|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-648 |
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: 1007.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 1 MAAYSKYLTARHSVV-------AGAAACALLCLLRKRRRAAAKHGKKNEKPTLQNNEK----EGKKERAVVDRVFVARIC 69
Cdd:TIGR00954 1 MAVLSKYRLLRSTSNnktdkqdSPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKhstiEGAKKKAHVNGVFLGKLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 70 RILKIMVPRTFCKETGYLILIAVMLIVRTYCDIWMIQNGTVIESAIIGRSRKDFKKYLFNFIAAMPAISLVNNFLKYGLN 149
Cdd:TIGR00954 81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 150 ELKLCFRVRLTKYLYEEYLQAYTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTNAIGAQ 229
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 230 GPATMMAYLIVSGFFLTRLRRPIGKMTIAEQKYEGEYRFVNSRLITNSEEIAFYNGNLREKQTIHKTFHKLVEHLHNFIL 309
Cdd:TIGR00954 241 GPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 310 FRFSMGFIDTIIAKYLATVVGYLVVSRPFLNLAHPRHQKSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFT 389
Cdd:TIGR00954 321 FRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 390 ARITELMQVLKDLNRGRYQRTMISQHEKDGDRTQTIPLIPGTGEIINTDNLIKFDHVPLATPNGDILIRDLNFEVRSGAN 469
Cdd:TIGR00954 401 ARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 470 VLICGPNGCGKSSLFRVLGELWPLFGGCLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDTVEDQRKKGISDQVLKEYLDN 549
Cdd:TIGR00954 481 LLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 550 VQLGQILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKS 629
Cdd:TIGR00954 561 VQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKS 640
|
650
....*....|....*....
gi 1985402263 630 LWKHHDFYLHMDGRGNYEF 648
Cdd:TIGR00954 641 LWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
71-339 |
1.69e-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: 367.32 E-value: 1.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 71 ILKIMVPRTFCKETGYLILIAVMLIVRTYCDIWMIQNGTVIESAIIGRSRKDFKKYLFNFIAAMPAISLVNNFLKYGLNE 150
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 151 LKLCFRVRLTKYLYEEYLQAYTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTNAIGAQG 230
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 231 PATMMAYLIVSGFFLTRLRRPIGKMTIAEQKYEGEYRFVNSRLITNSEEIAFYNGNLREKQTIHKTFHKLVEHLHNFILF 310
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 1985402263 311 RFSMGFIDTIIAKYLATVVGYLVVSRPFL 339
Cdd:pfam06472 241 RLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
85-651 |
5.54e-99 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 314.44 E-value: 5.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 85 GYLILIAVMLIVRTYCDIWMI-QNGTVIeSAIIGRSRKDFKKYLFNF---IAAMPAISLVNNFLKYGLnELKLcfRVRLT 160
Cdd:COG4178 25 GLLALLLLLTLASVGLNVLLNfWNRDFY-DALQARDAAAFWQQLGVFallAAISILLAVYQTYLRQRL-QIRW--REWLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 161 KYLYEEYLQAYTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKL-------TNAIG---AQG 230
Cdd:COG4178 101 ERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLISFIGILwslsgslTFTLGgysITI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 231 PATMM----AYLIVSGFFLTRLRRPIGKMTIAEQKYEGEYRFVNSRLITNSEEIAFYNGNLREKQTIHKTFHKLVEHLHN 306
Cdd:COG4178 181 PGYMVwaalIYAIIGTLLTHLIGRPLIRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 307 FILFRFSMGFIDTIIAkYLATVVGYLVVSrpflnlahPRhqksthselledyYQSGRMLL-----------RMSQALGRI 375
Cdd:COG4178 261 LIRRQRNLTFFTTGYG-QLAVIFPILVAA--------PR-------------YFAGEITLgglmqaasafgQVQGALSWF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 376 VlagREMTRLAGFTA---RITELMQVLkdlnrgryqrtmiSQHEKDGDRTQTIplipgtgeIINTDNLIKFDHVPLATPN 452
Cdd:COG4178 319 V---DNYQSLAEWRAtvdRLAGFEEAL-------------EAADALPEAASRI--------ETSEDGALALEDLTLRTPD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 453 GDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDTVED 532
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 533 qrkkgISDQVLKEYLDNVQLGQILEReggWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYS 612
Cdd:COG4178 455 -----FSDAELREALEAVGLGHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1985402263 613 HCRK--VGITLFTVSHRKSLWKHHDFYLHMDGRGNYEFKKI 651
Cdd:COG4178 527 LLREelPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPA 567
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
441-646 |
1.08e-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: 270.95 E-value: 1.08e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLTKPERGKLFYVPQRPYMTLGTL 520
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 521 RDQVIYPdtvedqrkkgisdqvlkeyldnvqlgqilereggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 600
Cdd:cd03223 81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1985402263 601 AVSVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHDFYLHMDGRGNY 646
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
441-626 |
2.88e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.38 E-value: 2.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILiRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT---------KPE--RGKLFYV 509
Cdd:COG4619 1 LELEGLSFRVGGKPIL-SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsamPPPewRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 510 PQRPYMTLGTLRDQVIYPDTVedqRKKGISDQVLKEYLDNVQLGQ-ILEREggwdsVQDwmdvLSGGEKQRMAMARLFYH 588
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQL---RERKFDRERALELLERLGLPPdILDKP-----VER----LSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1985402263 589 KPQFAILDECTSA---VSVD-VEGYIYSHCRKVGITLFTVSH 626
Cdd:COG4619 148 QPDVLLLDEPTSAldpENTRrVEELLREYLAEEGRAVLWVSH 189
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
85-627 |
1.70e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.57 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 85 GYLILIAVMLIVRTYCDIWMIQ-NGTVIESAIIGRSRKdfkkYLFNFIAAMPAISLVNNFLKYGLNEL--KLCFRV--RL 159
Cdd:COG1132 21 GLLILALLLLLLSALLELLLPLlLGRIIDALLAGGDLS----ALLLLLLLLLGLALLRALLSYLQRYLlaRLAQRVvaDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 160 TKYLYEEYL-QAYTYY---KMGNLDNRIanpdqllTQDVekfcNSVVDLYSNLSKPFLDIVLYIfkltnaIGAqgpATMM 235
Cdd:COG1132 97 RRDLFEHLLrLPLSFFdrrRTGDLLSRL-------TNDV----DAVEQFLAHGLPQLVRSVVTL------IGA---LVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 236 AYL------------IVSGFFLTRLRRPIGKMTIAEQKYEGEyrfVNSRL---ITNSEEIAFYNgnlREKQTIHKtFHKL 300
Cdd:COG1132 157 FVIdwrlalivllvlPLLLLVLRLFGRRLRKLFRRVQEALAE---LNGRLqesLSGIRVVKAFG---REERELER-FREA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 301 VEHLHNFIL-FRFSMGFIDTIIakYLATVVGYLVVsrpflnlahprhqksthselledYYQSGRMLLRMSQALGRIVLAg 379
Cdd:COG1132 230 NEELRRANLrAARLSALFFPLM--ELLGNLGLALV-----------------------LLVGGLLVLSGSLTVGDLVAF- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 380 reMTRLAGFTARITELMQVLKDLNRGR--YQR--TMISQHEKDGDRTQTIPLIPGTGEIintdnliKFDHVPLATPNGDI 455
Cdd:COG1132 284 --ILYLLRLFGPLRQLANVLNQLQRALasAERifELLDEPPEIPDPPGAVPLPPVRGEI-------EFENVSFSYPGDRP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGC----LTKPE-RGKLFYVPQRPYMTLGTLRDQV 524
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDptsgriLIDGVdirdLTLESlRRQIGVVPQDTFLFSGTIRENI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 525 IYPdtvedqrKKGISDQVLKEYLDNVQLGQILER-EGGWDSVqdwmdV------LSGGEKQRMAMARLFYHKPQFAILDE 597
Cdd:COG1132 435 RYG-------RPDATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGGQRQRIAIARALLKDPPILILDE 502
|
570 580 590
....*....|....*....|....*....|..
gi 1985402263 598 CTSAVSVDVEGYIYSHCRKV--GITLFTVSHR 627
Cdd:COG1132 503 ATSALDTETEALIQEALERLmkGRTTIVIAHR 534
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
456-642 |
1.51e-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: 107.56 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLfGGCLTKPerGKLFYVPQRPYMTLGTLRDQVIYPDTVEDQR 534
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKL-SGSVSVP--GSIAYVSQEPWIQNGTIRENILFGKPFDEER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 535 kkgisdqvLKEYLDNVQLGQILER-EGGwdsvqDWMDV------LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVE 607
Cdd:cd03250 97 --------YEKVIKACALEPDLEIlPDG-----DLTEIgekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVG 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1985402263 608 GYIYSHC----RKVGITLFTVSHRKSLWKHHDFYLHMDG 642
Cdd:cd03250 164 RHIFENCilglLLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
441-643 |
3.62e-25 |
|
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: 102.46 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT---------KPE--RGKLFY 508
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdlDLEslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 509 VPQRPYMTLGTLRDqviypdtvedqrkkgisdqvlkeyldNVqlgqilereggwdsvqdwmdvLSGGEKQRMAMARLFYH 588
Cdd:cd03228 81 VPQDPFLFSGTIRE--------------------------NI---------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1985402263 589 KPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHDFYLHMD-GR 643
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDdGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
441-642 |
4.55e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 109.85 E-value: 4.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGC----LTKPE-RGKLFYV 509
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlGFLPPysgsiLINGVdlsdLDPASwRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 510 PQRPYMTLGTLRDQV-IY-PDtvedqrkkgISDQVLKEYLDNVQLGQILER-EGGWDSVqdwmdV------LSGGEKQRM 580
Cdd:COG4988 417 PQNPYLFAGTIRENLrLGrPD---------ASDEELEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985402263 581 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHDFYLHMDG 642
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDD 546
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
429-627 |
1.43e-22 |
|
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: 102.15 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 429 PGTGEIINTDNLIKFDHVPLATPNGD-ILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGC---- 497
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpqsgsiTLGGVdlrd 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 498 LTKPERGKLF-YVPQRPYMTLGTLRD--QVIYPDtvedqrkkgISDQVLKEYLDNVQLGQILER-EGGWDSvqdWMDV-- 571
Cdd:COG4987 402 LDEDDLRRRIaVVPQRPHLFDTTLREnlRLARPD---------ATDEELWAALERVGLGDWLAAlPDGLDT---WLGEgg 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985402263 572 --LSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVE------GYIYSHCRkvGITLFTVSHR 627
Cdd:COG4987 470 rrLSGGERRRLALARALLRDAPILLLDEPTE--GLDAAteqallADLLEALA--GRTVLLITHR 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
441-630 |
4.20e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 100.44 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGCLT----KPERGKLFYV 509
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLlGFVDPtegsiaVNGVPLAdadaDSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 510 PQRPYMTLGTLRDQVIYpdtvedqRKKGISDQVLKEYLDNVQLGQIL-EREGGWDS-VQDWMDVLSGGEKQRMAMARLFY 587
Cdd:TIGR02857 402 PQHPFLFAGTIAENIRL-------ARPDASDAEIREALERAGLDEFVaALPQGLDTpIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1985402263 588 HKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSL 630
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
457-600 |
4.26e-22 |
|
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: 93.10 E-value: 4.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGCLTKPE----RGKLFYVPQ--RPYMTLgTLRDQ 523
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPtegtilLDGQDLTDDErkslRKEIGYVFQdpQLFPRL-TVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985402263 524 VIYPDTVEDQRKKGISDQVlKEYLDNVQLGQILEReggwdSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 600
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARA-EEALEKLGLGDLADR-----PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
452-643 |
1.04e-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: 93.75 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT---KP---ERGKLFYVPQRPYMtlgtLRDqvi 525
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgKPlekERKRIGYVPQRRSI----DRD--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 526 YPDTVED------QRKKGISDQVLKEYLDNVQlgQILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:cd03235 83 FPISVRDvvlmglYGHKGLFRRLSKADKAKVD--EALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1985402263 600 SAVSVDVEGYIYSHCRKV---GITLFTVSH-RKSLWKHHDFYLHMDGR 643
Cdd:cd03235 161 AGVDPKTQEDIYELLRELrreGMTILVVTHdLGLVLEYFDRVLLLNRT 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
367-647 |
1.95e-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: 99.14 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 367 RMSQALGRIVLAGREMTRLAGFTARITELMQVLKDlnrgryqrtmisqhEKDGDRTQTIPLIPGTgeiintdnlIKFDHV 446
Cdd:COG2274 423 RFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPE--------------REEGRSKLSLPRLKGD---------IELENV 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 447 PLA-TPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GelwplfggcLTKPERGKLFY--VPQRpYMTLGTLRD 522
Cdd:COG2274 480 SFRyPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlG---------LYEPTSGRILIdgIDLR-QIDPASLRR 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 523 QV--------IYPDTVED---QRKKGISDQVLKEYLDNVQLGQ-ILEREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHK 589
Cdd:COG2274 550 QIgvvlqdvfLFSGTIREnitLGDPDATDEEIIEAARLAGLHDfIEALPMGYDTvVGEGGSNLSGGQRQRLAIARALLRN 629
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985402263 590 PQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHDFYLHMDG-----RGNYE 647
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDKgriveDGTHE 694
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
441-629 |
6.57e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 92.29 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT-----------KPERGKLFYV 509
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 510 PQrpymtlgtlrDQVIYPDTVEDQRKKGISDQVLKEYLDNVQLGQILER----EGGWDSVqdwmdV------LSGGEKQR 579
Cdd:cd03253 81 PQ----------DTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKimrfPDGYDTI-----VgerglkLSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1985402263 580 MAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKS 629
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
452-641 |
6.48e-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: 86.92 E-value: 6.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggCLTKPERGKLFYvpqrpymtlgtlrdqviypdtve 531
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA--------GLLKPTSGEILI----------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 532 dqRKKGISDQVLKEYLDNVQ-LGQilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD----V 606
Cdd:cd00267 59 --DGKDIAKLPLEELRRRIGyVPQ-----------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAsrerL 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 1985402263 607 EGYIYSHCRKvGITLFTVSHR-KSLWKHHDFYLHMD 641
Cdd:cd00267 120 LELLRELAEE-GRTVIIVTHDpELAELAADRVIVLK 154
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
436-626 |
7.22e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 86.30 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 436 NTDNLIKFDHVPLATpNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRV-LGELWPL-----FGGCLTKPERGKLFYV 509
Cdd:COG1121 2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAiLGLLPPTsgtvrLFGKPPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 510 PQRPYMTLGtlrdqviYPDTVED------QRKKGISDQVLKEYLDNVQlgQILEREGGWDSVQDWMDVLSGGEKQRMAMA 583
Cdd:COG1121 81 PQRAEVDWD-------FPITVRDvvlmgrYGRRGLFRRPSRADREAVD--EALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1985402263 584 RLFYHKPQFAILDECTSAVSVDVEGYIYS---HCRKVGITLFTVSH 626
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTH 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
452-626 |
8.39e-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: 85.22 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGCLTKPE---RGKLFYVPQRP--YMTLg 518
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILagllppsaGEVL-WNGEPIRDARedyRRRLAYLGHADglKPEL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 519 TLRDQVIYpdtVEDQRKKGISDQVLKEYLDNVQLGQILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDEC 598
Cdd:COG4133 91 TVRENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 1985402263 599 TSAVSVD----VEGYIYSHCRKVGITLFTvSH 626
Cdd:COG4133 159 FTALDAAgvalLAELIAAHLARGGAVLLT-TH 189
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
452-626 |
1.23e-18 |
|
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: 85.87 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGC----LTKPERGKLF-YVPQRPYMTLG-T 519
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALaGLLKPssgevLLDGRdlasLSRRELARRIaYVPQEPPAPFGlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 520 LRDQVI---YP-------DTVEDQRkkgISDQVLKEyldnVQLGQILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHK 589
Cdd:COG1120 92 VRELVAlgrYPhlglfgrPSAEDRE---AVEEALER----TGLEHLADRP---------VDELSGGERQRVLIARALAQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1985402263 590 PQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 626
Cdd:COG1120 156 PPLLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLH 196
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
442-641 |
1.25e-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: 84.83 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 442 KFDHVPLATPNGD-ILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGCLTKPE----RGKLFY 508
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLngllgptsGEVL-VDGKDLTKLSlkelRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 509 VPQRPymtlgtlRDQVIYPdTVED---------QRKKGISDQVLKEYLDNVQLGQILEReggwdSVQDwmdvLSGGEKQR 579
Cdd:cd03225 80 VFQNP-------DDQFFGP-TVEEevafglenlGLPEEEIEERVEEALELVGLEGLRDR-----SPFT----LSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985402263 580 MAMARLFYHKPQFAILDECTSavSVDVEGY-----IYSHCRKVGITLFTVSHRKSLWKHH-DFYLHMD 641
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTA--GLDPAGRrelleLLKKLKAEGKTIIIVTHDLDLLLELaDRVIVLE 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
441-642 |
1.30e-18 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 85.35 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT-----------KPERGKLFYV 509
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 510 PQRPYMTLGTLRDQVIYPDtvedqrkKGISDQVLKEYLDNVQLGQILER-EGGWDS-VQDWMDVLSGGEKQRMAMARLFY 587
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGR-------PNATDEEVIEAAKEAGAHDFIMKlPNGYDTvLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1985402263 588 HKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHDFYLHMDG 642
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLSTIKNADKILVLDD 212
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
436-645 |
1.68e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.77 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 436 NTDNLIKFDHVPLATpNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggclTKPERGKLFYVPQrPYM 515
Cdd:PRK10247 3 ENSPLLQLQNVGYLA-GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL--------ISPTSGTLLFEGE-DIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 516 TLG--TLRDQVIY----P----DTVEDQ-------RKKGISDQVLKEYLDNVQLGQ-ILEReggwdSVQDwmdvLSGGEK 577
Cdd:PRK10247 73 TLKpeIYRQQVSYcaqtPtlfgDTVYDNlifpwqiRNQQPDPAIFLDDLERFALPDtILTK-----NIAE----LSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985402263 578 QRMAMARLFYHKPQFAILDECTSAVSVD----VEGYIYSHCRKVGITLFTVSHRKSLWKHHDFYLHMDGRGN 645
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAG 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
438-642 |
2.48e-18 |
|
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: 84.44 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 438 DNLIKFDHVPLATPN-GDILI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG-------CLTKPE----RG 504
Cdd:cd03248 9 KGIVKFQNVTFAYPTrPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGqvlldgkPISQYEhkylHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 505 KLFYVPQRPYMTLGTLRDQVIYPDTvedqrkkGISDQVLKEYLDNVQLGQ-ILEREGGWDS-VQDWMDVLSGGEKQRMAM 582
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQ-------SCSFECVKEAAQKAHAHSfISELASGYDTeVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985402263 583 ARLFYHKPQFAILDECTSAVSVDVEGYIYS--HCRKVGITLFTVSHRKSLWKHHDFYLHMDG 642
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
452-626 |
5.90e-18 |
|
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: 83.38 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCltkPERGKLFY---------------------VP 510
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA---PDEGEVLLdgkdiydldvdvlelrrrvgmVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 511 QRPYMTLGTLRDQVIYPDTVEDQRKKGISDQVLKEYLDNVQLgqilereggWDSVQDWMDV--LSGGEKQRMAMARLFYH 588
Cdd:cd03260 88 QKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAAL---------WDEVKDRLHAlgLSGGQQQRLCLARALAN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1985402263 589 KPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLftVSH 626
Cdd:cd03260 159 EPEVLLLDEPTSALdpisTAKIEELIAELKKEYTIVI--VTH 198
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
441-630 |
1.15e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 82.25 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDIL-IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWplfggcltKPERGKLF------------ 507
Cdd:cd03245 3 IEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY--------KPTSGSVLldgtdirqldpa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 508 -------YVPQRPYMTLGTLRDQVIYPDT-VEDQRKKGISD-QVLKEYLDNVQLGQILE-REGGwdsvqdwmDVLSGGEK 577
Cdd:cd03245 75 dlrrnigYVPQDVTLFYGTLRDNITLGAPlADDERILRAAElAGVTDFVNKHPNGLDLQiGERG--------RGLSGGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1985402263 578 QRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSL 630
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
456-630 |
1.40e-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: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPlfggcltkPERGK--LFYVPQRPYmTLGTLRDQVIYpdtvedq 533
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR--------PTSGRvrLDGADISQW-DPNELGDHVGY------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 534 rkkgisdqVLKEyldnVQL--GQILEreggwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIY 611
Cdd:cd03246 81 --------LPQD----DELfsGSIAE------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180
....*....|....*....|..
gi 1985402263 612 S---HCRKVGITLFTVSHRKSL 630
Cdd:cd03246 137 QaiaALKAAGATRIVIAHRPET 158
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
420-630 |
3.48e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.54 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 420 DRTQTIPLiPGTGEIINTDNLIKFDHVPLATPN-GDILI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGC 497
Cdd:TIGR00958 459 DRKPNIPL-TGTLAPLNLEGLIEFQDVSFSYPNrPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQ 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 498 LT-----------KPERGKLFYVPQRPYMTLGTLRDQVIY--PDTVEDQrkkgISDQVLKEYLDNVqlgqILEREGGWDS 564
Cdd:TIGR00958 538 VLldgvplvqydhHYLHRQVALVGQEPVLFSGSVRENIAYglTDTPDEE----IMAAAKAANAHDF----IMEFPNGYDT 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985402263 565 VQDWMDV-LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIY-SHCRKvGITLFTVSHRKSL 630
Cdd:TIGR00958 610 EVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQeSRSRA-SRTVLLIAHRLST 676
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
441-643 |
2.19e-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: 78.69 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDI---LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggCLTKPERGKLF---------- 507
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG--------GLDRPTSGEVRvdgtdiskls 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 508 -------------YVPQR----PYMTLgtlRDQVIYPDTVeDQRKKGISDQVLKEYLDNVQLGQILEREGGWdsvqdwmd 570
Cdd:cd03255 73 ekelaafrrrhigFVFQSfnllPDLTA---LENVELPLLL-AGVPKKERRERAEELLERVGLGDRLNHYPSE-------- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985402263 571 vLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHDFYLHM-DGR 643
Cdd:cd03255 141 -LSGGQQQRVAIARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELrDGK 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
441-627 |
3.90e-16 |
|
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: 77.92 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLA-TPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT-----------KPERGKLFY 508
Cdd:cd03244 3 IEFKNVSLRyRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiglHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 509 VPQRPYMTLGTLRDQV----IYpdtvedqrkkgiSDQVLKEYLDNVQLGQILE-REGGWDS-VQDWMDVLSGGEKQRMAM 582
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdpfgEY------------SDEELWQALERVGLKEFVEsLPGGLDTvVEEGGENLSVGQRQLLCL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1985402263 583 ARLFYHKPQFAILDECTSavSVDVEG------YIYSHCRkvGITLFTVSHR 627
Cdd:cd03244 151 ARALLRKSKILVLDEATA--SVDPETdaliqkTIREAFK--DCTVLTIAHR 197
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
458-626 |
4.97e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 78.31 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 458 RDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGCLTKPERGKLF----YVPQRPYMTL---GTLRD 522
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALaglerpwsGEVT-FDGRPVTRRRRKAFRrrvqMVFQDPYASLhprHTVDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 523 QVIYPDTVedQRKKGISDQVlKEYLDNVQLG-QILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSA 601
Cdd:COG1124 101 ILAEPLRI--HGLPDREERI-AELLEQVGLPpSFLDR---------YPHQLSGGQRQRVAIARALILEPELLLLDEPTSA 168
|
170 180
....*....|....*....|....*....
gi 1985402263 602 --VSVDVE--GYIYSHCRKVGITLFTVSH 626
Cdd:COG1124 169 ldVSVQAEilNLLKDLREERGLTYLFVSH 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
441-600 |
5.87e-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: 77.37 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGCLtKPERGKLFY--VPQRPYmTLG 518
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLR-------LLNGLL-KPTSGEVLVdgKDITKK-NLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 519 TLRDQVIY----PD------TVEDQ-----RKKGIS----DQVLKEYLDNVQLGQILEReggwdSVQDwmdvLSGGEKQR 579
Cdd:COG1122 72 ELRRKVGLvfqnPDdqlfapTVEEDvafgpENLGLPreeiRERVEEALELVGLEHLADR-----PPHE----LSGGQKQR 142
|
170 180
....*....|....*....|.
gi 1985402263 580 MAMARLFYHKPQFAILDECTS 600
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTA 163
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
452-626 |
6.44e-16 |
|
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: 75.93 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELwplfggcltKPERGKLfYVPQRPYMTLgtlrdqviypDTV 530
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLaGLL---------KPSSGEI-LLDGKDLASL----------SPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 531 EDQRKKGISDQVLKEyldnVQLGQILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDV 606
Cdd:cd03214 70 ELARKIAYVPQALEL----LGLAHLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLdiahQIEL 136
|
170 180
....*....|....*....|
gi 1985402263 607 EGYIYSHCRKVGITLFTVSH 626
Cdd:cd03214 137 LELLRRLARERGKTVVMVLH 156
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
429-627 |
8.41e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.02 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 429 PGTGEIINTDNLIKFDHVPLATPNG-DILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGCLT 499
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtrawdpqqGEI--LLNGQPI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 500 K--PE---RGKLFYVPQRPYMTLGTLRDQVIYPdtvedqrKKGISDQVLKEYLDNVQLGQILEREGGWDSvqdWMD---- 570
Cdd:PRK11160 405 AdySEaalRQAISVVSQRVHLFSATLRDNLLLA-------APNASDEALIEVLQQVGLEKLLEDDKGLNA---WLGeggr 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985402263 571 VLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYS----HCRkvGITLFTVSHR 627
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILEllaeHAQ--NKTVLMITHR 533
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
441-642 |
9.99e-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: 77.14 E-value: 9.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLA-TPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG---------CLTKPE--RGKLFY 508
Cdd:cd03252 1 ITFEHVRFRyKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghdlALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 509 VPQRPYMTLGTLRDQVIYPDTVEDqRKKGISDQVLKEYLDNvqlgqILEREGGWDSVQDWMDV-LSGGEKQRMAMARLFY 587
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMS-MERVIEAAKLAGAHDF-----ISELPEGYDTIVGEQGAgLSGGQRQRIAIARALI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1985402263 588 HKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHDFYLHMDG 642
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
423-619 |
2.94e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.02 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 423 QTIPLIPGTGEIINTDNLIKFDhVPLATPNgdilIRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGCLTKp 501
Cdd:PLN03232 604 QNPPLQPGAPAISIKNGYFSWD-SKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 502 eRGKLFYVPQRPYMTLGTLRDQVIYPDTVEDQRK-KGISDQVLKEYLD---NVQLGQILERegGWDsvqdwmdvLSGGEK 577
Cdd:PLN03232 678 -RGSVAYVPQVSWIFNATVRENILFGSDFESERYwRAIDVTALQHDLDllpGRDLTEIGER--GVN--------ISGGQK 746
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1985402263 578 QRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGI 619
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDEL 788
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
441-647 |
7.92e-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: 74.19 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWplfggcltKPERGKLFY--VPQRPYmTL 517
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFY--------DVDSGRILIdgHDVRDY-TL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 518 GTLRDQV--------IYPDTVEDQRKKGISDQVLKEYLDNVQLGQ----ILEREGGWDSVQDWMDV-LSGGEKQRMAMAR 584
Cdd:cd03251 72 ASLRRQIglvsqdvfLFNDTVAENIAYGRPGATREEVEEAARAANahefIMELPEGYDTVIGERGVkLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 585 LFYHKPQFAILDECTSAVSVDVEGYIYSHCRK--VGITLFTVSHRKSLWKHHDFYLHMDG-----RGNYE 647
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERlmKNRTTFVIAHRLSTIENADRIVVLEDgkiveRGTHE 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
441-629 |
1.23e-14 |
|
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: 73.73 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPN--GDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELW-PLFGGCLTKPE----------RGKLF 507
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYdPTSGEILLDGVdirdlnlrwlRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 508 YVPQRPYMTLGTLRDQVIY---PDTVEDQ----RKKGISDQVLK---EYldNVQLGqilerEGGwdsVQdwmdvLSGGEK 577
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYgkpDATDEEVeeaaKKANIHDFIMSlpdGY--DTLVG-----ERG---SQ-----LSGGQK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1985402263 578 QRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKS 629
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAHRLS 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
453-597 |
1.75e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 453 GDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELwPLFGGCLTKPERGKLFYVPQRPYMTLG-TLRDQVIYPDT- 529
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILaGEL-EPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLDGDAe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 530 ---VEDQRKK-----GISDQVLKEYLDnvqLGQILEREGGWD--------------SVQDW---MDVLSGGEKQRMAMAR 584
Cdd:COG0488 89 lraLEAELEEleaklAEPDEDLERLAE---LQEEFEALGGWEaearaeeilsglgfPEEDLdrpVSELSGGWRRRVALAR 165
|
170
....*....|...
gi 1985402263 585 LFYHKPQFAILDE 597
Cdd:COG0488 166 ALLSEPDLLLLDE 178
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
439-626 |
1.79e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 439 NLIKFDHVPLATPNGDILiRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLfGGCLTKPERGKLFYVPQRPYMTl 517
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAPD-EGVIKRNGKLRIGYVPQKLYLD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 518 GTLrdqviyPDTVED--QRKKGISDQVLKEYLDNVQLGQILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 595
Cdd:PRK09544 80 TTL------PLTVNRflRLRPGTKKEDILPALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*
gi 1985402263 596 DECTSAVSVDVEGYIYSHC----RKVGITLFTVSH 626
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIdqlrRELDCAVLMVSH 179
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
414-647 |
2.37e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 414 QHEKDGDRTQTIPLIPGTGEIINTDNLIKFdhvplaTPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL------ 487
Cdd:PRK11174 329 ETPLAHPQQGEKELASNDPVTIEAEDLEIL------SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpy 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 488 -GELwpLFGGC----LTKPE-RGKLFYVPQRPYMTLGTLRDQVIYpdtvedqRKKGISDQVLKEYLDNVQLGQILER-EG 560
Cdd:PRK11174 403 qGSL--KINGIelreLDPESwRKHLSWVGQNPQLPHGTLRDNVLL-------GNPDASDEQLQQALENAWVSEFLPLlPQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 561 GWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHDFY 637
Cdd:PRK11174 474 GLDTpIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQLEDLAQWDQI 553
|
250
....*....|....*
gi 1985402263 638 LHMDG-----RGNYE 647
Cdd:PRK11174 554 WVMQDgqivqQGDYA 568
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
435-605 |
2.81e-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: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 435 INTDNLIK-FDHVPLatpngdilIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGCLTKPE---R 503
Cdd:COG4555 2 IEVENLSKkYGKVPA--------LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLKPdsgsilIDGEDVRKEPreaR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 504 GKLFYVPQRPYMTLG-TLRDQV-----IYPDTVEDQRKKgisdqvLKEYLDNVQLGQILEReggwdSVQDwmdvLSGGEK 577
Cdd:COG4555 74 RQIGVLPDERGLYDRlTVRENIryfaeLYGLFDEELKKR------IEELIELLGLEEFLDR-----RVGE----LSTGMK 138
|
170 180
....*....|....*....|....*...
gi 1985402263 578 QRMAMARLFYHKPQFAILDECTSAVSVD 605
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVM 166
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
441-626 |
2.95e-14 |
|
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: 72.50 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDIL---IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT---------KPERGklfY 508
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgpGPDRG---Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 509 VPQR----PYMtlgTLRDQVIYPDTVEDQRKKGISDQVLkEYLDNVQLGqilereggwDSVQDWMDVLSGGEKQRMAMAR 584
Cdd:cd03293 78 VFQQdallPWL---TVLDNVALGLELQGVPKAEARERAE-ELLELVGLS---------GFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1985402263 585 LFYHKPQFAILDECTSAVSV----DVEGYIYSHCRKVGITLFTVSH 626
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTH 190
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
364-641 |
3.44e-14 |
|
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: 75.91 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 364 MLLRMSQALGRIVLAGremtrlaGFTARITELMQVLKDLNR-----GRYQRTMISQHEKDGDRTQTIPLIPGTGEIINTD 438
Cdd:TIGR02203 256 LFIALFQAQAGSLTAG-------DFTAFITAMIALIRPLKSltnvnAPMQRGLAAAESLFTLLDSPPEKDTGTRAIERAR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 439 NLIKFDHVPLATPNGDI-LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwPLFggclTKPERGKLFY--VPQRPYm 515
Cdd:TIGR02203 329 GDVEFRNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLI----PRF----YEPDSGQILLdgHDLADY- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 516 TLGTLRDQV--------IYPDTVEDQRKKGISDQV-------------LKEYLDNVQLGqiLEREGGWDSVQdwmdvLSG 574
Cdd:TIGR02203 400 TLASLRRQValvsqdvvLFNDTIANNIAYGRTEQAdraeieralaaayAQDFVDKLPLG--LDTPIGENGVL-----LSG 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985402263 575 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHDFYLHMD 641
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVMD 541
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
456-601 |
3.54e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 72.84 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCL--------TKPE-----RGKLfyvPQRPYMTLgtlr 521
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELTPSSGEVRlngrplaaWSPWelarrRAVL---PQHSSLAF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 522 dqviyPDTVED---------QRKKGISDQVLKEYLDNVQLGQILEReggwdSVQDwmdvLSGGEKQRMAMARLF------ 586
Cdd:COG4559 89 -----PFTVEEvvalgraphGSSAAQDRQIVREALALVGLAHLAGR-----SYQT----LSGGEQQRVQLARVLaqlwep 154
|
170
....*....|....*.
gi 1985402263 587 -YHKPQFAILDECTSA 601
Cdd:COG4559 155 vDGGPRWLFLDEPTSA 170
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
452-626 |
3.78e-14 |
|
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: 71.06 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGCLTKPERGKLFyvpqrpymtlgtLRDQVIYPDTVE 531
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCI--------AGLEEPDSGSIL------------IDGEDLTDLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 532 DQRKKGISDQVLKEY--------LDNVQLGqilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSA-- 601
Cdd:cd03229 71 LPPLRRRIGMVFQDFalfphltvLENIALG------------------LSGGQQQRVALARALAMDPDVLLLDEPTSAld 132
|
170 180
....*....|....*....|....*..
gi 1985402263 602 --VSVDVEGYIYSHCRKVGITLFTVSH 626
Cdd:cd03229 133 piTRREVRALLKSLQAQLGITVVLVTH 159
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
438-627 |
4.11e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 75.32 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 438 DNLIKFDHVPLATPNGDI-LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP---------LFGG----CLTKPER 503
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGrdllELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 504 GKLF-YVPQRPYMTL--GTLRDQVIYPDTVEDQRKKGISDQVLkEYLDNVQLGQILEReggwdsvqdWMDVLSGGEKQRM 580
Cdd:COG1123 82 GRRIgMVFQDPMTQLnpVTVGDQIAEALENLGLSRAEARARVL-ELLEAVGLERRLDR---------YPHQLSGGQRQRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1985402263 581 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSH----CRKVGITLFTVSHR 627
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLlrelQRERGTTVLLITHD 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
437-597 |
4.32e-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: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 437 TDNLIKFDHVPLA--TPNGDILI-RDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGCLTKP--ER 503
Cdd:COG1116 4 AAPALELRGVSKRfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptsGEVL-VDGKPVTGPgpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 504 GklfYVPQR----PYMTLgtlRDQVIYPDTVEDQRKKGISDQVLkEYLDNVQLGqilereggwDSVQDWMDVLSGGEKQR 579
Cdd:COG1116 83 G---VVFQEpallPWLTV---LDNVALGLELRGVPKAERRERAR-ELLELVGLA---------GFEDAYPHQLSGGMRQR 146
|
170
....*....|....*...
gi 1985402263 580 MAMARLFYHKPQFAILDE 597
Cdd:COG1116 147 VAIARALANDPEVLLMDE 164
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
392-642 |
5.28e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 75.75 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 392 ITELMQVLKDLNRgryQRTMISQHEKDGDRTQTIPLIPGTGEIINTDNlIKFDHVPLATPNgdilIRDLNFEVRSGANVL 471
Cdd:TIGR00957 597 ISSIVQASVSLKR---LRIFLSHEELEPDSIERRTIKPGEGNSITVHN-ATFTWARDLPPT----LNGITFSIPEGALVA 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 472 ICGPNGCGKSSLFR-VLGELWPLFGGCLTKperGKLFYVPQRPYMTLGTLRDQVIYPDTVEDQRKKGISDQ-VLKEYLDN 549
Cdd:TIGR00957 669 VVGQVGCGKSSLLSaLLAEMDKVEGHVHMK---GSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEAcALLPDLEI 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 550 VQLGQilEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRK-----VGITLFTV 624
Cdd:TIGR00957 746 LPSGD--RTEIGEKGVN-----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGpegvlKNKTRILV 818
|
250
....*....|....*...
gi 1985402263 625 SHRKSLWKHHDFYLHMDG 642
Cdd:TIGR00957 819 THGISYLPQVDVIIVMSG 836
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
451-608 |
5.68e-14 |
|
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: 70.91 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 451 PNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGCLTKPERGKLFYVPQRPYMTLGTLRDQV 524
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLnGLLRPqsgavLIDGEPLDYSRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 525 IYPDTVED----QRKKGISDQVLKEYLDNVqlgqiLEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 600
Cdd:TIGR01166 82 FAADVDQDvafgPLNLGLSEAEVERRVREA-----LTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
....*...
gi 1985402263 601 AvsVDVEG 608
Cdd:TIGR01166 157 G--LDPAG 162
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
457-626 |
5.81e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.40 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggclTKPERGKLFyVPQRPymtLGTLRDqviypDT---VEDQ 533
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL--------ETPSAGELL-AGTAP---LAEARE-----DTrlmFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 534 RkkgisdqVL--KEYLDNVQLG----------QILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSA 601
Cdd:PRK11247 91 R-------LLpwKKVIDNVGLGlkgqwrdaalQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180
....*....|....*....|....*....
gi 1985402263 602 VS----VDVEGYIYSHCRKVGITLFTVSH 626
Cdd:PRK11247 164 LDaltrIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
429-643 |
7.40e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.61 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 429 PGTGEIINTDNLIKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfggcltkpERgklFY 508
Cdd:PRK13657 323 PGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL--------------QR---VF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 509 VPQRPY----------MTLGTLRDQ--VIYPD------TVEDQRKKGISDQVLKEYLDNVQLGQ----ILEREGGWDS-V 565
Cdd:PRK13657 386 DPQSGRilidgtdirtVTRASLRRNiaVVFQDaglfnrSIEDNIRVGRPDATDEEMRAAAERAQahdfIERKPDGYDTvV 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 566 QDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEgyiyshcRKV---------GITLFTVSHRKSLWKHHDF 636
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE-------AKVkaaldelmkGRTTFIIAHRLSTVRNADR 538
|
....*...
gi 1985402263 637 YLHMD-GR 643
Cdd:PRK13657 539 ILVFDnGR 546
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
453-597 |
9.48e-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: 9.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 453 GDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGCLTKPERGKLFYVPQRpymtLGTLRDQviypDTVE 531
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPD-SGTVKLGETVKIGYFDQH----QEELDPD----KTVL 397
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985402263 532 DqrkkgisdqVLKEYLDN---VQLGQILER---EGgwDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDE 597
Cdd:COG0488 398 D---------ELRDGAPGgteQEVRGYLGRflfSG--DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
457-626 |
1.09e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.84 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggCLTKPERGKLF-----------------------YVPQR- 512
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG--------GLDRPTSGEVLidgqdisslserelarlrrrhigFVFQFf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 513 ---PYMTLgtlRDQVIYPDTVEDQRKKGISDQVlKEYLDNVQLGQILER---EggwdsvqdwmdvLSGGEKQRMAMARLF 586
Cdd:COG1136 96 nllPELTA---LENVALPLLLAGVSRKERRERA-RELLERVGLGDRLDHrpsQ------------LSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1985402263 587 YHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 626
Cdd:COG1136 160 VNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTH 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
457-626 |
1.35e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 70.86 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANV-LIcGPNGCGKSSLFRVL--------GELWpLFGG-CLTKPE--RGKLFYVPQRPYMtlgtlrdqv 524
Cdd:COG1131 16 LDGVSLTVEPGEIFgLL-GPNGAGKTTTIRMLlgllrptsGEVR-VLGEdVARDPAevRRRIGYVPQEPAL--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 525 iYPD-TVED-----QRKKGISDQVLKEYLDnvqlgQILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDEC 598
Cdd:COG1131 85 -YPDlTVREnlrffARLYGLPRKEARERID-----ELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190
....*....|....*....|....*....|....
gi 1985402263 599 TSAvsVDVEG------YIYSHCRKvGITLFTVSH 626
Cdd:COG1131 159 TSG--LDPEArrelweLLRELAAE-GKTVLLSTH 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
370-627 |
1.36e-13 |
|
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: 73.55 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 370 QALGRIVLAGREMTRLAGFTARITELMqvlkdlnrgryqrtmisqhekDGDRTQTIPLIPGTGEIINTDNLIKFDHVPLA 449
Cdd:TIGR02868 285 EAFAALPAAAQQLTRVRAAAERIVEVL---------------------DAAGPVAEGSAPAAGAVGLGKPTLELRDLSAG 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 450 TPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT-----------KPERGKLFYVPQRPYMTLG 518
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvssldqDEVRRRVSVCAQDAHLFDT 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 519 TLRDQVIYPdtvedqrKKGISDQVLKEYLDNVQLGQILER-EGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILD 596
Cdd:TIGR02868 424 TVRENLRLA-------RPDATDEELWAALERVGLADWLRAlPDGLDTvLGEGGARLSGGERQRLALARALLADAPILLLD 496
|
250 260 270
....*....|....*....|....*....|...
gi 1985402263 597 ECTSAVSVDVEGYIYSHCRKV--GITLFTVSHR 627
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAAlsGRTVVLITHH 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
404-630 |
2.27e-13 |
|
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: 73.24 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 404 RGRYQR--TMISQHEKDGDRTqtiPLIPGTGEIintdnliKFDHVPLATPNGD-ILIRDLNFEVRSGANVLICGPNGCGK 480
Cdd:COG4618 302 RQAYRRlnELLAAVPAEPERM---PLPRPKGRL-------SVENLTVVPPGSKrPILRGVSFSLEPGEVLGVIGPSGSGK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 481 SSLFRVLGELWPLFGGC----------LTKPERGKLF-YVPQRPymTL--GTLRD------QVIYPDTVEDQRKKGISDQ 541
Cdd:COG4618 372 STLARLLVGVWPPTAGSvrldgadlsqWDREELGRHIgYLPQDV--ELfdGTIAEniarfgDADPEKVVAAAKLAGVHEM 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 542 VLK---EYldNVQLGqilerEGGwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVEG------YIyS 612
Cdd:COG4618 450 ILRlpdGY--DTRIG-----EGG--------ARLSGGQRQRIGLARALYGDPRLVVLDEPNS--NLDDEGeaalaaAI-R 511
|
250
....*....|....*...
gi 1985402263 613 HCRKVGITLFTVSHRKSL 630
Cdd:COG4618 512 ALKARGATVVVITHRPSL 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
436-626 |
2.72e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 72.63 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 436 NTDNLIKFDHV----PLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------------GELWPLFGGC 497
Cdd:COG1123 256 AAEPLLEVRNLskryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLlgllrptsgsilfdGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 498 LTKPERGKLFYVPQRPYMTL---GTLRDQVIYP-DTVEDQRKKGISDQVlKEYLDNVQLG-QILER---Eggwdsvqdwm 569
Cdd:COG1123 336 SLRELRRRVQMVFQDPYSSLnprMTVGDIIAEPlRLHGLLSRAERRERV-AELLERVGLPpDLADRyphE---------- 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985402263 570 dvLSGGEKQRMAMARLFYHKPQFAILDECTSA--VSV--DVEGYIYSHCRKVGITLFTVSH 626
Cdd:COG1123 405 --LSGGQRQRVAIARALALEPKLLILDEPTSAldVSVqaQILNLLRDLQRELGLTYLFISH 463
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
452-626 |
4.07e-13 |
|
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: 68.70 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGC-LTK--PERGKLFYVPQR----PYMt 516
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaglerpdsGEI--LIDGRdVTGvpPERRNIGMVFQDyalfPHL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 517 lgTLRDQVIYPDTVEDQRKKGISDQVlKEYLDNVQLGQILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILD 596
Cdd:cd03259 88 --TVAENIAFGLKLRGVPKAEIRARV-RELLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1985402263 597 ECTSAvsVDVE------GYIYSHCRKVGITLFTVSH 626
Cdd:cd03259 156 EPLSA--LDAKlreelrEELKELQRELGITTIYVTH 189
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
441-599 |
5.41e-13 |
|
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: 68.37 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILiRDLNFEVRSGANVLIcGPNGCGKSSLFRVLGELWP------LFGG--CLTKPE--RGKLFYVP 510
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPpssgtiRIDGqdVLKQPQklRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 511 QRPymtlgtlrdqVIYPD-TVEDQ-----RKKGISDQVLKEYLDNVqlgqiLEREGGWDSVQDWMDVLSGGEKQRMAMAR 584
Cdd:cd03264 79 QEF----------GVYPNfTVREFldyiaWLKGIPSKEVKARVDEV-----LELVNLGDRAKKKIGSLSGGMRRRVGIAQ 143
|
170
....*....|....*
gi 1985402263 585 LFYHKPQFAILDECT 599
Cdd:cd03264 144 ALVGDPSILIVDEPT 158
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
457-626 |
7.06e-13 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 67.04 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGCLTKPE---RGKLFYVPQRPYmtlgtlrdqvI 525
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlgllkpdsGEIK-VLGKDIKKEPeevKRRIGYLPEEPS----------L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 526 YPD-TVEdqrkkgisdqvlkEYLDnvqlgqilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAV-- 602
Cdd:cd03230 85 YENlTVR-------------ENLK-----------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLdp 128
|
170 180
....*....|....*....|....*.
gi 1985402263 603 --SVDVEGYIYSHcRKVGITLFTVSH 626
Cdd:cd03230 129 esRREFWELLREL-KKEGKTILLSSH 153
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
452-621 |
1.01e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPlfggcltkPERGKLFYVPQRPymTLGTLRDQVIY----- 526
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP--------PAAGTIKLDGGDI--DDPDVAEACHYlghrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 527 ---PD-TVED-----QRKKGISDQVLKEYLDNVQLGQILEREGGwdsvqdwmdVLSGGEKQRMAMARLF-YHKPQFaILD 596
Cdd:PRK13539 83 amkPAlTVAEnlefwAAFLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARLLvSNRPIW-ILD 152
|
170 180
....*....|....*....|....*....
gi 1985402263 597 ECTSAVSVD----VEGYIYSHCRKVGITL 621
Cdd:PRK13539 153 EPTAALDAAavalFAELIRAHLAQGGIVI 181
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
456-626 |
1.28e-12 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 67.28 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGG--CLTKPERGKLFYVPQRPYMTLGTlrdqviyp 527
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKessgsiLLNGkpIKAKERRKSIGYVMQDVDYQLFT-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 528 DTVEDQ---RKKGISDqvlkeylDNVQLGQILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAV-- 602
Cdd:cd03226 87 DSVREElllGLKELDA-------GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLdy 159
|
170 180
....*....|....*....|....*
gi 1985402263 603 -SVDVEGYIYSHCRKVGITLFTVSH 626
Cdd:cd03226 160 kNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
457-642 |
1.92e-12 |
|
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: 66.97 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLF-RVLGELWPLFG--------------GCLTKPERGKLFYVPQRPYMTLGTLR 521
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwsnknesepsfEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 522 DQVIYPDTVEDQRKKGISDQV-LKEYLDNVQLG---QILERegGWDsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDE 597
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACsLQPDIDLLPFGdqtEIGER--GIN--------LSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1985402263 598 CTSAVSVdvegYIYSHCRKVGI---------TLFTVSHRKSLWKHHDFYLHM-DG 642
Cdd:cd03290 167 PFSALDI----HLSDHLMQEGIlkflqddkrTLVLVTHKLQYLPHADWIIAMkDG 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
441-599 |
2.58e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 66.61 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELwplfggcltKPERGKLFYVPQRpymtLGT 519
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLyGEE---------RPTSGQVLVNGQD----LSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 520 LRDQ----------VIYPD-------TVED----------QRKKGISDQVLkEYLDNVQLGQILEReggwdsvqdwM-DV 571
Cdd:COG2884 69 LKRReipylrrrigVVFQDfrllpdrTVYEnvalplrvtgKSRKEIRRRVR-EVLDLVGLSDKAKA----------LpHE 137
|
170 180
....*....|....*....|....*...
gi 1985402263 572 LSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPT 165
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
448-641 |
3.52e-12 |
|
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: 69.77 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 448 LATPNGDILIRDLNFEVRSGANVL--------------ICGPNGCGKSSLFRVL--------GELwpLFGGCLTK----- 500
Cdd:TIGR01193 467 LNNLNGDIVINDVSYSYGYGSNILsdisltikmnskttIVGMSGSGKSTLAKLLvgffqarsGEI--LLNGFSLKdidrh 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 501 PERGKLFYVPQRPYMTLGTLRDQVIY---PDTVEDQRKKGISDQVLKEYLDNVQLG--QILEREGGwdsvqdwmdVLSGG 575
Cdd:TIGR01193 545 TLRQFINYLPQEPYIFSGSILENLLLgakENVSQDEIWAACEIAEIKDDIENMPLGyqTELSEEGS---------SISGG 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985402263 576 EKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVG-ITLFTVSHRKSLWKHHDFYLHMD 641
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
440-626 |
3.94e-12 |
|
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: 66.38 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 440 LIKFDHVPLATPNGDI---LIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------------GELWPLFGGCLTKPE 502
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsgsiifdGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 503 RGKLFYVPQRPYMTLG---TLRDQVI------YPDTVEDQRKKgisdqvlKEYLDNVQLG---QILER---Eggwdsvqd 567
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprmTIGEQIAeplrihGKLSKKEARKE-------AVLLLLVGVGlpeEVLNRyphE-------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985402263 568 wmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSH----CRKVGITLFTVSH 626
Cdd:cd03257 146 ----LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkklQEELGLTLLFITH 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
456-601 |
6.14e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 66.33 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCL--------TKPE-----RGKLfyvPQRPYMTLGTLR 521
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPDSGEVRlngrpladWSPAelarrRAVL---PQHSSLSFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 522 DQVI----YPDTVEDQRKKGISDQVLKEyLDNVQLGQILEREggwdsvqdwmdvLSGGEKQRMAMARLF------YHKPQ 591
Cdd:PRK13548 94 EEVVamgrAPHGLSRAEDDALVAAALAQ-VDLAHLAGRDYPQ------------LSGGEQQRVQLARVLaqlwepDGPPR 160
|
170
....*....|
gi 1985402263 592 FAILDECTSA 601
Cdd:PRK13548 161 WLLLDEPTSA 170
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
451-627 |
7.57e-12 |
|
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: 65.13 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 451 PNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT-----------KPERGKLFYVPQRPYMTLGT 519
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidistiplEDLRSSLTIIPQDPTLFSGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 520 LRDQViypdtvedqrkkgisdQVLKEYlDNVQLGQILE-REGGwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILDEC 598
Cdd:cd03369 98 IRSNL----------------DPFDEY-SDEEIYGALRvSEGG--------LNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190
....*....|....*....|....*....|.
gi 1985402263 599 TSAVSVDVEGYIYSHCRK--VGITLFTVSHR 627
Cdd:cd03369 153 TASIDYATDALIQKTIREefTNSTILTIAHR 183
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
459-616 |
9.79e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 9.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 459 DLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGCLTKpeRGKLFYVPQRPYMTLGTLRDQVIYPDTVEDQR-KK 536
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI--RGTVAYVPQVSWIFNATVRDNILFGSPFDPERyER 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 537 GISDQVLKEYLDNV---QLGQILEReggwdSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSH 613
Cdd:PLN03130 713 AIDVTALQHDLDLLpggDLTEIGER-----GVN-----ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDK 782
|
...
gi 1985402263 614 CRK 616
Cdd:PLN03130 783 CIK 785
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
438-626 |
1.13e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.98 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 438 DNLIKFDHVPLATPNGDI-LIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP---------LFGGCLTKPE---- 502
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLLPddnpnskitVDGITLTAKTvwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 503 RGKLFYVPQRPymtlgtlrDQVIYPDTVEDQRKKGISD-QVLKEYLDNVqLGQILEREGGWDSVQDWMDVLSGGEKQRMA 581
Cdd:PRK13640 83 REKVGIVFQNP--------DNQFVGATVGDDVAFGLENrAVPRPEMIKI-VRDVLADVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1985402263 582 MARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV----GITLFTVSH 626
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
430-614 |
1.58e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 65.65 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 430 GTGEIINTDNLIKFDHVPL-ATPngdiLIRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGCltkPERGKLF 507
Cdd:cd03291 29 NDRKHSSDDNNLFFSNLCLvGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPSEGKI---KHSGRIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 508 YVPQRPYMTLGTLRDQVIYPDTVEDQRKKGISDQV-LKEYL------DNVQLGqilerEGGWdsvqdwmdVLSGGEKQRM 580
Cdd:cd03291 102 FSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACqLEEDItkfpekDNTVLG-----EGGI--------TLSGGQRARI 168
|
170 180 190
....*....|....*....|....*....|....
gi 1985402263 581 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSHC 614
Cdd:cd03291 169 SLARAVYKDADLYLLDSPFGYLDVFTEKEIFESC 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
455-626 |
1.98e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 455 ILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GelwplfggcLTKPERGKLFYVPQRpymtLGTLRDQV--------- 524
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILaG---------LARPDAGEVLWQGEP----IRRQRDEYhqdllylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 525 ---IYPD--TVEDQRkkgiSDQVLKEYLDNVQLGQILEREGgwdsVQDWMDV----LSGGEKQRMAMARLFYHKPQFAIL 595
Cdd:PRK13538 82 qpgIKTEltALENLR----FYQRLHGPGDDEALWEALAQVG----LAGFEDVpvrqLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1985402263 596 DECTSAVSV----DVEGYIYSHCRKVGITLFTvSH 626
Cdd:PRK13538 154 DEPFTAIDKqgvaRLEALLAQHAEQGGMVILT-TH 187
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
453-626 |
2.29e-11 |
|
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: 64.28 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 453 GDILIRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGCLT--KPERGKLFYVPQR----PYMTLgt 519
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFIKPdsgkilLNGKDITnlPPEKRDISYVPQNyalfPHMTV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 520 lRDQVIYPDTVEDQRKKGISDQVlKEYLDNVQLGQILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:cd03299 89 -YKNIAYGLKKRKVDKKEIERKV-LEIAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|.
gi 1985402263 600 SAVSVDVEGYIYSHCRKV----GITLFTVSH 626
Cdd:cd03299 158 SALDVRTKEKLREELKKIrkefGVTVLHVTH 188
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
441-599 |
2.66e-11 |
|
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: 61.70 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATpNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLTKPERGKLFYVPQrpymtlgtl 520
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985402263 521 rdqviypdtvedqrkkgisdqvlkeyldnvqlgqilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
455-654 |
2.79e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 455 ILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPlfggcltkpERgKLFYVPQRPYMTLGTLRDQVIY 526
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlsqfeiseGRVWA---------ER-SIAYVPQQAWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 527 PDtveDQRKKGISDQVLKEYL--DNVQLGQILEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSV 604
Cdd:PTZ00243 744 FD---EEDAARLADAVRVSQLeaDLAQLGGGLETEIGEKGVN-----LSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1985402263 605 DVEGYIYSHC---RKVGITLFTVSHRKSLWKHHDFYLHMdGRGNYEFKKITED 654
Cdd:PTZ00243 816 HVGERVVEECflgALAGKTRVLATHQVHVVPRADYVVAL-GDGRVEFSGSSAD 867
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
438-600 |
3.04e-11 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 63.95 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 438 DNLIKFDHVPLATpNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCLT---KpERGK--LF---- 507
Cdd:COG1119 1 DPLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLPPTYGNDVRlfgE-RRGGedVWelrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 508 ---YV-P--QRPYMTLGTLRDQVI---------YPDTVEDQRKKGisdqvlKEYLDNVQLGQILEREggwdsvqdwMDVL 572
Cdd:COG1119 79 rigLVsPalQLRFPRDETVLDVVLsgffdsiglYREPTDEQRERA------RELLELLGLAHLADRP---------FGTL 143
|
170 180
....*....|....*....|....*...
gi 1985402263 573 SGGEKQRMAMARLFYHKPQFAILDECTS 600
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTA 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
452-626 |
3.29e-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: 63.80 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggclTKPERGKLFY-------VP--QR---------- 512
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF--------ETPTSGEILLdgkditnLPphKRpvntvfqnya 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 513 --PYMTLGtlrDQVIYPDTVEDQRKKGISDQVlKEYLDNVQLGQILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKP 590
Cdd:cd03300 83 lfPHLTVF---ENIAFGLRLKKLPKAEIKERV-AEALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1985402263 591 QFAILDECTSAVSV----DVEGYIYSHCRKVGITLFTVSH 626
Cdd:cd03300 150 KVLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTH 189
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
436-600 |
4.22e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.86 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 436 NTDNLIKFDHVPLATPNGD-ILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWplfggcltKPERGKLF-YVPQRP 513
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL--------KPQSGEIKiDGITIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 514 YMTLGTLRDQV--IY--PD------TVED-----------QRKKgiSDQVLKEYLDNVQLGQILEREGgwdsvqdwmDVL 572
Cdd:PRK13632 75 KENLKEIRKKIgiIFqnPDnqfigaTVEDdiafglenkkvPPKK--MKDIIDDLAKKVGMEDYLDKEP---------QNL 143
|
170 180
....*....|....*....|....*...
gi 1985402263 573 SGGEKQRMAMARLFYHKPQFAILDECTS 600
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTS 171
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
452-626 |
4.62e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 62.25 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCLTKPERgKLFYVPQRpymtlGTLRDQviYPDTV 530
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRPTSGTVRRAGGA-RVAYVPQR-----SEVPDS--LPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 531 ED------------QRKKGISD-QVLKEYLDNVQLGQILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 597
Cdd:NF040873 75 RDlvamgrwarrglWRRLTRDDrAAVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|..
gi 1985402263 598 CTSAVSVDVEGYIYSHCRKV---GITLFTVSH 626
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEharGATVVVVTH 177
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
441-626 |
5.82e-11 |
|
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: 62.97 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggclTKPERGKLFY----VPQRPYMT 516
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL--------VEPTSGSVLIdgtdINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 517 LGTLRDQV--IYPD--TVEDQRkkgisdqvlkeYLDNVQLG------------------------QILEREGGWDSVQDW 568
Cdd:cd03256 73 LRQLRRQIgmIFQQfnLIERLS-----------VLENVLSGrlgrrstwrslfglfpkeekqralAALERVGLLDKAYQR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985402263 569 MDVLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 626
Cdd:cd03256 142 ADQLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLH 203
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
456-630 |
1.00e-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: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplFGGCLTKPERGKlFYVPQRPYMTLGTLRDQVIYPDTVEDQrk 535
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL------AGALKGTPVAGC-VDVPDNQFGREASLIDAIGRKGDFKDA-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 536 kgisdqvlKEYLDNVQLGqilereggwdSVQDWM---DVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVeGYIYS 612
Cdd:COG2401 116 --------VELLNAVGLS----------DAVLWLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT-AKRVA 176
|
170 180
....*....|....*....|...
gi 1985402263 613 H-----CRKVGITLFTVSHRKSL 630
Cdd:COG2401 177 RnlqklARRAGITLVVATHHYDV 199
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
457-597 |
1.03e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.59 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGcLTKPERGKLFY---------VPQR------------PYM 515
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAG-LEKPTEGQIFIdgedvthrsIQQRdicmvfqsyalfPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 516 TLGtlrDQVIYPDTVEDQRKKGISDQVlKEYLDNVQLGQILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAIL 595
Cdd:PRK11432 94 SLG---ENVGYGLKMLGVPKEERKQRV-KEALELVDLAGFEDR---------YVDQISGGQQQRVALARALILKPKVLLF 160
|
..
gi 1985402263 596 DE 597
Cdd:PRK11432 161 DE 162
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
436-614 |
2.05e-10 |
|
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: 64.16 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 436 NTDNLIKFDHVPL-ATPngdiLIRDLNFEVRSGANVLICGPNGCGKSSLFRV-LGELWPLFGGCltkPERGKLFYVPQRP 513
Cdd:TIGR01271 424 NGDDGLFFSNFSLyVTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMiMGELEPSEGKI---KHSGRISFSPQTS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 514 YMTLGTLRDQVIYPDTVEDQRKKGISDQV-LKEYL------DNVQLGqilerEGGWdsvqdwmdVLSGGEKQRMAMARLF 586
Cdd:TIGR01271 497 WIMPGTIKDNIIFGLSYDEYRYTSVIKACqLEEDIalfpekDKTVLG-----EGGI--------TLSGGQRARISLARAV 563
|
170 180
....*....|....*....|....*...
gi 1985402263 587 YHKPQFAILDECTSAVSVDVEGYIYSHC 614
Cdd:TIGR01271 564 YKDADLYLLDSPFTHLDVVTEKEIFESC 591
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
391-629 |
2.72e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.20 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 391 RITELMqvlkDLNRGRYqrtmisqhekdGDRTQtiPLIPGTgeiintdnlIKFDHVPLATPNGDILIRDLNFEVRSGANV 470
Cdd:PRK10790 317 RVFELM----DGPRQQY-----------GNDDR--PLQSGR---------IDIDNVSFAYRDDNLVLQNINLSVPSRGFV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 471 LICGPNGCGKSSLFRVLGELWPlfggcltkPERGKLfYVPQRPYMTL--GTLR--------DQVIYPDTVEDQRKKG--I 538
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYP--------LTEGEI-RLDGRPLSSLshSVLRqgvamvqqDPVVLADTFLANVTLGrdI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 539 SDQVLKEYLDNVQLGQILER--EGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRK 616
Cdd:PRK10790 442 SEEQVWQALETVQLAELARSlpDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
|
250
....*....|....*
gi 1985402263 617 V--GITLFTVSHRKS 629
Cdd:PRK10790 522 VreHTTLVVIAHRLS 536
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
459-626 |
2.91e-10 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 60.31 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 459 DLNFEVRSGANVLICGPNGCGKSSLFRVlgelwpLFGgcLTKPERGKL------FYVPQRPYMTLGTLRD-QVIYPD-TV 530
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKI------ILG--LIKPDSGEItfdgksYQKNIEALRRIGALIEaPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 531 ED-----QRKKGISDQVLKEYLDNVQLGQILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAvsVD 605
Cdd:cd03268 90 REnlrllARLLGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNG--LD 158
|
170 180
....*....|....*....|....*..
gi 1985402263 606 VEG------YIYSHcRKVGITLFTVSH 626
Cdd:cd03268 159 PDGikelreLILSL-RDQGITVLISSH 184
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
459-626 |
4.09e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.41 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 459 DLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggCLTKPERGKL------FYVPQRPYMTLG-TLRDQV------- 524
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLN--------LLEMPRSGTLniagnhFDFSKTPSDKAIrELRRNVgmvfqqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 525 -IYPD-TVEDQ------RKKGISDQVLKEyldnvQLGQILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILD 596
Cdd:PRK11124 92 nLWPHlTVQQNlieapcRVLGLSKDQALA-----RAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|...
gi 1985402263 597 ECTSAVSVDVEGYIYSHCRKV---GITLFTVSH 626
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELaetGITQVIVTH 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
457-626 |
5.23e-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: 60.05 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGElwplfggcLTKPERGKLFY---------VPQR------------PYM 515
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG--------LERPDSGTILFggedatdvpVQERnvgfvfqhyalfRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 516 tlgTLRDQVIYPDTVEDQRKKGISDQV---LKEYLDNVQLGQILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQF 592
Cdd:cd03296 90 ---TVFDNVAFGLRVKPRSERPPEAEIrakVHELLKLVQLDWLADR---------YPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1985402263 593 AILDECTSAVSVDVEGYIYSHCRK----VGITLFTVSH 626
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRlhdeLHVTTVFVTH 195
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
420-601 |
6.17e-10 |
|
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: 62.14 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 420 DRTQTIPLIPGTGEIintdnliKFDHVPLA-TPNGDILiRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCL 498
Cdd:COG5265 344 DAPDAPPLVVGGGEV-------RFENVSFGyDPERPIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 499 T---------KPE--RGKLFYVPQrpymtlgtlrDQVIYPDTVEDQ---RKKGISDQVLKEYLDNVQLGQILER-EGGWD 563
Cdd:COG5265 416 LidgqdirdvTQAslRAAIGIVPQ----------DTVLFNDTIAYNiayGRPDASEEEVEAAARAAQIHDFIESlPDGYD 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1985402263 564 SVqdwmdV------LSGGEKQRMAMARLFYHKPQFAILDECTSA 601
Cdd:COG5265 486 TR-----VgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
435-626 |
7.42e-10 |
|
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: 59.31 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 435 INTDNLIKfdhvplaTPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG----------CLTKPERG 504
Cdd:cd03265 1 IEVENLVK-------KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghdvvREPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 505 KLFYVPQRPymtlgTLRDQVIYPDTVEDQ-RKKGISDQVLKEYLDnvqlgQILEREGGWDSVQDWMDVLSGGEKQRMAMA 583
Cdd:cd03265 74 RIGIVFQDL-----SVDDELTGWENLYIHaRLYGVPGAERRERID-----ELLDFVGLLEAADRLVKTYSGGMRRRLEIA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1985402263 584 RLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV----GITLFTVSH 626
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkeefGMTILLTTH 190
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
456-659 |
1.11e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.67 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLTKperGKLFYVPQRPY---MTLGTLRDQV-------- 524
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVE---GRVEFFNQNIYerrVNLNRLRRQVsmvhpkpn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 525 IYPDTVEDQRKKGISdqvLKEYLDNVQLGQILEREGG----WDSVQDWMDV----LSGGEKQRMAMARLFYHKPQFAILD 596
Cdd:PRK14258 99 LFPMSVYDNVAYGVK---IVGWRPKLEIDDIVESALKdadlWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985402263 597 E-CTS---AVSVDVEGYIYSHCRKVGITLFTVSHR-KSLWKHHDFYLHMDGRGNyefkKITEdTVEFG 659
Cdd:PRK14258 176 EpCFGldpIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSDFTAFFKGNEN----RIGQ-LVEFG 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
458-601 |
1.17e-09 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 58.70 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 458 RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggclTKPERGKLfyvpqrpymtlgTLRDQVIYPDT--VEDQRK 535
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL--------EEPDSGTI------------IIDGLKLTDDKknINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 536 K-GIsdqVLKEY--------LDNVQLGQI-----------------LEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHK 589
Cdd:cd03262 77 KvGM---VFQQFnlfphltvLENITLAPIkvkgmskaeaeeralelLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170
....*....|..
gi 1985402263 590 PQFAILDECTSA 601
Cdd:cd03262 154 PKVMLFDEPTSA 165
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
457-626 |
1.27e-09 |
|
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: 58.42 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGElwplfggcLTKPERGKLF-------YVPQR--------------PYM 515
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG--------LEEPTSGRIYiggrdvtDLPPKdrdiamvfqnyalyPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 516 tlgTLRDQVIYPDTVEDQRKKGISDQVlKEYLDNVQLGQILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 595
Cdd:cd03301 88 ---TVYDNIAFGLKLRKVPKDEIDERV-REVAELLQIEHLLDRK---------PKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1985402263 596 DECTSAVS----VDVEGYIYSHCRKVGITLFTVSH 626
Cdd:cd03301 155 DEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTH 189
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
457-626 |
1.44e-09 |
|
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: 58.63 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGEL-WPLFGGCLTK--------PERGKLFyvpQR----PYMTLgtlRDQ 523
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitepgPDRMVVF---QNysllPWLTV---REN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 524 V-IYPDTVEDQRKKGISDQVLKEYLDNVQLGQILEREGGWdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAV 602
Cdd:TIGR01184 75 IaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ---------LSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180
....*....|....*....|....*...
gi 1985402263 603 SVDVEGYIYSH----CRKVGITLFTVSH 626
Cdd:TIGR01184 146 DALTRGNLQEElmqiWEEHRVTVLMVTH 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
457-597 |
1.71e-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: 58.21 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG-------------CLTKPERGkLFYVPQrpymtlgtlrDQ 523
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsirfdgrditglpPHERARAG-IGYVPE----------GR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 524 VIYPD-TVED-------QRKKGISDQVLKEYLDNV-QLGQILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAI 594
Cdd:cd03224 85 RIFPElTVEEnlllgayARRRAKRKARLERVYELFpRLKERRKQLAG---------TLSGGEQQMLAIARALMSRPKLLL 155
|
...
gi 1985402263 595 LDE 597
Cdd:cd03224 156 LDE 158
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
458-627 |
1.79e-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: 57.05 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 458 RDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplFGgcLTKPERGKLFyvpqrpymtlgtLRDQVIYPDTVEDQRKKG 537
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKIL------SG--LYKPDSGEIL------------VDGKEVSFASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 538 ISdqvlkeyldnvqlgqilereggwdSV-QdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRK 616
Cdd:cd03216 77 IA------------------------MVyQ-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR 127
|
170
....*....|....
gi 1985402263 617 V---GITLFTVSHR 627
Cdd:cd03216 128 LraqGVAVIFISHR 141
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
459-601 |
1.83e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.57 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 459 DLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG----------------CLTKPERGKLFyvpQR----PYMTlg 518
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglkvndpkvdeRLIRQEAGMVF---QQfylfPHLT-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 519 TLRDQVIYPDTVEDQRKKGISDQVlKEYLDNVQLGqilEREGGWDSVqdwmdvLSGGEKQRMAMARLFYHKPQFAILDEC 598
Cdd:PRK09493 94 ALENVMFGPLRVRGASKEEAEKQA-RELLAKVGLA---ERAHHYPSE------LSGGQQQRVAIARALAVKPKLMLFDEP 163
|
...
gi 1985402263 599 TSA 601
Cdd:PRK09493 164 TSA 166
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
440-630 |
1.84e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 440 LIKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCLTKPE-RGKLFYVPQRPYMTL 517
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIsGELQPSSGTVFRSAKvRMAVFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 518 GT---LRDQVIYPdtvedqrkkGISDQVLKEYLDNVQLGQILEREGgwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAI 594
Cdd:PLN03073 588 SSnplLYMMRCFP---------GVPEQKLRAHLGSFGVTGNLALQP--------MYTLSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1985402263 595 LDECTSAVSVD-VEGYIYshcrkvGITLF-----TVSHRKSL 630
Cdd:PLN03073 651 LDEPSNHLDLDaVEALIQ------GLVLFqggvlMVSHDEHL 686
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
403-607 |
2.14e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.33 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 403 NRGRYQR--TMISQHEKDGDRTQTIPLIPGT---GEIINTDNLIK-FDHvplatpngDILIRDLNFEVRSGANVLICGPN 476
Cdd:TIGR03719 286 SKARLARyeELLSQEFQKRNETAEIYIPPGPrlgDKVIEAENLTKaFGD--------KLLIDDLSFKLPPGGIVGVIGPN 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 477 GCGKSSLFRVL-GElwplfggclTKPERGKLfyvpqrpymTLGtlrdqviypDTVE----DQRKKGISD-----QVLKEY 546
Cdd:TIGR03719 358 GAGKSTLFRMItGQ---------EQPDSGTI---------EIG---------ETVKlayvDQSRDALDPnktvwEEISGG 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 547 LDNVQLG--QILERE-------GGWDSvQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVE 607
Cdd:TIGR03719 411 LDIIKLGkrEIPSRAyvgrfnfKGSDQ-QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTN--DLDVE 477
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
436-600 |
3.35e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.49 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 436 NTDNLIKFDHVPLATPNGDIL-IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPlfggcltkPERGKLfyvpqrpy 514
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL--------PEAGTI-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 515 mtlgTLRDQVIYPDTVEDQRKK-GISDQ------VLKEYLDNVQLG---------QILER-EGGWDSV--QDWMD----V 571
Cdd:PRK13635 65 ----TVGGMVLSEETVWDVRRQvGMVFQnpdnqfVGATVQDDVAFGlenigvpreEMVERvDQALRQVgmEDFLNrephR 140
|
170 180
....*....|....*....|....*....
gi 1985402263 572 LSGGEKQRMAMARLFYHKPQFAILDECTS 600
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
453-626 |
3.38e-09 |
|
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: 57.12 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 453 GDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPlfggcltkPERGKLFYVPQRPYMTLGTLRDQVIYPD---- 528
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP--------PLAGRVLLNGGPLDFQRDSIARGLLYLGhapg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 529 -----TVEDQ----RKKGISDQVLkEYLDNVQLGQILEREGGWdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:cd03231 84 ikttlSVLENlrfwHADHSDEQVE-EALARVGLNGFEDRPVAQ---------LSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|.
gi 1985402263 600 SAV---SVD-VEGYIYSHCRKVGITLFTVSH 626
Cdd:cd03231 154 TALdkaGVArFAEAMAGHCARGGMVVLTTHQ 184
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
441-641 |
3.47e-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: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWplfggcltKPERGKLFYVPQRPYMTLGT 519
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL--------KPQQGEITLDGVPVSDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 520 LRDQViypdTVEDQRKkgisdqvlkeYLDNVQLGQILEREggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:cd03247 73 LSSLI----SVLNQRP----------YLFDTTLRNNLGRR------------FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1985402263 600 saVSVDVE------GYIYSHCRkvGITLFTVSHRKSLWKHHDFYLHMD 641
Cdd:cd03247 127 --VGLDPIterqllSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLE 170
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
456-643 |
3.90e-09 |
|
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: 56.77 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplFGGCLTKPERGKLfyvpqrpymtlgTLRDQVIYPDTVEDQRK 535
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI------MGHPKYEVTEGEI------------LFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 536 KGI--SDQV--------LKEYLDNVQLGqilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD 605
Cdd:cd03217 77 LGIflAFQYppeipgvkNADFLRYVNEG------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1985402263 606 ----VEGYIySHCRKVGITLFTVSHRKSLWKHH--DF-YLHMDGR 643
Cdd:cd03217 139 alrlVAEVI-NKLREEGKSVLIITHYQRLLDYIkpDRvHVLYDGR 182
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
457-627 |
4.13e-09 |
|
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: 56.91 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGCLTKPERGKLFYVPQR----PYMtlgTLRDQVI 525
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRmILGIILPdsgevlFDGKPLDIAARNRIGYLPEErglyPKM---KVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 526 YPDTVEDQRKKGISDQVLkEYLDNVQLGQILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDECTSA---V 602
Cdd:cd03269 93 YLAQLKGLKKEEARRRID-EWLERLELSEYANKR---------VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGldpV 162
|
170 180
....*....|....*....|....*
gi 1985402263 603 SVDVEGYIYSHCRKVGITLFTVSHR 627
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTHQ 187
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
457-626 |
4.60e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 58.81 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGCLTK--PERGKLFYVPQR----PYMTLgtlRD 522
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIagfetpdsGRIM-LDGQDITHvpAENRHVNTVFQSyalfPHMTV---FE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 523 QVIYPDTVEDQRKKGISDQVLkEYLDNVQLGQILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAV 602
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVM-EALRMVQLEEFAQRK-----PHQ----LSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180
....*....|....*....|....*...
gi 1985402263 603 SVDVEGYIYSHC----RKVGITLFTVSH 626
Cdd:PRK09452 176 DYKLRKQMQNELkalqRKLGITFVFVTH 203
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
452-623 |
5.11e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.60 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG--CLTKPERGKLFYVPQRPYMTLGTLrdQVIYPD- 528
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGevRWNGTPLAEQRDEPHENILYLGHL--PGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 529 TVED-----QRKKGISDQVLKEYLDNVQLGQILEREGGWdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVS 603
Cdd:TIGR01189 89 SALEnlhfwAAIHGGAQRTIEDALAAVGLTGFEDLPAAQ---------LSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....
gi 1985402263 604 VD----VEGYIYSHCRKVGITLFT 623
Cdd:TIGR01189 160 KAgvalLAGLLRAHLARGGIVLLT 183
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
474-602 |
5.37e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.48 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 474 GPNGCGKSSLFRVL---GELWPLFGGCLTKPERGKLFYVPQRPYMTL----GTLRDQ------VIYPDTVEDQRKKGISD 540
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPEVTITGSIVYNGHNIYSPRTDTVDLrkeiGMVFQQpnpfpmSIYENVVYGLRLKGIKD 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985402263 541 qvlKEYLDNVqLGQILEREGGWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAV 602
Cdd:PRK14239 118 ---KQVLDEA-VEKSLKGASIWDEVKDRLHdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
441-626 |
5.74e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG---CLTKPERGKL-----FYVPQR 512
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisILGQPTRQALqknlvAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 513 PYMTLGtlrdqviYPDTVED-------------QRKKGISDQVLKEYLDNVQLGQILEREGGwdsvqdwmdVLSGGEKQR 579
Cdd:PRK15056 87 EEVDWS-------FPVLVEDvvmmgryghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIG---------ELSGGQKKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1985402263 580 MAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSH 626
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrdeGKTMLVSTH 200
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
459-601 |
7.83e-09 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 56.15 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 459 DLNFEVrSGANVLICGPNGCGKSSLFRVL--------GELW----PLFGGCL---TKPERGKLFYVPQR----PYMTLgt 519
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIaglekpdgGTIVlngtVLFDSRKkinLPPQQRKIGLVFQQyalfPHLNV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 520 lRDQVIYPDTVEDQRKKGISDQvlkEYLDNVQLGQILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:cd03297 93 -RENLAFGLKRKRNREDRISVD---ELLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
..
gi 1985402263 600 SA 601
Cdd:cd03297 160 SA 161
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
453-599 |
9.67e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 453 GDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGCLTKPERGKLFYVPQRPY------MTLGtlrdqvi 525
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvGELEPD-SGTVKWSENANIGYYAQDHAydfendLTLF------- 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985402263 526 ypDTVEDQRKKGISDQVLKEYLDNVQLGQilereggwDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:PRK15064 403 --DWMSQWRQEGDDEQAVRGTLGRLLFSQ--------DDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
452-626 |
1.10e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT--------------------KPERGKLFYVPQ 511
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlyfgkdifqidaiklRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 512 rPYMTLgTLRDQVIYPDTVEDQRKKGISDQVLKEYLDNVQLgqilereggWDSVQDWMDV----LSGGEKQRMAMARLFY 587
Cdd:PRK14246 101 -PFPHL-SIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGL---------WKEVYDRLNSpasqLSGGQQQRLTIARALA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1985402263 588 HKPQFAILDECTSAVSV----DVEGYIYSHCRKVGITLftVSH 626
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIvnsqAIEKLITELKNEIAIVI--VSH 210
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
452-597 |
2.02e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.46 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILiRDLNFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGC----LTKPERGK--LFYVPQRPY- 514
Cdd:COG0396 12 GKEIL-KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpkyevtsGSI--LLDGEdileLSPDERARagIFLAFQYPVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 515 ---MTLGT-LRdqviypDTVEDQRKKGIS----DQVLKEYLDNVQLGQ-ILER---EGgwdsvqdwmdvLSGGEKQRMAM 582
Cdd:COG0396 89 ipgVSVSNfLR------TALNARRGEELSarefLKLLKEKMKELGLDEdFLDRyvnEG-----------FSGGEKKRNEI 151
|
170
....*....|....*
gi 1985402263 583 ARLFYHKPQFAILDE 597
Cdd:COG0396 152 LQMLLLEPKLAILDE 166
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
453-626 |
3.24e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.19 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 453 GDILI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLfggcltkpERGKLFYVPQR----PYMTLG---TLRDQV 524
Cdd:PRK11000 14 GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDI--------TSGDLFIGEKRmndvPPAERGvgmVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 525 IYPD-TVEDQR---------KKGISDQVLKEYLDNVQLGQILEREGgwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAI 594
Cdd:PRK11000 86 LYPHlSVAENMsfglklagaKKEEINQRVNQVAEVLQLAHLLDRKP---------KALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1985402263 595 LDECTS----AVSVDVEGYIYSHCRKVGITLFTVSH 626
Cdd:PRK11000 157 LDEPLSnldaALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
451-605 |
3.57e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 451 PNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPLFGgcltkperGKLFYVPQRPYM--TLgTL 520
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfnGEARPQPG--------IKVGYLPQEPQLdpTK-TV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 521 RDQVIypDTVEDQRKK-----GIS----------DQVLKEyldNVQLGQILEREGGWD---SVQDWMD------------ 570
Cdd:TIGR03719 86 RENVE--EGVAEIKDAldrfnEISakyaepdadfDKLAAE---QAELQEIIDAADAWDldsQLEIAMDalrcppwdadvt 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1985402263 571 VLSGGEKQRMAMARLFYHKPQFAILDECTS---AVSVD 605
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNhldAESVA 198
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
459-626 |
6.34e-08 |
|
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: 55.12 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 459 DLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG-------CL--------TKPERGKLFYVPQR----PYMTLgt 519
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeivlngrTLfdsrkgifLPPEKRRIGYVFQEarlfPHLSV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 520 lRDQVIYPDTVEDQRKKGISDQVLKEYLDnvqLGQILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:TIGR02142 93 -RGNLRYGMKRARPSERRISFERVIELLG---IGHLLGRLPG---------RLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190
....*....|....*....|....*....|.
gi 1985402263 600 SAVSV----DVEGYIYSHCRKVGITLFTVSH 626
Cdd:TIGR02142 160 AALDDprkyEILPYLERLHAEFGIPILYVSH 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
446-600 |
6.56e-08 |
|
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: 53.81 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 446 VPLATPNGD---ILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-----------GELWplFGGCLTKPergKLF---- 507
Cdd:cd03234 9 VGLKAKNWNkyaRILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrvegggttsGQIL--FNGQPRKP---DQFqkcv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 508 -YVPQR----PYMtlgTLRDQVIYPDTVEDQRKKgiSDQVLKEYLDNVQLGQI-LEREGGwdsvqDWMDVLSGGEKQRMA 581
Cdd:cd03234 84 aYVRQDdillPGL---TVRETLTYTAILRLPRKS--SDAIRKKRVEDVLLRDLaLTRIGG-----NLVKGISGGERRRVS 153
|
170
....*....|....*....
gi 1985402263 582 MARLFYHKPQFAILDECTS 600
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTS 172
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
388-612 |
6.78e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.80 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 388 FTARITeLMQVLKDLNR--GRYQRTMIS----------QHEKDgdrtqtipliPGTGEIINTDNLIKFDHVPLATPNGDI 455
Cdd:PRK11176 288 FSSMIA-LMRPLKSLTNvnAQFQRGMAAcqtlfaildlEQEKD----------EGKRVIERAKGDIEFRNVTFTYPGKEV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 L-IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLTkpergkLFYVPQRPYmTLGTLRDQV--------IY 526
Cdd:PRK11176 357 PaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL------LDGHDLRDY-TLASLRNQValvsqnvhLF 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 527 PDTVEDQRKKGISDQVLKEYLDNVQ-----LGQILEREGGWDSVQDWMDV-LSGGEKQRMAMARLFYHKPQFAILDECTS 600
Cdd:PRK11176 430 NDTIANNIAYARTEQYSREQIEEAArmayaMDFINKMDNGLDTVIGENGVlLSGGQRQRIAIARALLRDSPILILDEATS 509
|
250
....*....|..
gi 1985402263 601 AVSVDVEGYIYS 612
Cdd:PRK11176 510 ALDTESERAIQA 521
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
457-626 |
8.68e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.97 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGcLTKPERGKLFYVPQRpyMTLGT---LRDQVIY----PD- 528
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVR-------LIDG-LLEAESGQIIIDGDL--LTEENvwdIRHKIGMvfqnPDn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 529 -----TVEDQ-----RKKGISDQVLKEYLDnvqlgQILEREGgwdsVQDWMDV----LSGGEKQRMAMARLFYHKPQFAI 594
Cdd:PRK13650 93 qfvgaTVEDDvafglENKGIPHEEMKERVN-----EALELVG----MQDFKEReparLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1985402263 595 LDECTSAvsVDVEG------YIYSHCRKVGITLFTVSH 626
Cdd:PRK13650 164 LDEATSM--LDPEGrlelikTIKGIRDDYQMTVISITH 199
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
456-600 |
9.27e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.76 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFggcltkPE---RGKLFYVPQRPY-MTLGTLRD--QVIYpdt 529
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELY------PEarvSGEVYLDGQDIFkMDVIELRRrvQMVF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 530 vedQRKKGISDQVLKEyldNVQLG------------------QILEREGGWDSVQDWMDV----LSGGEKQRMAMARLFY 587
Cdd:PRK14247 89 ---QIPNPIPNLSIFE---NVALGlklnrlvkskkelqervrWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARALA 162
|
170
....*....|...
gi 1985402263 588 HKPQFAILDECTS 600
Cdd:PRK14247 163 FQPEVLLADEPTA 175
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
457-626 |
1.16e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 54.33 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfgGcLTKPERGKLF-----------------YVPQR----PYM 515
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIA-------G-FETPDSGRILldgrdvtglppekrnvgMVFQDyalfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 516 TLgtlRDQVIYPDTVEDQRKKGISDQVlKEYLDNVQLGQILER---EggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQF 592
Cdd:COG3842 93 TV---AENVAFGLRMRGVPKAEIRARV-AELLELVGLEGLADRyphQ------------LSGGQQQRVALARALAPEPRV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1985402263 593 AILDECTSA------VSVDVEgyIYSHCRKVGITLFTVSH 626
Cdd:COG3842 157 LLLDEPLSAldaklrEEMREE--LRRLQRELGITFIYVTH 194
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
457-597 |
1.51e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 53.57 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGCLTKPERGKLFYVPQ-RpymtlGtlrdqvIYPD 528
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILAPdsgevlWDGEPLDPEDRRRIGYLPEeR-----G------LYPK 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985402263 529 -TVEDQ-----RKKGISDQV----LKEYLDNVQLGqilEREGgwDSVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDE 597
Cdd:COG4152 86 mKVGEQlvylaRLKGLSKAEakrrADEWLERLGLG---DRAN--KKVEE----LSKGNQQKVQLIAALLHDPELLILDE 155
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
440-630 |
1.82e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.57 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 440 LIKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGC-LTKPERGKLFYVP 510
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIcgierpsaGKIW--FSGHdITRLKNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 511 QRPYMTLGT---LRDQVIYPDTVEDQRKKGISDQVLKEyldnvQLGQILEREGGWDSVQDWMDVLSGGEKQRMAMARLFY 587
Cdd:PRK10908 79 RQIGMIFQDhhlLMDRTVYDNVAIPLIIAGASGDDIRR-----RVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1985402263 588 HKPQFAILDECT----SAVSVDVEgYIYSHCRKVGITLFTVSHRKSL 630
Cdd:PRK10908 154 NKPAVLLADEPTgnldDALSEGIL-RLFEEFNRVGVTVLMATHDIGL 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
453-607 |
1.89e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 453 GDILIRDLNFEVRSGANVLICGPNGCGKSSLFRV-LGELWPLFGG--CLTKPE-------RGKLfyVPQRPYMtlgtlrd 522
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQADSGRihCGTKLEvayfdqhRAEL--DPEKTVM------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 523 qviypDTVEDQRKK----GISDQVLKeYLdnvqlgqilereggwdsvQDWM----------DVLSGGEKQRMAMARLFYH 588
Cdd:PRK11147 402 -----DNLAEGKQEvmvnGRPRHVLG-YL------------------QDFLfhpkramtpvKALSGGERNRLLLARLFLK 457
|
170
....*....|....*....
gi 1985402263 589 KPQFAILDECTSavSVDVE 607
Cdd:PRK11147 458 PSNLLILDEPTN--DLDVE 474
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
434-626 |
2.32e-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: 52.20 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 434 IINTDNLIK-FDHVPLATPngdiLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGCLTKPERG 504
Cdd:cd03258 1 MIELKNVSKvFGDTGGKVT----ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptsGSVL-VDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 505 KLfyVPQRPYMTL----------GTLRDQVIYPDTVEDQRKKGISDQVLkEYLDNVQLGqilereggwDSVQDWMDVLSG 574
Cdd:cd03258 76 EL--RKARRRIGMifqhfnllssRTVFENVALPLEIAGVPKAEIEERVL-ELLELVGLE---------DKADAYPAQLSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1985402263 575 GEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 626
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALdpetTQSILALLRDINRELGLTIVLITH 199
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
474-602 |
2.51e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.48 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 474 GPNGCGKSSLFRVLGELWPLFGGCLTKperGKLFYvpqrpymtlgtlRDQVIYP---DTVEDQRKKGISDQ----VLKEY 546
Cdd:PRK14243 43 GPSGCGKSTILRCFNRLNDLIPGFRVE---GKVTF------------HGKNLYApdvDPVEVRRRIGMVFQkpnpFPKSI 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985402263 547 LDNVQLG-----------QILERE----GGWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAV 602
Cdd:PRK14243 108 YDNIAYGaringykgdmdELVERSlrqaALWDEVKDKLKqsglSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
453-597 |
2.80e-07 |
|
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: 51.91 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 453 GDILI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT---------KPE----RGkLFYVPQRpymtlg 518
Cdd:COG0410 14 GGIHVlHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglPPHriarLG-IGYVPEG------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 519 tlRDqvIYPD-TVED--------QRKKGISDQVLKEYLDNV-QLGQILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYH 588
Cdd:COG0410 87 --RR--IFPSlTVEEnlllgayaRRDRAEVRADLERVYELFpRLKERRRQRAG---------TLSGGEQQMLAIGRALMS 153
|
....*....
gi 1985402263 589 KPQFAILDE 597
Cdd:COG0410 154 RPKLLLLDE 162
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
409-629 |
2.87e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.56 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 409 RTMISQHEKDGDRTQTIPLIPGTGEIintdNLIKFdHVPLATPNgdiLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL- 487
Cdd:PRK10789 291 RAMLAEAPVVKDGSEPVPEGRGELDV----NIRQF-TYPQTDHP---ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIq 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 488 -------GELwpLFGGC-LTKPE----RGKLFYVPQRPYMTLGTLRDQVIY--PDTVEDQ-----RKKGISDQVLKeyld 548
Cdd:PRK10789 363 rhfdvseGDI--RFHDIpLTKLQldswRSRLAVVSQTPFLFSDTVANNIALgrPDATQQEiehvaRLASVHDDILR---- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 549 nvqLGQILEREGGWDSVqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGI--TLFTVSH 626
Cdd:PRK10789 437 ---LPQGYDTEVGERGV-----MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEgrTVIISAH 508
|
...
gi 1985402263 627 RKS 629
Cdd:PRK10789 509 RLS 511
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
434-626 |
3.11e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.10 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 434 IINTDNLIKFDHVPLATPnGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGCLTKPERGKLF 507
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPpsegeiLLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 508 -----YVPQR-PYMTLGTLRDQVI---YP-------DTVEDQRKkgisdqvLKEYLDNVQLGQILEReggwdsvqdWMDV 571
Cdd:PRK10575 84 arkvaYLPQQlPAAEGMTVRELVAigrYPwhgalgrFGAADREK-------VEEAISLVGLKPLAHR---------LVDS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1985402263 572 LSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 626
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
451-600 |
3.59e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.00 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 451 PNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCLTKPE------------RGKLFYVPQRPymtl 517
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFnGILKPTSGEVLIKGEpikydkksllevRKTVGIVFQNP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 518 gtlRDQVIYPdTVEDQRKKGISDQVLKEylDNVQ--LGQILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAIL 595
Cdd:PRK13639 88 ---DDQLFAP-TVEEDVAFGPLNLGLSK--EEVEkrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
....*
gi 1985402263 596 DECTS 600
Cdd:PRK13639 162 DEPTS 166
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
463-638 |
4.32e-07 |
|
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: 51.64 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 463 EVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCLTkpERGKLFYVPQrpYMtlgtlrdQVIYPDTVED-----QRKK 536
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLaGVLKPDEGDIEI--ELDTVSYKPQ--YI-------KADYEGTVRDllssiTKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 537 GISDQVLKEYLDNVQLGQILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDEcTSAvSVDVEGYIysHCRK 616
Cdd:cd03237 90 YTHPYFKTEIAKPLQIEQILDRE-----VPE----LSGGELQRVAIAACLSKDADIYLLDE-PSA-YLDVEQRL--MASK 156
|
170 180
....*....|....*....|...
gi 1985402263 617 VgITLFTVSHRKSLWK-HHDFYL 638
Cdd:cd03237 157 V-IRRFAENNEKTAFVvEHDIIM 178
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
456-629 |
4.45e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.83 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT-----------KPERGKLFYVPQRPYMTLGTLRDQV 524
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVidgidisklplHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 525 iypdtveDQRKKgISDQVLKEYLDNVQLGQILER-EGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAV 602
Cdd:cd03288 116 -------DPECK-CTDDRLWEALEIAQLKNMVKSlPGGLDAvVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190
....*....|....*....|....*....|...
gi 1985402263 603 SVDVEGYIyshcRKVGITLF------TVSHRKS 629
Cdd:cd03288 188 DMATENIL----QKVVMTAFadrtvvTIAHRVS 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
457-597 |
5.49e-07 |
|
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: 51.28 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELwplfggcltKPERGKLFY----VPQRPymtlgtlrdqviypdtvE 531
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFL---------RPTSGSVLFdgedITGLP-----------------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 532 DQR-KKGISD--QVLKEY-----LDNVQLGQILEREGGWDSVQDW----------------------MDV----LSGGEK 577
Cdd:cd03219 70 HEIaRLGIGRtfQIPRLFpeltvLENVMVAAQARTGSGLLLARARreereareraeellervgladlADRpageLSYGQQ 149
|
170 180
....*....|....*....|
gi 1985402263 578 QRMAMARLFYHKPQFAILDE 597
Cdd:cd03219 150 RRLEIARALATDPKLLLLDE 169
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
382-627 |
5.74e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 382 MTRLAGFTARITELMQ-VLKDLNRGRYQRTMIsqhekdgDRTQTIPLIPGTGEIINTDN----------LIKFDHVPLA- 449
Cdd:PLN03232 1172 MGLLLSYTLNITTLLSgVLRQASKAENSLNSV-------ERVGNYIDLPSEATAIIENNrpvsgwpsrgSIKFEDVHLRy 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 450 TPNGDILIRDLNFEVRSGANVLICGPNGCGKSS----LFRVL----GELwpLFGGC------LTKPERGkLFYVPQRPYM 515
Cdd:PLN03232 1245 RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSmlnaLFRIVelekGRI--MIDDCdvakfgLTDLRRV-LSIIPQSPVL 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 516 TLGTLRDQViypDTVEDQrkkgiSDQVLKEYLDNVQLGQILEREG-GWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFA 593
Cdd:PLN03232 1322 FSGTVRFNI---DPFSEH-----NDADLWEALERAHIKDVIDRNPfGLDAeVSEGGENFSVGQRQLLSLARALLRRSKIL 1393
|
250 260 270
....*....|....*....|....*....|....*.
gi 1985402263 594 ILDECTSAVSVDVEGYIYSHCRK--VGITLFTVSHR 627
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIREefKSCTMLVIAHR 1429
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
436-626 |
5.78e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.29 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 436 NTDNLIKFDHVPLATpNGD--ILIRDLNFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGcLTKPERGKLFYvpqrp 513
Cdd:PRK13648 3 DKNSIIVFKNVSFQY-QSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAK-------LMIG-IEKVKSGEIFY----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 514 ymtlgtlRDQVIYPDTVEDQRKK-GISDQV-----------------LKEYL---DNVQ--LGQILEREGGWDSVQDWMD 570
Cdd:PRK13648 69 -------NNQAITDDNFEKLRKHiGIVFQNpdnqfvgsivkydvafgLENHAvpyDEMHrrVSEALKQVDMLERADYEPN 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 571 VLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV----GITLFTVSH 626
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITH 201
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
459-630 |
8.42e-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: 50.96 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 459 DLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplFGgcLTKPERGKLFYVPQRPYMTLGTLRD------QVIYPDTVED 532
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLL------LG--LEKPAQGTVSFRGQDLYQLDRKQRRafrrdvQLVFQDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 533 QRKKGISDQVLKEYLDNV-------QLGQILE--REGGWDSvqDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:TIGR02769 101 VNPRMTVRQIIGEPLRHLtsldeseQKARIAEllDMVGLRS--EDADklprQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1985402263 600 SAVSVDVEGYIYSHCRKV----GITLFTVSHRKSL 630
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLqqafGTAYLFITHDLRL 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
403-585 |
8.79e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 403 NRGRYQR--TMISQHEKDGDRTQTIpLIPgTGEIINtDNLIKFDHVPLATpnGD-ILIRDLNFEVRSGANVLICGPNGCG 479
Cdd:PRK11819 288 SKARLARyeELLSEEYQKRNETNEI-FIP-PGPRLG-DKVIEAENLSKSF--GDrLLIDDLSFSLPPGGIVGIIGPNGAG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 480 KSSLFRVL-GElwplfggclTKPERGKLfyvpqrpymTLGtlrdqviypDTVE----DQRKKGISD-----QVLKEYLDN 549
Cdd:PRK11819 363 KSTLFKMItGQ---------EQPDSGTI---------KIG---------ETVKlayvDQSRDALDPnktvwEEISGGLDI 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1985402263 550 VQLGQileRE------------GGWDSvQDWMDVLSGGEKQRMAMARL 585
Cdd:PRK11819 416 IKVGN---REipsrayvgrfnfKGGDQ-QKKVGVLSGGERNRLHLAKT 459
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
462-606 |
8.95e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 462 FEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGCLTKPE-------RGKLFYVPQRPYMTLgtlrdqviy 526
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLLtmietptgGELY-YQGQDLLKADpeaqkllRQKIQIVFQNPYGSL--------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 527 pdtveDQRKKgISdQVLKEYLD-NVQLGQILEREggwdSVQDWMD--------------VLSGGEKQRMAMARLFYHKPQ 591
Cdd:PRK11308 106 -----NPRKK-VG-QILEEPLLiNTSLSAAERRE----KALAMMAkvglrpehydryphMFSGGQRQRIAIARALMLDPD 174
|
170
....*....|....*
gi 1985402263 592 FAILDECTSAVSVDV 606
Cdd:PRK11308 175 VVVADEPVSALDVSV 189
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
438-607 |
9.64e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 438 DNLIKFD-HVPLATPNGDILIR--DL-----NF-------EVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCLTKP 501
Cdd:PRK13409 321 PEPIEFEeRPPRDESERETLVEypDLtkklgDFsleveggEIYEGEVIGIVGPNGIGKTTFAKLLaGVLKPDEGEVDPEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 502 ergKLFYVPQRpymtlgtLRDQviYPDTVED---QRKKGISDQVLK-EYLDNVQLGQILEREggwdsvqdwMDVLSGGEK 577
Cdd:PRK13409 401 ---KISYKPQY-------IKPD--YDGTVEDllrSITDDLGSSYYKsEIIKPLQLERLLDKN---------VKDLSGGEL 459
|
170 180 190
....*....|....*....|....*....|
gi 1985402263 578 QRMAMARLFYHKPQFAILDEcTSAvSVDVE 607
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDE-PSA-HLDVE 487
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
438-626 |
1.35e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.62 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 438 DNLIKFDHVPLATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGCLTKPERGKLFYVPQ 511
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLnGILKPssgriLFDGKPIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 512 RPYMTLGTLRDQV----IYPDTVEDQRKKGISDQVLKEYLDNvqlgqILEREGGWDSVQDWMDVLSGGEKQRMAMARLFY 587
Cdd:PRK13636 83 SVGMVFQDPDNQLfsasVYQDVSFGAVNLKLPEDEVRKRVDN-----ALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1985402263 588 HKPQFAILDECTSAVS----VDVEGYIYSHCRKVGITLFTVSH 626
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATH 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
456-600 |
1.72e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.84 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 456 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPL------------FGGCLTKP---------ERGKLFYVPQR-P 513
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearvegevrlFGRNIYSPdvdpievrrEVGMVFQYPNPfP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 514 YMTlgtlrdqvIYPDTVEDQRKKGISDQvlKEYLDNVqLGQILEREGGWDSVQDWMD----VLSGGEKQRMAMARLFYHK 589
Cdd:PRK14267 99 HLT--------IYDNVAIGVKLNGLVKS--KKELDER-VEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMK 167
|
170
....*....|.
gi 1985402263 590 PQFAILDECTS 600
Cdd:PRK14267 168 PKILLMDEPTA 178
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
459-606 |
1.82e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.47 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 459 DLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGC----LTKPER--GKLF--YVPQRpYMTLGtlrD 522
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIaglehqtsGHI--RFHGTdvsrLHARDRkvGFVFqhYALFR-HMTVF---D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 523 QVIYPDTVEDQRKK---GISDQVLKEYLDNVQLGQILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:PRK10851 94 NIAFGLTVLPRRERpnaAAIKAKVTQLLEMVQLAHLADR---------YPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
....*..
gi 1985402263 600 SAVSVDV 606
Cdd:PRK10851 165 GALDAQV 171
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
464-600 |
2.13e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 464 VRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCLTKPE--------RG-------------------KLFYVPQRPYM 515
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILaGKLKPNLGKFDDPPDwdeildefRGselqnyftkllegdvkvivKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 516 TLGTLRDQViypdTVEDQRKKgisdqvLKEYLDNVQLGQILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 595
Cdd:cd03236 103 VKGKVGELL----KKKDERGK------LDELVDQLELRHVLDRN---------IDQLSGGELQRVAIAAALARDADFYFF 163
|
....*
gi 1985402263 596 DECTS 600
Cdd:cd03236 164 DEPSS 168
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
453-626 |
2.16e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.51 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 453 GDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT-------------KPERGkLFYVPQRP------ 513
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplhaRARRG-IGYLPQEAsifrrl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 514 -----YMTLGTLRDqviypDTVEDQRKKGiSDQVLKEY----LDNvQLGQilereggwdsvqdwmdVLSGGEKQRMAMAR 584
Cdd:PRK10895 94 svydnLMAVLQIRD-----DLSAEQREDR-ANELMEEFhiehLRD-SMGQ----------------SLSGGERRRVEIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1985402263 585 LFYHKPQFAILDECTSAVS----VDVEGyIYSHCRKVGITLFTVSH 626
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDpisvIDIKR-IIEHLRDSGLGVLITDH 195
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
457-616 |
2.28e-06 |
|
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: 48.58 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplFGgcLTKPERGKLfyvpqrpymtlgTLRDQVIYPDTVEDQRKK 536
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEAL------FG--LRPPASGEI------------TLDGKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 537 GISdqvlkeYL--DNVQLGQILEReggwdSVQDWM---DVLSGGEKQRMAMARLFYHKPQFAILDECTsaVSVDVEG--Y 609
Cdd:cd03215 76 GIA------YVpeDRKREGLVLDL-----SVAENIalsSLLSGGNQQKVVLARWLARDPRVLILDEPT--RGVDVGAkaE 142
|
....*..
gi 1985402263 610 IYSHCRK 616
Cdd:cd03215 143 IYRLIRE 149
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
455-605 |
2.60e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 49.18 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 455 ILiRDLNFEVRSGANVLICGPNGCGKSSLFRVL----------GELWpLFGGCLT--KPE---RGKLFYVPQRPYMTLGT 519
Cdd:TIGR01978 15 IL-KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpsyevtsGTIL-FKGQDLLelEPDeraRAGLFLAFQYPEEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 520 -----LRDQViypDTVEDQRKKGISD-----QVLKEYLDNVQL-GQILER---EGgwdsvqdwmdvLSGGEKQRMAMARL 585
Cdd:TIGR01978 93 snlefLRSAL---NARRSARGEEPLDlldfeKLLKEKLALLDMdEEFLNRsvnEG-----------FSGGEKKRNEILQM 158
|
170 180
....*....|....*....|
gi 1985402263 586 FYHKPQFAILDECTSAVSVD 605
Cdd:TIGR01978 159 ALLEPKLAILDEIDSGLDID 178
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
464-600 |
2.62e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 464 VRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCLTKPE--------RG-------------------KLFYVPQRPYM 515
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsGELIPNLGDYEEEPSwdevlkrfRGtelqnyfkklyngeikvvhKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 516 TLGTLRDQVIYPDtvedqrKKGISDQVLKEyldnVQLGQILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 595
Cdd:PRK13409 176 FKGKVRELLKKVD------ERGKLDEVVER----LGLENILDRD---------ISELSGGELQRVAIAAALLRDADFYFF 236
|
....*
gi 1985402263 596 DECTS 600
Cdd:PRK13409 237 DEPTS 241
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
450-604 |
2.78e-06 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 49.67 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 450 TPNGDI-LIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-----------GELwpLFGGC----LTKPE----RGK-LFY 508
Cdd:COG0444 13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlgllpppgitsGEI--LFDGEdllkLSEKElrkiRGReIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 509 VPQRPYMTLG---TLRDQVIYP------DTVEDQRKKGIsdqvlkEYLDNVQLgqilereggwDSVQDWMDV----LSGG 575
Cdd:COG0444 91 IFQDPMTSLNpvmTVGDQIAEPlrihggLSKAEARERAI------ELLERVGL----------PDPERRLDRypheLSGG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1985402263 576 EKQR----MAMArlfyHKPQFAILDECTSA--VSV 604
Cdd:COG0444 155 MRQRvmiaRALA----LEPKLLIADEPTTAldVTI 185
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
455-626 |
3.80e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.83 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 455 ILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGElwplfggcLTKPERGKLF--------YVPQRPYMTLGTLRDQVIY 526
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSR--------LMTPAHGHVWldgehiqhYASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 527 PD--TVEDQRKKG-ISDQVL-----KEylDNVQLGQILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDEC 598
Cdd:PRK10253 93 PGdiTVQELVARGrYPHQPLftrwrKE--DEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190
....*....|....*....|....*....|..
gi 1985402263 599 TSAV----SVDVEGYIYSHCRKVGITLFTVSH 626
Cdd:PRK10253 171 TTWLdishQIDLLELLSELNREKGYTLAAVLH 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
457-597 |
7.12e-06 |
|
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: 47.54 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGelwplfggcLTKPERGKLF--------------------YVPQRPYM 515
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYmIVG---------LVKPDSGKILldgqditklpmhkrarlgigYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 516 TLG-TLRDQV-----IYPDTVEDQRKKgisdqvLKEYLDNVQLGQILEREGgwdsvqdwmDVLSGGEKQRMAMARLFYHK 589
Cdd:cd03218 87 FRKlTVEENIlavleIRGLSKKEREEK------LEELLEEFHITHLRKSKA---------SSLSGGERRRVEIARALATN 151
|
....*...
gi 1985402263 590 PQFAILDE 597
Cdd:cd03218 152 PKFLLLDE 159
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
441-583 |
7.69e-06 |
|
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: 49.01 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFD-HVPLATPNGDILIR--DL-----NF-------EVRSGANVLICGPNGCGKSSLFRVL-GELwplfggcltKPERG 504
Cdd:COG1245 325 IEFEvHAPRREKEEETLVEypDLtksygGFsleveggEIREGEVLGIVGPNGIGKTTFAKILaGVL---------KPDEG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 505 KLF------YVPQRPymtlgtlrdQVIYPDTVEDQRKKGISDQV-----LKEYLDNVQLGQILEREggwdsvqdwMDVLS 573
Cdd:COG1245 396 EVDedlkisYKPQYI---------SPDYDGTVEEFLRSANTDDFgssyyKTEIIKPLGLEKLLDKN---------VKDLS 457
|
170
....*....|
gi 1985402263 574 GGEKQRMAMA 583
Cdd:COG1245 458 GGELQRVAIA 467
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
457-626 |
8.09e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCLT--------------KPERGKLFYVPQRPYMTLG---T 519
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtlspgklQALRRDIQFIFQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 520 LRDQVIYPDTVEDQRKKGISDQVLKEYLDNVQLgqilEREGGWDSVQDWmdvlSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAARVAWLLERVGL----LPEHAWRYPHEF----SGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190
....*....|....*....|....*....|.
gi 1985402263 600 SAVSVDVEGYIYSHC----RKVGITLFTVSH 626
Cdd:PRK10261 492 SALDVSIRGQIINLLldlqRDFGIAYLFISH 522
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
467-643 |
8.73e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 467 GANVLICGPNGCGKSSLFRVL-GELWPLFGGC-LTKperG-KLFYVPQRpymTLGTLRdqviyPDTVEDQRKKGISDQVL 543
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLaGELAPVSGEIgLAK---GiKLGYFAQH---QLEFLR-----ADESPLQHLARLAPQEL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 544 KEyldnvQLGQILereGGW----DSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGI 619
Cdd:PRK10636 407 EQ-----KLRDYL---GGFgfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG 478
|
170 180
....*....|....*....|....*.
gi 1985402263 620 TLFTVSHRKSLWKH--HDFYLHMDGR 643
Cdd:PRK10636 479 ALVVVSHDRHLLRSttDDLYLVHDGK 504
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
467-605 |
9.10e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 467 GANVLICGPNGCGKSSLFRVL--------GELWPLFGGcltkpergKLFYVPQRPYMTLG-TLRDQVIypDTVEDQRKK- 536
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMagvdkefeGEARPAPGI--------KVGYLPQEPQLDPEkTVRENVE--EGVAEVKAAl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 537 ----GIS----------DQVLKEYldnVQLGQILEREGGWDS---VQDWMD------------VLSGGEKQRMAMARLFY 587
Cdd:PRK11819 103 drfnEIYaayaepdadfDALAAEQ---GELQEIIDAADAWDLdsqLEIAMDalrcppwdakvtKLSGGERRRVALCRLLL 179
|
170 180
....*....|....*....|.
gi 1985402263 588 HKPQFAILDECTS---AVSVD 605
Cdd:PRK11819 180 EKPDMLLLDEPTNhldAESVA 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
457-610 |
9.21e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSS----LFRVL---GELW----PL--FGGCLTKPERGKLFYVPQRPYMTLGTLRD- 522
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIWfdgqPLhnLNRRQLLPVRHRIQVVFQDPNSSLNPRLNv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 523 --------QVIYPDTVEDQRkkgisDQVLKEYLDNVQLGQilereggwDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAI 594
Cdd:PRK15134 382 lqiieeglRVHQPTLSAAQR-----EQQVIAVMEEVGLDP--------ETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170
....*....|....*.
gi 1985402263 595 LDECTSAVSVDVEGYI 610
Cdd:PRK15134 449 LDEPTSSLDKTVQAQI 464
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
440-626 |
1.16e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.81 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 440 LIKFDHVPLA-TPNGDILIR---DLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGCLT--------------K 500
Cdd:PRK13643 1 MIKFEKVNYTyQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLnGLLQPTEGKVTVgdivvsstskqkeiK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 501 PERGKLFYVPQRPYmtlGTLRDQVIYPDTVEDQRKKGIS----DQVLKEYLDNVQLGQILEREGGWDsvqdwmdvLSGGE 576
Cdd:PRK13643 81 PVRKKVGVVFQFPE---SQLFEETVLKDVAFGPQNFGIPkekaEKIAAEKLEMVGLADEFWEKSPFE--------LSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1985402263 577 KQRMAMARLFYHKPQFAILDECTSAVSVDVE---GYIYSHCRKVGITLFTVSH 626
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
459-626 |
1.29e-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: 46.72 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 459 DLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGCLTKPERGKLFYVPQRPYMTLgtLRDQVIYPD-TVEDQRKK 536
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNlIAGFETPQSGRVLINGVDVTAAPPADRPVSML--FQENNLFAHlTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 537 GISDQVLKEYLDNVQLGQILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVS----VDVEGYIYS 612
Cdd:cd03298 94 GLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLD 173
|
170
....*....|....
gi 1985402263 613 HCRKVGITLFTVSH 626
Cdd:cd03298 174 LHAETKMTVLMVTH 187
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
441-626 |
1.56e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.13 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPL----ATPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGcLTKPERGKLFYV-----PQ 511
Cdd:PRK13641 3 IKFENVDYiyspGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQ-------HFNA-LLKPSSGTITIAgyhitPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 512 RPYMTLGTLRDQV----------IYPDTV-ED----QRKKGISDQVLKE----YLDNVQLGQILEREGGWDsvqdwmdvL 572
Cdd:PRK13641 75 TGNKNLKKLRKKVslvfqfpeaqLFENTVlKDvefgPKNFGFSEDEAKEkalkWLKKVGLSEDLISKSPFE--------L 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1985402263 573 SGGEKQRMAMARLFYHKPQFAILDEctSAVSVDVEGY-----IYSHCRKVGITLFTVSH 626
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDE--PAAGLDPEGRkemmqLFKDYQKAGHTVILVTH 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
460-626 |
1.87e-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: 47.87 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 460 LNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPLFGG---CLTKP---ERGKLfyvpqRPYMtlGTLRDQV- 524
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIagvleptsGEVNVRVGDewvDMTKPgpdGRGRA-----KRYI--GILHQEYd 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 525 IYPD-TVEDQRKKGISDQVLKEYldNVQLGQILEREGGWD-----SVQDWM-DVLSGGEKQRMAMARLFYHKPQFAILDE 597
Cdd:TIGR03269 376 LYPHrTVLDNLTEAIGLELPDEL--ARMKAVITLKMVGFDeekaeEILDKYpDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190
....*....|....*....|....*....|...
gi 1985402263 598 CTSAVS----VDVEGYIYSHCRKVGITLFTVSH 626
Cdd:TIGR03269 454 PTGTMDpitkVDVTHSILKAREEMEQTFIIVSH 486
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
460-659 |
2.86e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.24 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 460 LNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGC-------LTKPE----RGKLFYVPQRPymtlgtlrDQVIYPD 528
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKvkidgelLTAENvwnlRRKIGMVFQNP--------DNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 529 TVEDQRKKGISDQVL---------KEYLDNVQLGQILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 599
Cdd:PRK13642 98 TVEDDVAFGMENQGIpreemikrvDEALLAVNMLDFKTREPA---------RLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 600 SAVS----VDVEGYIYSHCRKVGITLFTVSHRKSLWKHHDFYLHMDG------RGNYEFKKITEDTVEFG 659
Cdd:PRK13642 169 SMLDptgrQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAgeiikeAAPSELFATSEDMVEIG 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
450-600 |
3.12e-05 |
|
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: 47.60 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 450 TPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFG---------GCLTKPERGKLF-YVPQRPYMTLGT 519
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiqidgvswNSVTLQTWRKAFgVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 520 LRDQVIYPDTVEDQRKKGISDQV-LKEYLDNV--QLGQILErEGGWdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILD 596
Cdd:TIGR01271 1308 FRKNLDPYEQWSDEEIWKVAEEVgLKSVIEQFpdKLDFVLV-DGGY--------VLSNGHKQLMCLARSILSKAKILLLD 1378
|
....
gi 1985402263 597 ECTS 600
Cdd:TIGR01271 1379 EPSA 1382
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
572-635 |
3.80e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 3.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985402263 572 LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD----VEGYIYSHCRKVGITLFTVSHRKSLWKHHD 635
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHRIASIKRSD 1426
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
392-602 |
4.66e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 392 ITELMQVLKDLNrGRYQ---RTMISQHEKDGDRTQTIPLIpgtgEIINtdnlIKFDHvplaTPNGDILI-RDLNFEVRSG 467
Cdd:PTZ00265 345 ITEYMKSLEATN-SLYEiinRKPLVENNDDGKKLKDIKKI----QFKN----VRFHY----DTRKDVEIyKDLNFTLTEG 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 468 ANVLICGPNGCGKSSLFRVLGELW-PLFGGCLT-----------KPERGKLFYVPQRPYMTLGTLRDQVIYP-------D 528
Cdd:PTZ00265 412 KTYAFVGESGCGKSTILKLIERLYdPTEGDIIIndshnlkdinlKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlE 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 529 TVEDQRKKGISDQ----------------VLKEYLDNVQLGQILEREGGWDSVQDW--MDV------------------- 571
Cdd:PTZ00265 492 ALSNYYNEDGNDSqenknkrnscrakcagDLNDMSNTTDSNELIEMRKNYQTIKDSevVDVskkvlihdfvsalpdkyet 571
|
250 260 270
....*....|....*....|....*....|....*....
gi 1985402263 572 --------LSGGEKQRMAMARLFYHKPQFAILDECTSAV 602
Cdd:PTZ00265 572 lvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
438-600 |
4.95e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 44.85 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 438 DNLIKFDHVPLATPNGDILiRDLNFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGCLTKPE--RGK 505
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLL-KNVSGKAKPGELTAIMGPSGAGKSTLLNALagrrtglgvsGEV--LINGRPLDKRsfRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 506 LFYVPQrpymtlgtlrDQVIYPD-TVEdqrkkgisdqvlkEYLDNVQLgqilereggwdsvqdwMDVLSGGEKQRMAMAR 584
Cdd:cd03213 84 IGYVPQ----------DDILHPTlTVR-------------ETLMFAAK----------------LRGLSGGERKRVSIAL 124
|
170
....*....|....*.
gi 1985402263 585 LFYHKPQFAILDECTS 600
Cdd:cd03213 125 ELVSNPSLLFLDEPTS 140
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
457-496 |
5.11e-05 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 45.22 E-value: 5.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG 496
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG 77
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
537-639 |
8.23e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.96 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 537 GISDQVLKE----YLDNVQlgqILEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYS 612
Cdd:PRK10619 122 GLSKQEAREravkYLAKVG---IDERAQGKYPVH-----LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR 193
|
90 100 110
....*....|....*....|....*....|...
gi 1985402263 613 HCRKV---GITLFTVSHRKSLWKH---HDFYLH 639
Cdd:PRK10619 194 IMQQLaeeGKTMVVVTHEMGFARHvssHVIFLH 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
452-629 |
1.07e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 44.36 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGCL---------TKPERGK----------------- 505
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtARSLSQQkglirqlrqhvgfvfqn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 506 --LFyvPQRpymtlgTLRDQVIYPDTVEDQRKKGISDQVLKEYLDNVQLgqilerEGGWDSvqdWMDVLSGGEKQRMAMA 583
Cdd:PRK11264 94 fnLF--PHR------TVLENIIEGPVIVKGEPKEEATARARELLAKVGL------AGKETS---YPRRLSGGQQQRVAIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1985402263 584 RLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVG---ITLFTVSHRKS 629
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqekRTMVIVTHEMS 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
457-603 |
1.15e-04 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 44.03 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGC-------LTKPE--RGKLFYVPQrpymtlgtlrDQVIY 526
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLtGELRPTSGTAyingysiRTDRKaaRQSLGYCPQ----------FDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 527 PD-TVEDQ-----RKKGIS----DQVLKEYLDNVQLGQILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFAILD 596
Cdd:cd03263 88 DElTVREHlrfyaRLKGLPkseiKEEVELLLRVLGLTDKANKR-----ART----LSGGMKRKLSLAIALIGGPSVLLLD 158
|
....*..
gi 1985402263 597 ECTSAVS 603
Cdd:cd03263 159 EPTSGLD 165
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
441-627 |
1.23e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLA-TPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggclTKPERGK-------------- 505
Cdd:PLN03130 1238 IKFEDVVLRyRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI--------VELERGRilidgcdiskfglm 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 506 -----LFYVPQRPYMTLGTLRDQViypDTVEDQrkkgiSDQVLKEYLDNVQLGQILEREG-GWDS-VQDWMDVLSGGEKQ 578
Cdd:PLN03130 1310 dlrkvLGIIPQAPVLFSGTVRFNL---DPFNEH-----NDADLWESLERAHLKDVIRRNSlGLDAeVSEAGENFSVGQRQ 1381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1985402263 579 RMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRK--VGITLFTVSHR 627
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREefKSCTMLIIAHR 1432
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
458-505 |
1.46e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.92 E-value: 1.46e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1985402263 458 RDLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfGgcLTKPERGK 505
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIA------G--ILEPTSGR 82
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
459-604 |
2.36e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 44.29 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 459 DLNFEVRSGANVLICGPNGCGKSSLFRVL-------GELWplFGG----CLT----KPERGKLFYVPQRPY------MTL 517
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALlrlipseGEIR--FDGqdldGLSrralRPLRRRMQVVFQDPFgslsprMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 518 GtlrdQVI-------YPDTVEDQRKKGIsDQVLKEyldnVQL-GQILER---EggwdsvqdwmdvLSGGEKQRMAMARLF 586
Cdd:COG4172 382 G----QIIaeglrvhGPGLSAAERRARV-AEALEE----VGLdPAARHRyphE------------FSGGQRQRIAIARAL 440
|
170 180
....*....|....*....|
gi 1985402263 587 YHKPQFAILDECTSA--VSV 604
Cdd:COG4172 441 ILEPKLLVLDEPTSAldVSV 460
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
432-597 |
4.31e-04 |
|
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: 42.53 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 432 GEIINTDNLIKFdhvplaTPNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFG---------GCLTKPE 502
Cdd:cd03289 1 GQMTVKDLTAKY------TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGdiqidgvswNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 503 RGKLF-YVPQRPYMTLGTLRDQVIYPDTVEDQRKKGISDQV-LKEYLDNV--QLGQILErEGGWdsvqdwmdVLSGGEKQ 578
Cdd:cd03289 75 WRKAFgVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVgLKSVIEQFpgQLDFVLV-DGGC--------VLSHGHKQ 145
|
170
....*....|....*....
gi 1985402263 579 RMAMARLFYHKPQFAILDE 597
Cdd:cd03289 146 LMCLARSVLSKAKILLLDE 164
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
451-597 |
6.52e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.52 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 451 PNGDILIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGCLT---KP-ERGkLFYVPQR----PY 514
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagleritsGEIW--IGGRVVnelEPaDRD-IAMVFQNyalyPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 515 MTL-----------GTLRDQViypdtveDQRkkgisdqvLKEYLDNVQLGQILER---EggwdsvqdwmdvLSGGEKQRM 580
Cdd:PRK11650 91 MSVrenmayglkirGMPKAEI-------EER--------VAEAARILELEPLLDRkprE------------LSGGQRQRV 143
|
170
....*....|....*..
gi 1985402263 581 AMARLFYHKPQFAILDE 597
Cdd:PRK11650 144 AMGRAIVREPAVFLFDE 160
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
547-630 |
7.62e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 41.69 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 547 LDNVQLGQILEREGGWDSVQDWMDVL----------------SGGEKQRMAMARLFYHKPQFAILDECTSAVS------- 603
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLeqlglgkrldhlpaqlSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqtgdki 185
|
90 100
....*....|....*....|....*..
gi 1985402263 604 VDVegyIYSHCRKVGITLFTVSHRKSL 630
Cdd:PRK10584 186 ADL---LFSLNREHGTTLILVTHDLQL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
457-597 |
1.86e-03 |
|
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: 40.41 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELwplfggcltKPERGKLFYVPQRpymtLGTLRDQVIYpdtvedqrK 535
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFY---------RPTSGRILFDGRD----ITGLPPHRIA--------R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 536 KGISD--QVLKEY-----LDNVQLGQILEREGGW------------------DSVQDWMDV-------------LSGGEK 577
Cdd:COG0411 79 LGIARtfQNPRLFpeltvLENVLVAAHARLGRGLlaallrlprarreerearERAEELLERvgladradepagnLSYGQQ 158
|
170 180
....*....|....*....|
gi 1985402263 578 QRMAMARLFYHKPQFAILDE 597
Cdd:COG0411 159 RRLEIARALATEPKLLLLDE 178
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
460-626 |
1.92e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.85 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 460 LNFEVRSGANVLicGPNGCGKSSLFRVLGELWPLFGGCLTKPErgklfyvpqrpyMTLGTlRDQVIYPDTVEDQRKKGIS 539
Cdd:PRK14271 42 MGFPARAVTSLM--GPTGSGKTTFLRTLNRMNDKVSGYRYSGD------------VLLGG-RSIFNYRDVLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 540 DQVLKEY----LDNVQLG----QILERE-------------GGWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAI 594
Cdd:PRK14271 107 FQRPNPFpmsiMDNVLAGvrahKLVPRKefrgvaqarltevGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190
....*....|....*....|....*....|....
gi 1985402263 595 LDECTSAVSVDVEGYIYSHCRKVG--ITLFTVSH 626
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLAdrLTVIIVTH 220
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
569-616 |
2.18e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 40.25 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1985402263 569 MDVLSGGEKQRMAMARLF----YHKPQFAILDECTSA---VSVD-VEGYIYSHCRK 616
Cdd:cd03275 153 MDNLSGGEKTMAALALLFaihsYQPAPFFVLDEVDAAldnTNVGkVASYIREQAGP 208
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
441-601 |
4.67e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.78 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 441 IKFDHVPLATPNGDILI---RDLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggCLTKPERGKLFyVPQRPYMTL 517
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCIN--------LLERPTSGRVL-VDGQDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 518 GT--LR----------------------DQVIYPDTVEDQRKKGISDQVLkEYLDNVQLgqilereggwdsvQDWMDV-- 571
Cdd:PRK11153 73 SEkeLRkarrqigmifqhfnllssrtvfDNVALPLELAGTPKAEIKARVT-ELLELVGL-------------SDKADRyp 138
|
170 180 190
....*....|....*....|....*....|..
gi 1985402263 572 --LSGGEKQRMAMARLFYHKPQFAILDECTSA 601
Cdd:PRK11153 139 aqLSGGQKQRVAIARALASNPKVLLCDEATSA 170
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
457-484 |
6.73e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 6.73e-03
10 20
....*....|....*....|....*...
gi 1985402263 457 IRDLNFEVRSGANvLICGPNGCGKSSLF 484
Cdd:pfam13476 9 FRDQTIDFSKGLT-LITGPNGSGKTTIL 35
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
457-602 |
7.53e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 39.25 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 457 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggclTKPERGKLFyvpqrpymtLGTLRDQVIYPDTVEDQRKK 536
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL--------IEPTRGQVL---------IDGVDIAKISDAELREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 537 GISdQVLKEY--------LDNVQLGQIL-------EREGGWDSVQD---------WMDVLSGGEKQRMAMARLFYHKPQF 592
Cdd:PRK10070 107 KIA-MVFQSFalmphmtvLDNTAFGMELaginaeeRREKALDALRQvglenyahsYPDELSGGMRQRVGLARALAINPDI 185
|
170
....*....|
gi 1985402263 593 AILDECTSAV 602
Cdd:PRK10070 186 LLMDEAFSAL 195
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
457-487 |
9.03e-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: 38.83 E-value: 9.03e-03
10 20 30
....*....|....*....|....*....|.
gi 1985402263 457 IRDLNFEVRSGANVLIcGPNGCGKSSLFRVL 487
Cdd:COG3593 14 IKDLSIELSDDLTVLV-GENNSGKSSILEAL 43
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
452-576 |
9.11e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.41 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985402263 452 NGDILIRDLNfevrsganvLICGPNGCGKSSLFRVLGELwplfggcltkpERGKLFYVP-QRpymtLGTLRdqvIYPDTV 530
Cdd:COG4938 14 EAELELKPLT---------LLIGPNGSGKSTLIQALLLL-----------LQSNFIYLPaER----SGPAR---LYPSLV 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1985402263 531 EDQRKKGISDQVLKEYLDNVQLGQIL--EREGGWDSVQDWMDVLSGGE 576
Cdd:COG4938 67 RELSDLGSRGEYTADFLAELENLEILddKSKELLEQVEEWLEKIFPGK 114
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
457-488 |
9.19e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.76 E-value: 9.19e-03
10 20 30
....*....|....*....|....*....|..
gi 1985402263 457 IRDLNFEVrSGANVLIcGPNGCGKSSLFRVLG 488
Cdd:COG4637 13 LRDLELPL-GPLTVLI-GANGSGKSNLLDALR 42
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
572-611 |
9.78e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 38.83 E-value: 9.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1985402263 572 LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIY 611
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIY 435
|
|
| |
