|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-612 |
0e+00 |
|
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: 1052.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 3 KKSGKPPLQNNEK----EGKKERAVVDKVFLSRLSQILKIMVPRTFCKETGYLILIAVMLVSRTYCDVWMIQNGTLIESG 78
Cdd:TIGR00954 46 DKSGKEELTIVGKhstiEGAKKKAHVNGVFLGKLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 79 IIGRSSKDFKRYLFNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTRYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDV 158
Cdd:TIGR00954 126 IVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 159 EKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRFVNSRLI 238
Cdd:TIGR00954 206 EKFCDSVVELYSNLTKPILDVILYSFKLLTALGSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 239 TNSEEIAFYNGNKREKQTIHSVFRKLVEHLHNFIFFRFSMGFIDSIIAKYIATVVGYLVVSRPFLDLAHPRHLHSTHSEL 318
Cdd:TIGR00954 286 MNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEEL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 319 LEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFTARITELMQVLKDLNHGKYERTMVSQQDKGIEGAQASPLIPGAGEI 398
Cdd:TIGR00954 366 MQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 399 INADNIIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPERGKLFYVPQRPY 478
Cdd:TIGR00954 446 EYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPY 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 479 MTLGTLRDQVIYPDGKEDQKKKGISDQVLKGYLDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAI 558
Cdd:TIGR00954 526 MTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1958749229 559 LDECTSAVSVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNYEF 612
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
35-303 |
1.88e-126 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 373.48 E-value: 1.88e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 35 ILKIMVPRTFCKETGYLILIAVMLVSRTYCDVWMIQNGTLIESGIIGRSSKDFKRYLFNFIAAMPLISLVNNFLKYGLNE 114
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 115 LKLCFRVRLTRYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQG 194
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 195 PASMMAYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRFVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHNFIFF 274
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 1958749229 275 RFSMGFIDSIIAKYIATVVGYLVVSRPFL 303
Cdd:pfam06472 241 RLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
49-615 |
5.07e-101 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 318.67 E-value: 5.07e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 49 GYLILIAVMLVSRTYCDVWMI-QNGTLIESgIIGRSSKDFKRYLFNF---IAAMPLISLVNNFLKYGLnELKLcfRVRLT 124
Cdd:COG4178 25 GLLALLLLLTLASVGLNVLLNfWNRDFYDA-LQARDAAAFWQQLGVFallAAISILLAVYQTYLRQRL-QIRW--REWLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 125 RYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQG---------- 194
Cdd:COG4178 101 ERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLISFIGILWSLSGSLTftlggysiti 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 195 PASMM----AYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRFVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHN 270
Cdd:COG4178 181 PGYMVwaalIYAIIGTLLTHLIGRPLIRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 271 FIFFRFSMGFIDSIIAkYIATVVGYLVVSrpfldlahPRhlhsthselledyYQSGRM----LLRMSQALGRIVLAGR-- 344
Cdd:COG4178 261 LIRRQRNLTFFTTGYG-QLAVIFPILVAA--------PR-------------YFAGEItlggLMQAASAFGQVQGALSwf 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 345 --EMTRLAGFTA---RITELMQVLkdlnhgkyertmvsqqdkgiEGAQASPLIPGAGEIINADNIIkFDHVPLATPNGDI 419
Cdd:COG4178 319 vdNYQSLAEWRAtvdRLAGFEEAL--------------------EAADALPEAASRIETSEDGALA-LEDLTLRTPDGRP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGKEDqkk 499
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA--- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 500 kgISDQVLKGYLDNVQLGHILEReggWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCR 579
Cdd:COG4178 455 --FSDAELREALEAVGLGHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
570 580 590
....*....|....*....|....*....|....*...
gi 1958749229 580 K--VGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKKI 615
Cdd:COG4178 530 EelPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPA 567
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
405-610 |
6.53e-88 |
|
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: 270.56 E-value: 6.53e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPERGKLFYVPQRPYMTLGTL 484
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 485 RDQVIYPdgkedqkkkgisdqvlkgyldnvqlghilereggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 564
Cdd:cd03223 81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958749229 565 AVSVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNY 610
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
405-590 |
4.61e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.61 E-value: 4.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILiQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT---------KPE--RGKLFYV 473
Cdd:COG4619 1 LELEGLSFRVGGKPIL-SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsamPPPewRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 474 PQRPYMTLGTLRDQVIYPDgkeDQKKKGISDQVLKGYLDNVQLGH-ILEREggwdsVQDwmdvLSGGEKQRMAMARLFYH 552
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPF---QLRERKFDRERALELLERLGLPPdILDKP-----VER----LSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958749229 553 KPQFAILDECTSA---VSVD-VEDYIYSHCRKVGITLFTVSH 590
Cdd:COG4619 148 QPDVLLLDEPTSAldpENTRrVEELLREYLAEEGRAVLWVSH 189
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
49-591 |
2.89e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 119.50 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 49 GYLILIAVMLVSRTYCDVWMIQ-NGTLIESGIIGRSSkdfkRYLFNFIAAMPLISLVNNFLKYGLNEL--KLCFRV--RL 123
Cdd:COG1132 21 GLLILALLLLLLSALLELLLPLlLGRIIDALLAGGDL----SALLLLLLLLLGLALLRALLSYLQRYLlaRLAQRVvaDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 124 TRYLYEEYL-QAFTYY---KMGNLDNRIanpdqllTQDVekfcNSVVDLYSNLskpFLDIVLYIFKLTSAIGaqgpasMM 199
Cdd:COG1132 97 RRDLFEHLLrLPLSFFdrrRTGDLLSRL-------TNDV----DAVEQFLAHG---LPQLVRSVVTLIGALV------VL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 200 AYL------------LVSGLFLTRLRRPIGKMTIMEQKYEGEyrfVNSRL---ITNSEEIAFYNGNKREKQTIHSVFRKL 264
Cdd:COG1132 157 FVIdwrlalivllvlPLLLLVLRLFGRRLRKLFRRVQEALAE---LNGRLqesLSGIRVVKAFGREERELERFREANEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 265 VEHLHNFIF----FRFSMGFIDSIIAKYIATVVGYLVVSRpfldlahprhlHSTHSELLEdYYQSGRMLLRMSQALGRIV 340
Cdd:COG1132 234 RRANLRAARlsalFFPLMELLGNLGLALVLLVGGLLVLSG-----------SLTVGDLVA-FILYLLRLFGPLRQLANVL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 341 lagREMTRLAGFTARITELMqvlkdlnhgkyertmvSQQDKGIEGAQASPLIPGAGEIinadniiKFDHVPLATPNGDIL 420
Cdd:COG1132 302 ---NQLQRALASAERIFELL----------------DEPPEIPDPPGAVPLPPVRGEI-------EFENVSFSYPGDRPV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGH----LTKPE-RGKLFYVPQRPYMTLGTLRDQVI 489
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDptsgriLIDGVdirdLTLESlRRQIGVVPQDTFLFSGTIRENIR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 490 YpdGKEDqkkkgISDQVLKGYLDNVQLGHILER-EGGWDSVqdwmdV------LSGGEKQRMAMARLFYHKPQFAILDEC 562
Cdd:COG1132 436 Y--GRPD-----ATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGGQRQRIAIARALLKDPPILILDEA 503
|
570 580 590
....*....|....*....|....*....|.
gi 1958749229 563 TSAVSVDVEDYIYSHCRKV--GITLFTVSHR 591
Cdd:COG1132 504 TSALDTETEALIQEALERLmkGRTTIVIAHR 534
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
420-606 |
3.56e-26 |
|
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: 106.40 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLfGGHLTKPerGKLFYVPQRPYMTLGTLRDQVIYpdGKE-DQ 497
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKL-SGSVSVP--GSIAYVSQEPWIQNGTIRENILF--GKPfDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 498 KKkgiSDQVLK-------------GylDNVQLGhilerEGGwdsvqdwmdV-LSGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:cd03250 95 ER---YEKVIKacalepdleilpdG--DLTEIG-----EKG---------InLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958749229 564 SAVSVDVEDYIYSHC----RKVGITLFTVSHRKSLWKHHEYYLHMDG 606
Cdd:cd03250 156 SAVDAHVGRHIFENCilglLLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
405-594 |
7.75e-26 |
|
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: 104.39 E-value: 7.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGH-LTKPE----RGKLFY 472
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDptsgeiLIDGVdLRDLDleslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 473 VPQRPYMTLGTLRDqviypdgkedqkkkgisdqvlkgyldNVqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYH 552
Cdd:cd03228 81 VPQDPFLFSGTIRE--------------------------NI---------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958749229 553 KPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSL 594
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALakGKTVIVIAHRLST 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
405-606 |
6.02e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 109.08 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGH----LTKPE-RGKLFYV 473
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlGFLPPysgsiLINGVdlsdLDPASwRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 474 PQRPYMTLGTLRDQV-IY-PDgkedqkkkgISDQVLKGYLDNVQLGHILER-EGGWDSVqdwmdV------LSGGEKQRM 544
Cdd:COG4988 417 PQNPYLFAGTIRENLrLGrPD---------ASDEELEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749229 545 AMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG 606
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDD 546
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
421-564 |
2.01e-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: 96.56 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGHLTKPE----RGKLFYVPQ--RPYMTLgTLRDQ 487
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPtegtilLDGQDLTDDErkslRKEIGYVFQdpQLFPRL-TVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749229 488 VIYPDGKEDQKKKGISDQVLKgYLDNVQLGHILEReggwdSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 564
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEE-ALEKLGLGDLADR-----PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
383-591 |
2.98e-23 |
|
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: 104.08 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 383 IEGAQASPLIPGAGEIINADNIIKFDHVPLATPNGD-ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP----- 456
Cdd:COG4987 312 LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpqsgs 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 457 -LFGGH----LTKPERGKLF-YVPQRPYMTLGTLRD--QVIYPDGKEDQkkkgisdqvLKGYLDNVQLGHILER-EGGWD 527
Cdd:COG4987 392 iTLGGVdlrdLDEDDLRRRIaVVPQRPHLFDTTLREnlRLARPDATDEE---------LWAALERVGLGDWLAAlPDGLD 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 528 SvqdWMDV----LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHR 591
Cdd:COG4987 463 T---WLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHR 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
336-594 |
6.81e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 99.67 E-value: 6.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 336 LGRIVLAGReMTRLAGFTARI--TELMQVLKDLN---HGKYERTMVSQQDKGIEGAQASPLIPGAGEIINADNIIKFDHV 410
Cdd:TIGR02857 249 IGFRLLAGD-LDLATGLFVLLlaPEFYLPLRQLGaqyHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 411 PLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGHLT----KPERGKLFYVPQRPYM 479
Cdd:TIGR02857 328 SVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLlGFVDPtegsiaVNGVPLAdadaDSWRDQIAWVPQHPFL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 480 TLGTLRDQVIY--PDGKEDQKKKGISDQVLKGYLDNVQLGhiLEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFA 557
Cdd:TIGR02857 408 FAGTIAENIRLarPDASDAEIREALERAGLDEFVAALPQG--LDTPIGEGGAG-----LSGGQAQRLALARAFLRDAPLL 480
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958749229 558 ILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSL 594
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
405-593 |
5.21e-21 |
|
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: 92.29 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT-----------KPERGKLFYV 473
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 474 PQRPYMTLGTLRDQVIY--PDGKEDQ-----KKKGISDQVLK---GYldNVQLGhilERegGWDsvqdwmdvLSGGEKQR 543
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYgrPDATDEEvieaaKAAQIHDKIMRfpdGY--DTIVG---ER--GLK--------LSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958749229 544 MAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKS 593
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
416-607 |
6.27e-21 |
|
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: 91.44 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGHLTKpERGKLFYVPQRPYM--------- 479
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPtsgsirVFGKPLEK-ERKRIGYVPQRRSIdrdfpisvr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 480 -TLGTLRDQVIYPDGKEDQKKKGISDQVLKgyldNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAI 558
Cdd:cd03235 89 dVVLMGLYGHKGLFRRLSKADKAKVDEALE----RVGLSELADRQ---------IGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958749229 559 LDECTSAVSVDVEDYIYSHCRKV---GITLFTVSH-RKSLWKHHEYYLHMDGR 607
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELrreGMTILVVTHdLGLVLEYFDRVLLLNRT 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
416-590 |
2.25e-20 |
|
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: 90.87 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG----------HLTKPERGKLF-YVPQRPYMTLG-T 483
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGevlldgrdlaSLSRRELARRIaYVPQEPPAPFGlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 484 LRDQVI---YP-------DGKEDQKkkgISDQVlkgyLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHK 553
Cdd:COG1120 92 VRELVAlgrYPhlglfgrPSAEDRE---AVEEA----LERTGLEHLADRP---------VDELSGGERQRVLIARALAQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958749229 554 PQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSH 590
Cdd:COG1120 156 PPLLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLH 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
405-611 |
6.46e-20 |
|
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: 94.13 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLA-TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGH----LTKPE-RGKL 470
Cdd:COG2274 474 IELENVSFRyPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlglyeptsGRI--LIDGIdlrqIDPASlRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 471 FYVPQRPYMTLGTLRDQVIY--PDGKEDQ-----KKKGISDQVLK---GYldNVQLGhilerEGGwdsvqdwmDVLSGGE 540
Cdd:COG2274 552 GVVLQDVFLFSGTIRENITLgdPDATDEEiieaaRLAGLHDFIEAlpmGY--DTVVG-----EGG--------SNLSGGQ 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749229 541 KQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG-----RGNYE 611
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDKgriveDGTHE 694
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
402-606 |
2.80e-19 |
|
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: 87.14 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 402 DNIIKFDHVPLATPN-GDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT---KP--------ERG 468
Cdd:cd03248 9 KGIVKFQNVTFAYPTrPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPisqyehkyLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 469 KLFYVPQRPYMTLGTLRDQVIYpdGKEDQKKKGISDQVLKGYLDnvqlGHILEREGGWDS-VQDWMDVLSGGEKQRMAMA 547
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAY--GLQSCSFECVKEAAQKAHAH----SFISELASGYDTeVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958749229 548 RLFYHKPQFAILDECTSAVSVDVEDYIYS--HCRKVGITLFTVSHRKSLWKHHEYYLHMDG 606
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
416-591 |
4.40e-19 |
|
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: 84.60 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggHLTKPERGKLFYvpqrpymtlgtlrdqviypDGKE 495
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA--------GLLKPTSGEILI-------------------DGKD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 496 dqkkkgISDQVLKGYLDNVQLGHilereggwdsvQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD----VE 571
Cdd:cd00267 63 ------IAKLPLEELRRRIGYVP-----------Q-----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAsrerLL 120
|
170 180
....*....|....*....|
gi 1958749229 572 DYIYSHCRKvGITLFTVSHR 591
Cdd:cd00267 121 ELLRELAEE-GRTVIIVTHD 139
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
400-609 |
1.06e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.54 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 400 NADNIIKFDHVPLATpNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGH---LTKPE--RG 468
Cdd:PRK10247 3 ENSPLLQLQNVGYLA-GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISptsgtlLFEGEdisTLKPEiyRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 469 KLFYVPQRPYMTLGTLRDQVIYP---DGKEDQKKKGISDqvlkgyLDNVQLG-HILEReggwdSVQDwmdvLSGGEKQRM 544
Cdd:PRK10247 82 QVSYCAQTPTLFGDTVYDNLIFPwqiRNQQPDPAIFLDD------LERFALPdTILTK-----NIAE----LSGGEKQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749229 545 AMARLFYHKPQFAILDECTSAVSVD----VEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGN 609
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAG 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
420-594 |
1.72e-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: 83.42 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTkpergkLFYVPQRPYmTLGTLRDQViypdgkedqkk 499
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR------LDGADISQW-DPNELGDHV----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 500 kgisdqvlkGYL-DNVQL--GHILEreggwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYS 576
Cdd:cd03246 79 ---------GYLpQDDELfsGSIAE------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180
....*....|....*....|.
gi 1958749229 577 ---HCRKVGITLFTVSHRKSL 594
Cdd:cd03246 138 aiaALKAAGATRIVIAHRPET 158
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
416-590 |
1.96e-18 |
|
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: 84.07 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGHLTKPE---RGKLFYVPQRP--YMTLg 482
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILagllppsaGEVL-WNGEPIRDARedyRRRLAYLGHADglKPEL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 483 TLRDQVIYpdgKEDQKKKGISDQVLKGYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDEC 562
Cdd:COG4133 91 TVRENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 1958749229 563 TSAVSVD----VEDYIYSHCRKVGITLFTvSH 590
Cdd:COG4133 159 FTALDAAgvalLAELIAAHLARGGAVLLT-TH 189
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
416-590 |
6.52e-18 |
|
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: 81.71 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggHLTKPERGKLfYVPQRPYMTLgtlrdqviypDGKE 495
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA--------GLLKPSSGEI-LLDGKDLASL----------SPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 496 DQKKKGISDQVLkgylDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVE 571
Cdd:cd03214 71 LARKIAYVPQAL----ELLGLAHLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLdiahQIELL 137
|
170
....*....|....*....
gi 1958749229 572 DYIYSHCRKVGITLFTVSH 590
Cdd:cd03214 138 ELLRRLARERGKTVVMVLH 156
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
405-593 |
6.62e-18 |
|
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: 83.04 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT-----------KPERGKLFYV 473
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 474 PQRPYMTLGTLRDQVIY--PDGKEDQ-----KKKGISDQVLK---GYLDNVqlghileREGGwdsvqdwmDVLSGGEKQR 543
Cdd:cd03254 83 LQDTFLFSGTIMENIRLgrPNATDEEvieaaKEAGAHDFIMKlpnGYDTVL-------GENG--------GNLSQGERQL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958749229 544 MAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKS 593
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLS 199
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
400-590 |
1.14e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 82.83 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 400 NADNIIKFDHVPLATpNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRV-LGELWPL-----FGGHLTKPERGKLFYV 473
Cdd:COG1121 2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAiLGLLPPTsgtvrLFGKPPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 474 PQRPYMTLG---TLRDQV---IYPD-------GKEDqkkKGISDQVlkgyLDNVQLGHILEReggwdsvqdWMDVLSGGE 540
Cdd:COG1121 81 PQRAEVDWDfpiTVRDVVlmgRYGRrglfrrpSRAD---REAVDEA----LERVGLEDLADR---------PIGELSGGQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958749229 541 KQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYS---HCRKVGITLFTVSH 590
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTH 197
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
405-594 |
2.97e-17 |
|
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: 81.10 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDIL-IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWplfgghltKPERGKLF------------ 471
Cdd:cd03245 3 IEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY--------KPTSGSVLldgtdirqldpa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 472 -------YVPQRPYMTLGTLRDQVI--YPDGKEDQ-----KKKGISDQVLK---GYldNVQLGhilerEGGwdsvqdwmD 534
Cdd:cd03245 75 dlrrnigYVPQDVTLFYGTLRDNITlgAPLADDERilraaELAGVTDFVNKhpnGL--DLQIG-----ERG--------R 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958749229 535 VLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSL 594
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
405-591 |
7.77e-17 |
|
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: 79.85 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLA-TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT-----------KPERGKLFY 472
Cdd:cd03244 3 IEFKNVSLRyRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiglHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 473 VPQRPYMTLGTLRDQvIYPDGKEdqkkkgiSDQVLKGYLDNVQL-GHILEREGGWDS-VQDWMDVLSGGEKQRMAMARLF 550
Cdd:cd03244 83 IPQDPVLFSGTIRSN-LDPFGEY-------SDEELWQALERVGLkEFVESLPGGLDTvVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958749229 551 YHKPQFAILDECTSavSVDVE------DYIYSHCRkvGITLFTVSHR 591
Cdd:cd03244 155 LRKSKILVLDEATA--SVDPEtdaliqKTIREAFK--DCTVLTIAHR 197
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
405-606 |
1.19e-16 |
|
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: 79.84 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLA-TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGH---LTKPE--RGKLFY 472
Cdd:cd03252 1 ITFEHVRFRyKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVpengrvLVDGHdlaLADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 473 VPQRPYMTLGTLRDQVIYPDGKEDQKKKgISDQVLKGYLDnvqlgHILEREGGWDSVQDWMDV-LSGGEKQRMAMARLFY 551
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERV-IEAAKLAGAHD-----FISELPEGYDTIVGEQGAgLSGGQRQRIAIARALI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749229 552 HKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG 606
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
405-594 |
1.62e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.23 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPN-GDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT-----------KPERGKLF 471
Cdd:TIGR00958 479 IEFQDVSFSYPNrPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgvplvqydhHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 472 YVPQRPYMTLGTLRDQVIYpdGKEDQKKKGISDQVLKGYLDNVqlghILEREGGWDSVQDWMDV-LSGGEKQRMAMARLF 550
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAY--GLTDTPDEEIMAAAKAANAHDF----IMEFPNGYDTEVGEKGSqLSGGQKQRIAIARAL 632
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958749229 551 YHKPQFAILDECTSAVSVDVEDYIY-SHCRKvGITLFTVSHRKSL 594
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAECEQLLQeSRSRA-SRTVLLIAHRLST 676
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
406-605 |
2.48e-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: 77.89 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 406 KFDHVPLATPNGD-ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFG---------GHLTKPE-RGKLFYV 473
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnGLLGPTSGevlvdgkdlTKLSLKElRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 474 PQRPymtlgtlRDQVIYPDGKED--------QKKKGISDQVLKGYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMA 545
Cdd:cd03225 81 FQNP-------DDQFFGPTVEEEvafglenlGLPEEEIEERVEEALELVGLEGLRDR-----SPFT----LSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958749229 546 MARLFYHKPQFAILDECTSavSVDvedyiYSHCRKV----------GITLFTVSHRKSLWKHH-EYYLHMD 605
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTA--GLD-----PAGRRELlellkklkaeGKTIIIVTHDLDLLLELaDRVIVLE 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
416-590 |
4.59e-16 |
|
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: 77.61 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGhltKPERGKLFY---------------------VP 474
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG---APDEGEVLLdgkdiydldvdvlelrrrvgmVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 475 QRPYMTLGTLRDQVIYPD---GKedQKKKGISDQVLKGyldnvqlghiLEREGGWDSVQDWMDV--LSGGEKQRMAMARL 549
Cdd:cd03260 88 QKPNPFPGSIYDNVAYGLrlhGI--KLKEELDERVEEA----------LRKAALWDEVKDRLHAlgLSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958749229 550 FYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLftVSH 590
Cdd:cd03260 156 LANEPEVLLLDEPTSALdpisTAKIEELIAELKKEYTIVI--VTH 198
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
405-593 |
5.62e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 77.58 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPN--GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGHLTKPE-----RGK 469
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptsGEI--LLDGVDIRDLnlrwlRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 470 LFYVPQRPYMTLGTLRDQVIY--PDGKEDQ-----KKKGISDQVLK---GYldNVQLGhilerEGGwdsVQdwmdvLSGG 539
Cdd:cd03249 79 IGLVSQEPVLFDGTIAENIRYgkPDATDEEveeaaKKANIHDFIMSlpdGY--DTLVG-----ERG---SQ-----LSGG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749229 540 EKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKS 593
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAHRLS 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
417-561 |
6.53e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 417 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELwPLFGGHLTKPERGKLFYVPQRPYMTLG-TLRDQVIYPDGK 494
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILaGEL-EPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLDGDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 495 EDQKKK---------GISDQVLKGYLDnvqLGHILEREGGWD--------------SVQDW---MDVLSGGEKQRMAMAR 548
Cdd:COG0488 89 LRALEAeleeleaklAEPDEDLERLAE---LQEEFEALGGWEaearaeeilsglgfPEEDLdrpVSELSGGWRRRVALAR 165
|
170
....*....|...
gi 1958749229 549 LFYHKPQFAILDE 561
Cdd:COG0488 166 ALLSEPDLLLLDE 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
422-590 |
8.35e-16 |
|
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: 77.54 E-value: 8.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 422 QDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGHLTKPERGKLFY-----VPQRPYMTL---GTLR 485
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALaglerpwsGEV--TFDGRPVTRRRRKAFRrrvqmVFQDPYASLhprHTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 486 DQVIYPdgKEDQKKKGISDQVLKGyLDNVQLG-HILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 564
Cdd:COG1124 100 RILAEP--LRIHGLPDREERIAEL-LEQVGLPpSFLDR---------YPHQLSGGQRQRVAIARALILEPELLLLDEPTS 167
|
170 180 190
....*....|....*....|....*....|
gi 1958749229 565 A--VSVDVE--DYIYSHCRKVGITLFTVSH 590
Cdd:COG1124 168 AldVSVQAEilNLLKDLREERGLTYLFVSH 197
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
387-591 |
2.41e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 387 QASPLI--PGAGEIINADNIIKFDHVPLATPNG-DILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELw 455
Cdd:PRK11160 319 EQKPEVtfPTTSTAAADQVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtrawdpqqGEI- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 456 pLFGGHLTK--PE---RGKLFYVPQRPYMTLGTLRDQVIYpdgkedqKKKGISDQVLKGYLDNVQLGHILEREGGWDSvq 530
Cdd:PRK11160 398 -LLNGQPIAdySEaalRQAISVVSQRVHLFSATLRDNLLL-------AAPNASDEALIEVLQQVGLEKLLEDDKGLNA-- 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749229 531 dWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYS----HCRkvGITLFTVSHR 591
Cdd:PRK11160 468 -WLGeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILEllaeHAQ--NKTVLMITHR 533
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
405-593 |
3.36e-15 |
|
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: 75.34 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT-----------KPERGKLFY 472
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 473 VPQRPYMTLGTLRDQVIYpdGKEDQKKKGISDQVLKGYLDNVqlghILEREGGWDSVQDWMDV-LSGGEKQRMAMARLFY 551
Cdd:cd03251 81 VSQDVFLFNDTVAENIAY--GRPGATREEVEEAARAANAHEF----IMELPEGYDTVIGERGVkLSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958749229 552 HKPQFAILDECTSAVSVDVEDYIYSHCRK--VGITLFTVSHRKS 593
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERlmKNRTTFVIAHRLS 198
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
334-591 |
3.72e-15 |
|
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: 78.56 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 334 QALGRIVLAGREMTRLAGFTARITELMqvlkdlnhgkyertmvsqqdkGIEGAQASPLIPGAGEIINADNIIKFDHVPLA 413
Cdd:TIGR02868 285 EAFAALPAAAQQLTRVRAAAERIVEVL---------------------DAAGPVAEGSAPAAGAVGLGKPTLELRDLSAG 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 414 TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT-----------KPERGKLFYVPQRPYMTLG 482
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvssldqDEVRRRVSVCAQDAHLFDT 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 483 TLRDQVIYpdGKEDqkkkgISDQVLKGYLDNVQLG-HILEREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILD 560
Cdd:TIGR02868 424 TVRENLRL--ARPD-----ATDEELWAALERVGLAdWLRALPDGLDTvLGEGGARLSGGERQRLALARALLADAPILLLD 496
|
250 260 270
....*....|....*....|....*....|...
gi 1958749229 561 ECTSAVSVDVEDYIYSHCRKV--GITLFTVSHR 591
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAAlsGRTVVLITHH 529
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
420-565 |
3.94e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 75.54 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGHLT--KPE-----RGKLfyvPQRPYMTLG-TL 484
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELTPssgevrLNGRPLAawSPWelarrRAVL---PQHSSLAFPfTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 485 RdQVI----YPDGKEDQKKKGISDQVlkgyLDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMAMARLF-------YHK 553
Cdd:COG4559 93 E-EVValgrAPHGSSAAQDRQIVREA----LALVGLAHLAGR-----SYQT----LSGGEQQRVQLARVLaqlwepvDGG 158
|
170
....*....|..
gi 1958749229 554 PQFAILDECTSA 565
Cdd:COG4559 159 PRWLFLDEPTSA 170
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
405-607 |
4.68e-15 |
|
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: 74.45 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILIQ---DLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT--------KPERGKLF-- 471
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdiskLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 472 -----YVPQR----PYMTLgtlRDQVIYPDGKEDQKKKGISDQVLKgYLDNVQLGHILEREGGWdsvqdwmdvLSGGEKQ 542
Cdd:cd03255 81 rrhigFVFQSfnllPDLTA---LENVELPLLLAGVPKKERRERAEE-LLERVGLGDRLNHYPSE---------LSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 543 RMAMARLFYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHM-DGR 607
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELrDGK 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
405-590 |
4.96e-15 |
|
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: 74.68 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGHLTKPERGKLF----- 471
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsGEV--LVDGKDITKKNLRELrrkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 472 YVPQRPymtlgtlRDQVIYPDGKED---------QKKKGISDQVLKgYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQ 542
Cdd:COG1122 79 LVFQNP-------DDQLFAPTVEEDvafgpenlgLPREEIRERVEE-ALELVGLEHLADR-----PPHE----LSGGQKQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958749229 543 RMAMARLFYHKPQFAILDECTSAV----SVDVEDYIYShCRKVGITLFTVSH 590
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLdprgRRELLELLKR-LNKEGKTVIIVTH 192
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
405-590 |
6.19e-15 |
|
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: 74.05 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDIL---IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT---------KPERGklfY 472
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgpGPDRG---Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 473 VPQR----PYMtlgTLRDQVIYPDGKEDQKKKGISDQVLKgYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMAR 548
Cdd:cd03293 78 VFQQdallPWL---TVLDNVALGLELQGVPKAEARERAEE-LLELVGLSGFENA---------YPHQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958749229 549 LFYHKPQFAILDECTSAVSV----DVEDYIYSHCRKVGITLFTVSH 590
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTH 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
408-594 |
8.97e-15 |
|
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: 77.48 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 408 DHVPLATPNGDI---------------LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG----------HL 462
Cdd:COG4618 320 ERMPLPRPKGRLsvenltvvppgskrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvrldgadlsQW 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 463 TKPERGKLF-YVPQRPymTL--GTLRdQVI--YPDGKEDQ-----KKKGISDQVLK---GYldNVQLGhilerEGGwdsv 529
Cdd:COG4618 400 DREELGRHIgYLPQDV--ELfdGTIA-ENIarFGDADPEKvvaaaKLAGVHEMILRlpdGY--DTRIG-----EGG---- 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958749229 530 qdwmDVLSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVE------DYIySHCRKVGITLFTVSHRKSL 594
Cdd:COG4618 466 ----ARLSGGQRQRIGLARALYGDPRLVVLDEPNS--NLDDEgeaalaAAI-RALKARGATVVVITHRPSL 529
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
403-590 |
9.42e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 403 NIIKFDHVPLATPNGDILiQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLfGGHLTKPERGKLFYVPQR----P 477
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAPD-EGVIKRNGKLRIGYVPQKlyldT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 478 YMTLGTLRDQVIYPdgkedqkkkGISDQVLKGYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFA 557
Cdd:PRK09544 81 TLPLTVNRFLRLRP---------GTKKEDILPALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958749229 558 ILDECTSAVSVD----VEDYIYSHCRKVGITLFTVSH 590
Cdd:PRK09544 143 VLDEPTQGVDVNgqvaLYDLIDQLRRELDCAVLMVSH 179
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
402-591 |
3.98e-14 |
|
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: 75.32 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 402 DNIIKFDHVPLATPNGDI-LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP---------LFGGH----LTKPER 467
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRdlleLSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 468 GKLF-YVPQRPYMTL--GTLRDQVIYPDGKEDQKKKGISDQVLKgYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRM 544
Cdd:COG1123 82 GRRIgMVFQDPMTQLnpVTVGDQIAEALENLGLSRAEARARVLE-LLEAVGLERRLDR---------YPHQLSGGQRQRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958749229 545 AMARLFYHKPQFAILDECTSAVSVDVEDYIYSH----CRKVGITLFTVSHR 591
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLlrelQRERGTTVLLITHD 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
417-561 |
4.00e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 417 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGHLTKPERGKLFYVPQ-RPYMTLG-TLRDQV--IYP 491
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPD-SGTVKLGETVKIGYFDQhQEELDPDkTVLDELrdGAP 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749229 492 DGKEdqkkkgisdQVLKGYLdnvqlghilereGGW----DSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDE 561
Cdd:COG0488 406 GGTE---------QEVRGYL------------GRFlfsgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
399-569 |
9.27e-14 |
|
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: 71.43 E-value: 9.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 399 INADNIIK-FDHVPLatpngdilIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGHLTKPE---R 467
Cdd:COG4555 2 IEVENLSKkYGKVPA--------LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLKPdsgsilIDGEDVRKEPreaR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 468 GKLFYVPQRPYMTLG-TLRDQV-----IYPDGKEDQKKKgISDqvlkgYLDNVQLGHILEReggwdSVQDwmdvLSGGEK 541
Cdd:COG4555 74 RQIGVLPDERGLYDRlTVRENIryfaeLYGLFDEELKKR-IEE-----LIELLGLEEFLDR-----RVGE----LSTGMK 138
|
170 180
....*....|....*....|....*...
gi 1958749229 542 QRMAMARLFYHKPQFAILDECTSAVSVD 569
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVM 166
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
416-590 |
9.50e-14 |
|
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: 70.63 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHL---------TKPERGKLFYVPQR----PYMtlg 482
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtgVPPERRNIGMVFQDyalfPHL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 483 TLRDQVIYPDGKEDQKKKGISDQVLKgYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDEC 562
Cdd:cd03259 88 TVAENIAFGLKLRGVPKAEIRARVRE-LLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190
....*....|....*....|....*....|..
gi 1958749229 563 TSAVSVDVEDYIYSH----CRKVGITLFTVSH 590
Cdd:cd03259 158 LSALDAKLREELREElkelQRELGITTIYVTH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
382-590 |
1.35e-13 |
|
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: 73.40 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 382 GIEGAQASPLIPGAGEIINADNIIKfdHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GE 453
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLEVRNLSK--RYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLlgllrptsGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 454 LwpLFGGH-LTKPERGKLF-------YVPQRPYMTL---GTLRDQVIYP-DGKEDQKKKGISDQVLKgYLDNVQLG-HIL 520
Cdd:COG1123 322 I--LFDGKdLTKLSRRSLRelrrrvqMVFQDPYSSLnprMTVGDIIAEPlRLHGLLSRAERRERVAE-LLERVGLPpDLA 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749229 521 ER---EggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSA--VSV--DVEDYIYSHCRKVGITLFTVSH 590
Cdd:COG1123 399 DRyphE------------LSGGQRQRVAIARALALEPKLLILDEPTSAldVSVqaQILNLLRDLQRELGLTYLFISH 463
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
412-605 |
1.39e-13 |
|
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: 74.01 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 412 LATPNGDILIQDLSFEVRSGANVL--------------ICGPNGCGKSSLFRVL--------GELwpLFGGHLTK----- 464
Cdd:TIGR01193 467 LNNLNGDIVINDVSYSYGYGSNILsdisltikmnskttIVGMSGSGKSTLAKLLvgffqarsGEI--LLNGFSLKdidrh 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 465 PERGKLFYVPQRPYMTLGTLRDQVIY---PDGKEDQKKKGISDQVLKGYLDNVQLGH--ILEREGGwdsvqdwmdVLSGG 539
Cdd:TIGR01193 545 TLRQFINYLPQEPYIFSGSILENLLLgakENVSQDEIWAACEIAEIKDDIENMPLGYqtELSEEGS---------SISGG 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749229 540 EKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKVG-ITLFTVSHRKSLWKHHEYYLHMD 605
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
399-611 |
1.41e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 399 INADNIIKFdhvplaTPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-------GELwpLFGGH----LTKPE- 466
Cdd:PRK11174 350 IEAEDLEIL------SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpyqGSL--KINGIelreLDPESw 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 467 RGKLFYVPQRPYMTLGTLRDQVIYpdGKEDqkkkgISDQVLKGYLDNVQLGHILER-EGGWDS-VQDWMDVLSGGEKQRM 544
Cdd:PRK11174 422 RKHLSWVGQNPQLPHGTLRDNVLL--GNPD-----ASDEQLQQALENAWVSEFLPLlPQGLDTpIGDQAAGLSVGQAQRL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749229 545 AMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG-----RGNYE 611
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQLEDLAQWDQIWVMQDgqivqQGDYA 568
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
416-590 |
1.42e-13 |
|
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: 69.14 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELwplfgghlTKPERGKLFyvpqrpymtlgtLRDQVIYPDGKE 495
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL--------EEPDSGSIL------------IDGEDLTDLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 496 DQKKKGISDQVLKGY--------LDNVQLGhilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSA-- 565
Cdd:cd03229 71 LPPLRRRIGMVFQDFalfphltvLENIALG------------------LSGGQQQRVALARALAMDPDVLLLDEPTSAld 132
|
170 180
....*....|....*....|....*..
gi 1958749229 566 --VSVDVEDYIYSHCRKVGITLFTVSH 590
Cdd:cd03229 133 piTRREVRALLKSLQAQLGITVVLVTH 159
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
386-583 |
1.64e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 386 AQASPLIPGAGEIINADNIIKFDhVPLATPNgdilIQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGHLTK 464
Cdd:PLN03232 603 AQNPPLQPGAPAISIKNGYFSWD-SKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 465 peRGKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKK-KGISDQVLKGYLDnVQLGHILErEGGWDSVQdwmdvLSGGEKQR 543
Cdd:PLN03232 678 --RGSVAYVPQVSWIFNATVRENILFGSDFESERYwRAIDVTALQHDLD-LLPGRDLT-EIGERGVN-----ISGGQKQR 748
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958749229 544 MAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKVGI 583
Cdd:PLN03232 749 VSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDEL 788
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
401-561 |
1.66e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 70.89 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 401 ADNIIKFDHVPLA--TPNGDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGHLTKP--ER 467
Cdd:COG1116 4 AAPALELRGVSKRfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptsGEVL-VDGKPVTGPgpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 468 GklfYVPQR----PYMTLgtlRDQVIYPDGKEDQKKKGISDQVLKgYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQR 543
Cdd:COG1116 83 G---VVFQEpallPWLTV---LDNVALGLELRGVPKAERRERARE-LLELVGLAGFEDA---------YPHQLSGGMRQR 146
|
170
....*....|....*...
gi 1958749229 544 MAMARLFYHKPQFAILDE 561
Cdd:COG1116 147 VAIARALANDPEVLLMDE 164
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
421-590 |
3.06e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 69.30 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGH----LTKPERGKL------FyVPQR----PY 478
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrptsGEVL--IDGQdissLSERELARLrrrhigF-VFQFfnllPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 479 MTLgtlRDQVIYP------DGKEDQKKkgisdqvLKGYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMARL 549
Cdd:COG1136 101 LTA---LENVALPlllagvSRKERRER-------ARELLERVGLGDRLDHrpsQ------------LSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958749229 550 FYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSH 590
Cdd:COG1136 159 LVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTH 203
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
393-607 |
4.49e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.92 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 393 PGAGEIINADNIIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT--------- 463
Cdd:PRK13657 323 PGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtv 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 464 --KPERGKLFYVPQRPYMTLGTLRD--QViypdGKEDQkkkgiSDQVLKGYLDNVQ-LGHILEREGGWDS-VQDWMDVLS 537
Cdd:PRK13657 403 trASLRRNIAVVFQDAGLFNRSIEDniRV----GRPDA-----TDEEMRAAAERAQaHDFIERKPDGYDTvVGERGRQLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 538 GGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEdyiyshcRKV---------GITLFTVSHRKSLWKHHEYYLHMD-GR 607
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETE-------AKVkaaldelmkGRTTFIIAHRLSTVRNADRILVFDnGR 546
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
404-590 |
4.79e-13 |
|
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: 68.69 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 404 IIKFDHVPLATPNGDI---LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------------GELWPLFGGHLTKPE 466
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsgsiifdGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 467 RGKLFYVPQRPYMTLG---TLRDQVIYP-----DGKEDQKKKGISDQVLKGYLDNVQLGHILEREggwdsvqdwmdvLSG 538
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprmTIGEQIAEPlrihgKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE------------LSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749229 539 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSH----CRKVGITLFTVSH 590
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkklQEELGLTLLFITH 204
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
416-585 |
4.85e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPERGKLF--------YVPQRPYM--TLgTLR 485
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaeachYLGHRNAMkpAL-TVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 486 DQVIYPDGKEDQKKKGISDQvlkgyLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLF-YHKPQFaILDECTS 564
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAAA-----LEAVGLAPLAHLPFG---------YLSAGQKRRVALARLLvSNRPIW-ILDEPTA 156
|
170 180
....*....|....*....|....*
gi 1958749229 565 AVSVD----VEDYIYSHCRKVGITL 585
Cdd:PRK13539 157 ALDAAavalFAELIRAHLAQGGIVI 181
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
421-590 |
7.43e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 68.55 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANV-LIcGPNGCGKSSLFRVL--------GELWpLFGGHLTKPE---RGKLFYVPQRP--YMTLgTLRD 486
Cdd:COG1131 16 LDGVSLTVEPGEIFgLL-GPNGAGKTTTIRMLlgllrptsGEVR-VLGEDVARDPaevRRRIGYVPQEPalYPDL-TVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 487 QV-----IYPDGKEDQKKKgiSDQVLkgylDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDE 561
Cdd:COG1131 93 NLrffarLYGLPRKEARER--IDELL----ELFGLTDAADR---------KVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1958749229 562 CTSAvsVDVE------DYIYSHCRKvGITLFTVSH 590
Cdd:COG1131 158 PTSG--LDPEarrelwELLRELAAE-GKTVLLSTH 189
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
89-605 |
7.48e-13 |
|
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: 71.29 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 89 RYLFNFIAAMpLISLVNNFLKYGlnelklcFRVRLtrylYEEYLQA----FTYYKMGNLDNRIanpdqllTQDVEKFCNS 164
Cdd:TIGR02203 67 RGICSFVSTY-LLSWVSNKVVRD-------IRVRM----FEKLLGLpvsfFDRQPTGTLLSRI-------TFDSEQVASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 165 VVDLYSNLSKP-----FLDIVL--YIFKLTSAIGAQGPASMmaylLVSGLFLTRLRRPIGKMtimeQKYEGEYRFVNSRL 237
Cdd:TIGR02203 128 ATDAFIVLVREtltviGLFIVLlyYSWQLTLIVVVMLPVLS----ILMRRVSKRLRRISKEI----QNSMGQVTTVAEET 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 238 ITNSEEIAFYNGNKREKQTIHSVFRKLVehlhnfiffRFSMgfidsiiakyiatvvgylvvsrpflDLAHPRHLHSTHSE 317
Cdd:TIGR02203 200 LQGYRVVKLFGGQAYETRRFDAVSNRNR---------RLAM-------------------------KMTSAGSISSPITQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 318 LLEDYYQSGRMLLRMSQALGRIVLAGremtrlaGFTARITELMQVLKDLNHgkyeRTMVSQQ-DKGIEGAQA------SP 390
Cdd:TIGR02203 246 LIASLALAVVLFIALFQAQAGSLTAG-------DFTAFITAMIALIRPLKS----LTNVNAPmQRGLAAAESlftlldSP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 391 LIPGAG--EIINADNIIKFDHVPLATPNGDI-LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFG 459
Cdd:TIGR02203 315 PEKDTGtrAIERARGDVEFRNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIprfyepdsGQI--LLD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 460 GH-----LTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGKE---DQKKKGISDQVLKGYLDNVQLGhiLEREGGWDSVQd 531
Cdd:TIGR02203 393 GHdladyTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQadrAEIERALAAAYAQDFVDKLPLG--LDTPIGENGVL- 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749229 532 wmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMD 605
Cdd:TIGR02203 470 ----LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVMD 541
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
421-590 |
7.77e-13 |
|
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: 67.04 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGHLTKPE---RGKLFYVPQRPYmtlgtlrdqvI 489
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlgllkpdsGEIK-VLGKDIKKEPeevKRRIGYLPEEPS----------L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 490 YPDgkedqkkkgisdqvLKGYlDNVQlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAV--- 566
Cdd:cd03230 85 YEN--------------LTVR-ENLK--------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLdpe 129
|
170 180
....*....|....*....|....*
gi 1958749229 567 -SVDVEDYIYSHcRKVGITLFTVSH 590
Cdd:cd03230 130 sRREFWELLREL-KKEGKTILLSSH 153
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
405-590 |
1.38e-12 |
|
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: 65.55 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATpNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPERGKLFYVPQrpymtlgtl 484
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 485 rdqviypdgkedqkkkgisdqvlkgyldnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTS 564
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|
gi 1958749229 565 ---AVSVD-VEDYIYSHcrkvGITLFTVSH 590
Cdd:cd03221 100 hldLESIEaLEEALKEY----PGTVILVSH 125
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
420-565 |
1.63e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.87 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFG---GHLTKPERGKLFYV-PQRPYMTLGTLRDQV 488
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPdsgevrLNGrplADWSPAELARRRAVlPQHSSLSFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 489 I----YPDGKEDQKKKGISDQVlkgyLDNVQLGHILEReggwdSVQdwmdVLSGGEKQRMAMARLF------YHKPQFAI 558
Cdd:PRK13548 97 VamgrAPHGLSRAEDDALVAAA----LAQVDLAHLAGR-----DYP----QLSGGEQQRVQLARVLaqlwepDGPPRWLL 163
|
....*..
gi 1958749229 559 LDECTSA 565
Cdd:PRK13548 164 LDEPTSA 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
404-563 |
1.86e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 67.00 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 404 IIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGHLTKPERGKLfyvpqr 476
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLyGEERPtsgqvlVNGQDLSRLKRREI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 477 PYmtlgtLRDQ--VIYPDGK--ED---------------QKKKGISDQVLKgYLDNVQLGHILEReggwdsvqdwM-DVL 536
Cdd:COG2884 75 PY-----LRRRigVVFQDFRllPDrtvyenvalplrvtgKSRKEIRRRVRE-VLDLVGLSDKAKA----------LpHEL 138
|
170 180
....*....|....*....|....*..
gi 1958749229 537 SGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:COG2884 139 SGGEQQRVAIARALVNRPELLLADEPT 165
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
421-590 |
2.67e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.40 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHL---TKPergklfyvpqrpymtLGTLRD--QVIYPDGKE 495
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagTAP---------------LAEAREdtRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 496 DQKKKGIsdqvlkgylDNVQLG----------HILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSA 565
Cdd:PRK11247 93 LPWKKVI---------DNVGLGlkgqwrdaalQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180
....*....|....*....|....*....
gi 1958749229 566 VS----VDVEDYIYSHCRKVGITLFTVSH 590
Cdd:PRK11247 164 LDaltrIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
415-566 |
4.27e-12 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 65.14 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 415 PNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGHLTKPERGKLFYVPQRPYMTLGTLRDQV 488
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLnGLLRPqsgavLIDGEPLDYSRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 489 IYPDGKED----QKKKGISDQVLKGYLDN----VQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILD 560
Cdd:TIGR01166 82 FAADVDQDvafgPLNLGLSEAEVERRVREaltaVGASGLRERP---------THCLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
....*.
gi 1958749229 561 ECTSAV 566
Cdd:TIGR01166 153 EPTAGL 158
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
417-590 |
5.53e-12 |
|
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: 65.82 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 417 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGHLT--KPERGKLFYVPQR----PYMTLgt 483
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFIKPdsgkilLNGKDITnlPPEKRDISYVPQNyalfPHMTV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 484 lRDQVIYPDGKEDQKKKGISDQVLKgYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:cd03299 89 -YKNIAYGLKKRKVDKKEIERKVLE-IAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|.
gi 1958749229 564 SAVSVDVEDYIYSHCRKV----GITLFTVSH 590
Cdd:cd03299 158 SALDVRTKEKLREELKKIrkefGVTVLHVTH 188
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
420-590 |
5.70e-12 |
|
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: 65.36 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGHLTKPE--RGKLFYVPQRPYMTLG--TLRDQVI 489
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKessgsiLLNGKPIKAKerRKSIGYVMQDVDYQLFtdSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 490 YPDgKEDQKKKGISDQVLKGY-LDNVQLGHILEreggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVsv 568
Cdd:cd03226 95 LGL-KELDAGNEQAETVLKDLdLYALKERHPLS--------------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGL-- 157
|
170 180 190
....*....|....*....|....*....|
gi 1958749229 569 dveDY--------IYSHCRKVGITLFTVSH 590
Cdd:cd03226 158 ---DYknmervgeLIRELAAQGKAVIVITH 184
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
405-590 |
6.29e-12 |
|
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: 65.67 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELwplfgghlTKPERGKLFY----VPQRPYMT 480
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL--------VEPTSGSVLIdgtdINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 481 LGTLRDQV--IYPDGkedqkkkGISDQ------VLKGYLDNVQLG----------------HILEREGGWDSVQDWMDVL 536
Cdd:cd03256 73 LRQLRRQIgmIFQQF-------NLIERlsvlenVLSGRLGRRSTWrslfglfpkeekqralAALERVGLLDKAYQRADQL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749229 537 SGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSH 590
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLH 203
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
402-564 |
6.46e-12 |
|
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: 65.88 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 402 DNIIKFDHVPLATpNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGHLT---KpERGK--LF---- 471
Cdd:COG1119 1 DPLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLPPTYGNDVRlfgE-RRGGedVWelrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 472 ---YV-P--QRPYMTLGTLRDQVI---------YPDGKEDQKKKgiSDQVlkgyLDNVQLGHILEREggwdsvqdwMDVL 536
Cdd:COG1119 79 rigLVsPalQLRFPRDETVLDVVLsgffdsiglYREPTDEQRER--AREL----LELLGLAHLADRP---------FGTL 143
|
170 180
....*....|....*....|....*...
gi 1958749229 537 SGGEKQRMAMARLFYHKPQFAILDECTS 564
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTA 171
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
402-590 |
1.03e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.98 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 402 DNIIKFDHVPLATPNGDI-LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP---------LFGGHLTKPE---- 466
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLLPddnpnskitVDGITLTAKTvwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 467 RGKLFYVPQRP--YMTLGTLRDQVIYpdGKEDqkkKGISDQVLKGYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRM 544
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAF--GLEN---RAVPRPEMIKIVRDV-----LADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958749229 545 AMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV----GITLFTVSH 590
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
373-577 |
1.10e-11 |
|
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: 68.43 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 373 RTMVSQQDKGIEGAQASPLIPGAGEIINADNIiKFDHVPLATPNgdilIQDLSFEVRSGANVLICGPNGCGKSSLFR-VL 451
Cdd:TIGR00957 611 RIFLSHEELEPDSIERRTIKPGEGNSITVHNA-TFTWARDLPPT----LNGITFSIPEGALVAVVGQVGCGKSSLLSaLL 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 452 GELWPLfGGHLTKpeRGKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKKKGISD--------QVLKGYlDNVQLGhilerE 523
Cdd:TIGR00957 686 AEMDKV-EGHVHM--KGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEacallpdlEILPSG-DRTEIG-----E 756
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958749229 524 GGWDsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSH 577
Cdd:TIGR00957 757 KGVN--------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
419-590 |
1.36e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 419 ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GelwplfgghLTKPERGKLFYVPQRpymtLGTLRD----QVIY--- 490
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILaG---------LARPDAGEVLWQGEP----IRRQRDeyhqDLLYlgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 491 -PdgkedqkkkGISD-----------QVLKGYLDNVQLGHILEREGgwdsVQDWMDV----LSGGEKQRMAMARLFYHKP 554
Cdd:PRK13538 82 qP---------GIKTeltalenlrfyQRLHGPGDDEALWEALAQVG----LAGFEDVpvrqLSAGQQRRVALARLWLTRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958749229 555 QFAILDECTSAVSV----DVEDYIYSHCRKVGITLFTvSH 590
Cdd:PRK13538 149 PLWILDEPFTAIDKqgvaRLEALLAQHAEQGGMVILT-TH 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
420-594 |
4.98e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplFGGHLTKPERGKlFYVPQRPYMTLGTLRDQvIYPDGKEDQKK 499
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL------AGALKGTPVAGC-VDVPDNQFGREASLIDA-IGRKGDFKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 500 K-----GISDQVLkgYLDNVqlghilereggwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEdYI 574
Cdd:COG2401 117 EllnavGLSDAVL--WLRRF-------------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA-KR 174
|
170 180
....*....|....*....|....*
gi 1958749229 575 YSH-----CRKVGITLFTVSHRKSL 594
Cdd:COG2401 175 VARnlqklARRAGITLVVATHHYDV 199
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
386-565 |
6.74e-11 |
|
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: 65.23 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 386 AQASPLIPGAGEIinadniiKFDHVPLA-TPNGDILiQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwp 456
Cdd:COG5265 346 PDAPPLVVGGGEV-------RFENVSFGyDPERPIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtsGRI-- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 457 LFGGH----LTKPE-RGKLFYVPQRPYMTLGTLRDQVIY--PDGKEDQKKKGIsdqvlkgylDNVQLGHILER-EGGWDS 528
Cdd:COG5265 416 LIDGQdirdVTQASlRAAIGIVPQDTVLFNDTIAYNIAYgrPDASEEEVEAAA---------RAAQIHDFIESlPDGYDT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958749229 529 VqdwmdV------LSGGEKQRMAMARLFYHKPQFAILDECTSA 565
Cdd:COG5265 487 R-----VgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
405-574 |
8.50e-11 |
|
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: 61.83 E-value: 8.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILiQDLSFEVRSGANVLIcGPNGCGKSSLFRVLGELWPLFGGHLT--------KPE--RGKLFYVP 474
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQklRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 475 Q--RPYMTLgTLRDQVIYPdgkedQKKKGISDQVLKGYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRMAMARLFYH 552
Cdd:cd03264 79 QefGVYPNF-TVREFLDYI-----AWLKGIPSKEVKARVDEV-----LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180
....*....|....*....|..
gi 1958749229 553 KPQFAILDECTsaVSVDVEDYI 574
Cdd:cd03264 148 DPSILIVDEPT--AGLDPEERI 167
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
421-606 |
1.06e-10 |
|
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: 61.96 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLF-RVLGELWPLFG--------------GHLTKPERGKLFYVPQRPYMTLGTLR 485
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwsnknesepsfEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 486 DQVIYPDGKEDQKKKGISDQV-LKGYLDNVQLGHilEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTS 564
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACsLQPDIDLLPFGD--QTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958749229 565 AVSVDVEDyiysHCRKVGI---------TLFTVSHRKSLWKHHEYYLHM-DG 606
Cdd:cd03290 170 ALDIHLSD----HLMQEGIlkflqddkrTLVLVTHKLQYLPHADWIIAMkDG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
415-591 |
1.07e-10 |
|
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: 61.66 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 415 PNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT-----------KPERGKLFYVPQRPYMTLGT 483
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidistiplEDLRSSLTIIPQDPTLFSGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 484 LRDQV-IYpdgkedqkkkgisdqvlkGYLDNVQLGHILE-REGGwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILDE 561
Cdd:cd03369 98 IRSNLdPF------------------DEYSDEEIYGALRvSEGG--------LNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190
....*....|....*....|....*....|..
gi 1958749229 562 CTSAVSVDVEDYIYSHCRK--VGITLFTVSHR 591
Cdd:cd03369 152 ATASIDYATDALIQKTIREefTNSTILTIAHR 183
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
417-590 |
1.42e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.97 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 417 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPlfgghltkPERGKLFYVPQRPYMTLGTLRDQVIYPdGKED 496
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP--------PLAGRVLLNGGPLDFQRDSIARGLLYL-GHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 497 QKKKGISdqvlkgYLDNVQLGH-ILEREGGWDSVQDwMDV----------LSGGEKQRMAMARLFYHKPQFAILDECTSA 565
Cdd:cd03231 83 GIKTTLS------VLENLRFWHaDHSDEQVEEALAR-VGLngfedrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*....
gi 1958749229 566 V---SVD-VEDYIYSHCRKVGITLFTVSH 590
Cdd:cd03231 156 LdkaGVArFAEAMAGHCARGGMVVLTTHQ 184
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
423-590 |
1.53e-10 |
|
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: 61.16 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 423 DLSFEVrSGANVLICGPNGCGKSSLFRVLGELWPLFGGHL---------------TKPERGKLFYVPQR----PYMTLgt 483
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVFQQyalfPHLNV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 484 lRDQVIYPDGKEDQKKKGISDQVLkgyLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:cd03297 93 -RENLAFGLKRKRNREDRISVDEL---LDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|.
gi 1958749229 564 SAVSVDVEDYIYSHCRKV----GITLFTVSH 590
Cdd:cd03297 160 SALDRALRLQLLPELKQIkknlNIPVIFVTH 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
416-590 |
1.92e-10 |
|
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: 61.10 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGG----HLTKPERG--------KLFyvpq 475
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIagfetptsGEI--LLDGkditNLPPHKRPvntvfqnyALF---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 476 rPYMTLGtlrDQVIYPDGKEDQKKKGISDQVLKgYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQ 555
Cdd:cd03300 85 -PHLTVF---ENIAFGLRLKKLPKAEIKERVAE-ALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958749229 556 FAILDECTSAVSV----DVEDYIYSHCRKVGITLFTVSH 590
Cdd:cd03300 151 VLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTH 189
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
419-618 |
2.04e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.03 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 419 ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPlfgghltkpERgKLFYVPQRPYMTLGTLRDQVIY 490
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlsqfeiseGRVWA---------ER-SIAYVPQQAWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 491 PDgKEDQKKKGISDQVLKGYLDNVQLGHILEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDV 570
Cdd:PTZ00243 744 FD-EEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVN-----LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958749229 571 EDYIYSHC---RKVGITLFTVSHRKSLWKHHEYYLHMdGRGNYEFKKITED 618
Cdd:PTZ00243 818 GERVVEECflgALAGKTRVLATHQVHVVPRADYVVAL-GDGRVEFSGSSAD 867
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
421-590 |
2.60e-10 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 61.20 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGG----HLTKPERGKLFyVPQR----PYMTLGT- 483
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIaglerpdsGTIL--FGGedatDVPVQERNVGF-VFQHyalfRHMTVFDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 484 ----LRDQVIYPDGKEDQKKKGISDqvlkgYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAIL 559
Cdd:cd03296 95 vafgLRVKPRSERPPEAEIRAKVHE-----LLKLVQLDWLADR---------YPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1958749229 560 DECTSAVSVDVEDYIYSHCRK----VGITLFTVSH 590
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRlhdeLHVTTVFVTH 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
400-590 |
2.87e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.57 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 400 NADNIIKFDHVPLATPNGDIL-IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFG----GHLTKPE------R 467
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLnGLLLPEAGtitvGGMVLSEetvwdvR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 468 GKLFYVPQRP--YMTLGTLRDQVIYpdGKEDQkkkGIS-DQVLKGYLDNVQLGHIlereggwdsvQDWMD----VLSGGE 540
Cdd:PRK13635 81 RQVGMVFQNPdnQFVGATVQDDVAF--GLENI---GVPrEEMVERVDQALRQVGM----------EDFLNrephRLSGGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958749229 541 KQRMAMARLFYHKPQFAILDECTSAVS----VDVEDYIYSHCRKVGITLFTVSH 590
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
421-591 |
3.00e-10 |
|
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: 60.37 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWP-----LFGGHLTKPERGKLF-YVPQR----PYMtlgTLRDQVI 489
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRmILGIILPdsgevLFDGKPLDIAARNRIgYLPEErglyPKM---KVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 490 YPDGKEDQKKKGISDQVLKgYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDECTSA---V 566
Cdd:cd03269 93 YLAQLKGLKKEEARRRIDE-WLERLELSEYANKR---------VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGldpV 162
|
170 180
....*....|....*....|....*
gi 1958749229 567 SVDVEDYIYSHCRKVGITLFTVSHR 591
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTHQ 187
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
423-580 |
3.19e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 423 DLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGHLTKpeRGKLFYVPQRPYMTLGTLRDQVIY-PDGKEDQKKK 500
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI--RGTVAYVPQVSWIFNATVRDNILFgSPFDPERYER 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 501 GISDQVLKGYLDNVQLGHILE-REGGWDsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCR 579
Cdd:PLN03130 713 AIDVTALQHDLDLLPGGDLTEiGERGVN--------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCI 784
|
.
gi 1958749229 580 K 580
Cdd:PLN03130 785 K 785
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
423-590 |
3.40e-10 |
|
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: 62.05 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 423 DLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHL---------------TKPERGKLFYVPQR----PYMTLgt 483
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgifLPPEKRRIGYVFQEarlfPHLSV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 484 lRDQVIYPDGKEDQKKKGISDQVLkgyLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:TIGR02142 93 -RGNLRYGMKRARPSERRISFERV---IELLGIGHLLGRLPG---------RLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190
....*....|....*....|....*....|.
gi 1958749229 564 SAVSVDVEDYIYSHCRKV----GITLFTVSH 590
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLhaefGIPILYVSH 190
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
421-590 |
3.88e-10 |
|
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: 59.92 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT--KPERGKLFYVPQRpymtLGTLRD-QVIYPD--GKE 495
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdGKSYQKNIEALRR----IGALIEaPGFYPNltARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 496 D----QKKKGISDQVLKGYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD-- 569
Cdd:cd03268 92 NlrllARLLGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDgi 162
|
170 180
....*....|....*....|...
gi 1958749229 570 --VEDYIYSHcRKVGITLFTVSH 590
Cdd:cd03268 163 keLRELILSL-RDQGITVLISSH 184
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
420-590 |
6.09e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.44 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGhlTKPErGKLFYVPQRPY---MTLGTLRDQV-------- 488
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESE--VRVE-GRVEFFNQNIYerrVNLNRLRRQVsmvhpkpn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 489 IYPDGKEDQKKKGISdqvLKGYLDNVQLGHILEREGG----WDSVQDWMDV----LSGGEKQRMAMARLFYHKPQFAILD 560
Cdd:PRK14258 99 LFPMSVYDNVAYGVK---IVGWRPKLEIDDIVESALKdadlWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190
....*....|....*....|....*....|....
gi 1958749229 561 E-CTS---AVSVDVEDYIYSHCRKVGITLFTVSH 590
Cdd:PRK14258 176 EpCFGldpIASMKVESLIQSLRLRSELTMVIVSH 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
405-591 |
8.56e-10 |
|
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: 58.09 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGH----LTKPERGKLFYV 473
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLKPqqgeiTLDGVpvsdLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 474 PQRPYMTLGTLRDQViypdGKEdqkkkgisdqvlkgyldnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHK 553
Cdd:cd03247 81 NQRPYLFDTTLRNNL----GRR----------------------------------------FSGGERQRLALARILLQD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958749229 554 PQFAILDECTsaVSVDVE------DYIYSHCRkvGITLFTVSHR 591
Cdd:cd03247 117 APIVLLDEPT--VGLDPIterqllSLIFEVLK--DKTLIWITHH 156
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
394-578 |
1.08e-09 |
|
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: 59.87 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 394 GAGEIINADNIIKFDHVPL-ATPngdiLIQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGghlTKPERGKLF 471
Cdd:cd03291 29 NDRKHSSDDNNLFFSNLCLvGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPSEG---KIKHSGRIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 472 YVPQRPYMTLGTLRDQVIYPDGKEDQKKKGI------SDQVLK-GYLDNVQLGhilerEGGWdsvqdwmdVLSGGEKQRM 544
Cdd:cd03291 102 FSSQFSWIMPGTIKENIIFGVSYDEYRYKSVvkacqlEEDITKfPEKDNTVLG-----EGGI--------TLSGGQRARI 168
|
170 180 190
....*....|....*....|....*....|....
gi 1958749229 545 AMARLFYHKPQFAILDECTSAVSVDVEDYIYSHC 578
Cdd:cd03291 169 SLARAVYKDADLYLLDSPFGYLDVFTEKEIFESC 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
417-571 |
1.30e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 417 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRV-LGELWPLFG----GhlTKPE-------RGKLfyVPQRpymtlgTL 484
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQADSGrihcG--TKLEvayfdqhRAEL--DPEK------TV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 485 RDQViyPDGKEDQKKKGISDQVLkGYLdnvqlghilereggwdsvQDWM----------DVLSGGEKQRMAMARLFYHKP 554
Cdd:PRK11147 401 MDNL--AEGKQEVMVNGRPRHVL-GYL------------------QDFLfhpkramtpvKALSGGERNRLLLARLFLKPS 459
|
170
....*....|....*..
gi 1958749229 555 QFAILDECTSavSVDVE 571
Cdd:PRK11147 460 NLLILDEPTN--DLDVE 474
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
422-565 |
1.56e-09 |
|
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: 58.31 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 422 QDLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGHLTKPERGKLfyvpqrpymtlgTLRDQVIYPDGKE-DQKKK 500
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCI--------NLLEEPDSGTI------------IIDGLKLTDDKKNiNELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 501 GISdQVLKGY--------LDNVQLG-----------------HILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQ 555
Cdd:cd03262 77 KVG-MVFQQFnlfphltvLENITLApikvkgmskaeaeeralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170
....*....|
gi 1958749229 556 FAILDECTSA 565
Cdd:cd03262 156 VMLFDEPTSA 165
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
405-593 |
1.70e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLtkpergklfYVPQRPymtLGTL 484
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI---------RLDGRP---LSSL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 485 RDQVIypdgkedqkKKGIS----DQVL--KGYLDNVQLGHILEREGGWD---SVQ--DWM---------------DVLSG 538
Cdd:PRK10790 409 SHSVL---------RQGVAmvqqDPVVlaDTFLANVTLGRDISEEQVWQaleTVQlaELArslpdglytplgeqgNNLSV 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749229 539 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKS 593
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLS 536
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
400-578 |
2.66e-09 |
|
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: 60.69 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 400 NADNIIKFDHVPL-ATPngdiLIQDLSFEVRSGANVLICGPNGCGKSSLFRV-LGELWPLFGghlTKPERGKLFYVPQRP 477
Cdd:TIGR01271 424 NGDDGLFFSNFSLyVTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMiMGELEPSEG---KIKHSGRISFSPQTS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 478 YMTLGTLRDQVIYPDGKEDQKKKGI-------SDQVLKGYLDNVQLGhilerEGGWdsvqdwmdVLSGGEKQRMAMARLF 550
Cdd:TIGR01271 497 WIMPGTIKDNIIFGLSYDEYRYTSVikacqleEDIALFPEKDKTVLG-----EGGI--------TLSGGQRARISLARAV 563
|
170 180
....*....|....*....|....*...
gi 1958749229 551 YHKPQFAILDECTSAVSVDVEDYIYSHC 578
Cdd:TIGR01271 564 YKDADLYLLDSPFTHLDVVTEKEIFESC 591
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
423-591 |
2.68e-09 |
|
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: 56.28 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 423 DLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplFGGHltKPERGKLFyvpqrpymtlgtLRDQVIYPDGKEDQKKKGI 502
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKIL------SGLY--KPDSGEIL------------VDGKEVSFASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 503 SdqvlkgyldnvqlghilereggwdSV-QdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV 581
Cdd:cd03216 78 A------------------------MVyQ-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL 128
|
170
....*....|...
gi 1958749229 582 ---GITLFTVSHR 591
Cdd:cd03216 129 raqGVAVIFISHR 141
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
410-564 |
3.13e-09 |
|
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: 57.67 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 410 VPLATPNGD---ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL---GELWPLFGGHLT---KPERGKLF-----YVPQ 475
Cdd:cd03234 9 VGLKAKNWNkyaRILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILfngQPRKPDQFqkcvaYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 476 R----PYMTL-------GTLRDQVIYPDGkedQKKKGISDQVLKgYLDNVQLGHILereggwdsvqdwMDVLSGGEKQRM 544
Cdd:cd03234 89 DdillPGLTVretltytAILRLPRKSSDA---IRKKRVEDVLLR-DLALTRIGGNL------------VKGISGGERRRV 152
|
170 180
....*....|....*....|
gi 1958749229 545 AMARLFYHKPQFAILDECTS 564
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTS 172
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
416-590 |
3.30e-09 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 56.86 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGHLTKPERGKLFYVPQR-------PY-----MTLG 482
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRPT-SGTVRRAGGARVAYVPQRsevpdslPLtvrdlVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 483 TLRDQVIY-PDGKEDQKkkgisdqVLKGYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 561
Cdd:NF040873 82 RWARRGLWrRLTRDDRA-------AVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|..
gi 1958749229 562 CTSAVSVDVEDYIYSHCRKV---GITLFTVSH 590
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEharGATVVVVTH 177
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
421-590 |
5.24e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 58.42 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGhLTKPERGKLF-------YVP--QR------------PYM 479
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLR-------LIAG-FETPDSGRIMldgqditHVPaeNRhvntvfqsyalfPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 480 TLgtlRDQVIYpdGKEDQK--KKGISDQVLKGyLDNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFA 557
Cdd:PRK09452 102 TV---FENVAF--GLRMQKtpAAEITPRVMEA-LRMVQLEEFAQRK-----PHQ----LSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958749229 558 ILDECTSAVsvdveDY---------IYSHCRKVGITLFTVSH 590
Cdd:PRK09452 167 LLDESLSAL-----DYklrkqmqneLKALQRKLGITFVFVTH 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
415-591 |
5.34e-09 |
|
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: 59.57 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 415 PNGDILIQDLSFEVRSGANVLICGPNGCGKSS----LFRVL----GELwPLFGGHLTK----PERGKLFYVPQRPYMTLG 482
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINesaeGEI-IIDGLNIAKiglhDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 483 TLRDQvIYPDGKEDQKKKGISDQV--LKGYLDNVQLGHILE-REGGwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAIL 559
Cdd:TIGR00957 1375 SLRMN-LDPFSQYSDEEVWWALELahLKTFVSALPDKLDHEcAEGG--------ENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190
....*....|....*....|....*....|....
gi 1958749229 560 DECTSAVSVDVEDYIYSHCRKV--GITLFTVSHR 591
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHR 1479
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
370-571 |
5.56e-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: 58.79 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 370 KYERTMVSQQDKGIEGAQAspLIPgAGEIInADNIIKFDHVPLATpnGD-ILIQDLSFEVRSGANVLICGPNGCGKSSLF 448
Cdd:TIGR03719 292 RYEELLSQEFQKRNETAEI--YIP-PGPRL-GDKVIEAENLTKAF--GDkLLIDDLSFKLPPGGIVGVIGPNGAGKSTLF 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 449 RVL-GELWPlFGGHLTKPERGKLFYVpqrpymtlgtlrdqviypdgkeDQKKKGISD-----QVLKGYLDNVQLG--HIL 520
Cdd:TIGR03719 366 RMItGQEQP-DSGTIEIGETVKLAYV----------------------DQSRDALDPnktvwEEISGGLDIIKLGkrEIP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749229 521 ERE-------GGWDSvQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVE 571
Cdd:TIGR03719 423 SRAyvgrfnfKGSDQ-QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTN--DLDVE 477
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
404-600 |
6.08e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.81 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 404 IIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGH----LTKPE----R 467
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIcgierpsaGKIW--FSGHditrLKNREvpflR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 468 GKLFYVPQRPYMTLG-TLRDQVIYP-----DGKEDQKKKgisdqvLKGYLDNVQLghilereggWDSVQDWMDVLSGGEK 541
Cdd:PRK10908 79 RQIGMIFQDHHLLMDrTVYDNVAIPliiagASGDDIRRR------VSAALDKVGL---------LDKAKNFPIQLSGGEQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958749229 542 QRMAMARLFYHKPQFAILDECTSAVSVDVEDYI---YSHCRKVGITLFTVSHRKSLWKHHEY 600
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNRVGVTVLMATHDIGLISRRSY 205
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
417-563 |
6.11e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 417 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGHLTKPERGKLFYVPQRPY------MTLGTLRDQvi 489
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvGELEPD-SGTVKWSENANIGYYAQDHAydfendLTLFDWMSQ-- 407
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749229 490 YPDGKEDqkkkgisDQVLKGYldnvqLGHILereGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:PRK15064 408 WRQEGDD-------EQAVRGT-----LGRLL---FSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
421-593 |
6.64e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGhLTKPERGKLFY---------VPQR------------PYM 479
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAG-LEKPTEGQIFIdgedvthrsIQQRdicmvfqsyalfPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 480 TLGtlrDQVIYPDGKEDQKKKGISDQVlKGYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAIL 559
Cdd:PRK11432 94 SLG---ENVGYGLKMLGVPKEERKQRV-KEALELVDLAGFEDR---------YVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958749229 560 DECTSAVSVDV----EDYIYSHCRKVGITLFTVSHRKS 593
Cdd:PRK11432 161 DEPLSNLDANLrrsmREKIRELQQQFNITSLYVTHDQS 198
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
438-590 |
9.09e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 438 GPNGCGKSSLFRVL---GELWP--------LFGGH-LTKPE------RGKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKK 499
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPevtitgsiVYNGHnIYSPRtdtvdlRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 500 KGISDQVLKGYLDNVQLghilereggWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVE 571
Cdd:PRK14239 118 KQVLDEAVEKSLKGASI---------WDEVKDRLHdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSALdpisAGKIE 188
|
170
....*....|....*....
gi 1958749229 572 DYIYShcRKVGITLFTVSH 590
Cdd:PRK14239 189 ETLLG--LKDDYTMLLVTR 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
421-561 |
1.77e-08 |
|
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: 55.13 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG----------HLTKPERGK--LFYVPQR----PYMT---- 480
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsirfdgrditGLPPHERARagIGYVPEGrrifPELTveen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 481 --LGtlrdqvIYPDGKEDQKKKgisdqvlkgyLDNV-----QLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHK 553
Cdd:cd03224 96 llLG------AYARRRAKRKAR----------LERVyelfpRLKERRKQLAG---------TLSGGEQQMLAIARALMSR 150
|
....*...
gi 1958749229 554 PQFAILDE 561
Cdd:cd03224 151 PKLLLLDE 158
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
400-564 |
2.54e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.38 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 400 NADNIIKFDHVPLATPNGD-ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWplfgghltKPERGKLF-YVPQRP 477
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL--------KPQSGEIKiDGITIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 478 YMTLGTLRDQV--IY--PDGK------EDQ-----KKKGISDQVLKGYLDN----VQLGHILEREGgwdsvqdwmDVLSG 538
Cdd:PRK13632 75 KENLKEIRKKIgiIFqnPDNQfigatvEDDiafglENKKVPPKKMKDIIDDlakkVGMEDYLDKEP---------QNLSG 145
|
170 180
....*....|....*....|....*.
gi 1958749229 539 GEKQRMAMARLFYHKPQFAILDECTS 564
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTS 171
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
416-590 |
2.90e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT--------------------KPERGKLFYVPQ 475
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlyfgkdifqidaiklRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 476 rPYMTLgTLRDQVIYPdgkedQKKKGISDQ-VLKGYLDNVqlghiLEREGGWDSVQDWMDV----LSGGEKQRMAMARLF 550
Cdd:PRK14246 101 -PFPHL-SIYDNIAYP-----LKSHGIKEKrEIKKIVEEC-----LRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958749229 551 YHKPQFAILDECTSAVSV----DVEDYIYSHCRKVGITLftVSH 590
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIvnsqAIEKLITELKNEIAIVI--VSH 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
404-594 |
3.33e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 404 IIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGHLTKPE-RGKLFYVPQRPYMTL 481
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIsGELQPSSGTVFRSAKvRMAVFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 482 GT---LRDQVIYPdgkedqkkkGISDQVLKGYLDNVQLGHILEREGgwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAI 558
Cdd:PLN03073 588 SSnplLYMMRCFP---------GVPEQKLRAHLGSFGVTGNLALQP--------MYTLSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958749229 559 LDECTSAVSVD-VEDYIYshcrkvGITLF-----TVSHRKSL 594
Cdd:PLN03073 651 LDEPSNHLDLDaVEALIQ------GLVLFqggvlMVSHDEHL 686
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
398-590 |
4.29e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.79 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 398 IINADNIIKFDHVPLATPnGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGHLTKPERGKLF 471
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPpsegeiLLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 472 -----YVPQR-PYMTLGTLRDQVI---YP-------DGKEDQKK--KGISDQVLKgyldnvQLGHILereggwdsvqdwM 533
Cdd:PRK10575 84 arkvaYLPQQlPAAEGMTVRELVAigrYPwhgalgrFGAADREKveEAISLVGLK------PLAHRL------------V 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958749229 534 DVLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSH 590
Cdd:PRK10575 146 DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
421-561 |
5.04e-08 |
|
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: 53.80 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHL---------TKPERGKLFYVPQR----PYMTLgtlRDQ 487
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdLPPKDRDIAMVFQNyalyPHMTV---YDN 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749229 488 VIYPDGKEDQKKKGISDQVLKgYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 561
Cdd:cd03301 93 IAFGLKLRKVPKDEIDERVRE-VAELLQIEHLLDRK---------PKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
421-591 |
7.02e-08 |
|
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: 53.59 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGH-LT--KPER------GKLFYVPqRPYMTLgTLR 485
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFLRPtsgsvLFDGEdITglPPHEiarlgiGRTFQIP-RLFPEL-TVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 486 DQVI----------YPDGKEDQKKKGISDQVLKgYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQ 555
Cdd:cd03219 94 ENVMvaaqartgsgLLLARARREEREARERAEE-LLERVGLADLADRPAG---------ELSYGQQRRLEIARALATDPK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958749229 556 FAILDECTSAVS----VDVEDYIyshcRKV---GITLFTVSHR 591
Cdd:cd03219 164 LLLLDEPAAGLNpeetEELAELI----RELrerGITVLLVEHD 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
399-570 |
8.18e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.70 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 399 INADNIIK-FDHVPLatpngdilIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT----------KPER 467
Cdd:PRK10851 3 IEIANIKKsFGRTQV--------LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdvsrlhARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 468 --GKLF--YVPQRpYMTLGtlrDQVIY-----PDgKEDQKKKGISDQVLKgYLDNVQLGHILEReggwdsvqdWMDVLSG 538
Cdd:PRK10851 75 kvGFVFqhYALFR-HMTVF---DNIAFgltvlPR-RERPNAAAIKAKVTQ-LLEMVQLAHLADR---------YPAQLSG 139
|
170 180 190
....*....|....*....|....*....|..
gi 1958749229 539 GEKQRMAMARLFYHKPQFAILDECTSAVSVDV 570
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
420-607 |
8.28e-08 |
|
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: 52.91 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGH----LTKPERGK--LFYVPQRPymtlgt 483
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkyevteGEI--LFKGEditdLPPEERARlgIFLAFQYP------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 484 lrdqVIYPdgkedqkkkGISdqvLKGYLDNVQLGhilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:cd03217 87 ----PEIP---------GVK---NADFLRYVNEG------------------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958749229 564 SAVSVD----VEDYIySHCRKVGITLFTVSHRKSLWKHHE---YYLHMDGR 607
Cdd:cd03217 133 SGLDIDalrlVAEVI-NKLREEGKSVLIITHYQRLLDYIKpdrVHVLYDGR 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
415-569 |
9.60e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 415 PNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPLFGGhltkpergKLFYVPQRPYM--TLgTL 484
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfnGEARPQPGI--------KVGYLPQEPQLdpTK-TV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 485 RDQVIypDGKEDQKKK-----GIS----------DQVLKgylDNVQLGHILEREGGWD---SVQDWMD------------ 534
Cdd:TIGR03719 86 RENVE--EGVAEIKDAldrfnEISakyaepdadfDKLAA---EQAELQEIIDAADAWDldsQLEIAMDalrcppwdadvt 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958749229 535 VLSGGEKQRMAMARLFYHKPQFAILDECTS---AVSVD 569
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNhldAESVA 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
400-590 |
9.80e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.60 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 400 NADNIIKFDHVPLATpNGD--ILIQDLSFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGhLTKPERGKLFYvpqrp 477
Cdd:PRK13648 3 DKNSIIVFKNVSFQY-QSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAK-------LMIG-IEKVKSGEIFY----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 478 ymtlgtlRDQVIYPDGKEDQKKK-GISDQ--------------VLKGyLDNVQLGH---------ILEREGGWDSVQDWM 533
Cdd:PRK13648 69 -------NNQAITDDNFEKLRKHiGIVFQnpdnqfvgsivkydVAFG-LENHAVPYdemhrrvseALKQVDMLERADYEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958749229 534 DVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV----GITLFTVSH 590
Cdd:PRK13648 141 NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITH 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
421-590 |
1.58e-07 |
|
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: 52.47 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGEL-WPLFGGHLTK--------PERGKLFyvpQR----PYMTLgtlRDQ 487
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitepgPDRMVVF---QNysllPWLTV---REN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 488 V-IYPDGKEDQKKKGISDQVLKGYLDNVQLGHILEREGGWdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAV 566
Cdd:TIGR01184 75 IaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ---------LSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180
....*....|....*....|....*...
gi 1958749229 567 SV----DVEDYIYSHCRKVGITLFTVSH 590
Cdd:TIGR01184 146 DAltrgNLQEELMQIWEEHRVTVLMVTH 173
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
423-590 |
1.62e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 423 DLSFEVRSGANVLICGPNGCGKSSLFRVL--------GEL----------------------------------WPlfgg 460
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsGTLniagnhfdfsktpsdkairelrrnvgmvfqqynlWP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 461 HLTKPErgKLFYVPQRpymTLGTLRDQviypdGKEDQKKkgisdqvlkgYLDNVQLGHILEReggwdsvqdWMDVLSGGE 540
Cdd:PRK11124 96 HLTVQQ--NLIEAPCR---VLGLSKDQ-----ALARAEK----------LLERLRLKPYADR---------FPLHLSGGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958749229 541 KQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV---GITLFTVSH 590
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELaetGITQVIVTH 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
417-590 |
1.91e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.49 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 417 GDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPERgKLFYVP--QR------------PYMTL 481
Cdd:PRK11000 14 GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-RMNDVPpaERgvgmvfqsyalyPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 482 GtlrDQVIYpdG-KEDQKKKGISDQVLKGYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILD 560
Cdd:PRK11000 93 A---ENMSF--GlKLAGAKKEEINQRVNQVAEVLQLAHLLDRKP---------KALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190
....*....|....*....|....*....|....
gi 1958749229 561 ECTS----AVSVDVEDYIYSHCRKVGITLFTVSH 590
Cdd:PRK11000 159 EPLSnldaALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
402-549 |
1.91e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 402 DNIIKFDHVPLATpnGD-ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPERGKLFYVpqrpymt 480
Cdd:PRK11819 322 DKVIEAENLSKSF--GDrLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYV------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 481 lgtlrdqviypdgkeDQKKKGISD-----QVLKGYLDNVQLGhilERE------------GGWDSvQDWMDVLSGGEKQR 543
Cdd:PRK11819 393 ---------------DQSRDALDPnktvwEEISGGLDIIKVG---NREipsrayvgrfnfKGGDQ-QKKVGVLSGGERNR 453
|
....*.
gi 1958749229 544 MAMARL 549
Cdd:PRK11819 454 LHLAKT 459
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
421-591 |
2.12e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 52.80 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGHLTKPERGKLFYVPQ----RPYMTLGtlrDQVI 489
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILAPdsgevlWDGEPLDPEDRRRIGYLPEerglYPKMKVG---EQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 490 Y------PDGKEDQKKkgisdqvLKGYLDNVQLGhilEREGgwDSVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:COG4152 94 YlarlkgLSKAEAKRR-------ADEWLERLGLG---DRAN--KKVEE----LSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190
....*....|....*....|....*....|...
gi 1958749229 564 S---AVSVDV-EDYIYSHCRKvGIT-LFTvSHR 591
Cdd:COG4152 158 SgldPVNVELlKDVIRELAAK-GTTvIFS-SHQ 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
383-564 |
2.58e-07 |
|
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: 54.15 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 383 IEGAQASPLIPGAGEIINADNIIKFdhvplaTPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFG--- 459
Cdd:TIGR01271 1203 IENPHAQKCWPSGGQMDVQGLTAKY------TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiq 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 460 ------GHLTKPERGKLF-YVPQRPYMTLGTLRDQVIYPDGKEDQKKKGISDQV-LKGYLDNV--QLGHILErEGGWdsv 529
Cdd:TIGR01271 1277 idgvswNSVTLQTWRKAFgVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVgLKSVIEQFpdKLDFVLV-DGGY--- 1352
|
170 180 190
....*....|....*....|....*....|....*
gi 1958749229 530 qdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTS 564
Cdd:TIGR01271 1353 -----VLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
373-593 |
2.78e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.56 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 373 RTMVSQQDKGIEGAQASPLIPGAGEIinadNIIKFdHVPLATPNgdiLIQDLSFEVRSGANVLICGPNGCGKSSLFRVL- 451
Cdd:PRK10789 291 RAMLAEAPVVKDGSEPVPEGRGELDV----NIRQF-TYPQTDHP---ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIq 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 452 -------GELwpLFGGH-LTKPE----RGKLFYVPQRPYMTLGTLRDQVIYpdGKEDQKKKGIsDQVLKgyLDNVqlgH- 518
Cdd:PRK10789 363 rhfdvseGDI--RFHDIpLTKLQldswRSRLAVVSQTPFLFSDTVANNIAL--GRPDATQQEI-EHVAR--LASV---Hd 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749229 519 -ILEREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKVGI--TLFTVSHRKS 593
Cdd:PRK10789 433 dILRLPQGYDTeVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEgrTVIISAHRLS 511
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
421-561 |
3.36e-07 |
|
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: 51.77 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGelwplfgghLTKPERGKLF--------------------YVPQRPYM 479
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYmIVG---------LVKPDSGKILldgqditklpmhkrarlgigYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 480 TLG-TLRDQV-----IYPDGKEDQKKKgisdqvLKGYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQRMAMARLFYHK 553
Cdd:cd03218 87 FRKlTVEENIlavleIRGLSKKEREEK------LEELLEEFHITHLRKSKA---------SSLSGGERRRVEIARALATN 151
|
....*...
gi 1958749229 554 PQFAILDE 561
Cdd:cd03218 152 PKFLLLDE 159
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
416-561 |
3.42e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 51.61 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILiQDLSFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGG----HLTKPERGK--LFYVPQRPY- 478
Cdd:COG0396 12 GKEIL-KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpkyevtsGSI--LLDGedilELSPDERARagIFLAFQYPVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 479 ---MTLGTL--------RDQVIypDGKEDQKKkgisdqvLKGYLDNVQLGH-ILER---EGgwdsvqdwmdvLSGGEKQR 543
Cdd:COG0396 89 ipgVSVSNFlrtalnarRGEEL--SAREFLKL-------LKEKMKELGLDEdFLDRyvnEG-----------FSGGEKKR 148
|
170
....*....|....*...
gi 1958749229 544 MAMARLFYHKPQFAILDE 561
Cdd:COG0396 149 NEILQMLLLEPKLAILDE 166
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
421-565 |
4.67e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 51.25 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG----------------HLTKPERGKLFyvpQR----PYMT 480
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglkvndpkvdeRLIRQEAGMVF---QQfylfPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 481 ------LGTLRdqvIYPDGKEDQKKKGisdqvlKGYLDNVQLGhilEREGGWDSVqdwmdvLSGGEKQRMAMARLFYHKP 554
Cdd:PRK09493 94 alenvmFGPLR---VRGASKEEAEKQA------RELLAKVGLA---ERAHHYPSE------LSGGQQQRVAIARALAVKP 155
|
170
....*....|.
gi 1958749229 555 QFAILDECTSA 565
Cdd:PRK09493 156 KLMLFDEPTSA 166
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
383-593 |
5.34e-07 |
|
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: 51.45 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 383 IEGAQASPLIPGAGEIINADNIIKFDHvplatpNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHL 462
Cdd:cd03288 5 ISGSSNSGLVGLGGEIKIHDLCVRYEN------NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 463 T-----------KPERGKLFYVPQRPYMTLGTLRDQViypdgkeDQKKKgISDQVLKGYLDNVQLGHILER-EGGWDS-V 529
Cdd:cd03288 79 VidgidisklplHTLRSRLSIILQDPILFSGSIRFNL-------DPECK-CTDDRLWEALEIAQLKNMVKSlPGGLDAvV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 530 QDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIyshcRKVGITLF------TVSHRKS 593
Cdd:cd03288 151 TEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENIL----QKVVMTAFadrtvvTIAHRVS 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
421-564 |
5.35e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFG-----GHLTKPE-----RGKLFYVPQRP--YMTLGTLRDQ 487
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIdGLLEAESGqiiidGDLLTEEnvwdiRHKIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 488 VIYpdGKEDqkkKGISDQVLKGYLDnvqlgHILEREGgwdsVQDWMDV----LSGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:PRK13650 103 VAF--GLEN---KGIPHEEMKERVN-----EALELVG----MQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
.
gi 1958749229 564 S 564
Cdd:PRK13650 169 S 169
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
404-590 |
6.02e-07 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 51.04 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 404 IIKFDHVP---LATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGHLTKPERGKLfy 472
Cdd:cd03258 1 MIELKNVSkvfGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptsGSVL-VDGTDLTLLSGKEL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 473 VPQRPYMTL----------GTLRDQVIYPDGKEDQKKKGISDQVLkgyldnvqlgHILEREGGWDSVQDWMDVLSGGEKQ 542
Cdd:cd03258 78 RKARRRIGMifqhfnllssRTVFENVALPLEIAGVPKAEIEERVL----------ELLELVGLEDKADAYPAQLSGGQKQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958749229 543 RMAMARLFYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSH 590
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALdpetTQSILALLRDINRELGLTIVLITH 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
421-590 |
6.38e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 51.64 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfgGHLTkPERGKLF-----------------YVPQR----PYM 479
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIA-------GFET-PDSGRILldgrdvtglppekrnvgMVFQDyalfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 480 TLgtlRDQVIYPDGKEDQKKKGISDQVLKgYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQF 556
Cdd:COG3842 93 TV---AENVAFGLRMRGVPKAEIRARVAE-LLELVGLEGLADRyphQ------------LSGGQQQRVALARALAPEPRV 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958749229 557 AILDECTSA----VSVDVEDYIYSHCRKVGITLFTVSH 590
Cdd:COG3842 157 LLLDEPLSAldakLREEMREELRRLQRELGITFIYVTH 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
402-590 |
7.96e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.00 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 402 DNIIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGHLTKPERGKLFYVPQ 475
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLnGILKPssgriLFDGKPIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 476 RPYMTLGTLRDQVIYPDGKEDQKKKGISDQVLKgylDNVQ--LGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHK 553
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPE---DEVRkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958749229 554 PQFAILDECTSAVS----VDVEDYIYSHCRKVGITLFTVSH 590
Cdd:PRK13636 160 PKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATH 200
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
421-590 |
8.34e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.94 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSL-------------FRVLGELwpLFGGH-LTKPE------RGKLFYVPQRPYMT 480
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnrlndlipgFRVEGKV--TFHGKnLYAPDvdpvevRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 481 LGTLRDQVIYpdGKEDQKKKGISDQVLKGYLDNVQLghilereggWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQF 556
Cdd:PRK14243 104 PKSIYDNIAY--GARINGYKGDMDELVERSLRQAAL---------WDEVKDKLKqsglSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958749229 557 AILDECTSAV----SVDVEDYIysHCRKVGITLFTVSH 590
Cdd:PRK14243 173 ILMDEPCSALdpisTLRIEELM--HELKEQYTIIIVTH 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
416-607 |
8.53e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.37 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggHLTKPERGK-------LFYVP--QRP--------- 477
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLA--------GFEQPTAGQimldgvdLSHVPpyQRPinmmfqsya 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 478 ---YMTLgtlrDQVIYPDGKEDQKKKG-ISDQVLKgYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQRMAMARLFYHK 553
Cdd:PRK11607 102 lfpHMTV----EQNIAFGLKQDKLPKAeIASRVNE-MLGLVHMQEFAKRKP---------HQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749229 554 PQFAILDECTSAVSVDVEDYIYSHC----RKVGITLFTVSHRKslwkhhEYYLHMDGR 607
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVvdilERVGVTCVMVTHDQ------EEAMTMAGR 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
428-564 |
8.58e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 428 VRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGHLTKPE--------RG-------------------KLFYVPQRPYM 479
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsGELIPNLGDYEEEPSwdevlkrfRGtelqnyfkklyngeikvvhKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 480 TLGTLRDQVIYPDgkedqkKKGISDQVLkgylDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 559
Cdd:PRK13409 176 FKGKVRELLKKVD------ERGKLDEVV----ERLGLENILDRD---------ISELSGGELQRVAIAAALLRDADFYFF 236
|
....*
gi 1958749229 560 DECTS 564
Cdd:PRK13409 237 DEPTS 241
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
417-561 |
1.13e-06 |
|
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: 49.98 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 417 GDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT---------KPE----RGkLFYVPQR----PY 478
Cdd:COG0410 14 GGIHVlHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglPPHriarLG-IGYVPEGrrifPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 479 MT------LG--TLRDQviyPDGKEDqkkkgisdqvlkgyLDNV-----QLGHILEREGGwdsvqdwmdVLSGGEKQRMA 545
Cdd:COG0410 93 LTveenllLGayARRDR---AEVRAD--------------LERVyelfpRLKERRRQRAG---------TLSGGEQQMLA 146
|
170
....*....|....*.
gi 1958749229 546 MARLFYHKPQFAILDE 561
Cdd:COG0410 147 IGRALMSRPKLLLLDE 162
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
420-564 |
1.22e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLG---ELWP---------LFGGHLTKPERGKL-------FYVPQrPYMT 480
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrliELYPearvsgevyLDGQDIFKMDVIELrrrvqmvFQIPN-PIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 481 LGTLRDQVIYPDGKEDQKKKGISDQVLKGYLDNVQLghilereggWDSVQDWMDV----LSGGEKQRMAMARLFYHKPQF 556
Cdd:PRK14247 97 LSIFENVALGLKLNRLVKSKKELQERVRWALEKAQL---------WDEVKDRLDApagkLSGGQQQRLCIARALAFQPEV 167
|
....*...
gi 1958749229 557 AILDECTS 564
Cdd:PRK14247 168 LLADEPTA 175
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
417-590 |
1.27e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 50.98 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 417 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT----------KPERGKLFYVPQRPYMTLG-TLR 485
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVPQFDNLDLEfTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 486 DQ-VIYpdGKEDQKKKGISDQVLKGYLDNVQLghilerEGGWDS-VQDwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:PRK13536 133 ENlLVF--GRYFGMSTREIEAVIPSLLEFARL------ESKADArVSD----LSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190
....*....|....*....|....*....|
gi 1958749229 564 SAVSVDVEDYIYSHCRKV---GITLFTVSH 590
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLlarGKTILLTTH 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
414-568 |
1.35e-06 |
|
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: 50.44 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 414 TPNGDI-LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-----------GELwpLFGG----HLTKPE----RGK-LFY 472
Cdd:COG0444 13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlgllpppgitsGEI--LFDGedllKLSEKElrkiRGReIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 473 VPQRPYMTLG---TLRDQVIYP------DGKEDQKKKGISdqvlkgYLDNVQLghilereggwDSVQDWMDV----LSGG 539
Cdd:COG0444 91 IFQDPMTSLNpvmTVGDQIAEPlrihggLSKAEARERAIE------LLERVGL----------PDPERRLDRypheLSGG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1958749229 540 EKQR----MAMArlfyHKPQFAILDECTSA--VSV 568
Cdd:COG0444 155 MRQRvmiaRALA----LEPKLLIADEPTTAldVTI 185
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
420-589 |
2.44e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.46 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPL------------FGGHLTKP---------ERGKLFYVPQR-P 477
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearvegevrlFGRNIYSPdvdpievrrEVGMVFQYPNPfP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 478 YMTlgtlrdqvIYPDGKEDQKKKGISDQvlKGYLDNVqLGHILEREGGWDSVQDWMD----VLSGGEKQRMAMARLFYHK 553
Cdd:PRK14267 99 HLT--------IYDNVAIGVKLNGLVKS--KKELDER-VEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958749229 554 PQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVS 589
Cdd:PRK14267 168 PKILLMDEPTANIdpvgTAKIEELLFELKKEYTIVLVTHS 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
421-590 |
3.11e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT--------------KPERGKLFYVPQRPYMTLG---T 483
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtlspgklQALRRDIQFIFQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 484 LRDQVIYP-------DGKEDQKKkgisdqvlkgyldnvqLGHILER-----EGGWDSVQDWmdvlSGGEKQRMAMARLFY 551
Cdd:PRK10261 420 VGDSIMEPlrvhgllPGKAAAAR----------------VAWLLERvgllpEHAWRYPHEF----SGGQRQRICIARALA 479
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958749229 552 HKPQFAILDECTSAVSVDVEDYIYSHC----RKVGITLFTVSH 590
Cdd:PRK10261 480 LNPKVIIADEAVSALDVSIRGQIINLLldlqRDFGIAYLFISH 522
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
405-591 |
4.41e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 405 IKFDHVPLA-TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPE-----------RGKLFY 472
Cdd:PLN03232 1235 IKFEDVHLRyRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 473 VPQRPYMTLGTLRDQViypDGKEDQKKKGISDQVLKGYLDNVqlghILEREGGWDS-VQDWMDVLSGGEKQRMAMARLFY 551
Cdd:PLN03232 1315 IPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDV----IDRNPFGLDAeVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958749229 552 HKPQFAILDECTSAVSVDVEDYIYSHCRK--VGITLFTVSHR 591
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAHR 1429
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
397-590 |
4.87e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.55 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 397 EIINADNIIkFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHL------TKPErGKL 470
Cdd:PRK13633 3 EMIKCKNVS-YKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldTSDE-ENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 471 FYVPQRPYMTLGTLRDQVIYPDGKED----QKKKGISDQVLKGYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRMAM 546
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATIVEEDvafgPENLGIPPEEIRERVDES-----LKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958749229 547 ARLFYHKPQFAILDECTSAVS----VDVEDYIYSHCRKVGITLFTVSH 590
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
421-591 |
6.90e-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: 47.36 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELwplfgghlTKPERGKL----FYVPQRPY---MTLG----------- 482
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--------LEPDAGFAtvdgFDVVKEPAearRRLGfvsdstglydr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 483 -TLRDQVIYPDGKEdqkkkGISDQVLKGYLDNV----QLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFA 557
Cdd:cd03266 93 lTARENLEYFAGLY-----GLKGDELTARLEELadrlGMEELLDRRVG---------GFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958749229 558 ILDECTSAVSV----DVEDYIySHCRKVGITLFTVSHR 591
Cdd:cd03266 159 LLDEPTTGLDVmatrALREFI-RQLRALGKCILFSTHI 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
421-590 |
7.42e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 49.03 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPLFGGH---LTKP---ERGKLfyvpqRPYM------- 479
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIagvleptsGEVNVRVGDEwvdMTKPgpdGRGRA-----KRYIgilhqey 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 480 -------TLGTLRDQVIYPDGKEDQKKKGISDQVLKGYlDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYH 552
Cdd:TIGR03269 375 dlyphrtVLDNLTEAIGLELPDELARMKAVITLKMVGF-DEEKAEEILDK---------YPDELSEGERHRVALAQVLIK 444
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958749229 553 KPQFAILDECTSAVS----VDVEDYIYSHCRKVGITLFTVSH 590
Cdd:TIGR03269 445 EPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSH 486
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
420-602 |
8.51e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.87 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWplfgghltKPERGKLFYVPQ----------------------RP 477
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL--------NPEKGEILFERQsikkdlctyqkqlcfvghrsgiNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 478 YMTLgtlRDQVIYpDGKEDQKKKGISDQVLKgyldnVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFA 557
Cdd:PRK13540 88 YLTL---RENCLY-DIHFSPGAVGITELCRL-----FSLEHLIDYPCG---------LLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958749229 558 ILDEctSAVSVD------VEDYIYSHCRKVGITLFTVSHRKSLWK--HHEYYL 602
Cdd:PRK13540 150 LLDE--PLVALDelslltIITKIQEHRAKGGAVLLTSHQDLPLNKadYEEYHL 200
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
414-561 |
8.59e-06 |
|
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: 47.93 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 414 TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFG---------GHLTKPERGKLF-YVPQRPYMTLGT 483
Cdd:cd03289 13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGdiqidgvswNSVPLQKWRKAFgVIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 484 LRdQVIYPDGK-EDQKKKGISDQV-LKGYLDNV--QLGHILErEGGWdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAIL 559
Cdd:cd03289 93 FR-KNLDPYGKwSDEEIWKVAEEVgLKSVIEQFpgQLDFVLV-DGGC--------VLSHGHKQLMCLARSVLSKAKILLL 162
|
..
gi 1958749229 560 DE 561
Cdd:cd03289 163 DE 164
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
421-590 |
9.82e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.78 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG-------HLTKPE----RGKLFYVPQRP--YMTLGTLRDQ 487
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgeLLTAENvwnlRRKIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 488 VIYpdGKEDQkkkGISDQVLKGYLDNVQLG-HILE---REGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 563
Cdd:PRK13642 103 VAF--GMENQ---GIPREEMIKRVDEALLAvNMLDfktREPA---------RLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190
....*....|....*....|....*....|.
gi 1958749229 564 SAVS----VDVEDYIYSHCRKVGITLFTVSH 590
Cdd:PRK13642 169 SMLDptgrQEIMRVIHEIKEKYQLTVLSITH 199
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
401-564 |
1.03e-05 |
|
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: 46.78 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 401 ADNIIKFDHVPLATPNGDILiQDLSFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGHLTKPE--RG 468
Cdd:cd03213 6 FRNLTVTVKSSPSKSGKQLL-KNVSGKAKPGELTAIMGPSGAGKSTLLNALagrrtglgvsGEV--LINGRPLDKRsfRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 469 KLFYVPQrpymtlgtlrdqviypdgkedqkkkgisdqvlkgylDNVQLGHILEREGGWDSVQdwMDVLSGGEKQRMAMAR 548
Cdd:cd03213 83 IIGYVPQ------------------------------------DDILHPTLTVRETLMFAAK--LRGLSGGERKRVSIAL 124
|
170
....*....|....*.
gi 1958749229 549 LFYHKPQFAILDECTS 564
Cdd:cd03213 125 ELVSNPSLLFLDEPTS 140
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
421-574 |
1.04e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSS----LFRVL---GELW----PL--FGGHLTKPERGKLFYVPQRPYMTLGT-LRD 486
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIWfdgqPLhnLNRRQLLPVRHRIQVVFQDPNSSLNPrLNV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 487 QVIYPDGKEDQKKkgisdqVLKGYLDNVQLGHILErEGGWD--SVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 564
Cdd:PRK15134 382 LQIIEEGLRVHQP------TLSAAQREQQVIAVME-EVGLDpeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170
....*....|
gi 1958749229 565 AVSVDVEDYI 574
Cdd:PRK15134 455 SLDKTVQAQI 464
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
394-576 |
1.39e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.09 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 394 GAGEIINADNIIKFDHVPLATPNGDIL-IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTkpergkLFY 472
Cdd:PRK11176 331 GKRVIERAKGDIEFRNVTFTYPGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL------LDG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 473 VPQRPYmTLGTLRDQV--------IYPD--------GKEDQKKKgisDQVLKGYLDNVQLGHILEREGGWDSVQDWMDV- 535
Cdd:PRK11176 405 HDLRDY-TLASLRNQValvsqnvhLFNDtianniayARTEQYSR---EQIEEAARMAYAMDFINKMDNGLDTVIGENGVl 480
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958749229 536 LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYS 576
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQA 521
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
419-590 |
1.43e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.90 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 419 ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGKEDQk 498
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 499 kkgisDQVLKGYL------------DNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAV 566
Cdd:PRK10253 100 -----ELVARGRYphqplftrwrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180
....*....|....*....|....*...
gi 1958749229 567 ----SVDVEDYIYSHCRKVGITLFTVSH 590
Cdd:PRK10253 175 dishQIDLLELLSELNREKGYTLAAVLH 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
423-590 |
1.92e-05 |
|
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: 45.95 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 423 DLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGHL--------TKPERGKLFYVPQR----PYMTLGTLRDQVI 489
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNlIAGFETPQSGRVLingvdvtaAPPADRPVSMLFQEnnlfAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 490 YPDGK---EDQKKkgisdqvLKGYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAV 566
Cdd:cd03298 96 SPGLKltaEDRQA-------IEVALARVGLAGLEKRLPG---------ELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180
....*....|....*....|....*...
gi 1958749229 567 S----VDVEDYIYSHCRKVGITLFTVSH 590
Cdd:cd03298 160 DpalrAEMLDLVLDLHAETKMTVLMVTH 187
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
401-594 |
2.17e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 46.31 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 401 ADNIIKFDHVPLATPNGD---ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwPLFGGHLTK---PE 466
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEhelSILTGVELVVKRGETIALIGESGSGKSTLLAILaglddgssGEV-SLVGQPLHQmdeEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 467 RGKLF-----YVPQRpYMTLGTLRDqviypdgkedqkkkgisdqvlkgyLDNVQLGHILEREGGWDSVQDWMDVL----- 536
Cdd:PRK10584 82 RAKLRakhvgFVFQS-FMLIPTLNA------------------------LENVELPALLRGESSRQSRNGAKALLeqlgl 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958749229 537 -----------SGGEKQRMAMARLFYHKPQFAILDECTSavSVD------VEDYIYSHCRKVGITLFTVSHRKSL 594
Cdd:PRK10584 137 gkrldhlpaqlSGGEQQRVALARAFNGRPDVLFADEPTG--NLDrqtgdkIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
424-569 |
4.22e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 424 LSFevRSGANVLICGPNGCGKSSLFRVL--------GELWPLFGGhltkpergKLFYVPQRPYMTLG-TLRDQVIypDGK 494
Cdd:PRK11819 28 LSF--FPGAKIGVLGLNGAGKSTLLRIMagvdkefeGEARPAPGI--------KVGYLPQEPQLDPEkTVRENVE--EGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 495 EDQKKK-----GISDQvlkgYLDNV-----------QLGHILEREGGWDS---VQDWMD------------VLSGGEKQR 543
Cdd:PRK11819 96 AEVKAAldrfnEIYAA----YAEPDadfdalaaeqgELQEIIDAADAWDLdsqLEIAMDalrcppwdakvtKLSGGERRR 171
|
170 180
....*....|....*....|....*....
gi 1958749229 544 MAMARLFYHKPQFAILDECTS---AVSVD 569
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNhldAESVA 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
421-463 |
4.43e-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: 45.22 E-value: 4.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT 463
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
431-607 |
4.91e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 431 GANVLICGPNGCGKSSLFRVL-GELWPLfGGHLTKPERGKLFYVPQR----------PYMTLGTLRDQViypdgkedqkk 499
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLaGELAPV-SGEIGLAKGIKLGYFAQHqleflradesPLQHLARLAPQE----------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 500 kgiSDQVLKGYLdnvqlghilereGGW----DSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIY 575
Cdd:PRK10636 406 ---LEQKLRDYL------------GGFgfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
|
170 180 190
....*....|....*....|....*....|....
gi 1958749229 576 SHCRKVGITLFTVSHRKSLWKH--HEYYLHMDGR 607
Cdd:PRK10636 471 EALIDFEGALVVVSHDRHLLRSttDDLYLVHDGK 504
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
536-591 |
5.33e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 5.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 536 LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD----VEDYIYSHCRKVGITLFTVSHR 591
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
418-564 |
8.83e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 44.62 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 418 DILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGElwplfgghLTKPERGKLFY-------------------VPQRPY 478
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFAR--------LLTPQSGTVFLgdkpismlssrqlarrlalLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 479 MTLG-TLRDQVIYPD-------GKEDQKKKGISDQVLKgyldNVQLGHILEReggwdSVQDwmdvLSGGEKQRMAMARLF 550
Cdd:PRK11231 87 TPEGiTVRELVAYGRspwlslwGRLSAEDNARVNQAME----QTRINHLADR-----RLTD----LSGGQRQRAFLAMVL 153
|
170
....*....|....
gi 1958749229 551 YHKPQFAILDECTS 564
Cdd:PRK11231 154 AQDTPVVLLDEPTT 167
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
421-590 |
1.00e-04 |
|
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: 44.26 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELwplfgghltKPERGKLfyvpqrpymtlgTLRDQVIypDGKEDQK- 498
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFY---------RPTSGRI------------LFDGRDI--TGLPPHRi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 499 -KKGIS-----DQVLKGY--LDNVQLG-HILEREGGWDSV--------------------------QDWMDV----LSGG 539
Cdd:COG0411 77 aRLGIArtfqnPRLFPELtvLENVLVAaHARLGRGLLAALlrlprarreereareraeellervglADRADEpagnLSYG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958749229 540 EKQRMAMARLFYHKPQFAILDECTSAVS----VDVEDYIYSHCRKVGITLFTVSH 590
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNpeetEELAELIRRLRDERGITILLIEH 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
422-469 |
2.28e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.15 E-value: 2.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1958749229 422 QDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfGghLTKPERGK 469
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIA------G--ILEPTSGR 82
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
422-566 |
2.58e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 422 QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLT------------KPERGKLFYVPQRPYMTLGTLRDQVI 489
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnlkdinlKWWRSKIGVVSQDPLLFSNSIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 490 YP-------------------DGKEDQKKKGISDQVLKGYLDNV----QLGHILEREGGWDSVQDW--MDV--------- 535
Cdd:PTZ00265 482 YSlyslkdlealsnyynedgnDSQENKNKRNSCRAKCAGDLNDMsnttDSNELIEMRKNYQTIKDSevVDVskkvlihdf 561
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958749229 536 ------------------LSGGEKQRMAMARLFYHKPQFAILDECTSAV 566
Cdd:PTZ00265 562 vsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
427-571 |
2.59e-04 |
|
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: 43.17 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 427 EVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGHLTkpERGKLFYVPQrpYMTL---GTLRDQViypdgKEDQKKKGI 502
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLaGVLKPDEGDIEI--ELDTVSYKPQ--YIKAdyeGTVRDLL-----SSITKDFYT 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749229 503 SDQVLKGYLDNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDEcTSAvSVDVE 571
Cdd:cd03237 92 HPYFKTEIAKPLQIEQILDRE-----VPE----LSGGELQRVAIAACLSKDADIYLLDE-PSA-YLDVE 149
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
422-568 |
2.60e-04 |
|
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: 43.90 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 422 QDLSFEVRSGANVLICGPNGCGKSSLFRVL-------GELWplFGGH----LT----KPERGKLFYVPQRPY------MT 480
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALlrlipseGEIR--FDGQdldgLSrralRPLRRRMQVVFQDPFgslsprMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 481 LGtlrdQVI-------YPDGKEDQKKKGISDQvlkgyLDNVQL-GHILER---EggwdsvqdwmdvLSGGEKQRMAMARL 549
Cdd:COG4172 381 VG----QIIaeglrvhGPGLSAAERRARVAEA-----LEEVGLdPAARHRyphE------------FSGGQRQRIAIARA 439
|
170 180
....*....|....*....|.
gi 1958749229 550 FYHKPQFAILDECTSA--VSV 568
Cdd:COG4172 440 LILEPKLLVLDEPTSAldVSV 460
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
421-575 |
7.59e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPERGKLFYVPQRpymtlgTLRDQVIYPdgKEDQKKK 500
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD------GLANGIVYI--SEDRKRD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 501 GIsdqVLK------------GYLDN--VQLGHILEREggwdSVQDWMDV--------------LSGGEKQRMAMARLFYH 552
Cdd:PRK10762 340 GL---VLGmsvkenmsltalRYFSRagGSLKHADEQQ----AVSDFIRLfniktpsmeqaiglLSGGNQQKVAIARGLMT 412
|
170 180
....*....|....*....|...
gi 1958749229 553 KPQFAILDECTSAVSVDVEDYIY 575
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIY 435
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
416-566 |
8.43e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 41.66 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 416 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHL---------TKPERGKLFYVPQrpymtlgtLRD 486
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtARSLSQQKGLIRQ--------LRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 487 QV--------IYPdgkedqkKKGISDQVLKGYL--------DNVQLGHILEREGGWDSVQD-WMDVLSGGEKQRMAMARL 549
Cdd:PRK11264 86 HVgfvfqnfnLFP-------HRTVLENIIEGPVivkgepkeEATARARELLAKVGLAGKETsYPRRLSGGQQQRVAIARA 158
|
170
....*....|....*..
gi 1958749229 550 FYHKPQFAILDECTSAV 566
Cdd:PRK11264 159 LAMRPEVILFDEPTSAL 175
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
404-590 |
9.31e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 41.64 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 404 IIKFDHVPLA----TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFG----GHLT----------K 464
Cdd:PRK13643 1 MIKFEKVNYTyqpnSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLnGLLQPTEGkvtvGDIVvsstskqkeiK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 465 PER---GKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKKKgiSDQVLKGYLDNVQLGHILEREGGWDsvqdwmdvLSGGEK 541
Cdd:PRK13643 81 PVRkkvGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEK--AEKIAAEKLEMVGLADEFWEKSPFE--------LSGGQM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958749229 542 QRMAMARLFYHKPQFAILDECTSAVSVDVE---DYIYSHCRKVGITLFTVSH 590
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
415-561 |
9.64e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.75 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 415 PNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGG----HLTKPERGkLFYVPQR----PY 478
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagleritsGEIW--IGGrvvnELEPADRD-IAMVFQNyalyPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 479 MtlgTLRDQVIYpdGKEDQK--KKGISDQVLKGyLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMARLFYHK 553
Cdd:PRK11650 91 M---SVRENMAY--GLKIRGmpKAEIEERVAEA-ARILELEPLLDRkprE------------LSGGQRQRVAMGRAIVRE 152
|
....*...
gi 1958749229 554 PQFAILDE 561
Cdd:PRK11650 153 PAVFLFDE 160
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
421-567 |
1.20e-03 |
|
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: 40.57 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 421 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGHLTKPERGKLF----YVPQR----PYMtlgTLRD 486
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLtGELRPtsgtaYINGYSIRTDRKAARqslgYCPQFdalfDEL---TVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 487 QV-IYpdgkedQKKKGIS----DQVLKGYLDNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDE 561
Cdd:cd03263 95 HLrFY------ARLKGLPkseiKEEVELLLRVLGLTDKANKR-----ART----LSGGMKRKLSLAIALIGGPSVLLLDE 159
|
....*.
gi 1958749229 562 CTSAVS 567
Cdd:cd03263 160 PTSGLD 165
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-607 |
1.74e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.85 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 520 LEREGGWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSHR 591
Cdd:PRK14271 144 LTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALdpttTEKIEEFIRSLADRLTVIIVTHNLA 223
|
90
....*....|....*.
gi 1958749229 592 KSLWKHHEYYLHMDGR 607
Cdd:PRK14271 224 QAARISDRAALFFDGR 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
420-603 |
2.71e-03 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 39.95 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 420 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggHLTKPERGKLFYVPQRPYMtlgtLRD---QVIYPDGKED 496
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCIN--------FLEKPSEGSIVVNGQTINL----VRDkdgQLKVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749229 497 QKKKGISDQVLKGY--------LDNVQLGHI-----------------LEREGGWDSVQDWMDV-LSGGEKQRMAMARLF 550
Cdd:PRK10619 88 RLLRTRLTMVFQHFnlwshmtvLENVMEAPIqvlglskqeareravkyLAKVGIDERAQGKYPVhLSGGQQQRVSIARAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749229 551 YHKPQFAILDECTSAVSVDVEDYIYSHCRKV---GITLFTVSHRKSLWKH---HEYYLH 603
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHvssHVIFLH 226
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
533-580 |
3.49e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 39.48 E-value: 3.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749229 533 MDVLSGGEKQRMAMARLF----YHKPQFAILDECTSA---VSVD-VEDYIYSHCRK 580
Cdd:cd03275 153 MDNLSGGEKTMAALALLFaihsYQPAPFFVLDEVDAAldnTNVGkVASYIREQAGP 208
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
421-451 |
5.93e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.22 E-value: 5.93e-03
10 20 30
....*....|....*....|....*....|.
gi 1958749229 421 IQDLSFEVRSGANVLIcGPNGCGKSSLFRVL 451
Cdd:COG3593 14 IKDLSIELSDDLTVLV-GENNSGKSSILEAL 43
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
536-590 |
6.73e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 38.88 E-value: 6.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749229 536 LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV----GITLFTVSH 590
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSH 203
|
|
| |
