|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-647 |
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: 1087.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 1 MAAFSKYLTARNTSL--------AGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEK----EGKKERAVVDKVFLSRLS 68
Cdd:TIGR00954 1 MAVLSKYRLLRSTSNnktdkqdsPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKhstiEGAKKKAHVNGVFLGKLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 69 QILKIMVPRTFCKETGYLLLIAVMLVSRTYCDVWMIQNGTLIESGIISRSVALFKESFFKFVAATPLISLVNNFLKYGLN 148
Cdd:TIGR00954 81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 149 ELKLCFRVRLTRYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQ 228
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 229 GPASMMAYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHNFIF 308
Cdd:TIGR00954 241 GPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 309 FRFSMGFIDSIIAKYVATVVGYLVVSRPFLDLAHPRHLHSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFT 388
Cdd:TIGR00954 321 FRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 389 ARITELMQVLKDLNHGRYERTMVSQQEKGIEGAQASPLVPGAGEIINTDNIIKFDHVPLATPNGDILIQDLSFEVRSGAN 468
Cdd:TIGR00954 401 ARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 469 VLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKKRGISDQVLKEYLDN 548
Cdd:TIGR00954 481 LLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 549 VQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKVGITLFTVSHRKS 628
Cdd:TIGR00954 561 VQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKS 640
|
650
....*....|....*....
gi 1907149462 629 LWKHHEYYLHMDGRGNYEF 647
Cdd:TIGR00954 641 LWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
70-338 |
2.55e-123 |
|
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: 366.55 E-value: 2.55e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 70 ILKIMVPRTFCKETGYLLLIAVMLVSRTYCDVWMIQNGTLIESGIISRSVALFKESFFKFVAATPLISLVNNFLKYGLNE 149
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 150 LKLCFRVRLTRYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQG 229
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 230 PASMMAYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHNFIFF 309
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 1907149462 310 RFSMGFIDSIIAKYVATVVGYLVVSRPFL 338
Cdd:pfam06472 241 RLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
84-650 |
2.51e-100 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 317.90 E-value: 2.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 84 GYLLLIAVMLVSRTYCDVWMI-QNGTLIESgIISRSVALFKESFFKF---VAATPLISLVNNFLKYGLnELKLcfRVRLT 159
Cdd:COG4178 25 GLLALLLLLTLASVGLNVLLNfWNRDFYDA-LQARDAAAFWQQLGVFallAAISILLAVYQTYLRQRL-QIRW--REWLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 160 RYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQG---------- 229
Cdd:COG4178 101 ERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLISFIGILWSLSGSLTftlggysiti 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 230 PASMM----AYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHN 305
Cdd:COG4178 181 PGYMVwaalIYAIIGTLLTHLIGRPLIRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 306 FIFFRFSMGFIDSIIAkYVATVVGYLVVSrpfldlahPRhlhsthselledyYQSGRM----LLRMSQALGRIVLAGR-- 379
Cdd:COG4178 261 LIRRQRNLTFFTTGYG-QLAVIFPILVAA--------PR-------------YFAGEItlggLMQAASAFGQVQGALSwf 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 380 --EMTRLAGFTA---RITELMQVLkdlnhgryertmvsqqekgiEGAQASPLVPGAGEIINTDNIIkFDHVPLATPNGDI 454
Cdd:COG4178 319 vdNYQSLAEWRAtvdRLAGFEEAL--------------------EAADALPEAASRIETSEDGALA-LEDLTLRTPDGRP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGKEDqkk 534
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA--- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 535 rgISDQVLKEYLDNVQLGHILEReggWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCR 614
Cdd:COG4178 455 --FSDAELREALEAVGLGHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
570 580 590
....*....|....*....|....*....|....*...
gi 1907149462 615 K--VGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKKI 650
Cdd:COG4178 530 EelPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPA 567
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
440-645 |
2.09e-87 |
|
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: 270.18 E-value: 2.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTL 519
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 520 RDQVIYPdgkedqkkrgisdqvlkeyldnvqlghilereggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:cd03223 81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907149462 600 AVSVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNY 645
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
440-625 |
7.36e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.22 E-value: 7.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILiQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFYV 508
Cdd:COG4619 1 LELEGLSFRVGGKPIL-SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsamPPPewRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 509 PQRPYMTLGTLRDQVIYPDgkeDQKKRGISDQVLKEYLDNVQLGH-ILEREggwdsVQDwmdvLSGGEKQRMAMARLFYH 587
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPF---QLRERKFDRERALELLERLGLPPdILDKP-----VER----LSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907149462 588 KPQFAILDECTSA---VSVD-VEDYIYSHCRKVGITLFTVSH 625
Cdd:COG4619 148 QPDVLLLDEPTSAldpENTRrVEELLREYLAEEGRAVLWVSH 189
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
84-626 |
4.22e-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: 4.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 84 GYLLLIAVMLVSRTYCDVWMIQ-NGTLIESGIISRSVALFKESFFKFVAATPLISLVNNFLKYGLNelKLCFRV--RLTR 160
Cdd:COG1132 21 GLLILALLLLLLSALLELLLPLlLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLA--RLAQRVvaDLRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 161 YLYEEYL-QAFTYY---KMGNLDNRIanpdqllTQDVekfcNSVVDLYSNLskpFLDIVLYIFKLTSAIGaqgpasMMAY 236
Cdd:COG1132 99 DLFEHLLrLPLSFFdrrRTGDLLSRL-------TNDV----DAVEQFLAHG---LPQLVRSVVTLIGALV------VLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 237 L------------LVSGLFLTRLRRPIGKMTIMEQKYEGEyryVNSRL---ITNSEEIAFYNGNKREKQTIHSVFRKLVE 301
Cdd:COG1132 159 IdwrlalivllvlPLLLLVLRLFGRRLRKLFRRVQEALAE---LNGRLqesLSGIRVVKAFGREERELERFREANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 302 HLHNFIF----FRFSMGFIDSIIAKYVATVVGYLVVSRpfldlahprhlHSTHSELLEdYYQSGRMLLRMSQALGRIVla 377
Cdd:COG1132 236 ANLRAARlsalFFPLMELLGNLGLALVLLVGGLLVLSG-----------SLTVGDLVA-FILYLLRLFGPLRQLANVL-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 378 gREMTRLAGFTARITELMqvlkdlnhgryertmvSQQEKGIEGAQASPLVPGAGEIintdniiKFDHVPLATPNGDILIQ 457
Cdd:COG1132 302 -NQLQRALASAERIFELL----------------DEPPEIPDPPGAVPLPPVRGEI-------EFENVSFSYPGDRPVLK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 458 DLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFYVPQRPYMTLGTLRDQVIYp 526
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdirdlTLEslRRQIGVVPQDTFLFSGTIRENIRY- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 527 dGKEDqkkrgISDQVLKEYLDNVQLGHILER-EGGWDSVqdwmdV------LSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:COG1132 437 -GRPD-----ATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGGQRQRIAIARALLKDPPILILDEATS 505
|
570 580
....*....|....*....|....*....
gi 1907149462 600 AVSVDVEDYIYSHCRKV--GITLFTVSHR 626
Cdd:COG1132 506 ALDTETEALIQEALERLmkGRTTIVIAHR 534
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
455-641 |
1.77e-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: 107.17 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLfGGRLTKPerGKLFYVPQRPYMTLGTLRDQVIYpdGKEDQK 533
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKL-SGSVSVP--GSIAYVSQEPWIQNGTIRENILF--GKPFDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 534 KRgiSDQVLK-----------EYLDNVQLGhilerEGGwdsvqdwmdV-LSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:cd03250 95 ER--YEKVIKacalepdleilPDGDLTEIG-----EKG---------InLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907149462 602 SVDVEDYIYSHC----RKVGITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:cd03250 159 DAHVGRHIFENCilglLLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
440-629 |
6.64e-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: 6.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFY 507
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdlDLEslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 508 VPQRPYMTLGTLRDqviypdgkedqkkrgisdqvlkeyldNVqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYH 587
Cdd:cd03228 81 VPQDPFLFSGTIRE--------------------------NI---------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907149462 588 KPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSL 629
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALakGKTVIVIAHRLST 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
440-641 |
2.25e-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: 110.62 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFYV 508
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdlDPAswRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 509 PQRPYMTLGTLRDQV-IYpdgkedqkKRGISDQVLKEYLDNVQLGHILER-EGGWDSVqdwmdV------LSGGEKQRMA 580
Cdd:COG4988 417 PQNPYLFAGTIRENLrLG--------RPDASDEELEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRLA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907149462 581 MARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDD 546
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
371-629 |
1.64e-23 |
|
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: 104.68 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 371 LGRIVLAGReMTRLAGFTARI--TELMQVLKDLN---HGRYERTMVSQQEKGIEGAQASPLVPGAGEIINTDNIIKFDHV 445
Cdd:TIGR02857 249 IGFRLLAGD-LDLATGLFVLLlaPEFYLPLRQLGaqyHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 446 PLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL-----------TKPERGKLFYVPQRPYM 514
Cdd:TIGR02857 328 SVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadADSWRDQIAWVPQHPFL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 515 TLGTLRDQVIY--PDGKEDQKKRGISDQVLKEYLDNVQLGhiLEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFA 592
Cdd:TIGR02857 408 FAGTIAENIRLarPDASDAEIREALERAGLDEFVAALPQG--LDTPIGEGGAG-----LSGGQAQRLALARAFLRDAPLL 480
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907149462 593 ILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSL 629
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
418-626 |
1.73e-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: 104.85 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 418 IEGAQASPLVPGAGEIINTDNIIKFDHVPLATPNGD-ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGR 496
Cdd:COG4987 312 LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 497 LT--------KPE---RGKLFYVPQRPYMTLGTLRD--QVIYPDGKEDQkkrgisdqvLKEYLDNVQLGHILER-EGGWD 562
Cdd:COG4987 392 ITlggvdlrdLDEddlRRRIAVVPQRPHLFDTTLREnlRLARPDATDEE---------LWAALERVGLGDWLAAlPDGLD 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 563 SvqdWMDV----LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHR 626
Cdd:COG4987 463 T---WLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHR 529
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
456-599 |
4.37e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 95.79 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLTKPE----RGKLFYVPQ--RPYMTLgTLRDQ 522
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPtegtilLDGQDLTDDErkslRKEIGYVFQdpQLFPRL-TVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907149462 523 VIYPDGKEDQKKRGISDQVlKEYLDNVQLGHILEReggwdSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARA-EEALEKLGLGDLADR-----PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
451-642 |
4.69e-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: 91.83 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFG-----GRLTKPERGKLFYVPQRPYMTLG---TLRD 521
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPTSGsirvfGKPLEKERKRIGYVPQRRSIDRDfpiSVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 522 QV-------IYPDGKEDQKKRGISDQVLKEyldnVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:cd03235 90 VVlmglyghKGLFRRLSKADKAKVDEALER----VGLSELADRQ---------IGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907149462 595 DECTSAVSVDVEDYIYSHCRKV---GITLFTVSH-RKSLWKHHEYYLHMDGR 642
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELrreGMTILVVTHdLGLVLEYFDRVLLLNRT 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
376-646 |
6.71e-21 |
|
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: 97.60 E-value: 6.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 376 LAGREMTRLAGFTARITELMQVLKDLNhgRYERTMVSQQEKGiEGAQASPLVPGAGEIintdniiKFDHVPLA-TPNGDI 454
Cdd:COG2274 420 LSGRFLAPVAQLIGLLQRFQDAKIALE--RLDDILDLPPERE-EGRSKLSLPRLKGDI-------ELENVSFRyPGDSPP 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLF-------------------YVPQRPYMT 515
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLL--------LGLYEPTSGRILidgidlrqidpaslrrqigVVLQDVFLF 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 516 LGTLRDQVIYpdGKEDqkkrgISDQVLKEYLDNVQLGH-ILEREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAI 593
Cdd:COG2274 562 SGTIRENITL--GDPD-----ATDEEIIEAARLAGLHDfIEALPMGYDTvVGEGGSNLSGGQRQRLAIARALLRNPRILI 634
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 594 LDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG-----RGNYE 646
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDKgriveDGTHE 694
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
451-625 |
9.51e-21 |
|
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: 92.03 E-value: 9.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGR----LTKPERGKLF-YVPQRPYMTLG-T 518
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALaGLLKPssgevLLDGRdlasLSRRELARRIaYVPQEPPAPFGlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 519 LRDQVI---YP-------DGKEDQKkrgISDQVLKEyldnVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHK 588
Cdd:COG1120 92 VRELVAlgrYPhlglfgrPSAEDRE---AVEEALER----TGLEHLADRP---------VDELSGGERQRVLIARALAQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907149462 589 PQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:COG1120 156 PPLLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLH 196
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
451-626 |
3.36e-20 |
|
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: 87.69 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLFYvpqrpymtlgtlrdqviypDGKE 530
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA--------GLLKPTSGEILI-------------------DGKD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 531 dqkkrgISDQVLKEYLDNVQLGHilereggwdsvQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD----VE 606
Cdd:cd00267 63 ------IAKLPLEELRRRIGYVP-----------Q-----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAsrerLL 120
|
170 180
....*....|....*....|
gi 1907149462 607 DYIYSHCRKvGITLFTVSHR 626
Cdd:cd00267 121 ELLRELAEE-GRTVIIVTHD 139
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
437-641 |
4.30e-20 |
|
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: 89.45 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 437 DNIIKFDHVPLATPN-GDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---KP--------ERG 503
Cdd:cd03248 9 KGIVKFQNVTFAYPTrPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPisqyehkyLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 504 KLFYVPQRPYMTLGTLRDQVIYpdgkedqkkrGISDQVLKEYLDNVQLGH----ILEREGGWDS-VQDWMDVLSGGEKQR 578
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAY----------GLQSCSFECVKEAAQKAHahsfISELASGYDTeVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907149462 579 MAMARLFYHKPQFAILDECTSAVSVDVEDYIYS--HCRKVGITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
440-628 |
6.27e-20 |
|
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: 89.21 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFYV 508
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 509 PQRPYMTLGTLRDQVIY--PDGKEDQ-----KKRGISDQvlkeyldnvqlghILEREGGWDSVqdwmdV------LSGGE 575
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYgrPDATDEEvieaaKAAQIHDK-------------IMRFPDGYDTI-----VgerglkLSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907149462 576 KQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKS 628
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
451-625 |
2.20e-19 |
|
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: 85.95 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLfYVPQRPYMTLgtlrdqviypDGKE 530
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTL--------AGLLKPSSGEI-LLDGKDLASL----------SPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 531 DQKKRGISDQVLKEyldnVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVE 606
Cdd:cd03214 71 LARKIAYVPQALEL----LGLAHLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLdiahQIELL 137
|
170
....*....|....*....
gi 1907149462 607 DYIYSHCRKVGITLFTVSH 625
Cdd:cd03214 138 ELLRRLARERGKTVVMVLH 156
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
451-625 |
3.71e-19 |
|
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: 86.38 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPE---RGKLFYVPQRP--YMTLg 517
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILagllppsaGEVL-WNGEPIRDARedyRRRLAYLGHADglKPEL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 518 TLRDQVIYpdgKEDQKKRGISDQVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDEC 597
Cdd:COG4133 91 TVRENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 1907149462 598 TSAVSVD----VEDYIYSHCRKVGITLFTvSH 625
Cdd:COG4133 159 FTALDAAgvalLAELIAAHLARGGAVLLT-TH 189
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
440-628 |
3.72e-19 |
|
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: 86.90 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFYV 508
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 509 PQRPYMTLGTLRDQVIYpdGKEDqkkrgISDQVLKEYLDNVQLGHILER-EGGWDS-VQDWMDVLSGGEKQRMAMARLFY 586
Cdd:cd03254 83 LQDTFLFSGTIMENIRL--GRPN-----ATDEEVIEAAKEAGAHDFIMKlPNGYDTvLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907149462 587 HKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKS 628
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLS 199
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
435-625 |
1.76e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 85.14 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 435 NTDNIIKFDHVPLATpNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRV-LGELWPL-----FGGRLTKPERGKLFYV 508
Cdd:COG1121 2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAiLGLLPPTsgtvrLFGKPPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 509 PQRPYMTLG---TLRDQV---IYPDGKEDQKKRGISDQVLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMA 582
Cdd:COG1121 81 PQRAEVDWDfpiTVRDVVlmgRYGRRGLFRRPSRADREAVDEALERVGLEDLADR---------PIGELSGGQQQRVLLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907149462 583 RLFYHKPQFAILDECTSAVSVDVEDYIYS---HCRKVGITLFTVSH 625
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTH 197
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
440-629 |
7.07e-18 |
|
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: 83.02 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDIL-IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLF------------ 506
Cdd:cd03245 3 IEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLA--------GLYKPTSGSVLldgtdirqldpa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 507 -------YVPQRPYMTLGTLRDQVI--YPDGKEDQKKRGISDQVLKEYLDNVQLGHILE-REGGwdsvqdwmDVLSGGEK 576
Cdd:cd03245 75 dlrrnigYVPQDVTLFYGTLRDNITlgAPLADDERILRAAELAGVTDFVNKHPNGLDLQiGERG--------RGLSGGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907149462 577 QRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSL 629
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
435-644 |
8.16e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.84 E-value: 8.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 435 NTDNIIKFDHVPLATpNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGR---LTKPE--RG 503
Cdd:PRK10247 3 ENSPLLQLQNVGYLA-GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISptsgtlLFEGEdisTLKPEiyRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 504 KLFYVPQRPYMTLGTLRDQVIYP---DGKEDQKKRGISDqvlkeyLDNVQLG-HILEReggwdSVQDwmdvLSGGEKQRM 579
Cdd:PRK10247 82 QVSYCAQTPTLFGDTVYDNLIFPwqiRNQQPDPAIFLDD------LERFALPdTILTK-----NIAE----LSGGEKQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907149462 580 AMARLFYHKPQFAILDECTSAVSVD----VEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGN 644
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAG 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
441-640 |
8.65e-18 |
|
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: 82.51 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 441 KFDHVPLATPNGD-ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFG-----GRLTKPE-----RGKLFYV 508
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnGLLGPTSGevlvdGKDLTKLslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 509 PQRPymtlgtlRDQVIYPDGKED----QKKRGIS----DQVLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMA 580
Cdd:cd03225 81 FQNP-------DDQFFGPTVEEEvafgLENLGLPeeeiEERVEEALELVGLEGLRDR-----SPFT----LSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907149462 581 MARLFYHKPQFAILDECTSavSVDvedyiYSHCRKV----------GITLFTVSHRKSLWKHH-EYYLHMD 640
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTA--GLD-----PAGRRELlellkklkaeGKTIIIVTHDLDLLLELaDRVIVLE 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
455-629 |
1.36e-17 |
|
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: 80.72 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTkpergkLFYVPQRPYmTLGTLRDQVIYpdgkedqkk 534
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR------LDGADISQW-DPNELGDHVGY--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 535 rgisdqvlkeYLDNVQL--GHILEreggwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYS- 611
Cdd:cd03246 81 ----------LPQDDELfsGSIAE------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQa 138
|
170 180
....*....|....*....|
gi 1907149462 612 --HCRKVGITLFTVSHRKSL 629
Cdd:cd03246 139 iaALKAAGATRIVIAHRPET 158
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
457-625 |
1.92e-17 |
|
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: 82.16 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 457 QDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRLTKPERGKLFY-----VPQRPYMTL---GTLR 520
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALaglerpwsGEV--TFDGRPVTRRRRKAFRrrvqmVFQDPYASLhprHTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 521 DQVIYP---DGKEDQKKRgisdqvLKEYLDNVQLG-HILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:COG1124 100 RILAEPlriHGLPDREER------IAELLEQVGLPpSFLDR---------YPHQLSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190
....*....|....*....|....*....|...
gi 1907149462 597 CTSA--VSVDVE--DYIYSHCRKVGITLFTVSH 625
Cdd:COG1124 165 PTSAldVSVQAEilNLLKDLREERGLTYLFVSH 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
440-626 |
3.41e-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: 81.00 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLA-TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFY 507
Cdd:cd03244 3 IEFKNVSLRyRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiglHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 508 VPQRPYMTLGTLRDQvIYPDGKEdqkkrgiSDQVLKEYLDNVQL-GHILEREGGWDS-VQDWMDVLSGGEKQRMAMARLF 585
Cdd:cd03244 83 IPQDPVLFSGTIRSN-LDPFGEY-------SDEELWQALERVGLkEFVESLPGGLDTvVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907149462 586 YHKPQFAILDECTSavSVDVE------DYIYSHCRkvGITLFTVSHR 626
Cdd:cd03244 155 LRKSKILVLDEATA--SVDPEtdaliqKTIREAFK--DCTVLTIAHR 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
451-625 |
3.45e-17 |
|
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: 81.07 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRltkPERGKLFY---------------------VP 509
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA---PDEGEVLLdgkdiydldvdvlelrrrvgmVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 510 QRPYMTLGTLRDQVIYPdgkedQKKRGISDQVLKEYLdnVQlgHILEREGGWDSVQDWMDV--LSGGEKQRMAMARLFYH 587
Cdd:cd03260 88 QKPNPFPGSIYDNVAYG-----LRLHGIKLKEELDER--VE--EALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALAN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907149462 588 KPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLftVSH 625
Cdd:cd03260 159 EPEVLLLDEPTSALdpisTAKIEELIAELKKEYTIVI--VTH 198
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
369-626 |
6.88e-17 |
|
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: 83.95 E-value: 6.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 369 QALGRIVLAGREMTRLAGFTARITELMqvlkdlnhgryertmvsqqekGIEGAQASPLVPGAGEIINTDNIIKFDHVPLA 448
Cdd:TIGR02868 285 EAFAALPAAAQQLTRVRAAAERIVEVL---------------------DAAGPVAEGSAPAAGAVGLGKPTLELRDLSAG 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 449 TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFYVPQRPYMTLG 517
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvssldqDEVRRRVSVCAQDAHLFDT 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 518 TLRDQVIYpdGKEDqkkrgISDQVLKEYLDNVQLG-HILEREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:TIGR02868 424 TVRENLRL--ARPD-----ATDEELWAALERVGLAdWLRALPDGLDTvLGEGGARLSGGERQRLALARALLADAPILLLD 496
|
250 260 270
....*....|....*....|....*....|...
gi 1907149462 596 ECTSAVSVDVEDYIYSHCRKV--GITLFTVSHR 626
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAAlsGRTVVLITHH 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
452-596 |
1.12e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELwPLFGGRLTKPERGKLFYVPQRPYMTLG-TLRDQVIYPDGK 529
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILaGEL-EPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLDGDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 530 EDQKKR---------GISDQVLKEYLDnvqLGHILEREGGWD--------------SVQDW---MDVLSGGEKQRMAMAR 583
Cdd:COG0488 89 LRALEAeleeleaklAEPDEDLERLAE---LQEEFEALGGWEaearaeeilsglgfPEEDLdrpVSELSGGWRRRVALAR 165
|
170
....*....|...
gi 1907149462 584 LFYHKPQFAILDE 596
Cdd:COG0488 166 ALLSEPDLLLLDE 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
440-625 |
2.20e-16 |
|
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: 78.91 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRLTKPERGKLF----- 506
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsGEV--LVDGKDITKKNLRELrrkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 507 YVPQRPymtlgtlRDQVIYPDGKED----QKKRGIS----DQVLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQR 578
Cdd:COG1122 79 LVFQNP-------DDQLFAPTVEEDvafgPENLGLPreeiRERVEEALELVGLEHLADR-----PPHE----LSGGQKQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907149462 579 MAMARLFYHKPQFAILDECTSAV----SVDVEDYIYShCRKVGITLFTVSH 625
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLdprgRRELLELLKR-LNKEGKTVIIVTH 192
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
440-641 |
2.73e-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: 78.68 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLA-TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGR---------LTKPE--RGKLFY 507
Cdd:cd03252 1 ITFEHVRFRyKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlvdghdlaLADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 508 VPQRPYMTLGTLRDQVIYPDGKEDQKKrgisdqvlKEYLDNVQLGH--ILEREGGWDSVQDWMDV-LSGGEKQRMAMARL 584
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMER--------VIEAAKLAGAHdfISELPEGYDTIVGEQGAgLSGGQRQRIAIARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907149462 585 FYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
440-629 |
4.81e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.08 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPN-GDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLF 506
Cdd:TIGR00958 479 IEFQDVSFSYPNrPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgvplvqydhHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 507 YVPQRPYMTLGTLRDQVIYpdGKEDQKKRGISDQVLKEYLDNVqlghILEREGGWDSVQDWMDV-LSGGEKQRMAMARLF 585
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAY--GLTDTPDEEIMAAAKAANAHDF----IMEFPNGYDTEVGEKGSqLSGGQKQRIAIARAL 632
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907149462 586 YHKPQFAILDECTSAVSVDVEDYIYSHCRKVGITLFTVSHRKSL 629
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLST 676
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
440-642 |
7.95e-16 |
|
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: 76.76 E-value: 7.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILIQ---DLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------KPERGKLF-- 506
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdiskLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 507 -----YVPQR----PYMTLgtlRDQVIYP-----DGKEDQKKRgisdqvLKEYLDNVQLGHILEREGGWdsvqdwmdvLS 572
Cdd:cd03255 81 rrhigFVFQSfnllPDLTA---LENVELPlllagVPKKERRER------AEELLERVGLGDRLNHYPSE---------LS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907149462 573 GGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHM-DGR 642
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELrDGK 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
422-626 |
8.46e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.02 E-value: 8.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 422 QASPLV--PGAGEIINTDNIIKFDHVPLATPNG-DILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELW 490
Cdd:PRK11160 319 EQKPEVtfPTTSTAAADQVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtrawdpqqGEIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 491 pLFGGRLTK-PE---RGKLFYVPQRPYMTLGTLRDQVIYPDGKedqkkrgISDQVLKEYLDNVQLGHILEREGGWDSvqd 566
Cdd:PRK11160 399 -LNGQPIADySEaalRQAISVVSQRVHLFSATLRDNLLLAAPN-------ASDEALIEVLQQVGLEKLLEDDKGLNA--- 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907149462 567 WMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYS----HCRkvGITLFTVSHR 626
Cdd:PRK11160 468 WLGeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILEllaeHAQ--NKTVLMITHR 533
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
455-600 |
8.76e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.46 E-value: 8.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLT--KPE-----RGKLfyvPQRPYMTLG-TL 519
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELTPssgevrLNGRPLAawSPWelarrRAVL---PQHSSLAFPfTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 520 RdQVI----YPDGKEDQKKRGISDQVLKEyldnVQLGHILEReggwdSVQDwmdvLSGGEKQRMAMARLF-------YHK 588
Cdd:COG4559 93 E-EVValgrAPHGSSAAQDRQIVREALAL----VGLAHLAGR-----SYQT----LSGGEQQRVQLARVLaqlwepvDGG 158
|
170
....*....|..
gi 1907149462 589 PQFAILDECTSA 600
Cdd:COG4559 159 PRWLFLDEPTSA 170
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
451-625 |
1.25e-15 |
|
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: 75.30 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLFyvpqrpymtlgtLRDQVIYPDGKE 530
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA--------GLEEPDSGSIL------------IDGEDLTDLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 531 DQKKRGISDQVLKEY--------LDNVQLGhilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSA-- 600
Cdd:cd03229 71 LPPLRRRIGMVFQDFalfphltvLENIALG------------------LSGGQQQRVALARALAMDPDVLLLDEPTSAld 132
|
170 180
....*....|....*....|....*..
gi 1907149462 601 --VSVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:cd03229 133 piTRREVRALLKSLQAQLGITVVLVTH 159
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
440-625 |
1.32e-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: 76.36 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDIL---IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPERGklfY 507
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgpGPDRG---Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 508 VPQR----PYMtlgTLRDQVIYPDGKEDQKKRGISDQVLkEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMAR 583
Cdd:cd03293 78 VFQQdallPWL---TVLDNVALGLELQGVPKAEARERAE-ELLELVGLSGFENA---------YPHQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907149462 584 LFYHKPQFAILDECTSAVSV----DVEDYIYSHCRKVGITLFTVSH 625
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTH 190
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
440-628 |
2.08e-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: 76.12 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFY 507
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 508 VPQRPYMTLGTLRDQVIYpdgkedqkkrGISDQVLKEYLDNVQLGH----ILEREGGWDSVQDWMDV-LSGGEKQRMAMA 582
Cdd:cd03251 81 VSQDVFLFNDTVAENIAY----------GRPGATREEVEEAARAANahefIMELPEGYDTVIGERGVkLSGGQRQRIAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907149462 583 RLFYHKPQFAILDECTSAVSVDVEDYIYSHCRK--VGITLFTVSHRKS 628
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERlmKNRTTFVIAHRLS 198
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
440-628 |
4.88e-15 |
|
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: 74.88 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPN--GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLF 506
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvdirdlnlRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 507 YVPQRPYMTLGTLRDQVIYpdGKEDQKKRGISDQVLKEYLDNVqlghILEREGGWDSV------QdwmdvLSGGEKQRMA 580
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRY--GKPDATDEEVEEAAKKANIHDF----IMSLPDGYDTLvgergsQ-----LSGGQKQRIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907149462 581 MARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKS 628
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAHRLS 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
438-625 |
7.10e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 438 NIIKFDHVPLATPNGDILiQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLfGGRLTKPERGKLFYVPQR----P 512
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAPD-EGVIKRNGKLRIGYVPQKlyldT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 513 YMTLGTLRDQVIYPdgkedqkkrGISDQVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFA 592
Cdd:PRK09544 81 TLPLTVNRFLRLRP---------GTKKEDILPALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907149462 593 ILDECTSAVSVD----VEDYIYSHCRKVGITLFTVSH 625
Cdd:PRK09544 143 VLDEPTQGVDVNgqvaLYDLIDQLRRELDCAVLMVSH 179
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
451-625 |
8.62e-15 |
|
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: 73.71 E-value: 8.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGR-LTK--PERGKLFYVPQR----PYMt 515
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaglerpdsGEI--LIDGRdVTGvpPERRNIGMVFQDyalfPHL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 516 lgTLRDQVIYPDGKEDQKKRGISDQVlKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:cd03259 88 --TVAENIAFGLKLRGVPKAEIRARV-RELLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190
....*....|....*....|....*....|....
gi 1907149462 596 ECTSAVSVDVEDYIYSH----CRKVGITLFTVSH 625
Cdd:cd03259 156 EPLSALDAKLREELREElkelQRELGITTIYVTH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
437-626 |
1.09e-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: 77.25 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 437 DNIIKFDHVPLATPNGDI-LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP---------LFGGR----LTKPER 502
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRdlleLSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 503 GKLF-YVPQRPYMTL--GTLRDQVIYPDGKEDQKKRGISDQVLkEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRM 579
Cdd:COG1123 82 GRRIgMVFQDPMTQLnpVTVGDQIAEALENLGLSRAEARARVL-ELLEAVGLERRLDR---------YPHQLSGGQRQRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907149462 580 AMARLFYHKPQFAILDECTSAVSVDVEDYIYSH----CRKVGITLFTVSHR 626
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLlrelQRERGTTVLLITHD 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
435-625 |
1.59e-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: 76.48 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 435 NTDNIIKFDHV----PLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------------GELWPLFGGR 496
Cdd:COG1123 256 AAEPLLEVRNLskryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLlgllrptsgsilfdGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 497 LTKPERGKLFYVPQRPYMTL---GTLRDQVIYP------DGKEDQKKRgisdqvLKEYLDNVQLG-HILER---Eggwds 563
Cdd:COG1123 336 SLRELRRRVQMVFQDPYSSLnprMTVGDIIAEPlrlhglLSRAERRER------VAELLERVGLPpDLADRyphE----- 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907149462 564 vqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSA--VSV--DVEDYIYSHCRKVGITLFTVSH 625
Cdd:COG1123 405 -------LSGGQRQRVAIARALALEPKLLILDEPTSAldVSVqaQILNLLRDLQRELGLTYLFISH 463
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
456-625 |
1.73e-14 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 73.17 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPE---RGKLFYVPQRP--YMTLgTLRDQ 522
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlgllrptsGEVR-VLGEDVARDPaevRRRIGYVPQEPalYPDL-TVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 523 V-----IYPDGKEDQKKRgisdqvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDEC 597
Cdd:COG1131 94 LrffarLYGLPRKEARER------IDELLELFGLTDAADR---------KVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190
....*....|....*....|....*....|....
gi 1907149462 598 TSAvsVDVE------DYIYSHCRKvGITLFTVSH 625
Cdd:COG1131 159 TSG--LDPEarrelwELLRELAAE-GKTVLLSTH 189
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
370-618 |
2.41e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.94 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 370 ALGRIVLAGREMTRLAGFTAriTELMQVLK----------------DLNHGRYERTMVSQqEKGIegAQASPLVPGAGEI 433
Cdd:PLN03232 541 SFGVFVLLGGDLTPARAFTS--LSLFAVLRsplnmlpnllsqvvnaNVSLQRIEELLLSE-ERIL--AQNPPLQPGAPAI 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 434 INTDNIIKFDhVPLATPNgdilIQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGRLTKpeRGKLFYVPQRP 512
Cdd:PLN03232 616 SIKNGYFSWD-SKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI--RGSVAYVPQVS 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 513 YMTLGTLRDQVIYPDGKEDQKK-RGISDQVLKEYLDnVQLGHILErEGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQF 591
Cdd:PLN03232 689 WIFNATVRENILFGSDFESERYwRAIDVTALQHDLD-LLPGRDLT-EIGERGVN-----ISGGQKQRVSMARAVYSNSDI 761
|
250 260
....*....|....*....|....*..
gi 1907149462 592 AILDECTSAVSVDVEDYIYSHCRKVGI 618
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFDSCMKDEL 788
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
456-604 |
2.65e-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: 72.97 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLTKPE---RGKLFYVPQRPYMTLG-TLRDQV- 523
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLKPdsgsilIDGEDVRKEPreaRRQIGVLPDERGLYDRlTVRENIr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 524 ----IYPDGKEDQKKRgisdqvLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:COG4555 97 yfaeLYGLFDEELKKR------IEELIELLGLEEFLDR-----RVGE----LSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
....*
gi 1907149462 600 AVSVD 604
Cdd:COG4555 162 GLDVM 166
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
436-596 |
4.27e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.81 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 436 TDNIIKFDHVPLA--TPNGDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKP--ER 502
Cdd:COG1116 4 AAPALELRGVSKRfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptsGEVL-VDGKPVTGPgpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 503 GklfYVPQR----PYMTLgtlRDQVIYPdgkedQKKRGIS----DQVLKEYLDNVQLGHILEReggwdsvqdWMDVLSGG 574
Cdd:COG1116 83 G---VVFQEpallPWLTV---LDNVALG-----LELRGVPkaerRERARELLELVGLAGFEDA---------YPHQLSGG 142
|
170 180
....*....|....*....|..
gi 1907149462 575 EKQRMAMARLFYHKPQFAILDE 596
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDE 164
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
456-625 |
8.19e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 71.23 E-value: 8.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGR----LTKPERGKL------FyVPQR----PY 513
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrptsGEVL--IDGQdissLSERELARLrrrhigF-VFQFfnllPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 514 MTLgtlRDQVIYP------DGKEDQKKrgisdqvLKEYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMARL 584
Cdd:COG1136 101 LTA---LENVALPlllagvSRKERRER-------ARELLERVGLGDRLDHrpsQ------------LSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907149462 585 FYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:COG1136 159 LVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTH 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
452-596 |
8.67e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQRpymtlgtlRDQViypdgke 530
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPD-SGTVKLGETVKIGYFDQH--------QEEL------- 390
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907149462 531 DQKKRGIsdQVLKEYLDNVQLGHI---LER---EGgwDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:COG0488 391 DPDKTVL--DELRDGAPGGTEQEVrgyLGRflfSG--DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
439-625 |
1.03e-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: 71.00 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 439 IIKFDHVPLATPNGDI---LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------------GELWPLFGGRLTKPE 501
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsgsiifdGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 502 RGKLFYVPQRPY------MTLGT-LRD--QVIYPDGKEDQKKRgisdqvlKEYLDNVQLG---HILER---Eggwdsvqd 566
Cdd:cd03257 81 RKEIQMVFQDPMsslnprMTIGEqIAEplRIHGKLSKKEARKE-------AVLLLLVGVGlpeEVLNRyphE-------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907149462 567 wmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSH----CRKVGITLFTVSH 625
Cdd:cd03257 146 ----LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkklQEELGLTLLFITH 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
449-646 |
1.28e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 449 TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-------GELwpLFGG----RLTKPE-RGKLFYVPQRPYMTL 516
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpyqGSL--KINGielrELDPESwRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 517 GTLRDQVIYpdGKEDqkkrgISDQVLKEYLDNVQLGHILER-EGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:PRK11174 437 GTLRDNVLL--GNPD-----ASDEQLQQALENAWVSEFLPLlPQGLDTpIGDQAAGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907149462 595 DECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG-----RGNYE 646
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQLEDLAQWDQIWVMQDgqivqQGDYA 568
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
450-601 |
1.49e-13 |
|
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: 69.76 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 450 PNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPERGKLFYVPQRPYMTLGTLRDQV 523
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLnGLLRPqsgavLIDGEPLDYSRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 524 IYPDGKED----QKKRGISD----QVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:TIGR01166 82 FAADVDQDvafgPLNLGLSEaeveRRVREALTAVGASGLRERP---------THCLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
....*.
gi 1907149462 596 ECTSAV 601
Cdd:TIGR01166 153 EPTAGL 158
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
451-620 |
1.54e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGklfyvpqrpyMTLGTLRDQVIYPdGKE 530
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----------IDDPDVAEACHYL-GHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 531 DQKK---------------RGISDQVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLF-YHKPQFaIL 594
Cdd:PRK13539 82 NAMKpaltvaenlefwaafLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARLLvSNRPIW-IL 151
|
170 180 190
....*....|....*....|....*....|
gi 1907149462 595 DECTSAVSVD----VEDYIYSHCRKVGITL 620
Cdd:PRK13539 152 DEPTAALDAAavalFAELIRAHLAQGGIVI 181
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
154-640 |
2.07e-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: 73.21 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 154 FRVRLtrylYEEYLQA----FTYYKMGNLDNRIanpdqllTQDVEKFCNSVVDLYSNLSKP-----FLDIVL--YIFKLT 222
Cdd:TIGR02203 89 IRVRM----FEKLLGLpvsfFDRQPTGTLLSRI-------TFDSEQVASAATDAFIVLVREtltviGLFIVLlyYSWQLT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 223 SAIGAQGPASMmaylLVSGLFLTRLRRPIGKMtimeQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQtihsvfrklveh 302
Cdd:TIGR02203 158 LIVVVMLPVLS----ILMRRVSKRLRRISKEI----QNSMGQVTTVAEETLQGYRVVKLFGGQAYETR------------ 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 303 lhnfiffRFsmGFIDSIIAKYVatvvgylvvsrpfLDLAHPRHLHSTHSELLEDYYQSGRMLLRMSQALGRIVLAGremt 382
Cdd:TIGR02203 218 -------RF--DAVSNRNRRLA-------------MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAG---- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 383 rlaGFTARITELMQVLKDLNHgryeRTMVSQQ-EKGIEGAQA------SPLVPGAG--EIINTDNIIKFDHVPLATPNGD 453
Cdd:TIGR02203 272 ---DFTAFITAMIALIRPLKS----LTNVNAPmQRGLAAAESlftlldSPPEKDTGtrAIERARGDVEFRNVTFRYPGRD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 454 I-LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFYVPQRPYMTLGTLRD 521
Cdd:TIGR02203 345 RpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILldghdladytlASLRRQVALVSQDVVLFNDTIAN 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 522 QVIYPDGKE---DQKKRGISDQVLKEYLDNVQLGhiLEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:TIGR02203 425 NIAYGRTEQadrAEIERALAAAYAQDFVDKLPLG--LDTPIGENGVL-----LSGGQRQRLAIARALLKDAPILILDEAT 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1907149462 599 SAVSVDVEDYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMD 640
Cdd:TIGR02203 498 SALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVMD 541
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
447-640 |
3.13e-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: 72.85 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 447 LATPNGDILIQDLSFEVRSGANVL--------------ICGPNGCGKSSLFRVL--------GELwpLFGGRLTK----- 499
Cdd:TIGR01193 467 LNNLNGDIVINDVSYSYGYGSNILsdisltikmnskttIVGMSGSGKSTLAKLLvgffqarsGEI--LLNGFSLKdidrh 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 500 PERGKLFYVPQRPYMTLGTLRDQVIY---PDGKEDQKKRGISDQVLKEYLDNVQLGH--ILEREGGwdsvqdwmdVLSGG 574
Cdd:TIGR01193 545 TLRQFINYLPQEPYIFSGSILENLLLgakENVSQDEIWAACEIAEIKDDIENMPLGYqtELSEEGS---------SISGG 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907149462 575 EKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKVG-ITLFTVSHRKSLWKHHEYYLHMD 640
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
428-642 |
4.47e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 72.30 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 428 PGAGEIINTDNIIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------- 498
Cdd:PRK13657 323 PGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtv 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 499 --KPERGKLFYVPQRPYMTLGTLRD--QViypdGKEDQkkrgiSDQVLKEYLDNVQ-LGHILEREGGWDS-VQDWMDVLS 572
Cdd:PRK13657 403 trASLRRNIAVVFQDAGLFNRSIEDniRV----GRPDA-----TDEEMRAAAERAQaHDFIERKPDGYDTvVGERGRQLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 573 GGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEdyiyshcRKV---------GITLFTVSHRKSLWKHHEYYLHMD-GR 642
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETE-------AKVkaaldelmkGRTTFIIAHRLSTVRNADRILVFDnGR 546
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
455-625 |
7.57e-13 |
|
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: 68.05 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGRLTKPE--RGKLFYVPQRPYMTLG--TLRDQVI 524
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKessgsiLLNGKPIKAKerRKSIGYVMQDVDYQLFtdSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 525 YPDgKEDQKKRGISDQVLKEY-LDNVQLGHILEreggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVsv 603
Cdd:cd03226 95 LGL-KELDAGNEQAETVLKDLdLYALKERHPLS--------------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGL-- 157
|
170 180 190
....*....|....*....|....*....|
gi 1907149462 604 dveDY--------IYSHCRKVGITLFTVSH 625
Cdd:cd03226 158 ---DYknmervgeLIRELAAQGKAVIVITH 184
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
455-600 |
7.88e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.03 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFG---GRLTKPERGKLFYV-PQRPYMTLGTLRDQV 523
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPdsgevrLNGrplADWSPAELARRRAVlPQHSSLSFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 524 I----YPDGKEDQKKRGISDQVLKEyldnVQLGHILEReggwdSVQdwmdVLSGGEKQRMAMARLF------YHKPQFAI 593
Cdd:PRK13548 97 VamgrAPHGLSRAEDDALVAAALAQ----VDLAHLAGR-----DYP----QLSGGEQQRVQLARVLaqlwepDGPPRWLL 163
|
....*..
gi 1907149462 594 LDECTSA 600
Cdd:PRK13548 164 LDEPTSA 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
439-598 |
7.99e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.16 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 439 IIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLTKPERGKLfyvpqr 511
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLyGEERPtsgqvlVNGQDLSRLKRREI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 512 PYmtlgtLRDQ--VIYPDGK--ED---------------QKKRGISDQVLkEYLDNVQLGHILEReggwdsvqdwM-DVL 571
Cdd:COG2884 75 PY-----LRRRigVVFQDFRllPDrtvyenvalplrvtgKSRKEIRRRVR-EVLDLVGLSDKAKA----------LpHEL 138
|
170 180
....*....|....*....|....*..
gi 1907149462 572 SGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:COG2884 139 SGGEQQRVAIARALVNRPELLLADEPT 165
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
437-625 |
1.05e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.06 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 437 DNIIKFDHVPLATPNGDI-LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP---------LFGGRLTKPE---- 501
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLLPddnpnskitVDGITLTAKTvwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 502 RGKLFYVPQRP--YMTLGTLRDQVIYpdGKEDqkkRGISDQVLKEYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRM 579
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAF--GLEN---RAVPRPEMIKIVRDV-----LADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907149462 580 AMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV----GITLFTVSH 625
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
440-625 |
1.07e-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: 68.36 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLFY----VPQRPYMT 515
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLN--------GLVEPTSGSVLIdgtdINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 516 LGTLRDQV--IYPD---------------GKEDQKK--RGISDQVLKEylDNVQLGHILEREGGWDSVQDWMDVLSGGEK 576
Cdd:cd03256 73 LRQLRRQIgmIFQQfnlierlsvlenvlsGRLGRRStwRSLFGLFPKE--EKQRALAALERVGLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907149462 577 QRMAMARLFYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLH 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
440-625 |
1.33e-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: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATpNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQrpymtlgtl 519
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 520 rdqviypdgkedqkkrgisdqvlkeyldnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|
gi 1907149462 600 ---AVSVD-VEDYIYSHcrkvGITLFTVSH 625
Cdd:cd03221 100 hldLESIEaLEEALKEY----PGTVILVSH 125
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
456-625 |
1.53e-12 |
|
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: 66.27 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPE---RGKLFYVPQRPYmtlgtlrdqvI 524
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlgllkpdsGEIK-VLGKDIKKEPeevKRRIGYLPEEPS----------L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 525 YPDgkedqkkrgisdqvL--KEYLDnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAV- 601
Cdd:cd03230 85 YEN--------------LtvRENLK-----------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLd 127
|
170 180
....*....|....*....|....*..
gi 1907149462 602 ---SVDVEDYIYSHcRKVGITLFTVSH 625
Cdd:cd03230 128 pesRREFWELLREL-KKEGKTILLSSH 153
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
443-629 |
1.58e-12 |
|
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: 70.55 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 443 DHVPLATPNGDI---------------LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG--RL-------- 497
Cdd:COG4618 320 ERMPLPRPKGRLsvenltvvppgskrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvRLdgadlsqw 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 498 TKPERGKLF-YVPQRPymTL--GTLRdQVI--YPDGKEDQ-----KKRGISDQVLK---EYldNVQLGhilerEGGwdsv 564
Cdd:COG4618 400 DREELGRHIgYLPQDV--ELfdGTIA-ENIarFGDADPEKvvaaaKLAGVHEMILRlpdGY--DTRIG-----EGG---- 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907149462 565 qdwmDVLSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVE------DYIySHCRKVGITLFTVSHRKSL 629
Cdd:COG4618 466 ----ARLSGGQRQRIGLARALYGDPRLVVLDEPNS--NLDDEgeaalaAAI-RALKARGATVVVITHRPSL 529
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
408-612 |
1.84e-12 |
|
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: 70.74 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 408 RTMVSQQEKGIEGAQASPLVPGAGEIINTDNIiKFDHVPLATPNgdilIQDLSFEVRSGANVLICGPNGCGKSSLFR-VL 486
Cdd:TIGR00957 611 RIFLSHEELEPDSIERRTIKPGEGNSITVHNA-TFTWARDLPPT----LNGITFSIPEGALVAVVGQVGCGKSSLLSaLL 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 487 GELWPLFGGRLTKperGKLFYVPQRPYMTLGTLRDQVIYpdGKEDQKKRgisdqvLKEYLDNVQLGHILEREGGWDSVQ- 565
Cdd:TIGR00957 686 AEMDKVEGHVHMK---GSVAYVPQQAWIQNDSLRENILF--GKALNEKY------YQQVLEACALLPDLEILPSGDRTEi 754
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907149462 566 -DWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSH 612
Cdd:TIGR00957 755 gEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
437-599 |
1.86e-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: 67.80 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 437 DNIIKFDHVPLATpNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-------LFGGRLTKPE----RGK 504
Cdd:COG1119 1 DPLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLPPtygndvrLFGERRGGEDvwelRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 505 LFYV-P--QRPYMTLGTLRDQVI---------YPDGKEDQKKRGisdqvlKEYLDNVQLGHILEREggwdsvqdwMDVLS 572
Cdd:COG1119 80 IGLVsPalQLRFPRDETVLDVVLsgffdsiglYREPTDEQRERA------RELLELLGLAHLADRP---------FGTLS 144
|
170 180
....*....|....*....|....*..
gi 1907149462 573 GGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTA 171
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
452-625 |
2.46e-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: 66.98 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGRLT--KPERGKLFYVPQR----PYMTLgt 518
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFIKPdsgkilLNGKDITnlPPEKRDISYVPQNyalfPHMTV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 519 lRDQVIYPDGKEDQKKRGISDQVlKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03299 89 -YKNIAYGLKKRKVDKKEIERKV-LEIAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|.
gi 1907149462 599 SAVSVDVEDYIYSHCRKV----GITLFTVSH 625
Cdd:cd03299 158 SALDVRTKEKLREELKKIrkefGVTVLHVTH 188
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
456-625 |
2.75e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.40 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggrlTKPERGKLfyvpqrpymtlgtLRDQVIYPDGKED---- 531
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL--------ETPSAGEL-------------LAGTAPLAEAREDtrlm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 532 -QKKRgisdqVL--KEYLDNVQLG----------HILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:PRK11247 87 fQDAR-----LLpwKKVIDNVGLGlkgqwrdaalQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190
....*....|....*....|....*....|.
gi 1907149462 599 SAVS----VDVEDYIYSHCRKVGITLFTVSH 625
Cdd:PRK11247 162 GALDaltrIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
421-600 |
2.92e-12 |
|
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: 69.85 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 421 AQASPLVPGAGEIintdniiKFDHVPLA-TPNGDILiQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT- 498
Cdd:COG5265 346 PDAPPLVVGGGEV-------RFENVSFGyDPERPIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILi 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 499 --------KPE--RGKLFYVPQRPYMTLGTLRDQVIYpdGKEDqkkrgISDQVLKEYLDNVQLGHILER-EGGWDSVqdw 567
Cdd:COG5265 418 dgqdirdvTQAslRAAIGIVPQDTVLFNDTIAYNIAY--GRPD-----ASEEEVEAAARAAQIHDFIESlPDGYDTR--- 487
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907149462 568 mdV------LSGGEKQRMAMARLFYHKPQFAILDECTSA 600
Cdd:COG5265 488 --VgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
456-625 |
7.71e-12 |
|
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: 64.93 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--KPERGKLFYVPQRpymtLGTLRD-QVIYPD--GKE 530
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdGKSYQKNIEALRR----IGALIEaPGFYPNltARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 531 D----QKKRGISDQVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD-- 604
Cdd:cd03268 92 NlrllARLLGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDgi 162
|
170 180
....*....|....*....|...
gi 1907149462 605 --VEDYIYSHcRKVGITLFTVSH 625
Cdd:cd03268 163 keLRELILSL-RDQGITVLISSH 184
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
458-625 |
2.21e-11 |
|
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: 65.90 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 458 DLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL---------------TKPERGKLFYVPQR----PYMTLgt 518
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgifLPPEKRRIGYVFQEarlfPHLSV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 519 lRDQVIYPDGKEDQKKRGISDQVLKEYLDnvqLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:TIGR02142 93 -RGNLRYGMKRARPSERRISFERVIELLG---IGHLLGRLPG---------RLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190
....*....|....*....|....*....|.
gi 1907149462 599 SAVSVDVEDYIYSHCRKV----GITLFTVSH 625
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLhaefGIPILYVSH 190
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
450-626 |
2.26e-11 |
|
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: 63.59 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 450 PNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplFggRLTKPERGK-------------------LFYVPQ 510
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILAL------F--RFLEAEEGKieidgidistipledlrssLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 511 RPYMTLGTLRDQViypdgkedqkkrgisdQVLKEYlDNVQLGHILE-REGGwdsvqdwmDVLSGGEKQRMAMARLFYHKP 589
Cdd:cd03369 90 DPTLFSGTIRSNL----------------DPFDEY-SDEEIYGALRvSEGG--------LNLSQGQRQLLCLARALLKRP 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907149462 590 QFAILDECTSAVSVDVEDYIYSHCRK--VGITLFTVSHR 626
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHR 183
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
451-625 |
3.58e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.27 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSL-----------FRVLGELWpLFGGRLTK--PERGKLFYVPQR----PY 513
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLlaaiagtlspaFSASGEVL-LNGRRLTAlpAEQRRIGILFQDdllfPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 514 MTLG-----TLRDQViypdGKEDQKKRgisdqvLKEYLDNVQLGHILEReggwDSVQdwmdvLSGGEKQRMAMARLFYHK 588
Cdd:COG4136 91 LSVGenlafALPPTI----GRAQRRAR------VEQALEEAGLAGFADR----DPAT-----LSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907149462 589 PQFAILDECTS----AVSVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:COG4136 152 PRALLLDEPFSkldaALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
451-625 |
4.74e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 63.02 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGR----LTKPERG--------KLFyvpq 510
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIagfetptsGEI--LLDGKditnLPPHKRPvntvfqnyALF---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 511 rPYMTLGtlrDQVIYP-----DGKEDQKKRgisdqvLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLF 585
Cdd:cd03300 85 -PHLTVF---ENIAFGlrlkkLPKAEIKER------VAEALDLVQLEGYANRK---------PSQLSGGQQQRVAIARAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907149462 586 YHKPQFAILDECTSAVSV----DVEDYIYSHCRKVGITLFTVSH 625
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTH 189
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
435-625 |
7.73e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.50 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 435 NTDNIIKFDHVPLATPNGDIL-IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPE-----R 502
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLnGLLLPeagtiTVGGMVLSEEtvwdvR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 503 GKLFYVPQRP--YMTLGTLRDQVIYpdGKEDQkkrGIS-DQVLK---EYLDNVQLGHILEREGGwdsvqdwmdVLSGGEK 576
Cdd:PRK13635 81 RQVGMVFQNPdnQFVGATVQDDVAF--GLENI---GVPrEEMVErvdQALRQVGMEDFLNREPH---------RLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907149462 577 QRMAMARLFYHKPQFAILDECTSAVS----VDVEDYIYSHCRKVGITLFTVSH 625
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
454-625 |
7.79e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 454 ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GelwplfggrLTKPERGKLFYvpqrpymtlgtlrdqviypDGKEDQ 532
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILaG---------LARPDAGEVLW-------------------QGEPIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 533 KKR--------------GISD-----------QVLKEYLDNVQLGHILEREGgwdsVQDWMDV----LSGGEKQRMAMAR 583
Cdd:PRK13538 67 RQRdeyhqdllylghqpGIKTeltalenlrfyQRLHGPGDDEALWEALAQVG----LAGFEDVpvrqLSAGQQRRVALAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907149462 584 LFYHKPQFAILDECTSAVSV----DVEDYIYSHCRKVGITLFTvSH 625
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAIDKqgvaRLEALLAQHAEQGGMVILT-TH 187
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
456-626 |
9.09e-11 |
|
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: 61.91 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLF---------------YVPQR----PYMtl 516
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMI--------LGIILPDSGEVLfdgkpldiaarnrigYLPEErglyPKM-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 517 gTLRDQVIYPDGKEDQKKRGISDQVLkEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:cd03269 86 -KVIDQLVYLAQLKGLKKEEARRRID-EWLERLELSEYANKR---------VEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|...
gi 1907149462 597 CTSA---VSVDVEDYIYSHCRKVGITLFTVSHR 626
Cdd:cd03269 155 PFSGldpVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
452-625 |
9.21e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.74 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERG----------KLFYVPQRPYM--TLGTL 519
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfqrdsiarGLLYLGHAPGIktTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 520 RD-QVIYPDGKEDQkkrgisdqvLKEYLDNVQLGHILEREGGWdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03231 92 ENlRFWHADHSDEQ---------VEEALARVGLNGFEDRPVAQ---------LSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|.
gi 1907149462 599 SAV---SVD-VEDYIYSHCRKVGITLFTVSH 625
Cdd:cd03231 154 TALdkaGVArFAEAMAGHCARGGMVVLTTHQ 184
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
455-629 |
1.08e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVlgelwpLFGGRLTKPERGKlFYVPQRPYMTLGTLRDQvIYPDGKEDQKk 534
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRL------LAGALKGTPVAGC-VDVPDNQFGREASLIDA-IGRKGDFKDA- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 535 rgisdqvlKEYLDNVQLGhilereggwdSVQDWM---DVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEdYIYS 611
Cdd:COG2401 116 --------VELLNAVGLS----------DAVLWLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA-KRVA 176
|
170 180
....*....|....*....|...
gi 1907149462 612 H-----CRKVGITLFTVSHRKSL 629
Cdd:COG2401 177 RnlqklARRAGITLVVATHHYDV 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
456-625 |
1.46e-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: 61.97 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGR----LTKPERGKLFyVPQR----PYMTLGT- 518
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIaglerpdsGTIL--FGGEdatdVPVQERNVGF-VFQHyalfRHMTVFDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 519 ----LRDQVIYPDGKEDQKKRGISdqvlkEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:cd03296 95 vafgLRVKPRSERPPEAEIRAKVH-----ELLKLVQLDWLADR---------YPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1907149462 595 DECTSAVSVDVEDYIYSHCRK----VGITLFTVSH 625
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRlhdeLHVTTVFVTH 195
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
458-625 |
1.47e-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: 61.54 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 458 DLSFEVrSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL---------------TKPERGKLFYVPQR----PYMTLgt 518
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVFQQyalfPHLNV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 519 lRDQVIYPDGKEDQKKRGISDQvlkEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03297 93 -RENLAFGLKRKRNREDRISVD---ELLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|.
gi 1907149462 599 SAVSVDVEDYIYSHCRKV----GITLFTVSH 625
Cdd:cd03297 160 SALDRALRLQLLPELKQIkknlNIPVIFVTH 190
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
454-653 |
1.84e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 454 ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPlfggrltkpERgKLFYVPQRPYMTLGTLRDQVIY 525
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlsqfeiseGRVWA---------ER-SIAYVPQQAWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 526 PDgKEDQKKRGISDQVLKEYLDNVQLGHILEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDV 605
Cdd:PTZ00243 744 FD-EEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVN-----LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907149462 606 EDYIYSHC---RKVGITLFTVSHRKSLWKHHEYYLHMdGRGNYEFKKITED 653
Cdd:PTZ00243 818 GERVVEECflgALAGKTRVLATHQVHVVPRADYVVAL-GDGRVEFSGSSAD 867
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
456-641 |
2.25e-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: 60.81 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLF-RVLGELWPLFG--------------GRLTKPERGKLFYVPQRPYMTLGTLR 520
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwsnknesepsfEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 521 DQVIYPDGKEDQKKRGISDQV-LKEYLDNVQLGHilEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACsLQPDIDLLPFGD--QTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907149462 600 AVSVDVEDyiysHCRKVGI---------TLFTVSHRKSLWKHHEYYLHM-DG 641
Cdd:cd03290 170 ALDIHLSD----HLMQEGIlkflqddkrTLVLVTHKLQYLPHADWIIAMkDG 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
440-609 |
2.43e-10 |
|
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: 60.67 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILiQDLSFEVRSGANVLIcGPNGCGKSSLFRVLGELWP------LFGGR--LTKPE--RGKLFYVP 509
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPpssgtiRIDGQdvLKQPQklRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 510 Q--RPYMTLgTLRDQVIYPdgkedQKKRGISDQVLKEYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRMAMARLFYH 587
Cdd:cd03264 79 QefGVYPNF-TVREFLDYI-----AWLKGIPSKEVKARVDEV-----LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180
....*....|....*....|..
gi 1907149462 588 KPQFAILDECTsaVSVDVEDYI 609
Cdd:cd03264 148 DPSILIVDEPT--AGLDPEERI 167
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
457-600 |
2.82e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 60.62 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 457 QDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLfyvpqrpymtlgTLRDQVIYPDGKEDQKKRG 536
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN--------LLEEPDSGTI------------IIDGLKLTDDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 537 ISDQVLKEY--------LDNVQLG-----------------HILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQF 591
Cdd:cd03262 77 KVGMVFQQFnlfphltvLENITLApikvkgmskaeaeeralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
....*....
gi 1907149462 592 AILDECTSA 600
Cdd:cd03262 157 MLFDEPTSA 165
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
456-628 |
3.10e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.43 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGrLTKPERGKLFY---------VPQR------------PYM 514
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAG-LEKPTEGQIFIdgedvthrsIQQRdicmvfqsyalfPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 515 TLGtlrDQVIY-----PDGKEDQKKRgisdqvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKP 589
Cdd:PRK11432 94 SLG---ENVGYglkmlGVPKEERKQR------VKEALELVDLAGFEDR---------YVDQISGGQQQRVALARALILKP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907149462 590 QFAILDECTSAVSVDV----EDYIYSHCRKVGITLFTVSHRKS 628
Cdd:PRK11432 156 KVLLFDEPLSNLDANLrrsmREKIRELQQQFNITSLYVTHDQS 198
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
435-599 |
4.15e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.16 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 435 NTDNIIKFDHVPLATPNGD-ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWplfggrltKPERGKLF-YVPQRP 512
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL--------KPQSGEIKiDGITIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 513 YMTLGTLRDQV--IY--PD--------------GKEDQK-KRGISDQVLKEYLDNVQLGHILEREGgwdsvqdwmDVLSG 573
Cdd:PRK13632 75 KENLKEIRKKIgiIFqnPDnqfigatveddiafGLENKKvPPKKMKDIIDDLAKKVGMEDYLDKEP---------QNLSG 145
|
170 180
....*....|....*....|....*.
gi 1907149462 574 GEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTS 171
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
458-615 |
5.93e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 458 DLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGRLTKpeRGKLFYVPQRPYMTLGTLRDQVIY-PDGKEDQKKR 535
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI--RGTVAYVPQVSWIFNATVRDNILFgSPFDPERYER 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 536 GISDQVLKEYLDNVQLGHILE-REGGWDsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCR 614
Cdd:PLN03130 713 AIDVTALQHDLDLLPGGDLTEiGERGVN--------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCI 784
|
.
gi 1907149462 615 K 615
Cdd:PLN03130 785 K 785
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
429-613 |
7.33e-10 |
|
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: 60.26 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 429 GAGEIINTDNIIKFDHVPL-ATPngdiLIQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGgrlTKPERGKLF 506
Cdd:cd03291 29 NDRKHSSDDNNLFFSNLCLvGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPSEG---KIKHSGRIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 507 YVPQRPYMTLGTLRDQVIYPDGKEDQKKRGISDQV-LKEYL------DNVQLGhilerEGGWdsvqdwmdVLSGGEKQRM 579
Cdd:cd03291 102 FSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACqLEEDItkfpekDNTVLG-----EGGI--------TLSGGQRARI 168
|
170 180 190
....*....|....*....|....*....|....
gi 1907149462 580 AMARLFYHKPQFAILDECTSAVSVDVEDYIYSHC 613
Cdd:cd03291 169 SLARAVYKDADLYLLDSPFGYLDVFTEKEIFESC 202
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
456-596 |
8.96e-10 |
|
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: 59.19 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL---------TKPERGKLFYVPQR----PYMtlgTLRDQ 522
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdLPPKDRDIAMVFQNyalyPHM---TVYDN 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907149462 523 VIYPDGKEDQKKRGISDQVlKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:cd03301 93 IAFGLKLRKVPKDEIDERV-REVAELLQIEHLLDRK---------PKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
451-625 |
1.02e-09 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 58.40 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQR-------PY-----MTLG 517
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRPT-SGTVRRAGGARVAYVPQRsevpdslPLtvrdlVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 518 TLRDQVIY-PDGKEDQKkrgisdqVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:NF040873 82 RWARRGLWrRLTRDDRA-------AVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|..
gi 1907149462 597 CTSAVSVDVEDYIYSHCRKV---GITLFTVSH 625
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEharGATVVVVTH 177
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
456-625 |
1.52e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 60.35 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGrLTKPERGKLF-------YVP--QR------------PYM 514
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLR-------LIAG-FETPDSGRIMldgqditHVPaeNRhvntvfqsyalfPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 515 TLgtlRDQVIYpdGKEDQK--KRGISDQVLkEYLDNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFA 592
Cdd:PRK09452 102 TV---FENVAF--GLRMQKtpAAEITPRVM-EALRMVQLEEFAQRK-----PHQ----LSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907149462 593 ILDECTSAVsvdveDY---------IYSHCRKVGITLFTVSH 625
Cdd:PRK09452 167 LLDESLSAL-----DYklrkqmqneLKALQRKLGITFVFVTH 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
440-628 |
2.22e-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: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLtkpergklfYVPQRPYMTL--G 517
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI---------RLDGRPLSSLshS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 518 TLR--------DQVIYPDGKEDQKK--RGISDQVLKEYLDNVQLGHILER--EGGWDSVQDWMDVLSGGEKQRMAMARLF 585
Cdd:PRK10790 412 VLRqgvamvqqDPVVLADTFLANVTlgRDISEEQVWQALETVQLAELARSlpDGLYTPLGEQGNNLSVGQKQLLALARVL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907149462 586 YHKPQFAILDECTSAVSVDVEDYIYSHCRKV--GITLFTVSHRKS 628
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLS 536
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
433-625 |
2.30e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.65 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 433 IINTDNIIKFDHVPLATPnGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGRLTKPERGKLF 506
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPpsegeiLLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 507 -----YVPQR-PYMTLGTLRDQVI---YP-------DGKEDQKKrgisdqvLKEYLDNVQLGHILEReggwdsvqdWMDV 570
Cdd:PRK10575 84 arkvaYLPQQlPAAEGMTVRELVAigrYPwhgalgrFGAADREK-------VEEAISLVGLKPLAHR---------LVDS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907149462 571 LSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
435-613 |
2.31e-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: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 435 NTDNIIKFDHVPL-ATPngdiLIQDLSFEVRSGANVLICGPNGCGKSSLFRV-LGELWPLFGgrlTKPERGKLFYVPQRP 512
Cdd:TIGR01271 424 NGDDGLFFSNFSLyVTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMiMGELEPSEG---KIKHSGRISFSPQTS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 513 YMTLGTLRDQVIYPDGKEDQKKRGISDQV-LKEYL------DNVQLGhilerEGGWdsvqdwmdVLSGGEKQRMAMARLF 585
Cdd:TIGR01271 497 WIMPGTIKDNIIFGLSYDEYRYTSVIKACqLEEDIalfpekDKTVLG-----EGGI--------TLSGGQRARISLARAV 563
|
170 180
....*....|....*....|....*...
gi 1907149462 586 YHKPQFAILDECTSAVSVDVEDYIYSHC 613
Cdd:TIGR01271 564 YKDADLYLLDSPFTHLDVVTEKEIFESC 591
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
451-625 |
2.42e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.52 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------------------KPERGKLFYVPQ 510
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlyfgkdifqidaiklRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 511 rPYMTLgTLRDQVIYPDGKEDQKKRGISDQVLKEYLDNVQLghilereggWDSVQDWMDV----LSGGEKQRMAMARLFY 586
Cdd:PRK14246 101 -PFPHL-SIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGL---------WKEVYDRLNSpasqLSGGQQQRLTIARALA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907149462 587 HKPQFAILDECTSAVSV----DVEDYIYSHCRKVGITLftVSH 625
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIvnsqAIEKLITELKNEIAIVI--VSH 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
458-626 |
2.50e-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: 56.67 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 458 DLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplFGgrLTKPERGKLFyvpqrpymtlgtLRDQVIYPDGKEDQKKRGI 537
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKIL------SG--LYKPDSGEIL------------VDGKEVSFASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 538 SdqvlkeyldnvqlghilereggwdSV-QdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV 616
Cdd:cd03216 78 A------------------------MVyQ-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL 128
|
170
....*....|...
gi 1907149462 617 ---GITLFTVSHR 626
Cdd:cd03216 129 raqGVAVIFISHR 141
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
456-596 |
2.69e-09 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 57.83 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGR-------LTK------PERGkLFYVPQR----PYMT--- 515
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrdITGlppherARAG-IGYVPEGrrifPELTvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 516 ---LGTLRdqviypdGKEDQKKRGIsDQVLkEYLDNvqLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFA 592
Cdd:cd03224 95 nllLGAYA-------RRRAKRKARL-ERVY-ELFPR--LKERRKQLAG---------TLSGGEQQMLAIARALMSRPKLL 154
|
....
gi 1907149462 593 ILDE 596
Cdd:cd03224 155 LLDE 158
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
440-626 |
4.08e-09 |
|
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: 56.55 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLATPNGDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFG---------GRLTKPERGKLFYV 508
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLKPQQGeitldgvpvSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 509 PQRPYMTLGTLRDQViypdGKEdqkkrgisdqvlkeyldnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHK 588
Cdd:cd03247 81 NQRPYLFDTTLRNNL----GRR----------------------------------------FSGGERQRLALARILLQD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907149462 589 PQFAILDECTsaVSVDVE------DYIYSHCRkvGITLFTVSHR 626
Cdd:cd03247 117 APIVLLDEPT--VGLDPIterqllSLIFEVLK--DKTLIWITHH 156
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
456-626 |
5.16e-09 |
|
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: 57.06 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGR-LT--KPER------GKLFYVPqRPYMTLgTLR 520
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFLRPtsgsvLFDGEdITglPPHEiarlgiGRTFQIP-RLFPEL-TVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 521 DQVI----------YPDGKEDQKKRGISDQVLkEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQ 590
Cdd:cd03219 94 ENVMvaaqartgsgLLLARARREEREARERAE-ELLERVGLADLADRPAG---------ELSYGQQRRLEIARALATDPK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907149462 591 FAILDECTSAVS----VDVEDYIyshcRKV---GITLFTVSHR 626
Cdd:cd03219 164 LLLLDEPAAGLNpeetEELAELI----RELrerGITVLLVEHD 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
456-625 |
5.65e-09 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 56.99 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT----------KPERGKLFYVPQRPYMTLGTLRDQVIY 525
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrepREVRRRIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 526 PDGKEDQKKRGISDQVLKEYLDNVQLghilereggWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDV 605
Cdd:cd03265 96 IHARLYGVPGAERRERIDELLDFVGL---------LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180
....*....|....*....|....
gi 1907149462 606 EDYIYSHCRKV----GITLFTVSH 625
Cdd:cd03265 167 RAHVWEYIEKLkeefGMTILLTTH 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
445-599 |
5.76e-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: 56.90 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 445 VPLATPNGD---ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL---GELWPLFGGRLT---KPERGKLF-----YVPQ 510
Cdd:cd03234 9 VGLKAKNWNkyaRILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILfngQPRKPDQFqkcvaYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 511 R----PYMTL-------GTLRDQVIYPDGkedQKKRGISDQVLKEyLDNVQLGHILereggwdsvqdwMDVLSGGEKQRM 579
Cdd:cd03234 89 DdillPGLTVretltytAILRLPRKSSDA---IRKKRVEDVLLRD-LALTRIGGNL------------VKGISGGERRRV 152
|
170 180
....*....|....*....|
gi 1907149462 580 AMARLFYHKPQFAILDECTS 599
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTS 172
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
456-583 |
5.96e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 58.16 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGRL---TKPERGKLFYVPQR----PYMTLgtlR 520
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagledptsGEIL--IGGRDvtdLPPKDRNIAMVFQSyalyPHMTV---Y 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907149462 521 DQVIYP-----DGKEDQKKRgisdqvLKEYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMAR 583
Cdd:COG3839 94 ENIAFPlklrkVPKAEIDRR------VREAAELLGLEDLLDRkpkQ------------LSGGQRQRVALGR 146
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
439-635 |
6.34e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.81 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 439 IIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGG----RLTKPE----R 502
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIcgierpsaGKIW--FSGhditRLKNREvpflR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 503 GKLFYVPQRPYMTLG-TLRDQVIYP-----DGKEDQKKRgisdqvLKEYLDNVQLghilereggWDSVQDWMDVLSGGEK 576
Cdd:PRK10908 79 RQIGMIFQDHHLLMDrTVYDNVAIPliiagASGDDIRRR------VSAALDKVGL---------LDKAKNFPIQLSGGEQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907149462 577 QRMAMARLFYHKPQFAILDECTSAVSVDVEDYI---YSHCRKVGITLFTVSHRKSLWKHHEY 635
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNRVGVTVLMATHDIGLISRRSY 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
456-600 |
6.77e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.02 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG----------------RLTKPERGKLFyvpQR----PYMT 515
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglkvndpkvdeRLIRQEAGMVF---QQfylfPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 516 ------LGTLRdqvIYPDGKEDQKKRGisdqvlKEYLDNVQLGhilEREGGWDSVqdwmdvLSGGEKQRMAMARLFYHKP 589
Cdd:PRK09493 94 alenvmFGPLR---VRGASKEEAEKQA------RELLAKVGLA---ERAHHYPSE------LSGGQQQRVAIARALAVKP 155
|
170
....*....|.
gi 1907149462 590 QFAILDECTSA 600
Cdd:PRK09493 156 KLMLFDEPTSA 166
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
452-625 |
7.32e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.83 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-------------KPERGkLFYVPQRP------ 512
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplhaRARRG-IGYLPQEAsifrrl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 513 -----YMTLGTLRDQViypdGKEDQKKRGisdqvlKEYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQRMAMARLFYH 587
Cdd:PRK10895 94 svydnLMAVLQIRDDL----SAEQREDRA------NELMEEFHIEHLRDSMG---------QSLSGGERRRVEIARALAA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907149462 588 KPQFAILDECTSAVS----VDVEDyIYSHCRKVGITLFTVSH 625
Cdd:PRK10895 155 NPKFILLDEPFAGVDpisvIDIKR-IIEHLRDSGLGVLITDH 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
452-606 |
7.92e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRV-LGELWPLfGGRL---TKPE-------RGKLfyVPQRpymtlgTLR 520
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQAD-SGRIhcgTKLEvayfdqhRAEL--DPEK------TVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 521 DQViyPDGKEDQKKRGISDQVLKeYLdnvqlghilereggwdsvQDWM----------DVLSGGEKQRMAMARLFYHKPQ 590
Cdd:PRK11147 402 DNL--AEGKQEVMVNGRPRHVLG-YL------------------QDFLfhpkramtpvKALSGGERNRLLLARLFLKPSN 460
|
170
....*....|....*.
gi 1907149462 591 FAILDECTSavSVDVE 606
Cdd:PRK11147 461 LLILDEPTN--DLDVE 474
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
455-625 |
8.78e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.97 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGrlTKPErGKLFYVPQRPY---MTLGTLRDQV-------- 523
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESE--VRVE-GRVEFFNQNIYerrVNLNRLRRQVsmvhpkpn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 524 IYPDGKEDQKKRGISdqvLKEYLDNVQLGHILEREGG----WDSVQDWMDV----LSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:PRK14258 99 LFPMSVYDNVAYGVK---IVGWRPKLEIDDIVESALKdadlWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190
....*....|....*....|....*....|....
gi 1907149462 596 E-CTS---AVSVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:PRK14258 176 EpCFGldpIASMKVESLIQSLRLRSELTMVIVSH 209
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
418-628 |
9.74e-09 |
|
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: 56.84 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 418 IEGAQASPLVPGAGEIINTDNIIKFDHvplatpNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL 497
Cdd:cd03288 5 ISGSSNSGLVGLGGEIKIHDLCVRYEN------NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 498 T-----------KPERGKLFYVPQRPYMTLGTLRDQViypdgkedQKKRGISDQVLKEYLDNVQLGHILER-EGGWDS-V 564
Cdd:cd03288 79 VidgidisklplHTLRSRLSIILQDPILFSGSIRFNL--------DPECKCTDDRLWEALEIAQLKNMVKSlPGGLDAvV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 565 QDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIyshcRKVGITLF------TVSHRKS 628
Cdd:cd03288 151 TEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENIL----QKVVMTAFadrtvvTIAHRVS 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
452-598 |
1.09e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQRPY------MTLGTLRDQVI 524
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvGELEPD-SGTVKWSENANIGYYAQDHAydfendLTLFDWMSQWR 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907149462 525 YPdGKEDQKKRGIsdqvlkeyldnvqLGHILereGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:PRK15064 410 QE-GDDEQAVRGT-------------LGRLL---FSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
405-606 |
1.19e-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: 58.02 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 405 RYERTMVSQQEKGIEGAQAS-PLVPGAGeiintDNIIKFDHVPLATpnGD-ILIQDLSFEVRSGANVLICGPNGCGKSSL 482
Cdd:TIGR03719 292 RYEELLSQEFQKRNETAEIYiPPGPRLG-----DKVIEAENLTKAF--GDkLLIDDLSFKLPPGGIVGVIGPNGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 483 FRVL-GELWPlFGGRLTKPERGKLFYVpqrpymtlgtlrdqviypdgkeDQKKRGISD-----QVLKEYLDNVQLG--HI 554
Cdd:TIGR03719 365 FRMItGQEQP-DSGTIEIGETVKLAYV----------------------DQSRDALDPnktvwEEISGGLDIIKLGkrEI 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907149462 555 LERE-------GGWDSvQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVE 606
Cdd:TIGR03719 422 PSRAyvgrfnfKGSDQ-QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTN--DLDVE 477
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
456-626 |
1.26e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 56.66 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGRLTKPERGKLFYVPQ----RPYMTLGtlrDQVI 524
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILAPdsgevlWDGEPLDPEDRRRIGYLPEerglYPKMKVG---EQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 525 Y-------PdgKEDQKKRgisdqvLKEYLDNVQLGhilEREGgwDSVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDEC 597
Cdd:COG4152 94 YlarlkglS--KAEAKRR------ADEWLERLGLG---DRAN--KKVEE----LSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190
....*....|....*....|....*....|....
gi 1907149462 598 TS---AVSVDV-EDYIYSHCRKvGIT-LFTvSHR 626
Cdd:COG4152 157 FSgldPVNVELlKDVIRELAAK-GTTvIFS-SHQ 188
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
456-625 |
1.36e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 57.03 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRL---TKPERGKLFYVPQR----PYMTLgtlR 520
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagfetpdsGRI--LLDGRDvtgLPPEKRNVGMVFQDyalfPHLTV---A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 521 DQVIYP-----DGKEDQKKRgisdqvLKEYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFA 592
Cdd:COG3842 96 ENVAFGlrmrgVPKAEIRAR------VAELLELVGLEGLADRyphQ------------LSGGQQQRVALARALAPEPRVL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907149462 593 ILDECTSA----VSVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:COG3842 158 LLDEPLSAldakLREEMREELRRLQRELGITFIYVTH 194
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
456-625 |
1.78e-08 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 55.55 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGEL-WPLFGGRLTK--------PERGKLFyvpQR----PYMTLgtlRDQ 522
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitepgPDRMVVF---QNysllPWLTV---REN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 523 V------IYPDGKEDQKKrgisdQVLKEYLDNVQLGHILEREGGWdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:TIGR01184 75 IalavdrVLPDLSKSERR-----AIVEEHIALVGLTEAADKRPGQ---------LSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190
....*....|....*....|....*....|...
gi 1907149462 597 CTSAVSV----DVEDYIYSHCRKVGITLFTVSH 625
Cdd:TIGR01184 141 PFGALDAltrgNLQEELMQIWEEHRVTVLMVTH 173
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
455-642 |
1.84e-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: 54.84 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGR----LTKPERGK--LFYVPQRPymtlgt 518
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkyevteGEI--LFKGEditdLPPEERARlgIFLAFQYP------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 519 lrdqVIYPdgkedqkkrGISdqvLKEYLDNVQLGhilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03217 87 ----PEIP---------GVK---NADFLRYVNEG------------------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907149462 599 SAVSVD----VEDYIySHCRKVGITLFTVSHRKSLWKHHE---YYLHMDGR 642
Cdd:cd03217 133 SGLDIDalrlVAEVI-NKLREEGKSVLIITHYQRLLDYIKpdrVHVLYDGR 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
458-625 |
2.10e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.41 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 458 DLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL----------TKPE-------RGKLFYVPQR----PYMTL 516
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfsKTPSdkairelRRNVGMVFQQynlwPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 517 gtlRDQVIYPD------GKEDQKKRGisdqvlKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQ 590
Cdd:PRK11124 100 ---QQNLIEAPcrvlglSKDQALARA------EKLLERLRLKPYADR---------FPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907149462 591 FAILDECTSAVSVDVEDYIYSHCRKV---GITLFTVSH 625
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELaetGITQVIVTH 199
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
450-626 |
2.34e-08 |
|
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: 57.65 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 450 PNGDILIQDLSFEVRSGANVLICGPNGCGKSS----LFRVL----GELwPLFGGRLTK----PERGKLFYVPQRPYMTLG 517
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINesaeGEI-IIDGLNIAKiglhDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 518 TLRDQvIYPDGKEDQKKRGISDQV--LKEYLDNVQLGHILE-REGGwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:TIGR00957 1375 SLRMN-LDPFSQYSDEEVWWALELahLKTFVSALPDKLDHEcAEGG--------ENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190
....*....|....*....|....*....|....
gi 1907149462 595 DECTSAVSVDVEDYIYSHCRKV--GITLFTVSHR 626
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHR 1479
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
450-604 |
2.66e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.87 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 450 PNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPLFGGrltkpergKLFYVPQRPYM--TLgTL 519
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfnGEARPQPGI--------KVGYLPQEPQLdpTK-TV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 520 RDQVIypDGKEDQKkrgisdQVLKEYlDNV-------------------QLGHILEREGGWD---SVQDWMD-------- 569
Cdd:TIGR03719 86 RENVE--EGVAEIK------DALDRF-NEIsakyaepdadfdklaaeqaELQEIIDAADAWDldsQLEIAMDalrcppwd 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907149462 570 ----VLSGGEKQRMAMARLFYHKPQFAILDECTS---AVSVD 604
Cdd:TIGR03719 157 advtKLSGGERRRVALCRLLLSKPDMLLLDEPTNhldAESVA 198
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
434-605 |
2.84e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.25 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 434 INTDNIIK-FDHVPLatpngdilIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGG----RLTKP 500
Cdd:PRK10851 3 IEIANIKKsFGRTQV--------LNDISLDIPSGQMVALLGPSGSGKTTLLRIIaglehqtsGHI--RFHGtdvsRLHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 501 ER--GKLF--YVPQRpYMTLGtlrDQVIY-----PdgKEDQKKRGISDQVLKEYLDNVQLGHILEReggwdsvqdWMDVL 571
Cdd:PRK10851 73 DRkvGFVFqhYALFR-HMTVF---DNIAFgltvlP--RRERPNAAAIKAKVTQLLEMVQLAHLADR---------YPAQL 137
|
170 180 190
....*....|....*....|....*....|....
gi 1907149462 572 SGGEKQRMAMARLFYHKPQFAILDECTSAVSVDV 605
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
439-629 |
3.98e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 439 IIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE-RGKLFYVPQRPYMTL 516
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIsGELQPSSGTVFRSAKvRMAVFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 517 GT---LRDQVIYPdgkedqkkrGISDQVLKEYLDNVQLGHILEREGgwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAI 593
Cdd:PLN03073 588 SSnplLYMMRCFP---------GVPEQKLRAHLGSFGVTGNLALQP--------MYTLSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907149462 594 LDECTSAVSVD-VEDYIYshcrkvGITLF-----TVSHRKSL 629
Cdd:PLN03073 651 LDEPSNHLDLDaVEALIQ------GLVLFqggvlMVSHDEHL 686
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
452-596 |
4.44e-08 |
|
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: 54.22 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE----RGkLFYVPQR----PY 513
Cdd:COG0410 14 GGIHVlHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglPPHriarLG-IGYVPEGrrifPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 514 MT------LGTLRdqviypdGKEDQKKRGISDQV------LKEYLDnvqlghileREGGwdsvqdwmdVLSGGEKQRMAM 581
Cdd:COG0410 93 LTveenllLGAYA-------RRDRAEVRADLERVyelfprLKERRR---------QRAG---------TLSGGEQQMLAI 147
|
170
....*....|....*
gi 1907149462 582 ARLFYHKPQFAILDE 596
Cdd:COG0410 148 GRALMSRPKLLLLDE 162
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
449-603 |
4.83e-08 |
|
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: 55.06 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 449 TPNGDI-LIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-----------GELwpLFGGR----LTKPE----RGK-LFY 507
Cdd:COG0444 13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlgllpppgitsGEI--LFDGEdllkLSEKElrkiRGReIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 508 VPQRPYMTLG---TLRDQVIYP------DGKEDQKKRGIsdqvlkEYLDNVQLghilereggwDSVQDWMDV----LSGG 574
Cdd:COG0444 91 IFQDPMTSLNpvmTVGDQIAEPlrihggLSKAEARERAI------ELLERVGL----------PDPERRLDRypheLSGG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1907149462 575 EKQR----MAMArlfyHKPQFAILDECTSA--VSV 603
Cdd:COG0444 155 MRQRvmiaRALA----LEPKLLIADEPTTAldVTI 185
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
451-596 |
7.08e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 53.92 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILiQDLSFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGR----LTKPERGK--LFYVPQRPY- 513
Cdd:COG0396 12 GKEIL-KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpkyevtsGSI--LLDGEdileLSPDERARagIFLAFQYPVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 514 ---MTLGTL--------RDQVIypDGKEDQKKrgisdqvLKEYLDNVQLGH-ILER---EGgwdsvqdwmdvLSGGEKQR 578
Cdd:COG0396 89 ipgVSVSNFlrtalnarRGEEL--SAREFLKL-------LKEKMKELGLDEdFLDRyvnEG-----------FSGGEKKR 148
|
170
....*....|....*...
gi 1907149462 579 MAMARLFYHKPQFAILDE 596
Cdd:COG0396 149 NEILQMLLLEPKLAILDE 166
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
435-625 |
7.73e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.99 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 435 NTDNIIKFDHVPLATpNGD--ILIQDLSFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGrLTKPERGKLFYvpqrp 512
Cdd:PRK13648 3 DKNSIIVFKNVSFQY-QSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAK-------LMIG-IEKVKSGEIFY----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 513 ymtlgtlRDQVIYPDGKEDQKKR-GISDQ--------VLKEY-----LDNVQLGH---------ILEREGGWDSVQDWMD 569
Cdd:PRK13648 69 -------NNQAITDDNFEKLRKHiGIVFQnpdnqfvgSIVKYdvafgLENHAVPYdemhrrvseALKQVDMLERADYEPN 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 570 VLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV----GITLFTVSH 625
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITH 201
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
458-583 |
8.46e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 54.72 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 458 DLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------------KPERGKLFYVPQ--R--PYMT-LG 517
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiflPPHRRRIGYVFQeaRlfPHLSvRG 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907149462 518 TLRdqviYPDGKEDQKKRGIS-DQVLkeylDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMAR 583
Cdd:COG4148 97 NLL----YGRKRAPRAERRISfDEVV----ELLGIGHLLDR---------RPATLSGGERQRVAIGR 146
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
473-625 |
9.04e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 9.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 473 GPNGCGKSSLFRVL---GELWP--------------LFGGRLTKPE-RGKLFYVPQRPYMTLGTLRDQVIYpdgkeDQKK 534
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPevtitgsivynghnIYSPRTDTVDlRKEIGMVFQQPNPFPMSIYENVVY-----GLRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 535 RGISDqvlKEYLDNVqLGHILEREGGWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVE 606
Cdd:PRK14239 113 KGIKD---KQVLDEA-VEKSLKGASIWDEVKDRLHdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSALdpisAGKIE 188
|
170
....*....|....*....
gi 1907149462 607 DYIYShcRKVGITLFTVSH 625
Cdd:PRK14239 189 ETLLG--LKDDYTMLLVTR 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
452-625 |
1.04e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.65 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILI-QDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRL------TKPERGKLF-----Yvpqr 511
Cdd:PRK11000 14 GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditsGDL--FIGEKRmndvppAERGVGMVFqsyalY---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 512 PYMTLGtlrDQVIYPDGKEDQKKRGIsDQVLKEYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQRMAMARLFYHKPQF 591
Cdd:PRK11000 88 PHLSVA---ENMSFGLKLAGAKKEEI-NQRVNQVAEVLQLAHLLDRKP---------KALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907149462 592 AILDECTS----AVSVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:PRK11000 155 FLLDEPLSnldaALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
451-642 |
1.09e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.46 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 451 NGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggrlTKPERGK-------LFYVP--QRP--------- 512
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF--------EQPTAGQimldgvdLSHVPpyQRPinmmfqsya 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 513 ---YMTLgtlrDQVIYPDGKEDQKKRG-ISDQVlKEYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQRMAMARLFYHK 588
Cdd:PRK11607 102 lfpHMTV----EQNIAFGLKQDKLPKAeIASRV-NEMLGLVHMQEFAKRKP---------HQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907149462 589 PQFAILDECTSAVSVDVEDYIYSHC----RKVGITLFTVSHRKslwkhhEYYLHMDGR 642
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVvdilERVGVTCVMVTHDQ------EEAMTMAGR 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
463-599 |
1.12e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 463 VRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE--------RG-------------------KLFYVPQRPYM 514
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsGELIPNLGDYEEEPSwdevlkrfRGtelqnyfkklyngeikvvhKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 515 TLGTLRDQVIYPDgkedqkKRGISDQVLKEyldnVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:PRK13409 176 FKGKVRELLKKVD------ERGKLDEVVER----LGLENILDRD---------ISELSGGELQRVAIAAALLRDADFYFF 236
|
....*
gi 1907149462 595 DECTS 599
Cdd:PRK13409 237 DEPTS 241
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
456-596 |
1.51e-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: 52.93 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTK-P--ERGKL--FYVPQRPYMTLG-TLRD 521
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIvglvkpdsGKIL-LDGQDITKlPmhKRARLgiGYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 522 QV-----IYPDGKEDQKKRgisdqvLKEYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:cd03218 95 NIlavleIRGLSKKEREEK------LEELLEEFHITHLRKSKA---------SSLSGGERRRVEIARALATNPKFLLLDE 159
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
456-599 |
1.63e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP-------LFGGRLTKPE----RGKLFYVPQRP--YMTLGTLRDQ 522
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEaesgqiiIDGDLLTEENvwdiRHKIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 523 VIYpdGKEDQkkrGISDQVLKEYLDnvqlgHILEREGgwdsVQDWMDV----LSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:PRK13650 103 VAF--GLENK---GIPHEEMKERVN-----EALELVG----MQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
.
gi 1907149462 599 S 599
Cdd:PRK13650 169 S 169
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
408-628 |
1.86e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.33 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 408 RTMVSQQEKGIEGAQASPLVPGAGEIintdNIIKFdHVPLATPNgdiLIQDLSFEVRSGANVLICGPNGCGKSSLFRVL- 486
Cdd:PRK10789 291 RAMLAEAPVVKDGSEPVPEGRGELDV----NIRQF-TYPQTDHP---ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIq 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 487 -------GEL----WPLFGGRLTKpERGKLFYVPQRPYMTLGTLRDQVIYpdGKEDQKKRGIsDQVLKeyLDNVQlGHIL 555
Cdd:PRK10789 363 rhfdvseGDIrfhdIPLTKLQLDS-WRSRLAVVSQTPFLFSDTVANNIAL--GRPDATQQEI-EHVAR--LASVH-DDIL 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907149462 556 EREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKVGI--TLFTVSHRKS 628
Cdd:PRK10789 436 RLPQGYDTeVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEgrTVIISAHRLS 511
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
456-615 |
1.91e-07 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 51.66 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---KPERGK---------LFYVPqrpymtlgtlrdqv 523
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITldgKPVTRRsprdairagIAYVP-------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 524 iypdgkEDQKKRGIsdqVLKEYL-DNVQLGHILereggwdsvqdwmdvlSGGEKQRMAMARLFYHKPQFAILDECTsaVS 602
Cdd:cd03215 82 ------EDRKREGL---VLDLSVaENIALSSLL----------------SGGNQQKVVLARWLARDPRVLILDEPT--RG 134
|
170
....*....|....*
gi 1907149462 603 VDVE--DYIYSHCRK 615
Cdd:cd03215 135 VDVGakAEIYRLIRE 149
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
455-629 |
2.09e-07 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 52.89 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplFGgrLTKPERGKLFYVPQRPYMTLGTLRD------QVIYPDG 528
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLL------LG--LEKPAQGTVSFRGQDLYQLDRKQRRafrrdvQLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 529 KEDQKKRGISDQVLKEYLDNV----------QLGHILEREGGWDSVQDWMDV-LSGGEKQRMAMARLFYHKPQFAILDEC 597
Cdd:TIGR02769 98 PSAVNPRMTVRQIIGEPLRHLtsldeseqkaRIAELLDMVGLRSEDADKLPRqLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907149462 598 TSAVSVDVEDYIYSHCRKV----GITLFTVSHRKSL 629
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLqqafGTAYLFITHDLRL 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
418-599 |
2.71e-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: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 418 IEGAQASPLVPGAGEIINTDNIIKFdhvplaTPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFG--- 494
Cdd:TIGR01271 1203 IENPHAQKCWPSGGQMDVQGLTAKY------TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiq 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 495 ------GRLTKPERGKLF-YVPQRPYMTLGTLRDQVIYPDGKEDQKKRGISDQV-LKEYLDNV--QLGHILErEGGWdsv 564
Cdd:TIGR01271 1277 idgvswNSVTLQTWRKAFgVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVgLKSVIEQFpdKLDFVLV-DGGY--- 1352
|
170 180 190
....*....|....*....|....*....|....*
gi 1907149462 565 qdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:TIGR01271 1353 -----VLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
432-625 |
2.89e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.40 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 432 EIINTDNIIkFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL------TKPErGKL 505
Cdd:PRK13633 3 EMIKCKNVS-YKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldTSDE-ENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 506 FYVPQRPYMTLGTLRDQVIYPDGKED----QKKRGISDQVLKEYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRMAM 581
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATIVEEDvafgPENLGIPPEEIRERVDES-----LKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907149462 582 ARLFYHKPQFAILDECTSAVS----VDVEDYIYSHCRKVGITLFTVSH 625
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
437-625 |
3.32e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.16 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 437 DNIIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPERGKLFYVPQ 510
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLnGILKPssgriLFDGKPIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 511 RPYMTLGTLRDQVIYPDGKEDqkkrgISDQVLKEYL--DNVQ--LGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFY 586
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQD-----VSFGAVNLKLpeDEVRkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907149462 587 HKPQFAILDECTSAVS----VDVEDYIYSHCRKVGITLFTVSH 625
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATH 200
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
433-625 |
3.41e-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: 51.81 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 433 IINTDNIIK-FDHVPLATPngdiLIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPERG 503
Cdd:cd03258 1 MIELKNVSKvFGDTGGKVT----ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptsGSVL-VDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 504 KLfyVPQRPYMTL----------GTLRDQVIYPDGKEDQKKRGISDQVLkEYLDNVQLGhilereggwDSVQDWMDVLSG 573
Cdd:cd03258 76 EL--RKARRRIGMifqhfnllssRTVFENVALPLEIAGVPKAEIEERVL-ELLELVGLE---------DKADAYPAQLSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907149462 574 GEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALdpetTQSILALLRDINRELGLTIVLITH 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
440-626 |
4.18e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFDHVPLA-TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPE-----------RGKLFY 507
Cdd:PLN03232 1235 IKFEDVHLRyRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 508 VPQRPYMTLGTLRDQvIYPDGKEDqkkrgisDQVLKEYLDNVQLGHILEREG-GWDS-VQDWMDVLSGGEKQRMAMARLF 585
Cdd:PLN03232 1315 IPQSPVLFSGTVRFN-IDPFSEHN-------DADLWEALERAHIKDVIDRNPfGLDAeVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907149462 586 YHKPQFAILDECTSAVSVDVEDYIYSHCRK--VGITLFTVSHR 626
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAHR 1429
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
455-599 |
4.32e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.84 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLG---ELWP--------LFGGR--------LTKPERGKLFYVPQrPYMT 515
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrliELYPearvsgevYLDGQdifkmdviELRRRVQMVFQIPN-PIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 516 LGTLRDQVIYPDGKEDQKKRGISDQVLKEYLDNVQLghilereggWDSVQDWMDV----LSGGEKQRMAMARLFYHKPQF 591
Cdd:PRK14247 97 LSIFENVALGLKLNRLVKSKKELQERVRWALEKAQL---------WDEVKDRLDApagkLSGGQQQRLCIARALAFQPEV 167
|
....*...
gi 1907149462 592 AILDECTS 599
Cdd:PRK14247 168 LLADEPTA 175
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
452-625 |
5.00e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.14 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT----------KPERGKLFYVPQRPYMTLG-TLR 520
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVPQFDNLDLEfTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 521 DQVIYPDGKEDQKKRGIsDQVLKEYLDNVQLghilerEGGWDS-VQDwmdvLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:PRK13536 133 ENLLVFGRYFGMSTREI-EAVIPSLLEFARL------ESKADArVSD----LSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180
....*....|....*....|....*....
gi 1907149462 600 AVSVDVEDYIYSHCRKV---GITLFTVSH 625
Cdd:PRK13536 202 GLDPHARHLIWERLRSLlarGKTILLTTH 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
463-599 |
5.23e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.60 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 463 VRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE--------RG-------------------KLFYVPQRPYM 514
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILaGKLKPNLGKFDDPPDwdeildefRGselqnyftkllegdvkvivKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 515 TLGTLRDQViypdgkEDQKKRGisdqVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:cd03236 103 VKGKVGELL------KKKDERG----KLDELVDQLELRHVLDRN---------IDQLSGGELQRVAIAAALARDADFYFF 163
|
....*
gi 1907149462 595 DECTS 599
Cdd:cd03236 164 DEPSS 168
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
456-626 |
5.57e-07 |
|
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: 50.83 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------KPE--RGKLFYVP--QRPYMTLgTLRDQV 523
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkEPAeaRRRLGFVSdsTGLYDRL-TARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 524 IYPDGKEDQKKRGISDQVlKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSV 603
Cdd:cd03266 100 EYFAGLYGLKGDELTARL-EELADRLGMEELLDRRVG---------GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180
....*....|....*....|....*..
gi 1907149462 604 ----DVEDYIySHCRKVGITLFTVSHR 626
Cdd:cd03266 170 matrALREFI-RQLRALGKCILFSTHI 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
437-584 |
6.77e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 437 DNIIKFDHVPLATpnGD-ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVpqrpymt 515
Cdd:PRK11819 322 DKVIEAENLSKSF--GDrLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYV------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 516 lgtlrdqviypdgkeDQKKRGISD-----QVLKEYLDNVQLGhilERE------------GGWDSvQDWMDVLSGGEKQR 578
Cdd:PRK11819 393 ---------------DQSRDALDPnktvwEEISGGLDIIKVG---NREipsrayvgrfnfKGGDQ-QKKVGVLSGGERNR 453
|
....*.
gi 1907149462 579 MAMARL 584
Cdd:PRK11819 454 LHLAKT 459
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
456-625 |
7.73e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.25 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG-------RLTKPE----RGKLFYVPQRP--YMTLGTLRDQ 522
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgeLLTAENvwnlRRKIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 523 VIYpdGKEDQkkrGISDQVLKEYLDNVQLG-HILE---REGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:PRK13642 103 VAF--GMENQ---GIPREEMIKRVDEALLAvNMLDfktREPA---------RLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190
....*....|....*....|....*....|.
gi 1907149462 599 SAVS----VDVEDYIYSHCRKVGITLFTVSH 625
Cdd:PRK13642 169 SMLDptgrQEIMRVIHEIKEKYQLTVLSITH 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
456-609 |
8.62e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSS----LFRVL---GELW----PL--FGGRLTKPERGKLFYVPQRPYMTLGT-LRD 521
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIWfdgqPLhnLNRRQLLPVRHRIQVVFQDPNSSLNPrLNV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 522 QVIYPDGKEDQKKRGISDQVLKEYLDNVQlghilerEGGWD--SVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:PRK15134 382 LQIIEEGLRVHQPTLSAAQREQQVIAVME-------EVGLDpeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170
....*....|
gi 1907149462 600 AVSVDVEDYI 609
Cdd:PRK15134 455 SLDKTVQAQI 464
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
454-625 |
2.09e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.60 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 454 ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLF--------YVPQRPYMTLGTLRDQVIY 525
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTL--------SRLMTPAHGHVWldgehiqhYASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 526 PDGKEDQK--KRG-ISDQVL-----KEylDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDEC 597
Cdd:PRK10253 93 PGDITVQElvARGrYPHQPLftrwrKE--DEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190
....*....|....*....|....*....|..
gi 1907149462 598 TSAV----SVDVEDYIYSHCRKVGITLFTVSH 625
Cdd:PRK10253 171 TTWLdishQIDLLELLSELNREKGYTLAAVLH 202
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
456-625 |
2.14e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.78 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRV---LGELWPLF---------GGRLTKPE------RGKLFYVPQRPYMTLG 517
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFrvegkvtfhGKNLYAPDvdpvevRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 518 TLRDQVIYpdGKEDQKKRGISDQVLKEYLDNVQLghilereggWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAI 593
Cdd:PRK14243 106 SIYDNIAY--GARINGYKGDMDELVERSLRQAAL---------WDEVKDKLKqsglSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907149462 594 LDECTSAV----SVDVEDYIysHCRKVGITLFTVSH 625
Cdd:PRK14243 175 MDEPCSALdpisTLRIEELM--HELKEQYTIIIVTH 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
453-599 |
2.47e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.24 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 453 DILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLFY-------------------VPQRPY 513
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--------RLLTPQSGTVFLgdkpismlssrqlarrlalLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 514 MTLG-TLRDQVIYPD-------GKEDQKKRGISDQVLKEyldnVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLF 585
Cdd:PRK11231 87 TPEGiTVRELVAYGRspwlslwGRLSAEDNARVNQAMEQ----TRINHLADRR-----LTD----LSGGQRQRAFLAMVL 153
|
170
....*....|....
gi 1907149462 586 YHKPQFAILDECTS 599
Cdd:PRK11231 154 AQDTPVVLLDEPTT 167
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
456-625 |
3.16e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------------KPERGKLFYVPQRPYMTLG---T 518
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtlspgklQALRRDIQFIFQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 519 LRDQVIYP-------DGKEDQKKrgisdqvLKEYLDNVQLghilEREGGWDSVQDWmdvlSGGEKQRMAMARLFYHKPQF 591
Cdd:PRK10261 420 VGDSIMEPlrvhgllPGKAAAAR-------VAWLLERVGL----LPEHAWRYPHEF----SGGQRQRICIARALALNPKV 484
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907149462 592 AILDECTSAVSVDVEDYIYSHC----RKVGITLFTVSH 625
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLldlqRDFGIAYLFISH 522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
418-626 |
3.25e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 418 IEGAQASPLVPGAGEIintdniiKFDHVPLA-TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVlgelwpLFggR 496
Cdd:PLN03130 1223 IENNRPPPGWPSSGSI-------KFEDVVLRyRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNA------LF--R 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 497 LTKPERGK-------------------LFYVPQRPYMTLGTLRDQvIYPDGKEdqkkrgiSDQVLKEYLDNVQLGHILER 557
Cdd:PLN03130 1288 IVELERGRilidgcdiskfglmdlrkvLGIIPQAPVLFSGTVRFN-LDPFNEH-------NDADLWESLERAHLKDVIRR 1359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907149462 558 EG-GWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRK--VGITLFTVSHR 626
Cdd:PLN03130 1360 NSlGLDAeVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREefKSCTMLIIAHR 1432
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
455-624 |
3.50e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.07 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPL------------FGGRLTKP---------ERGKLFYVPQR-P 512
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearvegevrlFGRNIYSPdvdpievrrEVGMVFQYPNPfP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 513 YMTlgtlrdqvIYPDGKEDQKKRGISDQvlKEYLDNVqLGHILEREGGWDSVQDWMD----VLSGGEKQRMAMARLFYHK 588
Cdd:PRK14267 99 HLT--------IYDNVAIGVKLNGLVKS--KKELDER-VEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907149462 589 PQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVS 624
Cdd:PRK14267 168 PKILLMDEPTANIdpvgTAKIEELLFELKKEYTIVLVTHS 207
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
431-596 |
4.33e-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: 48.70 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 431 GEIINTDNIIKFdhvplaTPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFG---------GRLTKPE 501
Cdd:cd03289 1 GQMTVKDLTAKY------TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGdiqidgvswNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 502 RGKLF-YVPQRPYMTLGTLRdQVIYPDGK-EDQKKRGISDQV-LKEYLDNV--QLGHILErEGGWdsvqdwmdVLSGGEK 576
Cdd:cd03289 75 WRKAFgVIPQKVFIFSGTFR-KNLDPYGKwSDEEIWKVAEEVgLKSVIEQFpgQLDFVLV-DGGC--------VLSHGHK 144
|
170 180
....*....|....*....|
gi 1907149462 577 QRMAMARLFYHKPQFAILDE 596
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDE 164
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
387-611 |
4.75e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.63 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 387 FTARITeLMQVLKDLNH--GRYERTMVS----------QQEKGIegaqasplvpGAGEIINTDNIIKFDHVPLATPNGDI 454
Cdd:PRK11176 288 FSSMIA-LMRPLKSLTNvnAQFQRGMAAcqtlfaildlEQEKDE----------GKRVIERAKGDIEFRNVTFTYPGKEV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 L-IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTkpergkLFYVPQRPYmTLGTLRDQV--------IY 525
Cdd:PRK11176 357 PaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL------LDGHDLRDY-TLASLRNQValvsqnvhLF 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 526 PD--------GKEDQKKRgisDQVLKEYLDNVQLGHILEREGGWDSVQDWMDV-LSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:PRK11176 430 NDtianniayARTEQYSR---EQIEEAARMAYAMDFINKMDNGLDTVIGENGVlLSGGQRQRIAIARALLRDSPILILDE 506
|
250
....*....|....*
gi 1907149462 597 CTSAVSVDVEDYIYS 611
Cdd:PRK11176 507 ATSALDTESERAIQA 521
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
450-596 |
5.22e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.07 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 450 PNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGRLT---KP-ERGkLFYVPQR----PY 513
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagleritsGEIW--IGGRVVnelEPaDRD-IAMVFQNyalyPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 514 MtlgTLRDQVIYpdgkeDQKKRGIS----DQVLKEYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMARLFY 586
Cdd:PRK11650 91 M---SVRENMAY-----GLKIRGMPkaeiEERVAEAARILELEPLLDRkprE------------LSGGQRQRVAMGRAIV 150
|
170
....*....|
gi 1907149462 587 HKPQFAILDE 596
Cdd:PRK11650 151 REPAVFLFDE 160
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
448-604 |
6.06e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 448 ATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGR----LTKPERGKL--FYVPQR 511
Cdd:CHL00131 15 ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaykileGDI--LFKGEsildLEPEERAHLgiFLAFQY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 512 PYMTLGTLRDQVIYPDGKEDQKKRGISD-------QVLKEYLDNVQLG-HILER---EGgwdsvqdwmdvLSGGEKQR-- 578
Cdd:CHL00131 93 PIEIPGVSNADFLRLAYNSKRKFQGLPEldpleflEIINEKLKLVGMDpSFLSRnvnEG-----------FSGGEKKRne 161
|
170 180
....*....|....*....|....*..
gi 1907149462 579 -MAMARLfyhKPQFAILDECTSAVSVD 604
Cdd:CHL00131 162 iLQMALL---DSELAILDETDSGLDID 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
455-637 |
6.20e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.64 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWplfggrltKPERGKLFYVPQ----------------------RP 512
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL--------NPEKGEILFERQsikkdlctyqkqlcfvghrsgiNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 513 YMtlgTLRDQVIYpDGKEDQKKRGISdqvlkEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFA 592
Cdd:PRK13540 88 YL---TLRENCLY-DIHFSPGAVGIT-----ELCRLFSLEHLIDYPCG---------LLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907149462 593 ILDEctSAVSVD------VEDYIYSHCRKVGITLFTVSHRKSLWK--HHEYYL 637
Cdd:PRK13540 150 LLDE--PLVALDelslltIITKIQEHRAKGGAVLLTSHQDLPLNKadYEEYHL 200
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
455-599 |
8.01e-06 |
|
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: 47.16 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplfGGRLTKPERGKLFYVPQRPyMTLGTLRDQVIYpdgkedqkk 534
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------AGRRTGLGVSGEVLINGRP-LDKRSFRKIIGY--------- 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907149462 535 rgiSDQvlkeylDNVQLGHILEREGGWDSVQdwMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:cd03213 87 ---VPQ------DDILHPTLTVRETLMFAAK--LRGLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
459-604 |
9.99e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 459 LSFevRSGANVLICGPNGCGKSSLFRVL--------GELWPLFGGRLtkperGklfYVPQRPYMTLG-TLRDQVIypDGK 529
Cdd:PRK11819 28 LSF--FPGAKIGVLGLNGAGKSTLLRIMagvdkefeGEARPAPGIKV-----G---YLPQEPQLDPEkTVRENVE--EGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 530 EDQKkrgisdQVLKEYlDNV-------------------QLGHILEREGGWDS---VQDWMD------------VLSGGE 575
Cdd:PRK11819 96 AEVK------AALDRF-NEIyaayaepdadfdalaaeqgELQEIIDAADAWDLdsqLEIAMDalrcppwdakvtKLSGGE 168
|
170 180 190
....*....|....*....|....*....|..
gi 1907149462 576 KQRMAMARLFYHKPQFAILDECTS---AVSVD 604
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNhldAESVA 200
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
456-625 |
1.02e-05 |
|
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: 47.34 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGR-LT--KPER----G--------KLFyvpqrPYM 514
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFYRPtsgriLFDGRdITglPPHRiarlGiartfqnpRLF-----PEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 515 T------------LGTLRDQVIYPDGKEDQKKRGISDQVLkEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMA 582
Cdd:COG0411 95 TvlenvlvaaharLGRGLLAALLRLPRARREEREARERAE-ELLERVGLADRADEPAG---------NLSYGQQRRLEIA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907149462 583 RLFYHKPQFAILDECTSAVS----VDVEDYIYSHCRKVGITLFTVSH 625
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNpeetEELAELIRRLRDERGITILLIEH 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
437-607 |
1.20e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 437 DNIIKFD-HVPLATPNGDILIQ---------DLSFEVRSGA----NVL-ICGPNGCGKSSLFRVL-GELWPLFGGRLTKP 500
Cdd:PRK13409 321 PEPIEFEeRPPRDESERETLVEypdltkklgDFSLEVEGGEiyegEVIgIVGPNGIGKTTFAKLLaGVLKPDEGEVDPEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 501 ergKLFYVPQrpYMTlgtlRDQviypDGKEDQKKRGISDQVLKEYLDN-----VQLGHILEREggwdsvqdwMDVLSGGE 575
Cdd:PRK13409 401 ---KISYKPQ--YIK----PDY----DGTVEDLLRSITDDLGSSYYKSeiikpLQLERLLDKN---------VKDLSGGE 458
|
170 180 190
....*....|....*....|....*....|..
gi 1907149462 576 KQRMAMARLFYHKPQFAILDEcTSAvSVDVED 607
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDE-PSA-HLDVEQ 488
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
464-599 |
2.16e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 464 RSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE--------RG-------------------KLFYVPQRPYMT 515
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILsGELKPNLGDYDEEPSwdevlkrfRGtelqdyfkklangeikvahKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 516 LGTLRDQViypdGKEDQkkRGISDQVLKEyLDnvqLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:COG1245 177 KGTVRELL----EKVDE--RGKLDELAEK-LG---LENILDRD---------ISELSGGELQRVAIAAALLRDADFYFFD 237
|
....
gi 1907149462 596 ECTS 599
Cdd:COG1245 238 EPSS 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
466-642 |
2.73e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 466 GANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQR----------PYMTLGTLRDQViypdgkedqkk 534
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLaGELAPV-SGEIGLAKGIKLGYFAQHqleflradesPLQHLARLAPQE----------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 535 rgiSDQVLKEYLdnvqlghilereGGW----DSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIY 610
Cdd:PRK10636 406 ---LEQKLRDYL------------GGFgfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
|
170 180 190
....*....|....*....|....*....|....
gi 1907149462 611 SHCRKVGITLFTVSHRKSLWKH--HEYYLHMDGR 642
Cdd:PRK10636 471 EALIDFEGALVVVSHDRHLLRSttDDLYLVHDGK 504
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
456-498 |
2.91e-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: 45.60 E-value: 2.91e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT 498
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
456-625 |
3.22e-05 |
|
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: 47.10 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPLFGGR---LTKP---ERGKLfyvpqRPYMtlGTLRD 521
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIagvleptsGEVNVRVGDEwvdMTKPgpdGRGRA-----KRYI--GILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 522 QV-IYPDGKE-DQKKRGISDQVLKEyLDNVQLGHILEREGGWD----SVQDWM-DVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:TIGR03269 373 EYdLYPHRTVlDNLTEAIGLELPDE-LARMKAVITLKMVGFDEekaeEILDKYpDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190
....*....|....*....|....*....|....*
gi 1907149462 595 DECTSAVS----VDVEDYIYSHCRKVGITLFTVSH 625
Cdd:TIGR03269 452 DEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSH 486
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
436-629 |
3.68e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.54 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 436 TDNIIKFDHVPLATPNGD---ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL--------GELwPLFGGRLTK---PE 501
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEhelSILTGVELVVKRGETIALIGESGSGKSTLLAILaglddgssGEV-SLVGQPLHQmdeEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 502 RGKLF-----YVPQRpYMTLGTL--RDQVIYP---DGKEDQKKRGISDQVLKEYLDNVQLGHILEReggwdsvqdwmdvL 571
Cdd:PRK10584 82 RAKLRakhvgFVFQS-FMLIPTLnaLENVELPallRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-------------L 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907149462 572 SGGEKQRMAMARLFYHKPQFAILDECTSavSVD------VEDYIYSHCRKVGITLFTVSHRKSL 629
Cdd:PRK10584 148 SGGEQQRVALARAFNGRPDVLFADEPTG--NLDrqtgdkIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
457-603 |
4.02e-05 |
|
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: 46.60 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 457 QDLSFEVRSGANVLICGPNGCGKSSLFRVL-------GELWplFGGR----LT----KPERGKLFYVPQRPY------MT 515
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALlrlipseGEIR--FDGQdldgLSrralRPLRRRMQVVFQDPFgslsprMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 516 LGT-----LRDQVIYPDGKEdqkKRGISDQVLKEyldnVQL-GHILER---EggwdsvqdwmdvLSGGEKQRMAMARLFY 586
Cdd:COG4172 381 VGQiiaegLRVHGPGLSAAE---RRARVAEALEE----VGLdPAARHRyphE------------FSGGQRQRIAIARALI 441
|
170
....*....|....*....
gi 1907149462 587 HKPQFAILDECTSA--VSV 603
Cdd:COG4172 442 LEPKLLVLDEPTSAldVSV 460
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
462-606 |
4.49e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 45.48 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 462 EVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTkpERGKLFYVPQrpYMTL---GTLRDQViypdgKEDQKKRGI 537
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLaGVLKPDEGDIEI--ELDTVSYKPQ--YIKAdyeGTVRDLL-----SSITKDFYT 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907149462 538 SDQVLKEYLDNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDEcTSAvSVDVE 606
Cdd:cd03237 92 HPYFKTEIAKPLQIEQILDRE-----VPE----LSGGELQRVAIAACLSKDADIYLLDE-PSA-YLDVE 149
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
457-504 |
4.70e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.46 E-value: 4.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907149462 457 QDLSFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGK 504
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLI--------AGILEPTSGR 82
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
458-625 |
4.84e-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: 44.79 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 458 DLSFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGRLTKPERGKLFYVPQRPYMTLgtLRDQVIYPDGKEDQ---- 532
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNlIAGFETPQSGRVLINGVDVTAAPPADRPVSML--FQENNLFAHLTVEQnvgl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 533 ------KKRGISDQVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAVS---- 602
Cdd:cd03298 94 glspglKLTAEDRQAIEVALARVGLAGLEKRLPG---------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalr 164
|
170 180
....*....|....*....|...
gi 1907149462 603 VDVEDYIYSHCRKVGITLFTVSH 625
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTH 187
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
571-626 |
5.75e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 5.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 571 LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD----VEDYIYSHCRKVGITLFTVSHR 626
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
452-642 |
9.75e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 44.70 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 452 GDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP-----------LFGGRLTKPER---------GKLFYVPQR 511
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrysgdvLLGGRSIFNYRdvlefrrrvGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 512 PYMT-----LGTLRDQVIYPDgkedQKKRGISDQVLKEYldnvqlghilereGGWDSVQDWMD----VLSGGEKQRMAMA 582
Cdd:PRK14271 113 FPMSimdnvLAGVRAHKLVPR----KEFRGVAQARLTEV-------------GLWDAVKDRLSdspfRLSGGQQQLLCLA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907149462 583 RLFYHKPQFAILDECTSAV----SVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGR 642
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALdpttTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGR 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
439-625 |
1.07e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 44.72 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 439 IIKFDHVPLA----TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGG--------------RLTK 499
Cdd:PRK13643 1 MIKFEKVNYTyqpnSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLnGLLQPTEGKvtvgdivvsstskqKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 500 PER---GKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKKRgiSDQVLKEYLDNVQLGHILEREGGWDsvqdwmdvLSGGEK 576
Cdd:PRK13643 81 PVRkkvGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEK--AEKIAAEKLEMVGLADEFWEKSPFE--------LSGGQM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907149462 577 QRMAMARLFYHKPQFAILDECTSAVSVDVE---DYIYSHCRKVGITLFTVSH 625
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
456-610 |
1.54e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 456 IQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRpymtlgTLRDQVIYPdgKEDQKKR 535
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD------GLANGIVYI--SEDRKRD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 536 GIsdqVL----KE--------YLDN--VQLGHILEREggwdSVQDWMDV--------------LSGGEKQRMAMARLFYH 587
Cdd:PRK10762 340 GL---VLgmsvKEnmsltalrYFSRagGSLKHADEQQ----AVSDFIRLfniktpsmeqaiglLSGGNQQKVAIARGLMT 412
|
170 180
....*....|....*....|...
gi 1907149462 588 KPQFAILDECTSAVSVDVEDYIY 610
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIY 435
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
440-582 |
2.22e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 440 IKFD-HVPLATPNGDILIQ---------DLSFEVRSGA----NVL-ICGPNGCGKSSLFRVL-GELwplfggrltKPERG 503
Cdd:COG1245 325 IEFEvHAPRREKEEETLVEypdltksygGFSLEVEGGEiregEVLgIVGPNGIGKTTFAKILaGVL---------KPDEG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 504 KLF------YVPQRP----YMTLGTLRDQVIYPDgkedqkkrgISDQVLK-EYLDNVQLGHILEREggwdsvqdwMDVLS 572
Cdd:COG1245 396 EVDedlkisYKPQYIspdyDGTVEEFLRSANTDD---------FGSSYYKtEIIKPLGLEKLLDKN---------VKDLS 457
|
170
....*....|
gi 1907149462 573 GGEKQRMAMA 582
Cdd:COG1245 458 GGELQRVAIA 467
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
449-625 |
2.76e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.50 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 449 TPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggrlTKPERGKLF---YVPQRPYMTLGTLRDQV-- 523
Cdd:PRK13637 16 TPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--------LKPTSGKIIidgVDITDKKVKLSDIRKKVgl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 524 -------------IYPDGKEDQKKRGISDQVL----KEYLDNVQLghilereggwdSVQDWMDV----LSGGEKQRMAMA 582
Cdd:PRK13637 88 vfqypeyqlfeetIEKDIAFGPINLGLSEEEIenrvKRAMNIVGL-----------DYEDYKDKspfeLSGGQKRRVAIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907149462 583 RLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV----GITLFTVSH 625
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSH 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
457-601 |
3.94e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 457 QDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT------------KPERGKLFYVPQRPYMTLGTLRDQVI 524
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnlkdinlKWWRSKIGVVSQDPLLFSNSIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 525 YP-------------------DGKEDQKKRGISDQV----LKEYLDNVQLGHILEREGGWDSVQDW--MDV--------- 570
Cdd:PTZ00265 482 YSlyslkdlealsnyynedgnDSQENKNKRNSCRAKcagdLNDMSNTTDSNELIEMRKNYQTIKDSevVDVskkvlihdf 561
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907149462 571 ------------------LSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:PTZ00265 562 vsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
455-638 |
6.62e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 41.88 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 455 LIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLFYVPQRPYMtlgtLRD---QVIYPDGKED 531
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCIN--------FLEKPSEGSIVVNGQTINL----VRDkdgQLKVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 532 QKKR------------------------------GISDQVLKE----YLDNVQlghILEREGGWDSVQdwmdvLSGGEKQ 577
Cdd:PRK10619 88 RLLRtrltmvfqhfnlwshmtvlenvmeapiqvlGLSKQEAREravkYLAKVG---IDERAQGKYPVH-----LSGGQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907149462 578 RMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKV---GITLFTVSHRKSLWKH---HEYYLH 638
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHvssHVIFLH 226
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
471-615 |
9.25e-04 |
|
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: 41.40 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 471 ICGPNGCGKSSL-----FrVLGE---------LWPL-FGGRLTKPergklfyVPQRPYMTLgtlrdQVIYPDGKEDQKKR 535
Cdd:cd03275 27 IIGPNGSGKSNLmdaisF-VLGEksshlrsknLKDLiYRARVGKP-------DSNSAYVTA-----VYEDDDGEEKTFRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 536 GISDQV-----------LKEYLDNVQLGHILER-------EGGWDSV----------QDwMDVLSGGEKQRMAMARLF-- 585
Cdd:cd03275 94 IITGGSssyringkvvsLKEYNEELEKINILVKarnflvfQGDVESIasknppgkrfRD-MDNLSGGEKTMAALALLFai 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907149462 586 --YHKPQFAILDECTSA---VSVD-VEDYIYSHCRK 615
Cdd:cd03275 173 hsYQPAPFFVLDEVDAAldnTNVGkVASYIREQAGP 208
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
454-599 |
3.99e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 40.42 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 454 ILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWP----------LFGGRLTKPE-RGKLFYVPQRPyMTLGTL--R 520
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkgsgsvlLNGMPIDAKEmRAISAYVQQDD-LFIPTLtvR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149462 521 DQVIY------PDGKEDQKKRGISDQVLKEY-LDNVQLGHIlereggwdSVQDWMDVLSGGEKQRMAMARLFYHKPQFAI 593
Cdd:TIGR00955 118 EHLMFqahlrmPRRVTKKEKRERVDEVLQALgLRKCANTRI--------GVPGRVKGLSGGERKRLAFASELLTDPPLLF 189
|
....*.
gi 1907149462 594 LDECTS 599
Cdd:TIGR00955 190 CDEPTS 195
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
456-486 |
5.73e-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: 39.60 E-value: 5.73e-03
10 20 30
....*....|....*....|....*....|.
gi 1907149462 456 IQDLSFEVRSGANVLIcGPNGCGKSSLFRVL 486
Cdd:COG3593 14 IKDLSIELSDDLTVLV-GENNSGKSSILEAL 43
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
456-483 |
9.81e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.86 E-value: 9.81e-03
10 20
....*....|....*....|....*...
gi 1907149462 456 IQDLSFEVRSGANvLICGPNGCGKSSLF 483
Cdd:pfam13476 9 FRDQTIDFSKGLT-LITGPNGSGKTTIL 35
|
|
| |
