 694 LSFANIIFRYPT------RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN 764
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
710-793 |
2.18e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.83 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 710 TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIV-----SLDGHnlKDLNLQ-----WLRSQIGIVSQEP 779
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSQQkglirQLRQHVGFVFQNF 94
|
90
....*....|....*
gi 2119559688 780 VLF-DRTIAENIAYG 793
Cdd:PRK11264 95 NLFpHRTVLENIIEG 109
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
712-809 |
2.24e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.25 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN-LQWLRSQIGIVSQEPVLF-DRTIAEN 789
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVpNLSVAEN 99
|
90 100
....*....|....*....|
gi 2119559688 790 IAYGdnsREVTMDEIIDAAR 809
Cdd:COG1129 100 IFLG---REPRRGGLIDWRA 116
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
708-793 |
2.38e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.61 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTER---FYDPA--DGIVSLDGHNLKDLNLQWLRSQIGIVSQEP-VL 781
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlieLYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90
....*....|..
gi 2119559688 782 FDRTIAENIAYG 793
Cdd:PRK14247 95 PNLSIFENVALG 106
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
694-804 |
2.46e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.09 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL--KDLNLQWLRSQ 771
Cdd:PRK13638 2 LATSDLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQ 78
|
90 100 110
....*....|....*....|....*....|....*
gi 2119559688 772 IGIVSQEP--VLFDRTIAENIAYGDNSREVTMDEI 804
Cdd:PRK13638 79 VATVFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEI 113
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
715-806 |
2.59e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.69 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 715 LDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNlQWLRSqIGIVSQEPVLFDR-TIAENIAYG 793
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRP-INMMFQSYALFPHmTVEQNIAFG 115
|
90
....*....|...
gi 2119559688 794 DNSREVTMDEIID 806
Cdd:PRK11607 116 LKQDKLPKAEIAS 128
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
78-266 |
2.66e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 78 YGVN---L----QIKRGQTVALVGSSGCGKSTIVQLLQrfydpeeGQIlidgvnlkdinlkwwRENIGIVSQEP----VL 146
Cdd:PRK13409 83 YGVNgfkLyglpIPKEGKVTGILGPNGIGKTTAVKILS-------GEL---------------IPNLGDYEEEPswdeVL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 --F-GTTIE---ENIRYGHLDVTK--EDIEQAAKM--ANAHDFIM--DLPQKYETLVGERG---------AQLSGGQKQR 205
Cdd:PRK13409 141 krFrGTELQnyfKKLYNGEIKVVHkpQYVDLIPKVfkGKVRELLKkvDERGKLDEVVERLGlenildrdiSELSGGELQR 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIktaDMIA 266
Cdd:PRK13409 221 VAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVL---DYLA 278
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
79-229 |
2.89e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLL--QRfyDPEEGQILIDGVNLKDINLKWWREN-IGIVSQEPVLFGT----TI 151
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRGLvpdmSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENI-----------RYGHLDvTKEDIEQAAKMANAHDfImdLPQKYETLVGergaQLSGGQKQRIAIARALVRNPKILL 220
Cdd:COG3845 354 AENLilgryrrppfsRGGFLD-RKAIRAFAEELIEEFD-V--RTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLI 425
|
....*....
gi 2119559688 221 LDEATSALD 229
Cdd:COG3845 426 AAQPTRGLD 434
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
711-793 |
2.94e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 711 ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwLRSQIGI--VSQEPVLF-DRTIA 787
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLSVK 104
|
....*.
gi 2119559688 788 ENIAYG 793
Cdd:PRK15439 105 ENILFG 110
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
415-623 |
3.03e-07 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 52.89 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 415 VLM--FVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRlatdasqVQGAAGIK- 491
Cdd:cd18588 43 VLAigLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFE--SRQVGDTVAR-------VRELESIRq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 492 --LGSSLMA---FCSVVTGIVIGFVFSWKITLLVIAFLPF-----VMIGGALEMQMMQ--GAAGKNKEALesagkiaIES 559
Cdd:cd18588 114 flTGSALTLvldLVFSVVFLAVMFYYSPTLTLIVLASLPLyallsLLVTPILRRRLEEkfQRGAENQSFL-------VET 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 560 IENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18588 187 VTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLV 250
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
710-777 |
3.28e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 3.28e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 710 TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQW---LRSQ-IGIVSQ 777
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQ 95
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
705-808 |
3.46e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 53.31 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 705 TRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVL--- 781
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfe 91
|
90 100
....*....|....*....|....*...
gi 2119559688 782 FD-RTIAENIAYGDNSREVTMDEIIDAA 808
Cdd:PRK09536 92 FDvRQVVEMGRTPHRSRFDTWTETDRAA 119
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1-32 |
4.42e-07 |
|
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: 52.48 E-value: 4.42e-07
10 20 30
....*....|....*....|....*....|..
gi 2119559688 1 VFFSVMIGAFSLGNAMPHLQTLATARGAAYYL 32
Cdd:cd18577 269 VFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
694-792 |
4.64e-07 |
|
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: 51.13 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNlqwlRSQIG 773
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100
....*....|....*....|
gi 2119559688 774 IVSQEPVLF-DRTIAENIAY 792
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVY 93
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
692-792 |
6.07e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 50.63 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 692 ANLSFANIIF---RYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQ-LTERFYDPAD-GIVSLDGHNLKdlnLQ 766
Cdd:cd03213 2 VTLSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRTGLGVsGEVLINGRPLD---KR 78
|
90 100
....*....|....*....|....*..
gi 2119559688 767 WLRSQIGIVSQEPVLFDR-TIAENIAY 792
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTlTVRETLMF 105
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
84-254 |
6.76e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 84 IKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkDINLKWwrenigiVSQE-PVLFGTTIEENIryghlDV 162
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----NWQLAW-------VNQEtPALPQPALEYVI-----DG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 163 TKE--DIEQAAKMANAHD---FIMDLPQKYETL----VGERGAQL------------------SGGQKQRIAIARALVRN 215
Cdd:PRK10636 88 DREyrQLEAQLHDANERNdghAIATIHGKLDAIdawtIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2119559688 216 PKILLLDEATSALDTesegivqDA---LEK--ASHGRTTIVIAH 254
Cdd:PRK10636 168 SDLLLLDEPTNHLDL-------DAviwLEKwlKSYQGTLILISH 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
694-803 |
8.57e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 51.66 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRY-PTRP-DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDG----HNLKDLNLQW 767
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 2119559688 768 LRSQIGIVSQEP--VLFDRTIAENIAYGDNSREVTMDE 803
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEK 119
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
694-780 |
8.77e-07 |
|
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: 49.35 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN-LQWLRSQI 772
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGI 77
|
....*...
gi 2119559688 773 GIVSQEPV 780
Cdd:cd03216 78 AMVYQLSV 85
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
698-822 |
9.49e-07 |
|
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: 51.39 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYpTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDpADGIVSLDGHNLKDLNLQWLRSQIGIVSQ 777
Cdd:cd03289 7 DLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQ 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2119559688 778 EPVLFDRTIAENI-AYGDNSREvtmdEIIDAARKANIHNFIASLPD 822
Cdd:cd03289 85 KVFIFSGTFRKNLdPYGKWSDE----EIWKVAEEVGLKSVIEQFPG 126
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
685-793 |
1.38e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.56 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 685 EQLHTFTANLSFANIIFRYPTRpdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN 764
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110
....*....|....*....|....*....|
gi 2119559688 765 LQWLRSQIGIVSQE-PVLFDRTIAENIAYG 793
Cdd:PRK10575 80 SKAFARKVAYLPQQlPAAEGMTVRELVAIG 109
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
79-229 |
1.51e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRENI--GIV------SQEPVLFGTT 150
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG---HEVVTRSPQDGLanGIVyisedrKRDGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIRYGHLDVTKED---IEQAAKMANAHDFIMDLPQK---YETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PRK10762 347 VKENMSLTALRYFSRAggsLKHADEQQAVSDFIRLFNIKtpsMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEP 422
|
....*
gi 2119559688 225 TSALD 229
Cdd:PRK10762 423 TRGVD 427
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
712-779 |
1.81e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.73 E-value: 1.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQIGIVSQEP 779
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP 101
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
59-263 |
1.99e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQL------------LQRFydpeeGQILIDGVNLK 126
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndLTLF-----GRRRGSGETIW 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 127 DInlkwwRENIGIVSQEPVL---FGTTIEENIRYGHLDVTkeDIEQAAKmanahDFIMDLPQKYETLVGERGAQ------ 197
Cdd:PRK10938 333 DI-----KKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSI--GIYQAVS-----DRQQKLAQQWLDILGIDKRTadapfh 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 198 -LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIV------------IAHRLSTIKTA 262
Cdd:PRK10938 401 sLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFVPDG 479
|
.
gi 2119559688 263 D 263
Cdd:PRK10938 480 D 480
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
410-807 |
2.00e-06 |
|
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: 51.87 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 410 KIIQYVLMFVGVGVISLI-------------AYFVQGYMFGRS-------GEYL------TLRLRSMSFKAMLRQEIAFF 463
Cdd:TIGR00957 326 KAIHDLMMFIGPQILSLLirfvndpmapdwqGYFYTGLLFVCAclqtlilHQYFhicfvsGMRIKTAVMGAVYRKALVIT 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 464 DD--HNNSVGALTTRLATDASQVqgaagIKLGSSLMAFCSVVTGIVIGFVFSWK----ITLLVIAFLPF-VMIGGALEMQ 536
Cdd:TIGR00957 406 NSarKSSTVGEIVNLMSVDAQRF-----MDLATYINMIWSAPLQVILALYFLWLnlgpSVLAGVAVMVLmVPLNAVMAMK 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 537 M--MQGAAGKNKEaleSAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAA 614
Cdd:TIGR00957 481 TktYQVAHMKSKD---NRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALI 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 615 SFWLGAYLikqSEVDYVDVFKAF-SAILFG---------GMAIGNASafapdaaKAEQSAKEIFKLIDKK---PD-IDNE 680
Cdd:TIGR00957 558 TFAVYVTV---DENNILDAEKAFvSLALFNilrfplnilPMVISSIV-------QASVSLKRLRIFLSHEelePDsIERR 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 681 SEKGEQLHTFTANlsfaNIIFRYpTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhnl 760
Cdd:TIGR00957 628 TIKPGEGNSITVH----NATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--- 699
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2119559688 761 kdlnlqwlrsQIGIVSQEPVLFDRTIAENIAYGDNSREVTMDEIIDA 807
Cdd:TIGR00957 700 ----------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEA 736
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
708-780 |
2.05e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 49.06 E-value: 2.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERF--YDPADGIVSLDGHNLKDLNLQwLRSQIGI--VSQEPV 780
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPP 87
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
73-316 |
2.40e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQI-LIDGVNLkdinlkwwreniGIVSQEPVLFGTTI 151
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKL------------GYFAQHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRygHLD-VTKEDIEQAAKmanahDFIMDLPQKYETlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 230
Cdd:PRK10636 392 ESPLQ--HLArLAPQELEQKLR-----DYLGGFGFQGDK-VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 231 ESEGIVQDAL---EKAshgrtTIVIAHRLSTIK-TADMIAGFKDGVVAE-QGTHNElmskqgiYQQ-LVTLQSMKSADDN 304
Cdd:PRK10636 464 DMRQALTEALidfEGA-----LVVVSHDRHLLRsTTDDLYLVHDGKVEPfDGDLED-------YQQwLSDVQKQENQTDE 531
|
250
....*....|....*...
gi 2119559688 305 EIEDFN------RDDTKR 316
Cdd:PRK10636 532 APKENNansaqaRKDQKR 549
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
197-269 |
3.03e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.12 E-value: 3.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 197 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTADMIAGFK 269
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
694-804 |
3.22e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.36 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTTiLKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110
....*....|....*....|....*....|...
gi 2119559688 774 IVSQEP--VLFDRTIAENIAYGDNSREVTMDEI 804
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAVPYDEM 119
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
698-807 |
3.49e-06 |
|
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: 48.91 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHN-LKDlnLQWLRSQIGIVS 776
Cdd:cd03265 5 NLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvVRE--PREVRRRIGIVF 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 2119559688 777 QEPVLFDR-TIAENIA-----YGDNSREVT--MDEIIDA 807
Cdd:cd03265 80 QDLSVDDElTGWENLYiharlYGVPGAERRerIDELLDF 118
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
75-258 |
3.64e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 75 KILY-GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI-DGVNLkdinlkwwreniGIVSQ--EPVLFGTT 150
Cdd:TIGR03719 335 KLLIdDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKL------------AYVDQsrDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIRYG--HLDVTKEDIEQAAKMAnAHDFIMDLPQKyetLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSAL 228
Cdd:TIGR03719 403 VWEEISGGldIIKLGKREIPSRAYVG-RFNFKGSDQQK---KVG----QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
170 180 190
....*....|....*....|....*....|....*.
gi 2119559688 229 DTESEGIVQDALEKasHGRTTIVIAH------RLST 258
Cdd:TIGR03719 475 DVETLRALEEALLN--FAGCAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
411-653 |
4.09e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 49.40 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 411 IIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVqgaAGI 490
Cdd:cd18540 41 LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRL---GEI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 491 kLGSSLM----AFCSVVTGIVIGFVFSWKITLLVIAFLPF-VMIGGALEMQMMQGaagkNKEALESAGKI--AI-ESIEN 562
Cdd:cd18540 116 -ISWGLVdlvwGITYMIGILIVMLILNWKLALIVLAVVPVlAVVSIYFQKKILKA----YRKVRKINSRItgAFnEGITG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 563 IRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLsqaVMFFAYAAS---FWLGAYLikqsevdyvdvfkafsa 639
Cdd:cd18540 191 AKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPI---VLFLGSIATalvLWYGGIL----------------- 250
|
250
....*....|....
gi 2119559688 640 ILFGGMAIGNASAF 653
Cdd:cd18540 251 VLAGAITIGTLVAF 264
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
698-793 |
4.99e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.22 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN-LQWLRSQIGIVS 776
Cdd:PRK13644 6 NVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVF 83
|
90
....*....|....*....
gi 2119559688 777 QEP--VLFDRTIAENIAYG 793
Cdd:PRK13644 84 QNPetQFVGRTVEEDLAFG 102
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
414-623 |
5.76e-06 |
|
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: 49.05 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 414 YVLmfvGVGVISLIAY-----FVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTtrlatdaSQVQGAA 488
Cdd:cd18783 42 YVL---TIGVVIALLFegilgYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFE--RTPAGVLT-------KHMQQIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 489 GIK---LGSSLMAFCSVVTGIV---IGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIEN 562
Cdd:cd18783 110 RIRqflTGQLFGTLLDATSLLVflpVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 563 IRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18783 190 IRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLV 250
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
692-737 |
5.95e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.46 E-value: 5.95e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2119559688 692 ANLSFANIIFRYPTrpDTTILKGLDLEVPQGQTVALVGSSGCGKST 737
Cdd:PRK11650 2 AGLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKST 45
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
697-811 |
6.79e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.55 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 697 ANIIFRYPTRPDTT---ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQW-LRSQI 772
Cdd:PRK13633 8 KNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKA 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2119559688 773 GIVSQEPvlfDRTIA-----ENIAYGDNSREVTMDEI---IDAARKA 811
Cdd:PRK13633 88 GMVFQNP---DNQIVativeEDVAFGPENLGIPPEEIrerVDESLKK 131
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
712-790 |
7.08e-06 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 48.20 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwLRSQIGIVS--QEPVLFDR-TIAE 788
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVLE 94
|
..
gi 2119559688 789 NI 790
Cdd:cd03219 95 NV 96
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
705-792 |
7.38e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.61 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 705 TRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWL---RSQIGIVSQEPVL 781
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
|
90
....*....|..
gi 2119559688 782 F-DRTIAENIAY 792
Cdd:PRK11831 96 FtDMNVFDNVAY 107
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
708-792 |
7.91e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.12 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL---KD---LNLQWLRSQIGIVSQEPVL 781
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDifqIDAIKLRKEVGMVFQQPNP 101
|
90
....*....|..
gi 2119559688 782 FDR-TIAENIAY 792
Cdd:PRK14246 102 FPHlSIYDNIAY 113
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
694-786 |
8.79e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.20 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRpdTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:PRK10522 323 LELRNVTFAYQDN--GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90
....*....|...
gi 2119559688 774 IVSQEPVLFDRTI 786
Cdd:PRK10522 401 AVFTDFHLFDQLL 413
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
712-792 |
9.02e-06 |
|
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: 47.75 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDlNLQWLRSQIGIVSQEPVLFDR-TIAENI 790
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENL 99
|
..
gi 2119559688 791 AY 792
Cdd:cd03266 100 EY 101
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
84-259 |
9.07e-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: 46.80 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 84 IKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNlkdINLKwwrenigivsqepvlfgttieeniryghldvt 163
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT---PVYK-------------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 164 kedieqaakmanahdfimdlPQKYEtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKA 243
Cdd:cd03222 67 --------------------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170
....*....|....*...
gi 2119559688 244 S-HG-RTTIVIAHRLSTI 259
Cdd:cd03222 118 SeEGkKTALVVEHDLAVL 135
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
77-261 |
1.02e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG-VNLKDINLKWWRENIGIVSQE--PVLFGTTIEE 153
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsAALIAISSGLNGQLTGIENIElkGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 niryghldvTKEDIEQAAKMANAHDFIMDLPQKYetlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALD-TES 232
Cdd:PRK13545 120 ---------IKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDqTFT 179
|
170 180
....*....|....*....|....*....
gi 2119559688 233 EGIVQDALEKASHGRTTIVIAHRLSTIKT 261
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKS 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
694-757 |
1.11e-05 |
|
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: 47.53 E-value: 1.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 694 LSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDG 757
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG 83
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
713-791 |
1.21e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.16 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 713 KGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN-LQWL--RSQIGIVSQEPV--LFDR-TI 786
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLasLNPRmTI 117
|
....*
gi 2119559688 787 AENIA 791
Cdd:PRK15079 118 GEIIA 122
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
712-822 |
1.45e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.11 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRS----QIGIVSQEPVLFDR-TI 786
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2119559688 787 AENIAYGDNSREVTMDE----IIDAARKANIHNFIASLPD 822
Cdd:PRK10070 124 LDNTAFGMELAGINAEErrekALDALRQVGLENYAHSYPD 163
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
66-237 |
1.48e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 66 FRYPSRPeakILY-GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILidgvnlkdinlKWWRENIGIVSQEp 144
Cdd:PLN03073 516 FGYPGGP---LLFkNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQH- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 vlfgttieenirygHLDVTkeDIEQAAKMANAHDFIMDLPQKYETLVGERGAQ----------LSGGQKQRIAIARALVR 214
Cdd:PLN03073 581 --------------HVDGL--DLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAFAKITFK 644
|
170 180
....*....|....*....|....
gi 2119559688 215 NPKILLLDEATSALDTES-EGIVQ 237
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
709-793 |
1.83e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 47.77 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 709 TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVLFDR-TIA 787
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVF 92
|
....*.
gi 2119559688 788 ENIAYG 793
Cdd:PRK10851 93 DNIAFG 98
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
689-793 |
2.05e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 689 TFTANLSFANIIFRYPTRP--DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGH----NLKD 762
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKK 81
|
90 100 110
....*....|....*....|....*....|....
gi 2119559688 763 LN-LQWLRSQIGIVSQEP--VLFDRTIAENIAYG 793
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFG 115
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
84-310 |
2.09e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.47 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 84 IKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG----VNLKDINlkwwrENIGIVSQ----EPVLFGTtiEENI 155
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksilTNISDVH-----QNMGYCPQfdaiDDLLTGR--EHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGHL-DVTKEDIEqaaKMANAHDFIMDLPQKYETLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEG 234
Cdd:TIGR01257 2035 LYARLrGVPAEEIE---KVANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 235 IVQDALEK-ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSKQGiYQQLVTLQsMKSADDNEIEDFN 310
Cdd:TIGR01257 2108 MLWNTIVSiIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG-DGYIVTMK-IKSPKDDLLPDLN 2183
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
695-785 |
2.10e-05 |
|
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: 46.37 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 695 SFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDlnlqwLRSQIGI 774
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGY 72
|
90
....*....|.
gi 2119559688 775 VSQEPvLFDRT 785
Cdd:cd03235 73 VPQRR-SIDRD 82
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
694-779 |
2.21e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRpdTTILKGLDLEVPQ----------GQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGH---NL 760
Cdd:PRK10261 314 LQVRNLVTRFPLR--SGLLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTL 391
|
90
....*....|....*....
gi 2119559688 761 KDLNLQWLRSQIGIVSQEP 779
Cdd:PRK10261 392 SPGKLQALRRDIQFIFQDP 410
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
712-810 |
2.50e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.00 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSL---DGHNLK----------DLNLQW----------- 767
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKktkekekvleKLVIQKtrfkkikkike 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2119559688 768 LRSQIGIVSQ--EPVLFDRTIAENIAYGDNSREVTMDEIIDAARK 810
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK 147
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
703-793 |
2.83e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.72 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 703 YPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEP--V 780
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90
....*....|...
gi 2119559688 781 LFDRTIAENIAYG 793
Cdd:PRK13652 91 IFSPTVEQDIAFG 103
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
80-289 |
2.87e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKD------IN-----LKWWRENIGIVSQEPVLFG 148
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneaINhgfalVTEERRSTGIYAYLDIGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYghldVTKEDIEQAAKMANAHDFIMDLPQ----KYETLVGergaQLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PRK10982 347 SLISNIRNY----KNKVGLLDNSRMKSDTQWVIDSMRvktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 225 TSALDTESE-GIVQDALEKASHGRTTIVIAHRL-STIKTADMIAGFKDGVVA-----EQGTHNELMSKQGIY 289
Cdd:PRK10982 419 TRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLVAgivdtKTTTQNEILRLASLH 490
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
388-641 |
3.39e-05 |
|
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: 46.40 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 388 FAVIFSEILGVFA------ILDE--GEQERKIIQYVLM-FVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQ 458
Cdd:cd18568 9 LASLLLQLLGLALplftqiILDRvlVHKNISLLNLILIgLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 459 EIAFFDDHNnsVGALTTRLA-TDASQ---VQGAAGIklgssLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALE 534
Cdd:cd18568 89 PLSFFASRK--VGDIITRFQeNQKIRrflTRSALTT-----ILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 535 MQMMQGAagkNKEALESAGKIA---IESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFA 611
Cdd:cd18568 162 SPKLKRN---SREIFQANAEQQsflVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLG 238
|
250 260 270
....*....|....*....|....*....|
gi 2119559688 612 YAASFWLGAYLIKQSEVDyVDVFKAFSAIL 641
Cdd:cd18568 239 TIAVLWYGAYLVISGQLT-IGQLVAFNMLF 267
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
707-807 |
3.97e-05 |
|
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: 45.78 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 707 PDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQ----IGIVSQEPVLF 782
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100
....*....|....*....|....*
gi 2119559688 783 DRTIAENIAYGDNSREVTMDEIIDA 807
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDA 116
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
707-800 |
4.11e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 46.98 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 707 PDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQ-LTERfYDPADGIVSLdGHNLKdlnlqwlrsqIGIVSQEPVLFD-- 783
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKlLAGE-LEPDSGTVKL-GETVK----------IGYFDQHQEELDpd 393
|
90
....*....|....*...
gi 2119559688 784 RTIAENIA-YGDNSREVT 800
Cdd:COG0488 394 KTVLDELRdGAPGGTEQE 411
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
714-790 |
4.47e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 45.75 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 714 GLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLrSQIGIVS--QEPVLF-DRTIAENI 790
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
176-285 |
6.00e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 176 AHDFIMDLP---QKYETL---------VGERGAQLSGGQKQRIAIARAL---VRNPKILLLDEATSALDTES-EGIVQDA 239
Cdd:PRK00635 776 AEKFFLDEPsihEKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDiKALIYVL 855
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 240 LEKASHGRTTIVIAHRLSTIKTADMI------AGFKDGVVAEQGTHNELMSK 285
Cdd:PRK00635 856 QSLTHQGHTVVIIEHNMHVVKVADYVlelgpeGGNLGGYLLASCSPEELIHL 907
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
692-793 |
6.41e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 46.18 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 692 ANLSFANIifrYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQ 771
Cdd:PRK11000 2 ASVTLRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERG 76
|
90 100
....*....|....*....|...
gi 2119559688 772 IGIVSQEPVLFDR-TIAENIAYG 793
Cdd:PRK11000 77 VGMVFQSYALYPHlSVAENMSFG 99
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
694-811 |
7.66e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.08 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNlqwlrSQIG 773
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERG 73
|
90 100 110
....*....|....*....|....*....|....*....
gi 2119559688 774 IVSQ-EPVLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQM 112
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
705-820 |
9.31e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.95 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 705 TRPD-TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNlkdlnlqwlrsQIGIVSQEPVLFD 783
Cdd:COG4178 371 RTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-----------RVLFLPQRPYLPL 439
|
90 100 110
....*....|....*....|....*....|....*..
gi 2119559688 784 RTIAENIAYGDNSREVTMDEIIDAARKANIHNFIASL 820
Cdd:COG4178 440 GTLREALLYPATAEAFSDAELREALEAVGLGHLAERL 476
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
712-793 |
1.03e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.55 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwLRSQ--IGIVSQEPVLFDR-TIAE 788
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQELSVIDElTVLE 99
|
....*
gi 2119559688 789 NIAYG 793
Cdd:PRK09700 100 NLYIG 104
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
390-807 |
1.13e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 390 VIFSEILgvfAILDEGEQerKIIQYV---LMFVGV--GVISLIAYFVQgymFGRSGeyltLRLRSMSFKAMLRQEIAFFD 464
Cdd:PLN03232 322 VILSHLL---QSMQEGDP--AWVGYVyafLIFFGVtfGVLCESQYFQN---VGRVG----FRLRSTLVAAIFHKSLRLTH 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 465 D--HNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVI----GfVFSWKITLLVIAFLPFVMIggalemqMM 538
Cdd:PLN03232 390 EarKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLyqqlG-VASLFGSLILFLLIPLQTL-------IV 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 539 QGAAGKNKEALESAGK---IAIESIENIRTVASLTREDMFQKKF----NHELQMpyniaLKKAHLIG-----IGFSLSQA 606
Cdd:PLN03232 462 RKMRKLTKEGLQWTDKrvgIINEILASMDTVKCYAWEKSFESRIqgirNEELSW-----FRKAQLLSafnsfILNSIPVV 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 607 VMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILfggMAIGNASAFAPDAAKAEQSAKEIF----KLIDKKPdidnese 682
Cdd:PLN03232 537 VTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPL---NMLPNLLSQVVNANVSLQRIEELLlseeRILAQNP------- 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 683 kgeQLHTFTANLSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADgIVSLDghnlkd 762
Cdd:PLN03232 607 ---PLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV------ 676
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2119559688 763 lnlqwLRSQIGIVSQEPVLFDRTIAENIAYGDNSREVTMDEIIDA 807
Cdd:PLN03232 677 -----IRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDV 716
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
59-278 |
1.38e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 59 VQIRGV--HFrypsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVqLLQRFYDPEEGQilidgvnlKDINLKWW--- 133
Cdd:NF000106 14 VEVRGLvkHF-----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR--------RPWRF*TWcan 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 ----RENIGIvsQEPVLFGT----TIEENIRY--GHLDVTKEDIEQAAKmanahdfimDLPQKYE--TLVGERGAQLSGG 201
Cdd:NF000106 80 rralRRTIG*--HRPVR*GRresfSGRENLYMigR*LDLSRKDARARAD---------ELLERFSltEAAGRAAAKYSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 202 QKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIV-----------IAHRLSTIKTADMIAgfkD 270
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHELTVIDRGRVIA---D 225
|
....*...
gi 2119559688 271 GVVAEQGT 278
Cdd:NF000106 226 GKVDELKT 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
709-791 |
1.42e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.04 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 709 TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDL---NLQWLRSQ-IGIVSQ-EPVLFD 783
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNQkLGFIYQfHHLLPD 101
|
....*...
gi 2119559688 784 RTIAENIA 791
Cdd:PRK11629 102 FTALENVA 109
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
197-254 |
1.50e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 197 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKAShgRTTIVIAH 254
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
197-288 |
1.50e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 197 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTA-DMIAGFKDGVVA 274
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
|
90
....*....|....
gi 2119559688 275 EQGTHNELMSKQGI 288
Cdd:PRK09700 489 QILTNRDDMSEEEI 502
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
711-790 |
1.90e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.19 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 711 ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDL-------------NLQWLRSQIGIVSQ 777
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQ 99
|
90
....*....|....
gi 2119559688 778 EPVLFDR-TIAENI 790
Cdd:PRK10619 100 HFNLWSHmTVLENV 113
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
694-756 |
2.80e-04 |
|
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: 41.67 E-value: 2.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 694 LSFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLD 756
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG 60
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
693-797 |
2.91e-04 |
|
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: 43.03 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 693 NLSFANIiFRYPTRPDTT--ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPAD---GIVSLDGHNLKdlNLQW 767
Cdd:cd03234 3 VLPWWDV-GLKAKNWNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK--PDQF 79
|
90 100 110
....*....|....*....|....*....|.
gi 2119559688 768 LRSqIGIVSQEPVLFDR-TIAENIAYGDNSR 797
Cdd:cd03234 80 QKC-VAYVRQDDILLPGlTVRETLTYTAILR 109
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
710-779 |
2.94e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 2.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 710 TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYdPADGIVSLDGHNLKDLNLQWL---RSQIGIVSQEP 779
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP 371
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
92-254 |
3.62e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 92 LVGSSGCGKSTIVQLLQRFYDPEEGQILIDgVNlkdinlkwwrENIGIVSQEP-----------VLFGTT-----IEENI 155
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD-PN----------ERLGKLRQDQfafeeftvldtVIMGHTelwevKQERD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 R-YGHLDVTKEDIEQAAKM-------------ANAHDFIM----DLPQKYETLvgergAQLSGGQKQRIAIARALVRNPK 217
Cdd:PRK15064 101 RiYALPEMSEEDGMKVADLevkfaemdgytaeARAGELLLgvgiPEEQHYGLM-----SEVAPGWKLRVLLAQALFSNPD 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 2119559688 218 ILLLDEATSALDTESEGIVQDAL-EKAShgrTTIVIAH 254
Cdd:PRK15064 176 ILLLDEPTNNLDINTIRWLEDVLnERNS---TMIIISH 210
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
198-278 |
3.94e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 198 LSGGQKQRIAIARALVR--NPKIL-LLDEATSAL---DtesegiVQ---DALEK-ASHGRTTIVIAHRLSTIKTADMI-- 265
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLhfhD------IRkllEVLHRlVDKGNTVVVIEHNLDVIKTADWIid 900
|
90
....*....|....*...
gi 2119559688 266 ----AGFKDG-VVAEqGT 278
Cdd:COG0178 901 lgpeGGDGGGeIVAE-GT 917
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
77-316 |
4.46e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG-VNLKDInlkwwreNIGIVSQepvLFGTtieENI 155
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAI-------SAGLSGQ---LTGI---ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGHLDV------TKEDIEQAAKMANAHDFIMDLPQKYetlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK13546 107 EFKMLCMgfkrkeIKAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 230 -TESEGIVQDALEKASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSKqgiYQQLvtLQSMKSADDNEIE 307
Cdd:PRK13546 176 qTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAF--LNDFKKKSKAEQK 250
|
250
....*....|
gi 2119559688 308 DFNRD-DTKR 316
Cdd:PRK13546 251 EFRNKlDESR 260
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
418-623 |
5.21e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 42.83 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 418 FVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFddHNNSVGALTTRLATdASQVQGAAGIKLGSSLM 497
Cdd:cd18567 48 FGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYF--EKRHLGDIVSRFGS-LDEIQQTLTTGFVEALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 498 AFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAagkNKEALESAGK---IAIESIENIRTVASLTREDM 574
Cdd:cd18567 125 DGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRA---TEEQIVASAKeqsHFLETIRGIQTIKLFGREAE 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2119559688 575 FQKKFNHELQMPYNIALKKAHLiGIGFSLSQAVMF-FAYAASFWLGAYLI 623
Cdd:cd18567 202 REARWLNLLVDAINADIRLQRL-QILFSAANGLLFgLENILVIYLGALLV 250
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
715-792 |
5.26e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.85 E-value: 5.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 715 LDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLkDLNLQWLRSQIGIVSQEPVLFDR-TIAENIAY 792
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILF 1026
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
701-779 |
5.98e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.47 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 701 FRYPT----RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWlRSQ-IGIV 775
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQrIRMI 92
|
....
gi 2119559688 776 SQEP 779
Cdd:PRK15112 93 FQDP 96
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
691-764 |
6.92e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 43.17 E-value: 6.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 691 TANLSFANIIFRYPTRPDTT-ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN 764
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLD 76
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
712-800 |
7.26e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQ-LTerfydpadGIVSLDGHNL----KDLNLQWLR-SQ---IGIVSQEPVLF 782
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKvLT--------GIYTRDAGSIlylgKEVTFNGPKsSQeagIGIIHQELNLI 91
|
90
....*....|....*....
gi 2119559688 783 DR-TIAENIAYGdnsREVT 800
Cdd:PRK10762 92 PQlTIAENIFLG---REFV 107
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
708-801 |
9.34e-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: 42.50 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPA--DGIVSLDGHNLKDLNLQWL-RSQIGIVSQEPVLF-D 783
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
|
90
....*....|....*...
gi 2119559688 784 RTIAENIAYGDnsrEVTM 801
Cdd:TIGR02633 93 LSVAENIFLGN---EITL 107
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
387-623 |
1.02e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 42.11 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 387 AFAVIFSEILGVFAIL---------DEGEQERKIIQYVLMFVGVGVISLIAY---FVQGYMFGRSGEYLTLRLRSMSFKA 454
Cdd:cd18555 5 ISILLLSLLLQLLTLLipiltqyviDNVIVPGNLNLLNVLGIGILILFLLYGlfsFLRGYIIIKLQTKLDKSLMSDFFEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 455 MLRQEIAFFDdhNNSVGALTTRlATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFlpfVMIGGALE 534
Cdd:cd18555 85 LLKLPYSFFE--NRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLL---GLLIVLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 535 MQMMQGAAGKNKEALESAGK---IAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFA 611
Cdd:cd18555 159 LLTRKKIKKLNQEEIVAQTKvqsYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIA 238
|
250
....*....|..
gi 2119559688 612 YAASFWLGAYLI 623
Cdd:cd18555 239 PLLILWIGAYLV 250
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
84-107 |
1.08e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 42.23 E-value: 1.08e-03
10 20
....*....|....*....|....*
gi 2119559688 84 IKRGQTVALVGSSGCGKSTIV-QLL 107
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
707-810 |
1.13e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.32 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 707 PDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhnlKDLNL----QWLRSQIGIVSQEPVLF 782
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIrsprDAIALGIGMVHQHFMLV 92
|
90 100 110
....*....|....*....|....*....|.
gi 2119559688 783 DR-TIAENIAYGdnsREVTMDEIID--AARK 810
Cdd:COG3845 93 PNlTVAENIVLG---LEPTKGGRLDrkAARA 120
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
709-737 |
1.14e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.10 E-value: 1.14e-03
10 20
....*....|....*....|....*....
gi 2119559688 709 TTILKGLDLEVPQGQTVALVGSSGCGKST 737
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKST 71
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
160-265 |
1.71e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 160 LDVTkedIEQAAkmanahDFIMDLPQ---KYETLV---------GERGAQLSGGQKQRIAIARALVRNP--KIL-LLDEA 224
Cdd:PRK00349 790 LDMT---VEEAL------EFFEAIPKiarKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEP 860
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2119559688 225 TSALDTES--------EGIVQdalekasHGRTTIVIAHRLSTIKTADMI 265
Cdd:PRK00349 861 TTGLHFEDirkllevlHRLVD-------KGNTVVVIEHNLDVIKTADWI 902
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
80-284 |
1.72e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFyDPEEGQILIDGVNLKDINL---------KWWRENIGIVSQEP------ 144
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIDLlrlsprerrKLVGHNVSMIFQEPqscldp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 -VLFGTTIEENI-----------RYGHLdvTKEDIEQAAKMA-NAHDFIM-DLPqkYEtlvgergaqLSGGQKQRIAIAR 210
Cdd:PRK15093 105 sERVGRQLMQNIpgwtykgrwwqRFGWR--KRRAIELLHRVGiKDHKDAMrSFP--YE---------LTEGECQKVMIAI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELVT 248
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
708-763 |
1.77e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.93 E-value: 1.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKST-TVQLTERF-YDPADGIVSLDGHNLKDL 763
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLEL 70
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
691-793 |
1.99e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.44 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 691 TANLSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQ-WLR 769
Cdd:PRK11288 2 SPYLSFDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALA 78
|
90 100
....*....|....*....|....*
gi 2119559688 770 SQIGIVSQEPVLF-DRTIAENIAYG 793
Cdd:PRK11288 79 AGVAIIYQELHLVpEMTVAENLYLG 103
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
709-807 |
2.02e-03 |
|
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: 41.82 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 709 TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhnlkdlnlqwlrsQIGIVSQEPVLFDRTIAE 788
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKD 505
|
90
....*....|....*....
gi 2119559688 789 NIAYGDNSREVTMDEIIDA 807
Cdd:TIGR01271 506 NIIFGLSYDEYRYTSVIKA 524
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
707-738 |
2.36e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.45 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|..
gi 2119559688 707 PDTTILKGLDLEVPQGQTVALVGSSGCGKSTT 738
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLT 45
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
694-737 |
2.44e-03 |
|
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: 39.44 E-value: 2.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2119559688 694 LSFANIIFRYPTrpDTTILKGLDLEVPQGQTVALVGSSGCGKST 737
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSS 42
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
178-277 |
2.49e-03 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 178 DFIMDLPQKYETLvgERGAQ-LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIA 253
Cdd:cd03270 119 GFLVDVGLGYLTL--SRSAPtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVE 196
|
90 100 110
....*....|....*....|....*....|
gi 2119559688 254 HRLSTIKTADMI------AGFKDGVVAEQG 277
Cdd:cd03270 197 HDEDTIRAADHVidigpgAGVHGGEIVAQG 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
694-817 |
2.84e-03 |
|
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: 39.94 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYP-TRPDTTILKGLDLEVPQGQTVALVGSSGCGKST----TVQLTERFYDPaDGIVSLDGHNLKDLNLQWl 768
Cdd:cd03233 4 LSWRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2119559688 769 RSQIGIVSQEpvlfDRTIAeniaygdnsrEVTMDEIIDAARKANIHNFI 817
Cdd:cd03233 82 PGEIIYVSEE----DVHFP----------TLTVRETLDFALRCKGNEFV 116
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
680-803 |
3.52e-03 |
|
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: 40.23 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 680 ESEKGEQLHTFTANLSFANIIFRYptrpdTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhn 759
Cdd:cd03291 26 QENNDRKHSSDDNNLFFSNLCLVG-----APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-- 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2119559688 760 lkdlnlqwlrsQIGIVSQEPVLFDRTIAENIAYGdnsreVTMDE 803
Cdd:cd03291 99 -----------RISFSSQFSWIMPGTIKENIIFG-----VSYDE 126
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
721-739 |
3.67e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 40.30 E-value: 3.67e-03
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
417-623 |
3.69e-03 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 40.11 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 417 MFVGVGVI---SLIAYFVQGYMFGRSGEYLTLRLRSMSF-KAM-LRqeiafFDDHNNSVGALttrlatdASQVQGAAGIK 491
Cdd:cd18587 44 LAIGVLIAllfDFILKLLRAYFIDVAGKRADVILSSRLFeRVLgLR-----LEARPASVGSF-------ANNLREFESVR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 492 lgsSLMAFCSVVTGIVIGFVFswkITLLVIAFL-------PFV----MIGGALEMQ---------MMQGAAGKNKeales 551
Cdd:cd18587 112 ---DFFTSATLTALIDLPFVL---LFLAVIALIggplalvPLVaiplVLLYGLLLQkplrrlveeSMRESAQKNA----- 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 552 agkIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18587 181 ---LLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLI 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
198-229 |
4.09e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 4.09e-03
10 20 30
....*....|....*....|....*....|..
gi 2119559688 198 LSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
694-761 |
5.22e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.16 E-value: 5.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 694 LSFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLK 761
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK 66
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
191-265 |
6.06e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 6.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 191 VGERGAQLSGGQKQRIAIARALVRNPK---ILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTADMI 265
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYL 1771
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
197-241 |
6.20e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 6.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2119559688 197 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE 241
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
721-769 |
6.21e-03 |
|
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: 38.12 E-value: 6.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2119559688 721 QGQTVALVGSSGCGKSTTVQLTERFYDPAD-GIVSLDGHNLKDLNLQWLR 769
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL 50
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
1-32 |
6.64e-03 |
|
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: 39.57 E-value: 6.64e-03
10 20 30
....*....|....*....|....*....|..
gi 2119559688 1 VFFSVMIGAFSLGNAMPHLQTLATARGAAYYL 32
Cdd:cd18558 281 VFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
86-117 |
9.70e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.15 E-value: 9.70e-03
10 20 30
....*....|....*....|....*....|..
gi 2119559688 86 RGQTVALVGSSGCGKSTIVQLLQrfydPEEGQ 117
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALL----PELVL 111
|
|
|