|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-647 |
0e+00 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 1065.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 1 MAAFSKYLTARNSSL--------AGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEK----EGKKERAVVDKVFFSRLA 68
Cdd:TIGR00954 1 MAVLSKYRLLRSTSNnktdkqdsPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKhstiEGAKKKAHVNGVFLGKLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 69 QILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLN 148
Cdd:TIGR00954 81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 149 ELKLCFRVRLTKYLYEEYLQSFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQ 228
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 229 GPASMMAYLVVSGLFLTRLRRPIGRMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFIL 308
Cdd:TIGR00954 241 GPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 309 FRFSMGFIDNIIAKYLATVVGYLVVSRPFLDLSHPRHLKSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFT 388
Cdd:TIGR00954 321 FRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 389 ARITELMQVLKDLNHGKYERTMVSQQEKGIEGVQVIPLIPGAGEIIIADNIIKFDHVPLATPNGDILIRDLNFEVQSGAN 468
Cdd:TIGR00954 401 ARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 469 VLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKGISDLVLKEYLDN 548
Cdd:TIGR00954 481 LLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 549 VQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKS 628
Cdd:TIGR00954 561 VQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKS 640
|
650
....*....|....*....
gi 966918915 629 LWKHHEYYLHMDGRGNYEF 647
Cdd:TIGR00954 641 LWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
70-338 |
3.61e-123 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 366.17 E-value: 3.61e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 70 ILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLNE 149
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 150 LKLCFRVRLTKYLYEEYLQSFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQG 229
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 230 PASMMAYLVVSGLFLTRLRRPIGRMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFILF 309
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 966918915 310 RFSMGFIDNIIAKYLATVVGYLVVSRPFL 338
Cdd:pfam06472 241 RLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
84-648 |
1.75e-97 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 310.59 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 84 GYLVLIAVMLVSRTYCDVWMI-QNGTLIESgIIGRSRKDFKRYLLNF---IAAMPLISLVNNFLKYGLnELKLcfRVRLT 159
Cdd:COG4178 25 GLLALLLLLTLASVGLNVLLNfWNRDFYDA-LQARDAAAFWQQLGVFallAAISILLAVYQTYLRQRL-QIRW--REWLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 160 KYLYEEYLQSFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQG---------- 229
Cdd:COG4178 101 ERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLISFIGILWSLSGSLTftlggysiti 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 230 PASMM----AYLVVSGLFLTRLRRPIGRMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHN 305
Cdd:COG4178 181 PGYMVwaalIYAIIGTLLTHLIGRPLIRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 306 FILFRFSMGFIDNIIAkYLATVVGYLVVSrpfldlshPRhlksthselledyYQSGRMLL-----------RMSQALGRI 374
Cdd:COG4178 261 LIRRQRNLTFFTTGYG-QLAVIFPILVAA--------PR-------------YFAGEITLgglmqaasafgQVQGALSWF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 375 VlagREMTRLAGFTA---RITELMQVLKDlnhgkyertmVSQQEKGIEGVqviplipgageIIIADNIIKFDHVPLATPN 451
Cdd:COG4178 319 V---DNYQSLAEWRAtvdRLAGFEEALEA----------ADALPEAASRI-----------ETSEDGALALEDLTLRTPD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 452 GDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGRED 531
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 532 qkrkgISDLVLKEYLDNVQLGHILEReggWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYS 611
Cdd:COG4178 455 -----FSDAELREALEAVGLGHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
570 580 590
....*....|....*....|....*....|....*....
gi 966918915 612 HCRK--VGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFK 648
Cdd:COG4178 527 LLREelPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLL 565
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
440-645 |
1.14e-86 |
|
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: 268.25 E-value: 1.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTL 519
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 520 RDQVIYPdgredqkrkgisdlvlkeyldnvqlghilereggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:cd03223 81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 966918915 600 AVSVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNY 645
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
440-625 |
1.74e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.99 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILiRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFYV 508
Cdd:COG4619 1 LELEGLSFRVGGKPIL-SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsamPPPewRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 509 PQRPYMTLGTLRDQVIYPDGREDQKrkgISDLVLKEYLDNVQLGH-ILEREggwdsVQDwmdvLSGGEKQRMAMARLFYH 587
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERK---FDRERALELLERLGLPPdILDKP-----VER----LSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 966918915 588 KPQFAILDECTSA---VSVD-VEGYIYSHCRKVGITLFTVSH 625
Cdd:COG4619 148 QPDVLLLDEPTSAldpENTRrVEELLREYLAEEGRAVLWVSH 189
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
84-626 |
3.75e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 119.50 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 84 GYLVLIAVMLVSRTYCDVWMIQ-NGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLNelKLCFRV--RLTK 160
Cdd:COG1132 21 GLLILALLLLLLSALLELLLPLlLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLA--RLAQRVvaDLRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 161 YLYEEYL-QSFTYY---KMGNLDNRIanpdqllTQDVekfcNSVVDLYSNLskpFLDIVLYIFKLTSAIGaqgpasMMAY 236
Cdd:COG1132 99 DLFEHLLrLPLSFFdrrRTGDLLSRL-------TNDV----DAVEQFLAHG---LPQLVRSVVTLIGALV------VLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 237 L------------VVSGLFLTRLRRPIGRMTITEQKYEGEyryVNSRL---ITNSEEIAFYNGNKREKQTVHSVFRKLVE 301
Cdd:COG1132 159 IdwrlalivllvlPLLLLVLRLFGRRLRKLFRRVQEALAE---LNGRLqesLSGIRVVKAFGREERELERFREANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 302 HLHNFI----LFRFSMGFIDNIIAkYLATVVGYLVVSRPFLDLShprhlksthsELLEdYYQSGRMLLRMSQALGRIVla 377
Cdd:COG1132 236 ANLRAArlsaLFFPLMELLGNLGL-ALVLLVGGLLVLSGSLTVG----------DLVA-FILYLLRLFGPLRQLANVL-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 378 gREMTRLAGFTARITELMqvlkdlnhgkyertmvSQQEKGIEGVQVIPLIPGAGEIiiadniiKFDHVPLATPNGDILIR 457
Cdd:COG1132 302 -NQLQRALASAERIFELL----------------DEPPEIPDPPGAVPLPPVRGEI-------EFENVSFSYPGDRPVLK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 458 DLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFYVPQRPYMTLGTLRDQVIYp 526
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdirdlTLEslRRQIGVVPQDTFLFSGTIRENIRY- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 527 dGREDqkrkgISDLVLKEYLDNVQLGHILER-EGGWDSVqdwmdV------LSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:COG1132 437 -GRPD-----ATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGGQRQRIAIARALLKDPPILILDEATS 505
|
570 580
....*....|....*....|....*....
gi 966918915 600 AVSVDVEGYIYSHCRKV--GITLFTVSHR 626
Cdd:COG1132 506 ALDTETEALIQEALERLmkGRTTIVIAHR 534
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
455-641 |
1.48e-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: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFR-VLGELWPLfGGRLTKPerGKLFYVPQRPYMTLGTLRDQVIYpdGRE-DQ 532
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKL-SGSVSVP--GSIAYVSQEPWIQNGTIRENILF--GKPfDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 533 KR--KGIS------DLVLKEYLDNVQLGhilerEGGwdsvqdwmdV-LSGGEKQRMAMARLFYHKPQFAILDECTSAVSV 603
Cdd:cd03250 95 ERyeKVIKacalepDLEILPDGDLTEIG-----EKG---------InLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 966918915 604 DVEGYIYSHC----RKVGITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:cd03250 161 HVGRHIFENCilglLLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
440-629 |
4.30e-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: 102.08 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILI-RDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFY 507
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdlDLEslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 508 VPQRPYMTLGTLRDqviypdgredqkrkgisdlvlkeyldNVqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYH 587
Cdd:cd03228 81 VPQDPFLFSGTIRE--------------------------NI---------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 966918915 588 KPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSL 629
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALakGKTVIVIAHRLST 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
440-641 |
9.23e-24 |
|
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: 105.61 E-value: 9.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFYV 508
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdlDPAswRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 509 PQRPYMTLGTLRDQV-IY-PDGREDQkrkgisdlvLKEYLDNVQLGHILER-EGGWDSVqdwmdV------LSGGEKQRM 579
Cdd:COG4988 417 PQNPYLFAGTIRENLrLGrPDASDEE---------LEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966918915 580 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDD 546
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
371-629 |
2.22e-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: 101.21 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 371 LGRIVLAGReMTRLAGFTARI--TELMQVLKDLN---HGKYERTMVSQQEKGIEGVQVIPLiPGAGEIIIADNI-IKFDH 444
Cdd:TIGR02857 249 IGFRLLAGD-LDLATGLFVLLlaPEFYLPLRQLGaqyHARADGVAAAEALFAVLDAAPRPL-AGKAPVTAAPASsLEFSG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 445 VPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL-----------TKPERGKLFYVPQRPY 513
Cdd:TIGR02857 327 VSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadADSWRDQIAWVPQHPF 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 514 MTLGTLRDQVIYpdgredqKRKGISDLVLKEYLDNVQLGHIL-EREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQF 591
Cdd:TIGR02857 407 LFAGTIAENIRL-------ARPDASDAEIREALERAGLDEFVaALPQGLDTpIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 966918915 592 AILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSL 629
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
428-626 |
8.65e-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: 99.84 E-value: 8.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 428 PGAGEIIIADNIIKFDHVPLATPNGD-ILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-------- 498
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrd 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 499 KPE---RGKLFYVPQRPYMTLGTLRD--QVIYPDGREDQkrkgisdlvLKEYLDNVQLGHILER-EGGWDSvqdWMDV-- 570
Cdd:COG4987 402 LDEddlRRRIAVVPQRPHLFDTTLREnlRLARPDATDEE---------LWAALERVGLGDWLAAlPDGLDT---WLGEgg 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966918915 571 --LSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVE------GYIYSHCRkvGITLFTVSHR 626
Cdd:COG4987 470 rrLSGGERRRLALARALLRDAPILLLDEPTE--GLDAAteqallADLLEALA--GRTVLLITHR 529
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
456-599 |
3.90e-21 |
|
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: 90.01 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLTKPE----RGKLFYVPQ--RPYMTLgTLRDQ 522
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPtegtilLDGQDLTDDErkslRKEIGYVFQdpQLFPRL-TVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966918915 523 VIYPDGREDQKRKGISDlVLKEYLDNVQLGHILEReggwdSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:pfam00005 80 LRLGLLLKGLSKREKDA-RAEEALEKLGLGDLADR-----PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
451-642 |
2.73e-20 |
|
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: 89.51 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFR-VLGELWPLFG-----GRLTKPERGKLFYVPQRPY----------- 513
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPTSGsirvfGKPLEKERKRIGYVPQRRSidrdfpisvrd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 514 -MTLGTLRDQVIYPDGREDQKRKgisdlvLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFA 592
Cdd:cd03235 90 vVLMGLYGHKGLFRRLSKADKAK------VDEALERVGLSELADRQ---------IGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 966918915 593 ILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSH-RKSLWKHHEYYLHMDGR 642
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELrreGMTILVVTHdLGLVLEYFDRVLLLNRT 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
440-628 |
9.44e-20 |
|
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: 88.44 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFYV 508
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 509 PQRPYMTLGTLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLGHILER-EGGWDS-VQDWMDVLSGGEKQRMAMARLFY 586
Cdd:cd03254 83 LQDTFLFSGTIMENIRL--GRPN-----ATDEEVIEAAKEAGAHDFIMKlPNGYDTvLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 966918915 587 HKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKS 628
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLS 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
440-628 |
9.62e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 88.83 E-value: 9.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFYV 508
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 509 PQRPYMTLGTLRDQVIY--PDGREDQ-----KRKGISDLvlkeyldnvqlghILEREGGWDSVqdwmdV------LSGGE 575
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYgrPDATDEEvieaaKAAQIHDK-------------IMRFPDGYDTI-----VgerglkLSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 966918915 576 KQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKS 628
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
451-625 |
1.89e-19 |
|
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: 88.18 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGR----LTKPERGKLF-YVPQRPYMTLG-T 518
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALaGLLKPssgevLLDGRdlasLSRRELARRIaYVPQEPPAPFGlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 519 LRDQVI---YP-------DGREDQKrkgisdlVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHK 588
Cdd:COG1120 92 VRELVAlgrYPhlglfgrPSAEDRE-------AVEEALERTGLEHLADRP---------VDELSGGERQRVLIARALAQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 966918915 589 PQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:COG1120 156 PPLLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLH 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
440-646 |
2.06e-19 |
|
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: 92.59 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLA-TPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLF------------ 506
Cdd:COG2274 474 IELENVSFRyPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL--------LGLYEPTSGRILidgidlrqidpa 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 507 -------YVPQRPYMTLGTLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLGH-ILEREGGWDS-VQDWMDVLSGGEKQ 577
Cdd:COG2274 546 slrrqigVVLQDVFLFSGTIRENITL--GDPD-----ATDEEIIEAARLAGLHDfIEALPMGYDTvVGEGGSNLSGGQRQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966918915 578 RMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG-----RGNYE 646
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDKgriveDGTHE 694
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
451-626 |
3.01e-19 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 84.99 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLFYvpqrpymtlgtlrdqviypDGre 530
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAI--------AGLLKPTSGEILI-------------------DG-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 531 dqkrKGISDLVLKEYLDNVQLGHilereggwdsvQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD----VE 606
Cdd:cd00267 61 ----KDIAKLPLEELRRRIGYVP-----------Q-----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAsrerLL 120
|
170 180
....*....|....*....|
gi 966918915 607 GYIYSHCRKvGITLFTVSHR 626
Cdd:cd00267 121 ELLRELAEE-GRTVIIVTHD 139
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
451-625 |
7.39e-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: 7.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPE---RGKLFYVPQRP--YMTLg 517
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILagllppsaGEVL-WNGEPIRDARedyRRRLAYLGHADglKPEL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 518 TLRDQVIYpdgreDQKRKG--ISDLVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:COG4133 91 TVRENLRF-----WAALYGlrADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....
gi 966918915 596 ECTSAVSVD----VEGYIYSHCRKVGITLFTvSH 625
Cdd:COG4133 157 EPFTALDAAgvalLAELIAAHLARGGAVLLT-TH 189
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
436-625 |
3.35e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 84.37 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 436 ADNIIKFDHVPLATpNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRV-LGELWPL-----FGGRLTKPERGKLFYVP 509
Cdd:COG1121 3 MMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAiLGLLPPTsgtvrLFGKPPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 510 QRPYMTLG---TLRDQV---IYPD-------GREDQKRkgisdlvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEK 576
Cdd:COG1121 82 QRAEVDWDfpiTVRDVVlmgRYGRrglfrrpSRADREA-------VDEALERVGLEDLADR---------PIGELSGGQQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 966918915 577 QRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYS---HCRKVGITLFTVSH 625
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTH 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
437-641 |
4.33e-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: 83.67 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 437 DNIIKFDHVPLATPN-GDILI-RDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---KP--------ERG 503
Cdd:cd03248 9 KGIVKFQNVTFAYPTrPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPisqyehkyLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 504 KLFYVPQRPYMTLGTLRDQVIYpdgredqkrkGISDLVLKEYLDNVQLGH----ILEREGGWDS-VQDWMDVLSGGEKQR 578
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAY----------GLQSCSFECVKEAAQKAHahsfISELASGYDTeVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966918915 579 MAMARLFYHKPQFAILDECTSAVSVDVEGYIYS--HCRKVGITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
455-629 |
6.18e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 81.88 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTkpergkLFYVPQRPYmTLGTLRDQVIYpdgredqkr 534
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR------LDGADISQW-DPNELGDHVGY--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 535 kgisdlvlkeYLDNVQL--GHILEreggwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYS- 611
Cdd:cd03246 81 ----------LPQDDELfsGSIAE------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQa 138
|
170 180
....*....|....*....|
gi 966918915 612 --HCRKVGITLFTVSHRKSL 629
Cdd:cd03246 139 iaALKAAGATRIVIAHRPET 158
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
441-640 |
9.88e-18 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 82.13 E-value: 9.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 441 KFDHVPLATPNGD-ILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWPLFG-----GRLTKPE-----RGKLFYV 508
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnGLLGPTSGevlvdGKDLTKLslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 509 PQRPymtlgtlRDQVIYPDGRED----QKRKGIS----DLVLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMA 580
Cdd:cd03225 81 FQNP-------DDQFFGPTVEEEvafgLENLGLPeeeiEERVEEALELVGLEGLRDR-----SPFT----LSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966918915 581 MARLFYHKPQFAILDECTSavSVDVEGY-----IYSHCRKVGITLFTVSHRKSLWKHH-EYYLHMD 640
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTA--GLDPAGRrelleLLKKLKAEGKTIIIVTHDLDLLLELaDRVIVLE 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
440-629 |
1.67e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 81.87 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDIL-IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLF------------ 506
Cdd:cd03245 3 IEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLA--------GLYKPTSGSVLldgtdirqldpa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 507 -------YVPQRPYMTLGTLRDQVIYPDGREDQKR-------KGISDLVLKEYL-DNVQLGhilerEGGwdsvqdwmDVL 571
Cdd:cd03245 75 dlrrnigYVPQDVTLFYGTLRDNITLGAPLADDERilraaelAGVTDFVNKHPNgLDLQIG-----ERG--------RGL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 572 SGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSL 629
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
451-625 |
4.95e-17 |
|
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: 79.40 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKlfyvpqrpymtlgtlrdqvIYPDGR- 529
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA--------GLLKPSSGE-------------------ILLDGKd 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 530 -EDQKRKGISDLV--LKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAV----S 602
Cdd:cd03214 63 lASLSPKELARKIayVPQALELLGLAHLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLdiahQ 133
|
170 180
....*....|....*....|...
gi 966918915 603 VDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLH 156
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
440-626 |
5.44e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 80.23 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLA-TPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFY 507
Cdd:cd03244 3 IEFKNVSLRyRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiglHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 508 VPQRPYMTLGTLRDQV----IYPDGRedqkrkgisdlvLKEYLDNVQL-GHILEREGGWDS-VQDWMDVLSGGEKQRMAM 581
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdpfgEYSDEE------------LWQALERVGLkEFVESLPGGLDTvVEEGGENLSVGQRQLLCL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 966918915 582 ARLFYHKPQFAILDECTSavSVDVEG------YIYSHCRkvGITLFTVSHR 626
Cdd:cd03244 151 ARALLRKSKILVLDEATA--SVDPETdaliqkTIREAFK--DCTVLTIAHR 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
452-596 |
6.72e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 452 GDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELwPLFGGRLTKPERGKLFYVPQRPYMTLG-TLRDQVIYPDGR 529
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILaGEL-EPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLDGDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 530 EDQKRK---------GISDLVLKEYLDnvqLGHILEREGGWD--------------SVQDW---MDVLSGGEKQRMAMAR 583
Cdd:COG0488 89 LRALEAeleeleaklAEPDEDLERLAE---LQEEFEALGGWEaearaeeilsglgfPEEDLdrpVSELSGGWRRRVALAR 165
|
170
....*....|...
gi 966918915 584 LFYHKPQFAILDE 596
Cdd:COG0488 166 ALLSEPDLLLLDE 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
451-625 |
1.05e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 79.53 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRltkPERGKLFY---------------------VP 509
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA---PDEGEVLLdgkdiydldvdvlelrrrvgmVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 510 QRPYMTLGTLRDQVIYPDG-REDQKRKGISDLVLKeyldnvqlghILEREGGWDSVQDWMDV--LSGGEKQRMAMARLFY 586
Cdd:cd03260 88 QKPNPFPGSIYDNVAYGLRlHGIKLKEELDERVEE----------ALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 966918915 587 HKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLftVSH 625
Cdd:cd03260 158 NEPEVLLLDEPTSALdpisTAKIEELIAELKKEYTIVI--VTH 198
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
436-644 |
1.48e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 79.37 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 436 ADNIIKFDHVPLATpNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWP------LFGGR---LTKPE--RGK 504
Cdd:PRK10247 4 NSPLLQLQNVGYLA-GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISptsgtlLFEGEdisTLKPEiyRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 505 LFYVPQRPYMTLGTLRDQVIYP---DGREDQKRKGISDLVLKEyLDNvqlgHILEReggwdSVQDwmdvLSGGEKQRMAM 581
Cdd:PRK10247 83 VSYCAQTPTLFGDTVYDNLIFPwqiRNQQPDPAIFLDDLERFA-LPD----TILTK-----NIAE----LSGGEKQRISL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966918915 582 ARLFYHKPQFAILDECTSAVSVD----VEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGN 644
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAG 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
440-628 |
4.69e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 77.97 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPN--GDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLF 506
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvdirdlnlRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 507 YVPQRPYMTLGTLRDQVIYpdGREDQKRKGISDLVLKEYLDNVqlghILEREGGWDSV------QdwmdvLSGGEKQRMA 580
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRY--GKPDATDEEVEEAAKKANIHDF----IMSLPDGYDTLvgergsQ-----LSGGQKQRIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 966918915 581 MARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKS 628
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAHRLS 199
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
457-625 |
5.20e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 77.92 E-value: 5.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 457 RDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRLTKPERGKLFY-----VPQRPYMTL---GTLR 520
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALaglerpwsGEV--TFDGRPVTRRRRKAFRrrvqmVFQDPYASLhprHTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 521 DQVIYP---DGREDQKRKgisdlvLKEYLDNVQLG-HILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:COG1124 100 RILAEPlriHGLPDREER------IAELLEQVGLPpSFLDR---------YPHQLSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190
....*....|....*....|....*....|...
gi 966918915 597 CTSA--VSVDVE--GYIYSHCRKVGITLFTVSH 625
Cdd:COG1124 165 PTSAldVSVQAEilNLLKDLREERGLTYLFVSH 197
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
440-641 |
6.27e-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: 77.53 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLA-TPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGR---------LTKPE--RGKLFY 507
Cdd:cd03252 1 ITFEHVRFRyKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlvdghdlaLADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 508 VPQRPYMTLGTLRDQVIYPDGREDQKRKgisdlvlkEYLDNVQLGH--ILEREGGWDSVQDWMDV-LSGGEKQRMAMARL 584
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERV--------IEAAKLAGAHdfISELPEGYDTIVGEQGAgLSGGQRQRIAIARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 966918915 585 FYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
440-599 |
8.80e-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: 76.99 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRLTKPERGKLF----- 506
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsGEV--LVDGKDITKKNLRELrrkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 507 YVPQRPymtlgtlRDQVIYPDGRED---------QKRKGISDLVlKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQ 577
Cdd:COG1122 79 LVFQNP-------DDQLFAPTVEEDvafgpenlgLPREEIRERV-EEALELVGLEHLADR-----PPHE----LSGGQKQ 141
|
170 180
....*....|....*....|..
gi 966918915 578 RMAMARLFYHKPQFAILDECTS 599
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTA 163
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
440-642 |
1.45e-15 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 75.99 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDI---LIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------KPERGKLF-- 506
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdiskLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 507 -----YVPQR----PYMTLgtlRDQVIYP---DGREDQKRKgisdLVLKEYLDNVQLGHILEREGGWdsvqdwmdvLSGG 574
Cdd:cd03255 81 rrhigFVFQSfnllPDLTA---LENVELPlllAGVPKKERR----ERAEELLERVGLGDRLNHYPSE---------LSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966918915 575 EKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHM-DGR 642
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELrDGK 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
451-625 |
1.55e-15 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 74.92 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLFyvpqrpymtlgtLRDQVIYPDGRE 530
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCI--------AGLEEPDSGSIL------------IDGEDLTDLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 531 DQKRKGISDLVLKEY--------LDNVQLGhilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSA-- 600
Cdd:cd03229 71 LPPLRRRIGMVFQDFalfphltvLENIALG------------------LSGGQQQRVALARALAMDPDVLLLDEPTSAld 132
|
170 180
....*....|....*....|....*..
gi 966918915 601 --VSVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03229 133 piTRREVRALLKSLQAQLGITVVLVTH 159
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
440-628 |
1.68e-15 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 76.50 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILI-RDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFY 507
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 508 VPQRPYMTLGTLRDQVIYpdGREDQKRKGISDLVLKEYLDNVqlghILEREGGWDSVQDWMDV-LSGGEKQRMAMARLFY 586
Cdd:cd03251 81 VSQDVFLFNDTVAENIAY--GRPGATREEVEEAARAANAHEF----IMELPEGYDTVIGERGVkLSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 966918915 587 HKPQFAILDECTSAVSVDVEGYIYSHCRK--VGITLFTVSHRKS 628
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERlmKNRTTFVIAHRLS 198
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
443-629 |
3.03e-15 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 79.02 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 443 DHVPLATPNGDI---------------LIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGG--RL-------- 497
Cdd:COG4618 320 ERMPLPRPKGRLsvenltvvppgskrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvRLdgadlsqw 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 498 TKPERGKLF-YVPQRPymTL--GTLRdQVI--YPDGREDQ-----KRKGISDLVLK---EYldNVQLGhilerEGGwdsv 564
Cdd:COG4618 400 DREELGRHIgYLPQDV--ELfdGTIA-ENIarFGDADPEKvvaaaKLAGVHEMILRlpdGY--DTRIG-----EGG---- 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966918915 565 qdwmDVLSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVEG------YIySHCRKVGITLFTVSHRKSL 629
Cdd:COG4618 466 ----ARLSGGQRQRIGLARALYGDPRLVVLDEPNS--NLDDEGeaalaaAI-RALKARGATVVVITHRPSL 529
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
455-600 |
4.58e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 75.54 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLT--KPE-----RGKLfyvPQRPYMTLG-TL 519
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELTPssgevrLNGRPLAawSPWelarrRAVL---PQHSSLAFPfTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 520 RdQVI----YPDGREDQKRKGIsdlvLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMAMARLF-------YHK 588
Cdd:COG4559 93 E-EVValgrAPHGSSAAQDRQI----VREALALVGLAHLAGR-----SYQT----LSGGEQQRVQLARVLaqlwepvDGG 158
|
170
....*....|..
gi 966918915 589 PQFAILDECTSA 600
Cdd:COG4559 159 PRWLFLDEPTSA 170
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
440-629 |
4.95e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.61 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPN-GDILI-RDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLF 506
Cdd:TIGR00958 479 IEFQDVSFSYPNrPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgvplvqydhHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 507 YVPQRPYMTLGTLRDQVIYpdgredqkrkGISDLVLKEYLDNVQLGH----ILEREGGWDSVQDWMDV-LSGGEKQRMAM 581
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAY----------GLTDTPDEEIMAAAKAANahdfIMEFPNGYDTEVGEKGSqLSGGQKQRIAI 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 966918915 582 ARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKSL 629
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLST 676
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
369-626 |
6.18e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.79 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 369 QALGRIVLAGREMTRLAGFTARITELMQvlkdlnhGKYERTMVSQQEKGIEGVQVIPLipgageiiiadniiKFDHVPLA 448
Cdd:TIGR02868 285 EAFAALPAAAQQLTRVRAAAERIVEVLD-------AAGPVAEGSAPAAGAVGLGKPTL--------------ELRDLSAG 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 449 TPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFYVPQRPYMTLG 517
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvssldqDEVRRRVSVCAQDAHLFDT 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 518 TLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLG-HILEREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:TIGR02868 424 TVRENLRL--ARPD-----ATDEELWAALERVGLAdWLRALPDGLDTvLGEGGARLSGGERQRLALARALLADAPILLLD 496
|
250 260 270
....*....|....*....|....*....|...
gi 966918915 596 ECTSAVSVDVEGYIYSHCRKV--GITLFTVSHR 626
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAAlsGRTVVLITHH 529
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
425-618 |
6.23e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.86 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 425 PLIPGAGEIIIADNIIKFDhVPLATPNgdilIRDLNFEVQSGANVLICGPNGCGKSSLFR-VLGELWPLFGGRLTKpeRG 503
Cdd:PLN03232 607 PLQPGAPAISIKNGYFSWD-SKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI--RG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 504 KLFYVPQRPYMTLGTLRDQVIYPDGREDQKR-KGISDLVLKEYLDnVQLGHILErEGGWDSVQdwmdvLSGGEKQRMAMA 582
Cdd:PLN03232 680 SVAYVPQVSWIFNATVRENILFGSDFESERYwRAIDVTALQHDLD-LLPGRDLT-EIGERGVN-----ISGGQKQRVSMA 752
|
170 180 190
....*....|....*....|....*....|....*.
gi 966918915 583 RLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGI 618
Cdd:PLN03232 753 RAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDEL 788
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
437-626 |
1.17e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 76.87 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 437 DNIIKFDHVPLATPNGDI-LIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWP---------LFGGR----LTKPER 502
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRdlleLSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 503 GKLF-YVPQRPYMTL--GTLRDQVIYPDGREDQKRKGISDLVLkEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRM 579
Cdd:COG1123 82 GRRIgMVFQDPMTQLnpVTVGDQIAEALENLGLSRAEARARVL-ELLEAVGLERRLDR---------YPHQLSGGQRQRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 966918915 580 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSH----CRKVGITLFTVSHR 626
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLlrelQRERGTTVLLITHD 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
440-626 |
2.80e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.02 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNG-DILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTK-PE---RGKLF 506
Cdd:PRK11160 339 LTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtrawdpqqGEIL-LNGQPIADySEaalRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 507 YVPQRPYMTLGTLRDQVIYPDgredqkrKGISDLVLKEYLDNVQLGHILEREGGWDSvqdWMD----VLSGGEKQRMAMA 582
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAA-------PNASDEALIEVLQQVGLEKLLEDDKGLNA---WLGeggrQLSGGEQRRLGIA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 966918915 583 RLFYHKPQFAILDECTSAVSVDVEGYIYS----HCRkvGITLFTVSHR 626
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILEllaeHAQ--NKTVLMITHR 533
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
440-625 |
4.42e-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: 71.73 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDIL---IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPERGklfY 507
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgpGPDRG---Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 508 VPQR----PYMtlgTLRDQVIYPDGREDQKRKGISDLVLkEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMAR 583
Cdd:cd03293 78 VFQQdallPWL---TVLDNVALGLELQGVPKAEARERAE-ELLELVGLSGFENA---------YPHQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 966918915 584 LFYHKPQFAILDECTSAVSV----DVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTH 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
456-625 |
5.06e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 71.61 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWplFGGR----LTKPERGKL------FyVPQR----PY 513
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrptsGEVL--IDGQdissLSERELARLrrrhigF-VFQFfnllPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 514 MTLgtlRDQVIYP------DGREDQKRkgisdlvLKEYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMARL 584
Cdd:COG1136 101 LTA---LENVALPlllagvSRKERRER-------ARELLERVGLGDRLDHrpsQ------------LSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 966918915 585 FYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:COG1136 159 LVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTH 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
438-625 |
5.30e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 438 NIIKFDHVPLATPNGDILiRDLNFEVQSGANVLICGPNGCGKSSLFR-VLGELWPLfGGRLTKPERGKLFYVPQRPYMTl 516
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAPD-EGVIKRNGKLRIGYVPQKLYLD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 517 GTLRDQViypdGREDQKRKGISDLVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:PRK09544 80 TTLPLTV----NRFLRLRPGTKKEDILPALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|...
gi 966918915 597 CTSAVSVDVEGYIYSHC----RKVGITLFTVSH 625
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIdqlrRELDCAVLMVSH 179
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
456-625 |
6.36e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.02 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELwplfggrlTKPERGKLFyVPQRPymtLGTLRD--QVIYPDGREdqk 533
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL--------ETPSAGELL-AGTAP---LAEAREdtRLMFQDARL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 534 rkgisdLVLKEYLDNVQLG----------HILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVS- 602
Cdd:PRK11247 93 ------LPWKKVIDNVGLGlkgqwrdaalQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDa 166
|
170 180
....*....|....*....|....*.
gi 966918915 603 ---VDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK11247 167 ltrIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
451-620 |
6.74e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.06 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGklfyvpqrpyMTLGTLRDQVIY---PD 527
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----------IDDPDVAEACHYlghRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 528 G-------RED----QKRKGISDLVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLF-YHKPQFaILD 595
Cdd:PRK13539 83 AmkpaltvAENlefwAAFLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARLLvSNRPIW-ILD 152
|
170 180
....*....|....*....|....*....
gi 966918915 596 ECTSAVSVD----VEGYIYSHCRKVGITL 620
Cdd:PRK13539 153 EPTAALDAAavalFAELIRAHLAQGGIVI 181
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
452-596 |
6.78e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 452 GDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQ-RPYMTLG-TLRDQVIypDG 528
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPD-SGTVKLGETVKIGYFDQhQEELDPDkTVLDELR--DG 403
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966918915 529 REDQKRKGISDLvlkeyldnvqLGHILEREggwDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:COG0488 404 APGGTEQEVRGY----------LGRFLFSG---DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
436-596 |
6.88e-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: 72.04 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 436 ADNIIKFDHVPLA--TPNGDILI-RDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKP--ER 502
Cdd:COG1116 4 AAPALELRGVSKRfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptsGEVL-VDGKPVTGPgpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 503 GklfYVPQR----PYMTLgtlRDQVIYP---DGREDQKRKGISDlvlkEYLDNVQLGHILEReggwdsvqdWMDVLSGGE 575
Cdd:COG1116 83 G---VVFQEpallPWLTV---LDNVALGlelRGVPKAERRERAR----ELLELVGLAGFEDA---------YPHQLSGGM 143
|
170 180
....*....|....*....|.
gi 966918915 576 KQRMAMARLFYHKPQFAILDE 596
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDE 164
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
450-607 |
7.41e-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: 70.53 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 450 PNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPERGKLFYVPQRPYMTLGTLRDQV 523
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLnGLLRPqsgavLIDGEPLDYSRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 524 IYPDGRED----QKRKGISD----LVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:TIGR01166 82 FAADVDQDvafgPLNLGLSEaeveRRVREALTAVGASGLRERP---------THCLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170
....*....|..
gi 966918915 596 ECTSAvsVDVEG 607
Cdd:TIGR01166 153 EPTAG--LDPAG 162
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
451-625 |
8.42e-14 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 71.01 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGR-LTK--PERGKLFYVPQR----PYMt 515
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaglerpdsGEI--LIDGRdVTGvpPERRNIGMVFQDyalfPHL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 516 lgTLRDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:cd03259 88 --TVAENIAFGLKLRGVPKAEIRARV-RELLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 966918915 596 ECTSAvsVDVE------GYIYSHCRKVGITLFTVSH 625
Cdd:cd03259 156 EPLSA--LDAKlreelrEELKELQRELGITTIYVTH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
436-625 |
1.54e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 73.40 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 436 ADNIIKFDHV----PLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------------GELWPLFGGRL 497
Cdd:COG1123 257 AEPLLEVRNLskryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLlgllrptsgsilfdGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 498 TKPERGKLFYVPQRPYMTL---GTLRDQVIYP-DGREDQKRKGISDLVlKEYLDNVQLG-HILER---Eggwdsvqdwmd 569
Cdd:COG1123 337 LRELRRRVQMVFQDPYSSLnprMTVGDIIAEPlRLHGLLSRAERRERV-AELLERVGLPpDLADRyphE----------- 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 570 vLSGGEKQRMAMARLFYHKPQFAILDECTSA--VSV--DVEGYIYSHCRKVGITLFTVSH 625
Cdd:COG1123 405 -LSGGQRQRVAIARALALEPKLLILDEPTSAldVSVqaQILNLLRDLQRELGLTYLFISH 463
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
434-604 |
1.77e-13 |
|
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: 70.66 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 434 IIADNIIK-FDHVPLatpngdilIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLTKPE---R 502
Cdd:COG4555 2 IEVENLSKkYGKVPA--------LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLKPdsgsilIDGEDVRKEPreaR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 503 GKLFYVPQRPYMTLG-TLRDQV-----IYPDGREDQKRKgisdlvLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEK 576
Cdd:COG4555 74 RQIGVLPDERGLYDRlTVRENIryfaeLYGLFDEELKKR------IEELIELLGLEEFLDR-----RVGE----LSTGMK 138
|
170 180
....*....|....*....|....*...
gi 966918915 577 QRMAMARLFYHKPQFAILDECTSAVSVD 604
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVM 166
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
456-625 |
1.97e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 70.09 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPE---RGKLFYVPQRP--YMTLgTLRDQ 522
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlgllrptsGEVR-VLGEDVARDPaevRRRIGYVPQEPalYPDL-TVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 523 V-----IYPDGREDQKRKgisdlvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDEC 597
Cdd:COG1131 94 LrffarLYGLPRKEARER------IDELLELFGLTDAADR---------KVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190
....*....|....*....|....*....|....
gi 966918915 598 TSAvsVDVEG------YIYSHCRKvGITLFTVSH 625
Cdd:COG1131 159 TSG--LDPEArrelweLLRELAAE-GKTVLLSTH 189
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
439-598 |
3.05e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 69.31 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 439 IIKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLTKPERGKLfyvpqr 511
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLyGEERPtsgqvlVNGQDLSRLKRREI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 512 PYM--TLGT-------LRD-----------QVIYPDGREDQKRkgisdlvLKEYLDNVQLGHILEReggwdsvqdwM-DV 570
Cdd:COG2884 75 PYLrrRIGVvfqdfrlLPDrtvyenvalplRVTGKSRKEIRRR-------VREVLDLVGLSDKAKA----------LpHE 137
|
170 180
....*....|....*....|....*...
gi 966918915 571 LSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPT 165
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
124-640 |
4.18e-13 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 72.44 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 124 RYLLNFIAAMpLISLVNNFLKYGlnelklcFRVRLtkylYEEYLQ-SFTYYKMGNLDNRIANpdqlLTQDVEKFCNSVVD 202
Cdd:TIGR02203 67 RGICSFVSTY-LLSWVSNKVVRD-------IRVRM----FEKLLGlPVSFFDRQPTGTLLSR----ITFDSEQVASAATD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 203 LYSNLSKP-----FLDIVL--YIFKLTSAIGAQGPASMMAYLVVSglflTRLRRPIGRMtiteQKYEGEYRYVNSRLITN 275
Cdd:TIGR02203 131 AFIVLVREtltviGLFIVLlyYSWQLTLIVVVMLPVLSILMRRVS----KRLRRISKEI----QNSMGQVTTVAEETLQG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 276 SEEIAFYNGNKREKQtvhsvfrklvehlhnfilfRFsmGFIDNIIAKYLATVVGYLVVSRPFldlshprhlksthSELLE 355
Cdd:TIGR02203 203 YRVVKLFGGQAYETR-------------------RF--DAVSNRNRRLAMKMTSAGSISSPI-------------TQLIA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 356 DYYQSGRMLLRMSQALGRIVLAGremtrlaGFTARITELMQVLKDLNHgkyeRTMVSQQ-EKGIEGVQVI------PLIP 428
Cdd:TIGR02203 249 SLALAVVLFIALFQAQAGSLTAG-------DFTAFITAMIALIRPLKS----LTNVNAPmQRGLAAAESLftlldsPPEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 429 GAGEIII--ADNIIKFDHVPLATPNGDI-LIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT------- 498
Cdd:TIGR02203 318 DTGTRAIerARGDVEFRNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILldghdla 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 499 ----KPERGKLFYVPQRPYMTLGTLRDQVIYPDGRE---DQKRKGISDLVLKEYLDNVQLGhiLEREGGWDSVQdwmdvL 571
Cdd:TIGR02203 398 dytlASLRRQVALVSQDVVLFNDTIANNIAYGRTEQadrAEIERALAAAYAQDFVDKLPLG--LDTPIGENGVL-----L 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966918915 572 SGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMD 640
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVMD 541
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
456-625 |
5.09e-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: 67.42 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPE---RGKLFYVPQRPYmtlgtlrdqvI 524
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlgllkpdsGEIK-VLGKDIKKEPeevKRRIGYLPEEPS----------L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 525 YPdgredqkrkgisDLVLKEYLDnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAV--- 601
Cdd:cd03230 85 YE------------NLTVRENLK-----------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLdpe 129
|
170 180
....*....|....*....|....*
gi 966918915 602 -SVDVEGYIYSHcRKVGITLFTVSH 625
Cdd:cd03230 130 sRREFWELLREL-KKEGKTILLSSH 153
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
408-612 |
1.52e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.13 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 408 RTMVSQQEKGIEGVQVIPLIPGAG-EIIIADNIIKFDHVPLATPNGdilirdLNFEVQSGANVLICGPNGCGKSSLFR-V 485
Cdd:TIGR00957 611 RIFLSHEELEPDSIERRTIKPGEGnSITVHNATFTWARDLPPTLNG------ITFSIPEGALVAVVGQVGCGKSSLLSaL 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 486 LGELWPLFGGRLTKperGKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKGI-------SDLVLKEYLDNVQLGhilerE 558
Cdd:TIGR00957 685 LAEMDKVEGHVHMK---GSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVleacallPDLEILPSGDRTEIG-----E 756
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 966918915 559 GGWDsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSH 612
Cdd:TIGR00957 757 KGVN--------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
439-625 |
1.59e-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: 67.53 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 439 IIKFDHVPLATPNGDI---LIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------------GELWPLFGGRLTKPE 501
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsgsiifdGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 502 RGKLFYVPQRPYMTLG---TLRDQVIYP-----DGREDQKRKGISDLVLKEYLDNVQLGHILEREggwdsvqdwmdvLSG 573
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprmTIGEQIAEPlrihgKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE------------LSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 966918915 574 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSH----CRKVGITLFTVSH 625
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkklQEELGLTLLFITH 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
440-625 |
1.84e-12 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 67.59 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLFY----VPQRPYMT 515
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLN--------GLVEPTSGSVLIdgtdINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 516 LGTLRDQV--IYPDGRedqkrkgisdLVLKEY-LDNVQLG------------------------HILEREGGWDSVQDWM 568
Cdd:cd03256 73 LRQLRRQIgmIFQQFN----------LIERLSvLENVLSGrlgrrstwrslfglfpkeekqralAALERVGLLDKAYQRA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966918915 569 DVLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLH 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
434-598 |
3.16e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.49 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 434 IIADNIIKFdhvplaTPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-------GELwpLFGG----RLTKPE- 501
Cdd:PRK11174 350 IEAEDLEIL------SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpyqGSL--KINGielrELDPESw 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 502 RGKLFYVPQRPYMTLGTLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLGHILER-EGGWDS-VQDWMDVLSGGEKQRM 579
Cdd:PRK11174 422 RKHLSWVGQNPQLPHGTLRDNVLL--GNPD-----ASDEQLQQALENAWVSEFLPLlPQGLDTpIGDQAAGLSVGQAQRL 494
|
170
....*....|....*....
gi 966918915 580 AMARLFYHKPQFAILDECT 598
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPT 513
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
455-600 |
3.41e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.10 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP------LFG---GRLTKPERGKLFYV-PQRPYMTLGTLRDQV 523
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPdsgevrLNGrplADWSPAELARRRAVlPQHSSLSFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 524 I----YPDGREDQKRKGISDlvlkEYLDNVQLGHILEReggwdSVQdwmdVLSGGEKQRMAMARLF------YHKPQFAI 593
Cdd:PRK13548 97 VamgrAPHGLSRAEDDALVA----AALAQVDLAHLAGR-----DYP----QLSGGEQQRVQLARVLaqlwepDGPPRWLL 163
|
....*..
gi 966918915 594 LDECTSA 600
Cdd:PRK13548 164 LDEPTSA 170
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
440-598 |
5.10e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.01 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATpNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQrpymtlgtl 519
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966918915 520 rdqviypdgredqkrkgisdlvlkeyldnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
428-600 |
6.43e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 68.69 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 428 PGAGEIIIADNIIKFDHVPLA-TPNGDILiRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-------- 498
Cdd:COG5265 346 PDAPPLVVGGGEVRFENVSFGyDPERPIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILidgqdird 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 499 -KPE--RGKLFYVPQRPYMTLGTLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLGHILER-EGGWDSVqdwmdV---- 570
Cdd:COG5265 425 vTQAslRAAIGIVPQDTVLFNDTIAYNIAY--GRPD-----ASEEEVEAAARAAQIHDFIESlPDGYDTR-----Vgerg 492
|
170 180 190
....*....|....*....|....*....|..
gi 966918915 571 --LSGGEKQRMAMARLFYHKPQFAILDECTSA 600
Cdd:COG5265 493 lkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
455-625 |
7.74e-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: 64.97 E-value: 7.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWP------LFGGRLTKPE--RGKLFYVPQRPYMTLG--TLRDQVI 524
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKessgsiLLNGKPIKAKerRKSIGYVMQDVDYQLFtdSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 525 Y----PDGREDQKRKGISDLVLKEYLDNvqlgHILEreggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSA 600
Cdd:cd03226 95 LglkeLDAGNEQAETVLKDLDLYALKER----HPLS--------------LSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180
....*....|....*....|....*...
gi 966918915 601 V---SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03226 157 LdykNMERVGELIRELAAQGKAVIVITH 184
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
437-599 |
8.14e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 65.88 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 437 DNIIKFDHVPLATpNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP-------LFGGRLTKPE----RGK 504
Cdd:COG1119 1 DPLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLPPtygndvrLFGERRGGEDvwelRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 505 LFYV-P--QRPYMTLGTLRDQVI---------YPDGREDQKRKGisdlvlKEYLDNVQLGHILEREggwdsvqdwMDVLS 572
Cdd:COG1119 80 IGLVsPalQLRFPRDETVLDVVLsgffdsiglYREPTDEQRERA------RELLELLGLAHLADRP---------FGTLS 144
|
170 180
....*....|....*....|....*..
gi 966918915 573 GGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTA 171
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
428-626 |
1.35e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 64.36 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 428 PGAGEIIIADNIIKFdhvplaTPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplFggRLTKPERGK--- 504
Cdd:cd03369 2 PEHGEIEVENLSVRY------APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILAL------F--RFLEAEEGKiei 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 505 ----------------LFYVPQRPYMTLGTLRdqviypdgredqkrkgiSDL-VLKEYlDNVQLGHILE-REGGwdsvqd 566
Cdd:cd03369 68 dgidistipledlrssLTIIPQDPTLFSGTIR-----------------SNLdPFDEY-SDEEIYGALRvSEGG------ 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966918915 567 wmDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRK--VGITLFTVSHR 626
Cdd:cd03369 124 --LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHR 183
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
447-640 |
1.42e-11 |
|
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: 67.46 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 447 LATPNGDILIRDLNFEVQSGANVL--------------ICGPNGCGKSSLFRVL--------GELwpLFGGRLTK----- 499
Cdd:TIGR01193 467 LNNLNGDIVINDVSYSYGYGSNILsdisltikmnskttIVGMSGSGKSTLAKLLvgffqarsGEI--LLNGFSLKdidrh 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 500 PERGKLFYVPQRPYMTLGTLRDQVIY---PDGREDQKRKGISDLVLKEYLDNVQLGH--ILEREGGwdsvqdwmdVLSGG 574
Cdd:TIGR01193 545 TLRQFINYLPQEPYIFSGSILENLLLgakENVSQDEIWAACEIAEIKDDIENMPLGYqtELSEEGS---------SISGG 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966918915 575 EKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVG-ITLFTVSHRKSLWKHHEYYLHMD 640
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
452-625 |
1.46e-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: 64.66 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 452 GDILIRDLNFEVQSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGRLT--KPERGKLFYVPQR----PYMTLgt 518
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFIKPdsgkilLNGKDITnlPPEKRDISYVPQNyalfPHMTV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 519 lRDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03299 89 -YKNIAYGLKKRKVDKKEIERKV-LEIAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|.
gi 966918915 599 SAVSVDVEGYIYSHCRKV----GITLFTVSH 625
Cdd:cd03299 158 SALDVRTKEKLREELKKIrkefGVTVLHVTH 188
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
454-625 |
1.59e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 454 ILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GelwplfggrLTKPERGKLFYVPQRpymtlgtLRDQviypdgREDQ 532
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILaG---------LARPDAGEVLWQGEP-------IRRQ------RDEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 533 KRK--------GISDLV-----------LKEYLDNVQLGHILEREGgwdsVQDWMDV----LSGGEKQRMAMARLFYHKP 589
Cdd:PRK13538 73 HQDllylghqpGIKTELtalenlrfyqrLHGPGDDEALWEALAQVG----LAGFEDVpvrqLSAGQQRRVALARLWLTRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 966918915 590 QFAILDECTSAVSV----DVEGYIYSHCRKVGITLFTvSH 625
Cdd:PRK13538 149 PLWILDEPFTAIDKqgvaRLEALLAQHAEQGGMVILT-TH 187
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
451-596 |
2.15e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.65 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSL-----------FRVLGELWpLFGGRLTK--PERGKLFYVPQR----PY 513
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLlaaiagtlspaFSASGEVL-LNGRRLTAlpAEQRRIGILFQDdllfPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 514 MTLG-----TLRDQViypdGREDQKRKgisdlvLKEYLDNVQLGHILEReggwDSVQdwmdvLSGGEKQRMAMARLFYHK 588
Cdd:COG4136 91 LSVGenlafALPPTI----GRAQRRAR------VEQALEEAGLAGFADR----DPAT-----LSGGQRARVALLRALLAE 151
|
....*...
gi 966918915 589 PQFAILDE 596
Cdd:COG4136 152 PRALLLDE 159
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
457-600 |
2.85e-11 |
|
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: 63.32 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 457 RDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLfyvpqrpymtlgTLRDQVIYPDGRE-DQKRK 535
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCI--------NLLEEPDSGTI------------IIDGLKLTDDKKNiNELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 536 GISdLVLKEY--------LDNVQLG-----------------HILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQ 590
Cdd:cd03262 77 KVG-MVFQQFnlfphltvLENITLApikvkgmskaeaeeralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170
....*....|
gi 966918915 591 FAILDECTSA 600
Cdd:cd03262 156 VMLFDEPTSA 165
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
454-653 |
2.91e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 454 ILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWPlfggrltkpERgKLFYVPQRPYMTLGTLRDQVIY 525
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlsqfeiseGRVWA---------ER-SIAYVPQQAWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 526 PDgREDQKRkgISDLVLKEYL--DNVQLGHILEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSV 603
Cdd:PTZ00243 744 FD-EEDAAR--LADAVRVSQLeaDLAQLGGGLETEIGEKGVN-----LSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 966918915 604 DVEGYIYSHC---RKVGITLFTVSHRKSLWKHHEYYLHMdGRGNYEFKQITED 653
Cdd:PTZ00243 816 HVGERVVEECflgALAGKTRVLATHQVHVVPRADYVVAL-GDGRVEFSGSSAD 867
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
440-598 |
2.93e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 63.37 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILiRDLNFEVQSGANVLIcGPNGCGKSSLFRVLGELWPLFGGRLT--------KPE--RGKLFYVP 509
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQklRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 510 Q--RPYMTLgTLRDQVIYpdgredQKR-KGISDLVLKEYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRMAMARLFY 586
Cdd:cd03264 79 QefGVYPNF-TVREFLDY------IAWlKGIPSKEVKARVDEV-----LELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170
....*....|..
gi 966918915 587 HKPQFAILDECT 598
Cdd:cd03264 147 GDPSILIVDEPT 158
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
455-629 |
3.95e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFRVlgelwpLFGGRLTKPERGKlFYVPQRPYMTLGTLRDQvIYPDGREDQKr 534
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRL------LAGALKGTPVAGC-VDVPDNQFGREASLIDA-IGRKGDFKDA- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 535 kgisdlvlKEYLDNVQLGhilereggwdSVQDWM---DVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVeGYIYS 611
Cdd:COG2401 116 --------VELLNAVGLS----------DAVLWLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT-AKRVA 176
|
170 180
....*....|....*....|...
gi 966918915 612 H-----CRKVGITLFTVSHRKSL 629
Cdd:COG2401 177 RnlqklARRAGITLVVATHHYDV 199
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
428-642 |
5.42e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.75 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 428 PGAGEIIIADNIIKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------- 498
Cdd:PRK13657 323 PGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtv 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 499 --KPERGKLFYVPQRPYMTLGTLRD--QViypdGREDQkrkgiSDLVLKEYLDNVQ-LGHILEREGGWDS-VQDWMDVLS 572
Cdd:PRK13657 403 trASLRRNIAVVFQDAGLFNRSIEDniRV----GRPDA-----TDEEMRAAAERAQaHDFIERKPDGYDTvVGERGRQLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 573 GGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEgyiyshcRKV---------GITLFTVSHRKSLWKHHEYYLHMD-GR 642
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETE-------AKVkaaldelmkGRTTFIIAHRLSTVRNADRILVFDnGR 546
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
458-615 |
5.82e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.91 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 458 DLNFEVQSGANVLICGPNGCGKSSLFR-VLGELWPLFGGRLTKpeRGKLFYVPQRPYMTLGTLRDQVIYpdGRE-DQKR- 534
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI--RGTVAYVPQVSWIFNATVRDNILF--GSPfDPERy 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 535 -KGISDLVLKEYLDNVQLGHILE-REGGWDsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSH 612
Cdd:PLN03130 711 eRAIDVTALQHDLDLLPGGDLTEiGERGVN--------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDK 782
|
...
gi 966918915 613 CRK 615
Cdd:PLN03130 783 CIK 785
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
456-641 |
8.32e-11 |
|
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: 62.35 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLF-RVLGELWPLFG--------------GRLTKPERGKLFYVPQRPYMTLGTLR 520
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwsnknesepsfEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 521 DQVIYPDGREDQKRKGIS-------DLVLKEYLDNVQLGhilerEGGWDsvqdwmdvLSGGEKQRMAMARLFYHKPQFAI 593
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTdacslqpDIDLLPFGDQTEIG-----ERGIN--------LSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 966918915 594 LDECTSAVSVdvegYIYSHCRKVGI---------TLFTVSHRKSLWKHHEYYLHM-DG 641
Cdd:cd03290 164 LDDPFSALDI----HLSDHLMQEGIlkflqddkrTLVLVTHKLQYLPHADWIIAMkDG 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
451-622 |
1.02e-10 |
|
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: 61.61 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTkpergklfyVPQRPYMTLGTLRDQVIYPDGRE 530
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVR---------WNGTPLAEQRDEPHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 531 DqkrkGI-SDLVLKEYLDNVQLGHILEREGGWDSVQDwMDV----------LSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:TIGR01189 82 P----GLkPELSALENLHFWAAIHGGAQRTIEDALAA-VGLtgfedlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*..
gi 966918915 600 AVSVD----VEGYIYSHCRKVGITLFT 622
Cdd:TIGR01189 157 ALDKAgvalLAGLLRAHLARGGIVLLT 183
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
456-625 |
1.13e-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: 62.36 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWplFGGR----LTKPERGKLFyVPQR----PYMTLGT- 518
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIaglerpdsGTIL--FGGEdatdVPVQERNVGF-VFQHyalfRHMTVFDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 519 ----LRDQVIYPDGREDQKRKGISDLvlkeyLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:cd03296 95 vafgLRVKPRSERPPEAEIRAKVHEL-----LKLVQLDWLADR---------YPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 966918915 595 DECTSAVSVDVEGYIYSHCRK----VGITLFTVSH 625
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRlhdeLHVTTVFVTH 195
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
437-625 |
1.21e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.90 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 437 DNIIKFDHVPLATPNGDI-LIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP---------LFGGRLTKPE---- 501
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLLPddnpnskitVDGITLTAKTvwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 502 RGKLFYVPQRP--YMTLGTLRDQVIYpdGREDqkrKGISDLVLKEYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRM 579
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAF--GLEN---RAVPRPEMIKIVRDV-----LADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 966918915 580 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV----GITLFTVSH 625
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
458-625 |
1.23e-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: 61.46 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 458 DLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--KPERGKLFYVPQRpymtLGTLRD-QVIYPD--GRED- 531
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdGKSYQKNIEALRR----IGALIEaPGFYPNltARENl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 532 ---QKRKGISDLVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAvsVDVEG- 607
Cdd:cd03268 94 rllARLLGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNG--LDPDGi 162
|
170 180
....*....|....*....|...
gi 966918915 608 -----YIYSHcRKVGITLFTVSH 625
Cdd:cd03268 163 kelreLILSL-RDQGITVLISSH 184
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
458-625 |
1.30e-10 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 63.59 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 458 DLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL---------------TKPERGKLFYVPQR----PYMTLgt 518
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgifLPPEKRRIGYVFQEarlfPHLSV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 519 lRDQVIYPDGREDQKRKGISDLVLKEYLDnvqLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:TIGR02142 93 -RGNLRYGMKRARPSERRISFERVIELLG---IGHLLGRLPG---------RLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190
....*....|....*....|....*....|.
gi 966918915 599 SAVSV----DVEGYIYSHCRKVGITLFTVSH 625
Cdd:TIGR02142 160 AALDDprkyEILPYLERLHAEFGIPILYVSH 190
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
451-625 |
1.30e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 61.10 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQR-------PY-----MTLG 517
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRPT-SGTVRRAGGARVAYVPQRsevpdslPLtvrdlVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 518 TLRDQVIY-PDGREDQkrkgisdLVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:NF040873 82 RWARRGLWrRLTRDDR-------AAVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|..
gi 966918915 597 CTSAVSVDVEGYIYSHCRKV---GITLFTVSH 625
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEharGATVVVVTH 177
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
452-625 |
2.06e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.58 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 452 GDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERG----------KLFYVPQRPYM--TLGTL 519
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfqrdsiarGLLYLGHAPGIktTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 520 RD-QVIYPDGREDQkrkgisdlvLKEYLDNVQLGHILEREGGWdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03231 92 ENlRFWHADHSDEQ---------VEEALARVGLNGFEDRPVAQ---------LSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|.
gi 966918915 599 SAV---SVD-VEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03231 154 TALdkaGVArFAEAMAGHCARGGMVVLTTHQ 184
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
456-596 |
4.68e-10 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 59.96 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL---------TKPERGKLFYVPQR----PYMtlgTLRDQ 522
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdLPPKDRDIAMVFQNyalyPHM---TVYDN 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966918915 523 VIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:cd03301 93 IAFGLKLRKVPKDEIDERV-REVAELLQIEHLLDRK---------PKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
449-613 |
5.74e-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: 63.01 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 449 TPNGDI-------------LIRDLNFEVQSGANVLICGPNGCGKSSLFRV-LGELWPLFGgrlTKPERGKLFYVPQRPYM 514
Cdd:TIGR01271 422 QPNGDDglffsnfslyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMiMGELEPSEG---KIKHSGRISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 515 TLGTLRDQVIYPDGREDQKRKGI-------SDLVLKEYLDNVQLGhilerEGGWdsvqdwmdVLSGGEKQRMAMARLFYH 587
Cdd:TIGR01271 499 MPGTIKDNIIFGLSYDEYRYTSVikacqleEDIALFPEKDKTVLG-----EGGI--------TLSGGQRARISLARAVYK 565
|
170 180
....*....|....*....|....*.
gi 966918915 588 KPQFAILDECTSAVSVDVEGYIYSHC 613
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKEIFESC 591
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
436-599 |
6.69e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.41 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 436 ADNIIKFDHVPLATPNGDIL-IRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPE-----RG 503
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLnGLLLPeagtiTVGGMVLSEEtvwdvRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 504 KLFYVPQRP--YMTLGTLRDQVIYpdGREDQkrkGI--SDLV--LKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQ 577
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDDVAF--GLENI---GVprEEMVerVDQALRQVGMEDFLNREPH---------RLSGGQKQ 147
|
170 180
....*....|....*....|..
gi 966918915 578 RMAMARLFYHKPQFAILDECTS 599
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATS 169
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
451-625 |
6.94e-10 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 59.56 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGR----LTKPERG--------KLFyvpq 510
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIagfetptsGEI--LLDGKditnLPPHKRPvntvfqnyALF---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 511 rPYMTLGtlrDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQ 590
Cdd:cd03300 85 -PHLTVF---ENIAFGLRLKKLPKAEIKERV-AEALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 966918915 591 FAILDECTSAVSV----DVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03300 151 VLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTH 189
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
437-613 |
7.40e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.26 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 437 DNIIKFDHVPL-ATPngdiLIRDLNFEVQSGANVLICGPNGCGKSSLFR-VLGELWPLFGgrlTKPERGKLFYVPQRPYM 514
Cdd:cd03291 37 DNNLFFSNLCLvGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPSEG---KIKHSGRISFSSQFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 515 TLGTLRDQVIYPDGREDQKRKGI-------SDLVLKEYLDNVQLGhilerEGGWdsvqdwmdVLSGGEKQRMAMARLFYH 587
Cdd:cd03291 110 MPGTIKENIIFGVSYDEYRYKSVvkacqleEDITKFPEKDNTVLG-----EGGI--------TLSGGQRARISLARAVYK 176
|
170 180
....*....|....*....|....*.
gi 966918915 588 KPQFAILDECTSAVSVDVEGYIYSHC 613
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTEKEIFESC 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
440-599 |
8.89e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.00 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGD-ILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWplfggrltKPERGKLF-YVPQRPYMTLG 517
Cdd:PRK13632 8 IKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL--------KPQSGEIKiDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 518 TLRDQV--IY--PD--------------GREDQK--RKGISDLVLkEYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQ 577
Cdd:PRK13632 80 EIRKKIgiIFqnPDnqfigatveddiafGLENKKvpPKKMKDIID-DLAKKVGMEDYLDKEP---------QNLSGGQKQ 149
|
170 180
....*....|....*....|..
gi 966918915 578 RMAMARLFYHKPQFAILDECTS 599
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTS 171
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
456-596 |
2.82e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 59.35 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRvlgelwpLFGGrLTKPERGKLFY---------VPQR------------PYM 514
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAG-LEKPTEGQIFIdgedvthrsIQQRdicmvfqsyalfPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 515 TLGtlrDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:PRK11432 94 SLG---ENVGYGLKMLGVPKEERKQRV-KEALELVDLAGFEDR---------YVDQISGGQQQRVALARALILKPKVLLF 160
|
..
gi 966918915 595 DE 596
Cdd:PRK11432 161 DE 162
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
440-628 |
3.51e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.73 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLtkpergklfYVPQRPymtLGTL 519
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI---------RLDGRP---LSSL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 520 RDQVIypdgredqkRKGIS-----DLVLKE-YLDNVQLGHILEREGGWD---SVQ--DWM---------------DVLSG 573
Cdd:PRK10790 409 SHSVL---------RQGVAmvqqdPVVLADtFLANVTLGRDISEEQVWQaleTVQlaELArslpdglytplgeqgNNLSV 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 966918915 574 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKS 628
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLS 536
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
458-600 |
3.98e-09 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 57.30 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 458 DLNFEVqSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL---------------TKPERGKLFYVPQR----PYMTLgt 518
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVFQQyalfPHLNV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 519 lRDQVIYPDGREDQKRKGISdlvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03297 93 -RENLAFGLKRKRNREDRIS---VDELLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
..
gi 966918915 599 SA 600
Cdd:cd03297 160 SA 161
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
456-625 |
4.32e-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: 57.48 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGEL-WPLFGGRLTK--------PERGKLFyvpQR----PYMTLgtlRDQ 522
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitepgPDRMVVF---QNysllPWLTV---REN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 523 V------IYPDGREDQKRKgisdlVLKEYLDNVQLGHILEREGGWdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:TIGR01184 75 IalavdrVLPDLSKSERRA-----IVEEHIALVGLTEAADKRPGQ---------LSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190
....*....|....*....|....*....|...
gi 966918915 597 CTSAVSVDVEGYIYSH----CRKVGITLFTVSH 625
Cdd:TIGR01184 141 PFGALDALTRGNLQEElmqiWEEHRVTVLMVTH 173
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
451-625 |
4.36e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.75 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------------------KPERGKLFYVPQ 510
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlyfgkdifqidaiklRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 511 rPYMTLgTLRDQVIYPDGREDQKRKGISDLVLKEYLDNVQLghilereggWDSVQDWMDV----LSGGEKQRMAMARLFY 586
Cdd:PRK14246 101 -PFPHL-SIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGL---------WKEVYDRLNSpasqLSGGQQQRLTIARALA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 966918915 587 HKPQFAILDECTSAVSV----DVEGYIYSHCRKVGITLftVSH 625
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIvnsqAIEKLITELKNEIAIVI--VSH 210
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
426-628 |
4.54e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 57.61 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 426 LIPGAGEIIIADNIIKFDHvplatpNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT------- 498
Cdd:cd03288 13 LVGLGGEIKIHDLCVRYEN------NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVidgidis 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 499 ----KPERGKLFYVPQRPYMTLGTLRDQViypdgreDQKRKgISDLVLKEYLDNVQLGHILER-EGGWDS-VQDWMDVLS 572
Cdd:cd03288 87 klplHTLRSRLSIILQDPILFSGSIRFNL-------DPECK-CTDDRLWEALEIAQLKNMVKSlPGGLDAvVTEGGENFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966918915 573 GGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIyshcRKVGITLF------TVSHRKS 628
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENIL----QKVVMTAFadrtvvTIAHRVS 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
455-642 |
5.31e-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: 56.38 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGR----LTKPERGK--LFYVPQRPYmtlgt 518
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkyevteGEI--LFKGEditdLPPEERARlgIFLAFQYPP----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 519 lrdqviypdgredqkrkGISDLVLKEYLDNVQLGhilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03217 88 -----------------EIPGVKNADFLRYVNEG------------------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 966918915 599 SAVSVD----VEGYIySHCRKVGITLFTVSHRKSLWKHHE---YYLHMDGR 642
Cdd:cd03217 133 SGLDIDalrlVAEVI-NKLREEGKSVLIITHYQRLLDYIKpdrVHVLYDGR 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
405-606 |
5.64e-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: 59.18 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 405 KYERTMVSQQEKGIEGVQV-IPLIPGAGEIII-ADNIIK-FDHvplatpngDILIRDLNFEVQSGANVLICGPNGCGKSS 481
Cdd:TIGR03719 292 RYEELLSQEFQKRNETAEIyIPPGPRLGDKVIeAENLTKaFGD--------KLLIDDLSFKLPPGGIVGVIGPNGAGKST 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 482 LFRVL-GELWPlFGGRLTKPERGKLFYVpqrpymtlgtlrdqviypdgreDQKRKGISD--LVLKEY---LDNVQLG--H 553
Cdd:TIGR03719 364 LFRMItGQEQP-DSGTIEIGETVKLAYV----------------------DQSRDALDPnkTVWEEIsggLDIIKLGkrE 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 554 ILERE-------GGWDSvQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVE 606
Cdd:TIGR03719 421 IPSRAyvgrfnfKGSDQ-QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTN--DLDVE 477
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
458-600 |
5.84e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.02 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 458 DLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGG----------------RLTKPERGKLFyvpQR----PYMT-- 515
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglkvndpkvdeRLIRQEAGMVF---QQfylfPHLTal 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 516 ----LGTLRdqvIYPDGREDQKRKGisdlvlKEYLDNVQLGhilEREGGWDSVqdwmdvLSGGEKQRMAMARLFYHKPQF 591
Cdd:PRK09493 96 envmFGPLR---VRGASKEEAEKQA------RELLAKVGLA---ERAHHYPSE------LSGGQQQRVAIARALAVKPKL 157
|
....*....
gi 966918915 592 AILDECTSA 600
Cdd:PRK09493 158 MLFDEPTSA 166
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
457-626 |
6.15e-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: 55.51 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 457 RDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplFGgrLTKPERGKLFyvpqrpymtlgtLRDQVIYPDGREDQKRKG 536
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKIL------SG--LYKPDSGEIL------------VDGKEVSFASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 537 ISdLVlkeyldnvqlgHilereggwdsvQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV 616
Cdd:cd03216 77 IA-MV-----------Y-----------Q-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL 128
|
170
....*....|...
gi 966918915 617 ---GITLFTVSHR 626
Cdd:cd03216 129 raqGVAVIFISHR 141
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
439-629 |
6.89e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 439 IIKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE-RGKLFYVPQRPYMTL 516
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIsGELQPSSGTVFRSAKvRMAVFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 517 GT---LRDQVIYPdGREDQKrkgisdlvLKEYLDNVQLGHILEREGgwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAI 593
Cdd:PLN03073 588 SSnplLYMMRCFP-GVPEQK--------LRAHLGSFGVTGNLALQP--------MYTLSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 966918915 594 LDECTSAVSVD-VEGYIYshcrkvGITLF-----TVSHRKSL 629
Cdd:PLN03073 651 LDEPSNHLDLDaVEALIQ------GLVLFqggvlMVSHDEHL 686
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
456-596 |
7.19e-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: 56.67 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGR-------LTK------PERGkLFYVPQR----PYMT--- 515
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrdITGlppherARAG-IGYVPEGrrifPELTvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 516 ---LGTLRDqviyPDGREDQKRKGISDL--VLKEyldnvqlghILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQ 590
Cdd:cd03224 95 nllLGAYAR----RRAKRKARLERVYELfpRLKE---------RRKQLAG---------TLSGGEQQMLAIARALMSRPK 152
|
....*.
gi 966918915 591 FAILDE 596
Cdd:cd03224 153 LLLLDE 158
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
452-625 |
9.13e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.73 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 452 GDILI-RDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRL------TKPERGKLF-----Yvpqr 511
Cdd:PRK11000 14 GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditsGDL--FIGEKRmndvppAERGVGMVFqsyalY---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 512 PYMTLGtlrDQVIY------PDGREDQKRkgisdlvLKEYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQRMAMARLF 585
Cdd:PRK11000 88 PHLSVA---ENMSFglklagAKKEEINQR-------VNQVAEVLQLAHLLDRKP---------KALSGGQRQRVAIGRTL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 966918915 586 YHKPQFAILDECTS----AVSVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK11000 149 VAEPSVFLLDEPLSnldaALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
456-626 |
9.59e-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: 56.13 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLF---------------YVPQR----PYMtl 516
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMI--------LGIILPDSGEVLfdgkpldiaarnrigYLPEErglyPKM-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 517 gTLRDQVIYPDGREDQKRKGISDLVLkEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:cd03269 86 -KVIDQLVYLAQLKGLKKEEARRRID-EWLERLELSEYANKR---------VEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|...
gi 966918915 597 CTSA---VSVDVEGYIYSHCRKVGITLFTVSHR 626
Cdd:cd03269 155 PFSGldpVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
445-599 |
1.16e-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: 56.13 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 445 VPLATPNGD---ILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL---GELWPLFGGRLT---KPERGKLF-----YVPQ 510
Cdd:cd03234 9 VGLKAKNWNkyaRILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILfngQPRKPDQFqkcvaYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 511 R----PYMTL-------GTLRDQVIYPDGredQKRKGISDLVLKEyLDNVQLGHILereggwdsvqdwMDVLSGGEKQRM 579
Cdd:cd03234 89 DdillPGLTVretltytAILRLPRKSSDA---IRKKRVEDVLLRD-LALTRIGGNL------------VKGISGGERRRV 152
|
170 180
....*....|....*....|
gi 966918915 580 AMARLFYHKPQFAILDECTS 599
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTS 172
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
456-625 |
1.44e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 57.26 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRvlgelwpLFGGrLTKPERGKLF-------YVP--QR------------PYM 514
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLR-------LIAG-FETPDSGRIMldgqditHVPaeNRhvntvfqsyalfPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 515 TLgtlRDQVIYpdGREDQKR--KGISDLVLkEYLDNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFA 592
Cdd:PRK09452 102 TV---FENVAF--GLRMQKTpaAEITPRVM-EALRMVQLEEFAQRK-----PHQ----LSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 966918915 593 ILDECTSAVSVDVEGYIYSHC----RKVGITLFTVSH 625
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELkalqRKLGITFVFVTH 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
458-625 |
1.78e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.79 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 458 DLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL----------TKPE-------RGKLFYVPQR----PYMT- 515
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfsKTPSdkairelRRNVGMVFQQynlwPHLTv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 516 -----------LGTLRDQVIypdgreDQKRKGISDLVLKEYLDNVQLgHilereggwdsvqdwmdvLSGGEKQRMAMARL 584
Cdd:PRK11124 100 qqnlieapcrvLGLSKDQAL------ARAEKLLERLRLKPYADRFPL-H-----------------LSGGQQQRVAIARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 966918915 585 FYHKPQFAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSH 625
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELaetGITQVIVTH 199
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
451-596 |
2.17e-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: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILiRDLNFEVQSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGR----LTKPERGK--LFYVPQRPY- 513
Cdd:COG0396 12 GKEIL-KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpkyevtsGSI--LLDGEdileLSPDERARagIFLAFQYPVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 514 ---MTLGTL--------RDQVIypDGREDQKRkgisdlvLKEYLDNVQLGH-ILER---EGgwdsvqdwmdvLSGGEKQR 578
Cdd:COG0396 89 ipgVSVSNFlrtalnarRGEEL--SAREFLKL-------LKEKMKELGLDEdFLDRyvnEG-----------FSGGEKKR 148
|
170
....*....|....*...
gi 966918915 579 MAMARLFYHKPQFAILDE 596
Cdd:COG0396 149 NEILQMLLLEPKLAILDE 166
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
440-604 |
2.19e-08 |
|
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: 54.24 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILI-RDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWPLFG---------GRLTKPERGKLFYV 508
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLKPQQGeitldgvpvSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 509 PQRPYMTLGTLRDQViypdGREdqkrkgisdlvlkeyldnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHK 588
Cdd:cd03247 81 NQRPYLFDTTLRNNL----GRR----------------------------------------FSGGERQRLALARILLQD 116
|
170
....*....|....*.
gi 966918915 589 PQFAILDECTsaVSVD 604
Cdd:cd03247 117 APIVLLDEPT--VGLD 130
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
450-626 |
2.26e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 450 PNGDILIRDLNFEVQSGANVLICGPNGCGKSS----LFRVL----GELwPLFGGRLTK----PERGKLFYVPQRPYMTLG 517
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINesaeGEI-IIDGLNIAKiglhDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 518 TLRDQVIYPDGREDQKRKGISDLV-LKEYLDNVQLGHILE-REGGwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:TIGR00957 1375 SLRMNLDPFSQYSDEEVWWALELAhLKTFVSALPDKLDHEcAEGG--------ENLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190
....*....|....*....|....*....|...
gi 966918915 596 ECTSAVSVDVEGYIYSHCRKV--GITLFTVSHR 626
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQfeDCTVLTIAHR 1479
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
452-598 |
2.28e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 452 GDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQRPY------MTLGTLRDQVI 524
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvGELEPD-SGTVKWSENANIGYYAQDHAydfendLTLFDWMSQWR 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966918915 525 YPdGREDQKRKGIsdlvlkeyldnvqLGHILereGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:PRK15064 410 QE-GDDEQAVRGT-------------LGRLL---FSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
437-625 |
2.58e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.62 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 437 DNIIKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPERGKLFYVPQ 510
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLnGILKPssgriLFDGKPIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 511 RPYMTLGTLRDQVIYPDGREDQKRkGISDLVLKEylDNVQ--LGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHK 588
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQDVSF-GAVNLKLPE--DEVRkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 966918915 589 PQFAILDECTSAVS----VDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK13636 160 PKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATH 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
452-606 |
2.77e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 452 GDILIRDLNFEVQSGANVLICGPNGCGKSSLFRV-LGELWPLfGGRL---TKPE-------RGKLfyVPQRpymtlgTLR 520
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQAD-SGRIhcgTKLEvayfdqhRAEL--DPEK------TVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 521 DQViyPDGREDQKRKGISDLVLKeYLdnvqlghilereggwdsvQDWM----------DVLSGGEKQRMAMARLFYHKPQ 590
Cdd:PRK11147 402 DNL--AEGKQEVMVNGRPRHVLG-YL------------------QDFLfhpkramtpvKALSGGERNRLLLARLFLKPSN 460
|
170
....*....|....*.
gi 966918915 591 FAILDECTSavSVDVE 606
Cdd:PRK11147 461 LLILDEPTN--DLDVE 474
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
437-625 |
3.20e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 437 DNIIKFDHVPLATPnGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWP------LFGGRLTKPERGKLF---- 506
Cdd:PRK10575 9 DTTFALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPpsegeiLLDAQPLESWSSKAFarkv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 507 -YVPQR-PYMTLGTLRDQVI---YP-------DGREDQKRkgisdlvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGG 574
Cdd:PRK10575 88 aYLPQQlPAAEGMTVRELVAigrYPwhgalgrFGAADREK-------VEEAISLVGLKPLAHR---------LVDSLSGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 966918915 575 EKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
433-625 |
3.62e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.90 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 433 IIIADNIIKfdhvplaTPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-------------K 499
Cdd:PRK10895 3 TLTAKNLAK-------AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplhaR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 500 PERGkLFYVPQRP--YMTLGTLRDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQ 577
Cdd:PRK10895 76 ARRG-IGYLPQEAsiFRRLSVYDNLMAVLQIRDDLSAEQREDRA-NELMEEFHIEHLRDSMG---------QSLSGGERR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 966918915 578 RMAMARLFYHKPQFAILDECTSAVS----VDVEGyIYSHCRKVGITLFTVSH 625
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDpisvIDIKR-IIEHLRDSGLGVLITDH 195
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
434-625 |
3.66e-08 |
|
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: 54.30 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 434 IIADNIIKfdhvplaTPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT----------KPERG 503
Cdd:cd03265 1 IEVENLVK-------KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrepREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 504 KLFYVPQRPymtlgTLRDQVIypdGRED----QKRKGISDLVLKEYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRM 579
Cdd:cd03265 74 RIGIVFQDL-----SVDDELT---GWENlyihARLYGVPGAERRERIDEL-----LDFVGLLEAADRLVKTYSGGMRRRL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 966918915 580 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV----GITLFTVSH 625
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkeefGMTILLTTH 190
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
456-625 |
3.87e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 55.87 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRL---TKPERGKLFYVPQR----PYMTLgtlR 520
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagfetpdsGRI--LLDGRDvtgLPPEKRNVGMVFQDyalfPHLTV---A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 521 DQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDEC 597
Cdd:COG3842 96 ENVAFGLRMRGVPKAEIRARV-AELLELVGLEGLADRyphQ------------LSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190
....*....|....*....|....*....|....
gi 966918915 598 TSA------VSVDVEgyIYSHCRKVGITLFTVSH 625
Cdd:COG3842 163 LSAldaklrEEMREE--LRRLQRELGITFIYVTH 194
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
452-596 |
3.97e-08 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 54.60 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 452 GDILI-RDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE----RGkLFYVPQR----PY 513
Cdd:COG0410 14 GGIHVlHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglPPHriarLG-IGYVPEGrrifPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 514 MT------LG--TLRDQviyPDGREDQKRkgISDL--VLKEYLDnvqlghileREGGwdsvqdwmdVLSGGEKQRMAMAR 583
Cdd:COG0410 93 LTveenllLGayARRDR---AEVRADLER--VYELfpRLKERRR---------QRAG---------TLSGGEQQMLAIGR 149
|
170
....*....|...
gi 966918915 584 LFYHKPQFAILDE 596
Cdd:COG0410 150 ALMSRPKLLLLDE 162
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
455-599 |
4.52e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.53 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFggrltkPE---RGKLFYVPQRPY-MTLGTLRD--QVIYpdg 528
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELY------PEarvSGEVYLDGQDIFkMDVIELRRrvQMVF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 529 redQKRKGISDLVLKEyldNVQLG------------------HILEREGGWDSVQDWMDV----LSGGEKQRMAMARLFY 586
Cdd:PRK14247 89 ---QIPNPIPNLSIFE---NVALGlklnrlvkskkelqervrWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARALA 162
|
170
....*....|...
gi 966918915 587 HKPQFAILDECTS 599
Cdd:PRK14247 163 FQPEVLLADEPTA 175
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
408-628 |
4.63e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.26 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 408 RTMVSQQEKGIEGVQVIPLIPGAgeiiIADNIIKFdHVPLATPNgdiLIRDLNFEVQSGANVLICGPNGCGKSSLFRVL- 486
Cdd:PRK10789 291 RAMLAEAPVVKDGSEPVPEGRGE----LDVNIRQF-TYPQTDHP---ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIq 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 487 -------GEL----WPLFGGRLTKpERGKLFYVPQRPYMTLGTLRDQVIYpdGREDQKRKGISDLVlkeYLDNVQlGHIL 555
Cdd:PRK10789 363 rhfdvseGDIrfhdIPLTKLQLDS-WRSRLAVVSQTPFLFSDTVANNIAL--GRPDATQQEIEHVA---RLASVH-DDIL 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966918915 556 EREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGI--TLFTVSHRKS 628
Cdd:PRK10789 436 RLPQGYDTeVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEgrTVIISAHRLS 511
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
434-605 |
8.16e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.70 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 434 IIADNIIK-FDHVPLATpngdilirDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELwpLFGG----RLTKP 500
Cdd:PRK10851 3 IEIANIKKsFGRTQVLN--------DISLDIPSGQMVALLGPSGSGKTTLLRIIaglehqtsGHI--RFHGtdvsRLHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 501 ER--GKLF--YVPQRpYMTLGtlrDQVIY-----PDgREDQKRKGISDLVLKeYLDNVQLGHILEReggwdsvqdWMDVL 571
Cdd:PRK10851 73 DRkvGFVFqhYALFR-HMTVF---DNIAFgltvlPR-RERPNAAAIKAKVTQ-LLEMVQLAHLADR---------YPAQL 137
|
170 180 190
....*....|....*....|....*....|....
gi 966918915 572 SGGEKQRMAMARLFYHKPQFAILDECTSAVSVDV 605
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
455-625 |
8.67e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.89 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGrlTKPErGKLFYVPQRPY---MTLGTLRDQV-------- 523
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESE--VRVE-GRVEFFNQNIYerrVNLNRLRRQVsmvhpkpn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 524 IYPDGREDQKRKGISdlvLKEYLDNVQLGHILEREGG----WDSVQDWMDV----LSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:PRK14258 99 LFPMSVYDNVAYGVK---IVGWRPKLEIDDIVESALKdadlWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190
....*....|....*....|....*....|....
gi 966918915 596 E-CTS---AVSVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK14258 176 EpCFGldpIASMKVESLIQSLRLRSELTMVIVSH 209
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
458-583 |
1.00e-07 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 54.34 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 458 DLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------------KPERGKLFYVPQ--R--PYMT-LG 517
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiflPPHRRRIGYVFQeaRlfPHLSvRG 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966918915 518 TLRdqviYPDGREDQKRKGISdlvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMAR 583
Cdd:COG4148 97 NLL----YGRKRAPRAERRIS---FDEVVELLGIGHLLDR---------RPATLSGGERQRVAIGR 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
450-604 |
1.03e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 450 PNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWPLFGGrltkpergKLFYVPQRPYM--TLgTL 519
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfnGEARPQPGI--------KVGYLPQEPQLdpTK-TV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 520 RDQVIypDGREDQKRkgisdlVLKEYlDNV-------------------QLGHILEREGGWD---SVQDWMD-------- 569
Cdd:TIGR03719 86 RENVE--EGVAEIKD------ALDRF-NEIsakyaepdadfdklaaeqaELQEIIDAADAWDldsQLEIAMDalrcppwd 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 966918915 570 ----VLSGGEKQRMAMARLFYHKPQFAILDECTS---AVSVD 604
Cdd:TIGR03719 157 advtKLSGGERRRVALCRLLLSKPDMLLLDEPTNhldAESVA 198
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
439-635 |
1.07e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.95 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 439 IIKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWplFGG----RLTKPE----R 502
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIcgierpsaGKIW--FSGhditRLKNREvpflR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 503 GKLFYVPQRPYMTLG-TLRDQVIYP-----DGREDQKRKgisdlvLKEYLDNVQLghilereggWDSVQDWMDVLSGGEK 576
Cdd:PRK10908 79 RQIGMIFQDHHLLMDrTVYDNVAIPliiagASGDDIRRR------VSAALDKVGL---------LDKAKNFPIQLSGGEQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966918915 577 QRMAMARLFYHKPQFAILDECT----SAVSVDVEgYIYSHCRKVGITLFTVSHRKSLWKHHEY 635
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTgnldDALSEGIL-RLFEEFNRVGVTVLMATHDIGLISRRSY 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
440-633 |
1.16e-07 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 52.80 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWPLFG-----GRLTKPERGKlfyvpQRPY 513
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIyKEELPTSGtirvnGQDVSDLRGR-----AIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 514 M--TLGT-LRD-----------------QVIYPDGREDQKRkgisdlvLKEYLDNVQLGHilereggwdSVQDWMDVLSG 573
Cdd:cd03292 76 LrrKIGVvFQDfrllpdrnvyenvafalEVTGVPPREIRKR-------VPAALELVGLSH---------KHRALPAELSG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966918915 574 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSHRKSLWKHH 633
Cdd:cd03292 140 GEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInkaGTTVVVATHAKELVDTT 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
473-601 |
1.18e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 473 GPNGCGKSSLFRVL---GELWP--------------LFGGRLTKPE-RGKLFYVPQRPYMTLGTLRDQVIYpdgreDQKR 534
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPevtitgsivynghnIYSPRTDTVDlRKEIGMVFQQPNPFPMSIYENVVY-----GLRL 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966918915 535 KGISDlvlKEYLDNVqLGHILEREGGWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:PRK14239 113 KGIKD---KQVLDEA-VEKSLKGASIWDEVKDRLHdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
456-596 |
1.18e-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: 53.21 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGR-LT--KPER------GKLFYVPqRPYMTLgTLR 520
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFLRPtsgsvLFDGEdITglPPHEiarlgiGRTFQIP-RLFPEL-TVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 521 DQVIYpdGREDQKRKGISDLVLK-----------EYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKP 589
Cdd:cd03219 94 ENVMV--AAQARTGSGLLLARARreereareraeELLERVGLADLADRPAG---------ELSYGQQRRLEIARALATDP 162
|
....*..
gi 966918915 590 QFAILDE 596
Cdd:cd03219 163 KLLLLDE 169
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
456-596 |
1.68e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 53.19 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGRLTKPERGKLFYVPQ----RPYMTLGtlrDQVI 524
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILAPdsgevlWDGEPLDPEDRRRIGYLPEerglYPKMKVG---EQLV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966918915 525 Y------PDGREDQKRkgisdlvLKEYLDNVQLGhilEREGgwDSVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:COG4152 94 YlarlkgLSKAEAKRR-------ADEWLERLGLG---DRAN--KKVEE----LSKGNQQKVQLIAALLHDPELLILDE 155
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
381-626 |
2.26e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 381 MTRLAGFTARITELMQ-VLKDLNhgKYERTMVSqqekgIEGVQVIPLIPGAGEIIIADN----------IIKFDHVPLA- 448
Cdd:PLN03232 1172 MGLLLSYTLNITTLLSgVLRQAS--KAENSLNS-----VERVGNYIDLPSEATAIIENNrpvsgwpsrgSIKFEDVHLRy 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 449 TPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPE-----------RGKLFYVPQRPYMTLG 517
Cdd:PLN03232 1245 RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlRRVLSIIPQSPVLFSG 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 518 TLRDQV-IYPDGREDQKRKGISDLVLKEYLDNVQLGHILE-REGGwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:PLN03232 1325 TVRFNIdPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEvSEGG--------ENFSVGQRQLLSLARALLRRSKILVLD 1396
|
250 260 270
....*....|....*....|....*....|...
gi 966918915 596 ECTSAVSVDVEGYIYSHCRK--VGITLFTVSHR 626
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREefKSCTMLVIAHR 1429
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
405-584 |
3.67e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 405 KYERtMVSQQEKGIEGVQ--VIPLIPGAGEIII-ADNIIK-FdhvplatpnGD-ILIRDLNFEVQSGANVLICGPNGCGK 479
Cdd:PRK11819 294 RYEE-LLSEEYQKRNETNeiFIPPGPRLGDKVIeAENLSKsF---------GDrLLIDDLSFSLPPGGIVGIIGPNGAGK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 480 SSLFRVLGELWPLFGGRLTKPERGKLFYVpqrpymtlgtlrdqviypdgreDQKRKGISD-----LVLKEYLDNVQLGhi 554
Cdd:PRK11819 364 STLFKMITGQEQPDSGTIKIGETVKLAYV----------------------DQSRDALDPnktvwEEISGGLDIIKVG-- 419
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 966918915 555 lERE------------GGWDSvQDWMDVLSGGEKQRMAMARL 584
Cdd:PRK11819 420 -NREipsrayvgrfnfKGGDQ-QKKVGVLSGGERNRLHLAKT 459
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
449-603 |
5.64e-07 |
|
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: 51.98 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 449 TPNGDI-LIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-----------GELwpLFGGR----LTKPE----RGK-LFY 507
Cdd:COG0444 13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlgllpppgitsGEI--LFDGEdllkLSEKElrkiRGReIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 508 VPQRPYMTLG---TLRDQVIYP------DGREDQKRKGIsdlvlkEYLDNVQLghilereggwDSVQDWMDV----LSGG 574
Cdd:COG0444 91 IFQDPMTSLNpvmTVGDQIAEPlrihggLSKAEARERAI------ELLERVGL----------PDPERRLDRypheLSGG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 966918915 575 EKQR----MAMArlfyHKPQFAILDECTSA--VSV 603
Cdd:COG0444 155 MRQRvmiaRALA----LEPKLLIADEPTTAldVTI 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
440-625 |
7.07e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.42 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---KPERGKL-----FYVPQR 511
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgQPTRQALqknlvAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 512 P------------------YMTLGTLRdqviYPDGREDQkrkgisdlVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSG 573
Cdd:PRK15056 87 EevdwsfpvlvedvvmmgrYGHMGWLR----RAKKRDRQ--------IVTAALARVDMVEFRHRQIG---------ELSG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 966918915 574 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSH 625
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrdeGKTMLVSTH 200
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
387-611 |
1.03e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 387 FTARITeLMQVLKDLNH--GKYERTMVS----------QQEKGIegvqviplipGAGEIIIADNIIKFDHVPLATPNGDI 454
Cdd:PRK11176 288 FSSMIA-LMRPLKSLTNvnAQFQRGMAAcqtlfaildlEQEKDE----------GKRVIERAKGDIEFRNVTFTYPGKEV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 L-IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTkpergkLFYVPQRPYmTLGTLRDQV--------IY 525
Cdd:PRK11176 357 PaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL------LDGHDLRDY-TLASLRNQValvsqnvhLF 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 526 PD--------GREDQ-KRKGISDLVLKEYldnvQLGHILEREGGWDSVQDWMDV-LSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:PRK11176 430 NDtianniayARTEQySREQIEEAARMAY----AMDFINKMDNGLDTVIGENGVlLSGGQRQRIAIARALLRDSPILILD 505
|
250
....*....|....*.
gi 966918915 596 ECTSAVSVDVEGYIYS 611
Cdd:PRK11176 506 EATSALDTESERAIQA 521
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
455-599 |
1.45e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.23 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPL------------FGGRLTKP---------ERGKLFYVPQR-P 512
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearvegevrlFGRNIYSPdvdpievrrEVGMVFQYPNPfP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 513 YMTlgtlrdqvIYPDGREDQKRKGIsdLVLKEYLDNVqLGHILEREGGWDSVQDWMD----VLSGGEKQRMAMARLFYHK 588
Cdd:PRK14267 99 HLT--------IYDNVAIGVKLNGL--VKSKKELDER-VEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMK 167
|
170
....*....|.
gi 966918915 589 PQFAILDECTS 599
Cdd:PRK14267 168 PKILLMDEPTA 178
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
456-603 |
1.46e-06 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 49.67 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------KPE--RGKLFYVP--QRPYMTLgTLRDQV 523
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkEPAeaRRRLGFVSdsTGLYDRL-TARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 524 IYPDGREDQKRKGISDLVlKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSV 603
Cdd:cd03266 100 EYFAGLYGLKGDELTARL-EELADRLGMEELLDRRVG---------GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
450-599 |
1.58e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.08 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 450 PNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE------------RGKLFYVPQRPymtl 516
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFnGILKPTSGEVLIKGEpikydkksllevRKTVGIVFQNP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 517 gtlRDQVIYPDGREDQKRkGISDLVLKEylDNVQ--LGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:PRK13639 88 ---DDQLFAPTVEEDVAF-GPLNLGLSK--EEVEkrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
....*
gi 966918915 595 DECTS 599
Cdd:PRK13639 162 DEPTS 166
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
456-625 |
1.70e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------------KPERGKLFYVPQRPYMTLG---T 518
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtlspgklQALRRDIQFIFQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 519 LRDQVIYP-------DGREDQKRkgisdlvLKEYLDNVQLghilEREGGWDSVQDWmdvlSGGEKQRMAMARLFYHKPQF 591
Cdd:PRK10261 420 VGDSIMEPlrvhgllPGKAAAAR-------VAWLLERVGL----LPEHAWRYPHEF----SGGQRQRICIARALALNPKV 484
|
170 180 190
....*....|....*....|....*....|....*...
gi 966918915 592 AILDECTSAVSVDVEGYIYSHC----RKVGITLFTVSH 625
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLldlqRDFGIAYLFISH 522
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
434-596 |
1.82e-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: 49.46 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 434 IIADNIIKFdhvplatPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTK-P--ER 502
Cdd:cd03218 1 LRAENLSKR-------YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIvglvkpdsGKIL-LDGQDITKlPmhKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 503 GKL--FYVPQRPYMTLG-TLRDQV-----IYPDGREDQKRKgisdlvLKEYLDNVQLGHILEREGgwdsvqdwmDVLSGG 574
Cdd:cd03218 73 ARLgiGYLPQEASIFRKlTVEENIlavleIRGLSKKEREEK------LEELLEEFHITHLRKSKA---------SSLSGG 137
|
170 180
....*....|....*....|..
gi 966918915 575 EKQRMAMARLFYHKPQFAILDE 596
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDE 159
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
448-604 |
1.91e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.64 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 448 ATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGR----LTKPERGKL--FYVPQR 511
Cdd:CHL00131 15 ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaykileGDI--LFKGEsildLEPEERAHLgiFLAFQY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 512 PYMTLGT-----LRdqVIYPDGREDQKRKGISDL----VLKEYLDNVQLG-HILER---EGgwdsvqdwmdvLSGGEKQR 578
Cdd:CHL00131 93 PIEIPGVsnadfLR--LAYNSKRKFQGLPELDPLefleIINEKLKLVGMDpSFLSRnvnEG-----------FSGGEKKR 159
|
170 180
....*....|....*....|....*....
gi 966918915 579 ---MAMARLfyhKPQFAILDECTSAVSVD 604
Cdd:CHL00131 160 neiLQMALL---DSELAILDETDSGLDID 185
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
456-625 |
1.93e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.12 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWP-------LFGGRLTKPE----RGKLFYVPQRP--YMTLGTLRDQ 522
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEaesgqiiIDGDLLTEENvwdiRHKIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 523 VIYpdGREDqkrKGISdlvLKEYLDNVQlgHILEREGgwdsVQDWMDV----LSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:PRK13650 103 VAF--GLEN---KGIP---HEEMKERVN--EALELVG----MQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190
....*....|....*....|....*....|...
gi 966918915 599 SAvsVDVEG------YIYSHCRKVGITLFTVSH 625
Cdd:PRK13650 169 SM--LDPEGrlelikTIKGIRDDYQMTVISITH 199
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
463-599 |
2.23e-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: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 463 VQSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE--------RG-------------------KLFYVPQRPYM 514
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILaGKLKPNLGKFDDPPDwdeildefRGselqnyftkllegdvkvivKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 515 TLGTLRDQVIYPDGREdqkrkgisdlVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:cd03236 103 VKGKVGELLKKKDERG----------KLDELVDQLELRHVLDRN---------IDQLSGGELQRVAIAAALARDADFYFF 163
|
....*
gi 966918915 595 DECTS 599
Cdd:cd03236 164 DEPSS 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
471-599 |
2.38e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 471 ICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE--------RG-------------------KLFYVPQRPYMTLGTLRDQ 522
Cdd:PRK13409 104 ILGPNGIGKTTAVKILsGELIPNLGDYEEEPSwdevlkrfRGtelqnyfkklyngeikvvhKPQYVDLIPKVFKGKVREL 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966918915 523 VIYPDGREdqkrkgisdlVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:PRK13409 184 LKKVDERG----------KLDEVVERLGLENILDRD---------ISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
439-625 |
3.99e-06 |
|
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: 48.35 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 439 IIKFDHVP---LATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPERGKLfy 507
Cdd:cd03258 1 MIELKNVSkvfGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptsGSVL-VDGTDLTLLSGKEL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 508 VPQRPYMTL----------GTLRDQVIYP-----DGREDQKRKgisdlvLKEYLDNVQLGhilereggwDSVQDWMDVLS 572
Cdd:cd03258 78 RKARRRIGMifqhfnllssRTVFENVALPleiagVPKAEIEER------VLELLELVGLE---------DKADAYPAQLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 966918915 573 GGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALdpetTQSILALLRDINRELGLTIVLITH 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
418-599 |
9.46e-06 |
|
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: 49.14 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 418 IEGVQVIPLIPGAGEIIIADNIIKFdhvplaTPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFG--- 494
Cdd:TIGR01271 1203 IENPHAQKCWPSGGQMDVQGLTAKY------TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiq 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 495 ------GRLTKPERGKLF-YVPQRPYMTLGTLRDQVIYPDGREDQKRKGISDLV-LKEYLDNV--QLGHILErEGGWdsv 564
Cdd:TIGR01271 1277 idgvswNSVTLQTWRKAFgVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVgLKSVIEQFpdKLDFVLV-DGGY--- 1352
|
170 180 190
....*....|....*....|....*....|....*
gi 966918915 565 qdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:TIGR01271 1353 -----VLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
459-625 |
1.18e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.40 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 459 LNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGG-------RLTKPE----RGKLFYVPQRP--YMTLGTLRDQVIY 525
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgeLLTAENvwnlRRKIGMVFQNPdnQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 526 pdGREDQkrkGISDLVLKEYLDNVQLG-HILE---REGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:PRK13642 106 --GMENQ---GIPREEMIKRVDEALLAvNMLDfktREPA---------RLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180
....*....|....*....|....*...
gi 966918915 602 S----VDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK13642 172 DptgrQEIMRVIHEIKEKYQLTVLSITH 199
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
436-599 |
1.29e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 46.39 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 436 ADNIIKFDHVPLATPNGDILiRDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplfGGRLTKPERGKLFYVPQRPyMT 515
Cdd:cd03213 6 FRNLTVTVKSSPSKSGKQLL-KNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------AGRRTGLGVSGEVLINGRP-LD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 516 LGTLRDQVIYPDgREDQKrkgISDLVLKEYLDNVQLghilereggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:cd03213 77 KRSFRKIIGYVP-QDDIL---HPTLTVRETLMFAAK----------------LRGLSGGERKRVSIALELVSNPSLLFLD 136
|
....
gi 966918915 596 ECTS 599
Cdd:cd03213 137 EPTS 140
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
454-625 |
1.30e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 47.29 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 454 ILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLF--------YVPQRPYMTLGTLRDQVIY 525
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTL--------SRLMTPAHGHVWldgehiqhYASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 526 PdgredqkrkgiSDLVLKEYLDNVQLGH----ILEREGGWDSVQDWM-------------DVLSGGEKQRMAMARLFYHK 588
Cdd:PRK10253 93 P-----------GDITVQELVARGRYPHqplfTRWRKEDEEAVTKAMqatgithladqsvDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 966918915 589 PQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK10253 162 TAIMLLDEPTTWLdishQIDLLELLSELNREKGYTLAAVLH 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
437-625 |
1.37e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.44 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 437 DNIIKFDHVPLATpNGD--ILIRDLNFEVQSGANVLICGPNGCGKSSLFRvlgelwpLFGGrLTKPERGKLFYvpqrpym 514
Cdd:PRK13648 5 NSIIVFKNVSFQY-QSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAK-------LMIG-IEKVKSGEIFY------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 515 tlgtlRDQVIYPDGREDQkRKGISdLVLK-----------EY-----LDNVQLGH---------ILEREGGWDSVQDWMD 569
Cdd:PRK13648 69 -----NNQAITDDNFEKL-RKHIG-IVFQnpdnqfvgsivKYdvafgLENHAVPYdemhrrvseALKQVDMLERADYEPN 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 570 VLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV----GITLFTVSH 625
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITH 201
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
455-637 |
1.55e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 455 LIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWplfggrltKPERGKLFYVPQ----------------------RP 512
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL--------NPEKGEILFERQsikkdlctyqkqlcfvghrsgiNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 513 YMTLgtlRDQVIYpDGREDQKRKGISDLVLKeyldnVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFA 592
Cdd:PRK13540 88 YLTL---RENCLY-DIHFSPGAVGITELCRL-----FSLEHLIDYPCG---------LLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 966918915 593 ILDEctSAVSVD------VEGYIYSHCRKVGITLFTVSHRKSLWK--HHEYYL 637
Cdd:PRK13540 150 LLDE--PLVALDelslltIITKIQEHRAKGGAVLLTSHQDLPLNKadYEEYHL 200
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
466-604 |
1.59e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 466 GANVLICGPNGCGKSSLFRVL--------GELWPLFGGRLtkperGklfYVPQRPYMTLG-TLRDQVIypDGREDQKRKg 536
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMagvdkefeGEARPAPGIKV-----G---YLPQEPQLDPEkTVRENVE--EGVAEVKAA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 537 isdlvLKEYlDNV-------------------QLGHILEREGGWDS---VQDWMD------------VLSGGEKQRMAMA 582
Cdd:PRK11819 102 -----LDRF-NEIyaayaepdadfdalaaeqgELQEIIDAADAWDLdsqLEIAMDalrcppwdakvtKLSGGERRRVALC 175
|
170 180
....*....|....*....|....*
gi 966918915 583 RLFYHKPQFAILDECTS---AVSVD 604
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNhldAESVA 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
456-615 |
1.60e-05 |
|
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: 45.89 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---KPERGK---------LFYVPqrpymtlgtlrdqv 523
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITldgKPVTRRsprdairagIAYVP-------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 524 iypdgrEDQKRKGisdLVLKEYL-DNVQLGHILereggwdsvqdwmdvlSGGEKQRMAMARLFYHKPQFAILDECTsaVS 602
Cdd:cd03215 82 ------EDRKREG---LVLDLSVaENIALSSLL----------------SGGNQQKVVLARWLARDPRVLILDEPT--RG 134
|
170
....*....|....*
gi 966918915 603 VDVEG--YIYSHCRK 615
Cdd:cd03215 135 VDVGAkaEIYRLIRE 149
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
456-498 |
1.65e-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: 46.37 E-value: 1.65e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT 498
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
473-601 |
1.93e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 46.70 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 473 GPNGCGKSSLFRV---LGELWPLF---------GGRLTKPE------RGKLFYVPQRPYMTLGTLRDQVIYpdGREDQKR 534
Cdd:PRK14243 43 GPSGCGKSTILRCfnrLNDLIPGFrvegkvtfhGKNLYAPDvdpvevRRRIGMVFQKPNPFPKSIYDNIAY--GARINGY 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966918915 535 KGISDLVLKEYLDNVQLghilereggWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:PRK14243 121 KGDMDELVERSLRQAAL---------WDEVKDKLKqsglSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
471-606 |
4.78e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 45.48 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 471 ICGPNGCGKSSLFRVL-GELWPLFGGRLTkpERGKLFYVPQrpYMTL---GTLRDQViypdgREDQKRKGISDLVLKEYL 546
Cdd:cd03237 30 ILGPNGIGKTTFIKMLaGVLKPDEGDIEI--ELDTVSYKPQ--YIKAdyeGTVRDLL-----SSITKDFYTHPYFKTEIA 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 547 DNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDEcTSAvSVDVE 606
Cdd:cd03237 101 KPLQIEQILDRE-----VPE----LSGGELQRVAIAACLSKDADIYLLDE-PSA-YLDVE 149
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
453-599 |
5.45e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 45.39 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 453 DILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLFY-------------------VPQRPY 513
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCF--------ARLLTPQSGTVFLgdkpismlssrqlarrlalLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 514 MTLG-TLRDQVIYpdGR------------EDQKRkgisdlvLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMA 580
Cdd:PRK11231 87 TPEGiTVRELVAY--GRspwlslwgrlsaEDNAR-------VNQAMEQTRINHLADR-----RLTD----LSGGQRQRAF 148
|
170
....*....|....*....
gi 966918915 581 MARLFYHKPQFAILDECTS 599
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTT 167
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
457-504 |
5.48e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.07 E-value: 5.48e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 966918915 457 RDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGK 504
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLI--------AGILEPTSGR 82
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
571-626 |
7.43e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 7.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 571 LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD----VEGYIYSHCRKVGITLFTVSHR 626
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
431-596 |
7.80e-05 |
|
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: 44.85 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 431 GEIIIADNIIKFdhvplaTPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFG---------GRLTKPE 501
Cdd:cd03289 1 GQMTVKDLTAKY------TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGdiqidgvswNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 502 RGKLF-YVPQRPYMTLGTLRdQVIYPDGR-EDQKRKGISDLV-LKEYLDNV--QLGHILErEGGWdsvqdwmdVLSGGEK 576
Cdd:cd03289 75 WRKAFgVIPQKVFIFSGTFR-KNLDPYGKwSDEEIWKVAEEVgLKSVIEQFpgQLDFVLV-DGGC--------VLSHGHK 144
|
170 180
....*....|....*....|
gi 966918915 577 QRMAMARLFYHKPQFAILDE 596
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDE 164
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
456-610 |
8.72e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRpymtlgTLRDQVIYPDgrEDQKRK 535
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD------GLANGIVYIS--EDRKRD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 536 GisdLVL----KE--------YLDN--VQLGHILEREggwdSVQDWMDV--------------LSGGEKQRMAMARLFYH 587
Cdd:PRK10762 340 G---LVLgmsvKEnmsltalrYFSRagGSLKHADEQQ----AVSDFIRLfniktpsmeqaiglLSGGNQQKVAIARGLMT 412
|
170 180
....*....|....*....|...
gi 966918915 588 KPQFAILDECTSAVSVDVEGYIY 610
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIY 435
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
439-625 |
9.98e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 44.72 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 439 IIKFDHVPLA-TPNGDILIR---DLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWPLFGG--------------RLTK 499
Cdd:PRK13643 1 MIKFEKVNYTyQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLnGLLQPTEGKvtvgdivvsstskqKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 500 PER---GKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKgiSDLVLKEYLDNVQLGHILEREGGWDsvqdwmdvLSGGEK 576
Cdd:PRK13643 81 PVRkkvGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEK--AEKIAAEKLEMVGLADEFWEKSPFE--------LSGGQM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 966918915 577 QRMAMARLFYHKPQFAILDECTSAVSVDVE---GYIYSHCRKVGITLFTVSH 625
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
456-609 |
1.03e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSS----LFRVL---GELW----PL--FGGRLTKPERGKLFYVPQRPYMTLGT-LRD 521
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIWfdgqPLhnLNRRQLLPVRHRIQVVFQDPNSSLNPrLNV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 522 QVIYPDG------------REDQKRKgisdlVLKEY-LDNvqlghilereggwDSVQDWMDVLSGGEKQRMAMARLFYHK 588
Cdd:PRK15134 382 LQIIEEGlrvhqptlsaaqREQQVIA-----VMEEVgLDP-------------ETRHRYPAEFSGGQRQRIAIARALILK 443
|
170 180
....*....|....*....|.
gi 966918915 589 PQFAILDECTSAVSVDVEGYI 609
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQI 464
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
451-628 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 451 NGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTK------------------------------- 499
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqkglirqlrqhvgfvfqn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 500 ----PERGKLFYVPQRPYMTLGTLRDQVIyPDGREDQKRKGISdlvlkeyldnvqlghilereGGWDSvqdWMDVLSGGE 575
Cdd:PRK11264 94 fnlfPHRTVLENIIEGPVIVKGEPKEEAT-ARARELLAKVGLA--------------------GKETS---YPRRLSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 966918915 576 KQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVG---ITLFTVSHRKS 628
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqekRTMVIVTHEMS 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
435-606 |
1.36e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 435 IADNIIKFD-HVPLATPNGDILIR---------DLNFEVQSGA----NVL-ICGPNGCGKSSLFRVL-GELWPLFGGRLT 498
Cdd:PRK13409 319 IRPEPIEFEeRPPRDESERETLVEypdltkklgDFSLEVEGGEiyegEVIgIVGPNGIGKTTFAKLLaGVLKPDEGEVDP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 499 KPergKLFYVPQrpYMTlgtlRDQviypDGREDQKRKGISDLVLKEYLDN-----VQLGHILEREggwdsvqdwMDVLSG 573
Cdd:PRK13409 399 EL---KISYKPQ--YIK----PDY----DGTVEDLLRSITDDLGSSYYKSeiikpLQLERLLDKN---------VKDLSG 456
|
170 180 190
....*....|....*....|....*....|...
gi 966918915 574 GEKQRMAMARLFYHKPQFAILDEcTSAvSVDVE 606
Cdd:PRK13409 457 GELQRVAIAACLSRDADLYLLDE-PSA-HLDVE 487
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
440-626 |
1.49e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 440 IKFDHVPLA-TPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLgelwplFggRLTKPERGK-------------- 504
Cdd:PLN03130 1238 IKFEDVVLRyRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNAL------F--RIVELERGRilidgcdiskfglm 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 505 -----LFYVPQRPYMTLGTLRDQViypDGREDQkrkgiSDLVLKEYLDNVQLGHILEREG-GWDS-VQDWMDVLSGGEKQ 577
Cdd:PLN03130 1310 dlrkvLGIIPQAPVLFSGTVRFNL---DPFNEH-----NDADLWESLERAHLKDVIRRNSlGLDAeVSEAGENFSVGQRQ 1381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 966918915 578 RMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRK--VGITLFTVSHR 626
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREefKSCTMLIIAHR 1432
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
450-596 |
1.50e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.45 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 450 PNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVL--------GELWplFGGRLT---KP-ERGkLFYVPQR----PY 513
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagleritsGEIW--IGGRVVnelEPaDRD-IAMVFQNyalyPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 514 MTL-----------GTLRDQViypdgredQKRkgisdlvLKEYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRM 579
Cdd:PRK11650 91 MSVrenmayglkirGMPKAEI--------EER-------VAEAARILELEPLLDRkprE------------LSGGQRQRV 143
|
170
....*....|....*..
gi 966918915 580 AMARLFYHKPQFAILDE 596
Cdd:PRK11650 144 AMGRAIVREPAVFLFDE 160
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
456-596 |
1.53e-04 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 43.87 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGR-LT--KPER----G--------KLFyvpqrPYM 514
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFYRPtsgriLFDGRdITglPPHRiarlGiartfqnpRLF-----PEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 515 T------------LGTLRDQVIYPDGREDQKRKGISDLVLkEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMA 582
Cdd:COG0411 95 TvlenvlvaaharLGRGLLAALLRLPRARREEREARERAE-ELLERVGLADRADEPAG---------NLSYGQQRRLEIA 164
|
170
....*....|....
gi 966918915 583 RLFYHKPQFAILDE 596
Cdd:COG0411 165 RALATEPKLLLLDE 178
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
464-599 |
1.74e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.78 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 464 QSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE--------RG-------------------KLFYVPQRPYMT 515
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILsGELKPNLGDYDEEPSwdevlkrfRGtelqdyfkklangeikvahKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 516 LGTLRDQVIYPDGREdqkrkgisdlVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:COG1245 177 KGTVRELLEKVDERG----------KLDELAEKLGLENILDRD---------ISELSGGELQRVAIAAALLRDADFYFFD 237
|
....
gi 966918915 596 ECTS 599
Cdd:COG1245 238 EPSS 241
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
457-601 |
2.68e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 457 RDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT------------KPERGKLFYVPQRPYMTLGTLRDQVI 524
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnlkdinlKWWRSKIGVVSQDPLLFSNSIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 525 YP-------------------------DGREDQKRKGISDLvlKEYLDNVQLGHILEREGGWDSVQDW--MDV------- 570
Cdd:PTZ00265 482 YSlyslkdlealsnyynedgndsqenkNKRNSCRAKCAGDL--NDMSNTTDSNELIEMRKNYQTIKDSevVDVskkvlih 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 966918915 571 --------------------LSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:PTZ00265 560 dfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
458-625 |
3.06e-04 |
|
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: 42.48 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 458 DLNFEVQSGANVLICGPNGCGKSSLFR-VLGELWPLFGGRL--------TKPERGKLFYVPQR----PYMTLGTLRDQVI 524
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNlIAGFETPQSGRVLingvdvtaAPPADRPVSMLFQEnnlfAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 525 YPDGR---EDQKRkgisdlvLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:cd03298 96 SPGLKltaEDRQA-------IEVALARVGLAGLEKRLPG---------ELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180
....*....|....*....|....*...
gi 966918915 602 S----VDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03298 160 DpalrAEMLDLVLDLHAETKMTVLMVTH 187
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
571-638 |
4.26e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 42.65 E-value: 4.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966918915 571 LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSHRKSLWKH---HEYYLH 638
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHvssHVIFLH 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-642 |
7.39e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.01 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 471 ICGPNGCGKSSLFRVLGELWP-----------LFGGRLTKPER---------GKLFyvpQRPYMTLGTLRDQVIYpdGRE 530
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDkvsgyrysgdvLLGGRSIFNYRdvlefrrrvGMLF---QRPNPFPMSIMDNVLA--GVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 531 DQKrkgisdLVLKEYLDNVQLGHILErEGGWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAV----S 602
Cdd:PRK14271 127 AHK------LVPRKEFRGVAQARLTE-VGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALdpttT 199
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 966918915 603 VDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGR 642
Cdd:PRK14271 200 EKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGR 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
458-603 |
8.65e-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: 42.36 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 458 DLNFEVQSGANVLICGPNGCGKSSLFRVL-------GELWplFGGR----LT----KPERGKLFYVPQRPY------MTL 516
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALlrlipseGEIR--FDGQdldgLSrralRPLRRRMQVVFQDPFgslsprMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 517 GtlrdQVI-------YPDGREDQKRKGISDLvlkeyLDNVQL-GHILER---EggwdsvqdwmdvLSGGEKQRMAMARLF 585
Cdd:COG4172 382 G----QIIaeglrvhGPGLSAAERRARVAEA-----LEEVGLdPAARHRyphE------------FSGGQRQRIAIARAL 440
|
170 180
....*....|....*....|
gi 966918915 586 YHKPQFAILDECTSA--VSV 603
Cdd:COG4172 441 ILEPKLLVLDEPTSAldVSV 460
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
459-625 |
9.55e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 41.46 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 459 LNFEVQSGANVLICGPNGCGKSSLFRVLGELWP-----LFGGR----LTKPE----RGKL-------FYVPQRPYMTLGT 518
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPgsgsiQFAGQpleaWSAAElarhRAYLsqqqtppFAMPVFQYLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 519 lrdqviyPDG-REDQKRKGISDLVlkeylDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMAMARLFYH-----KP--Q 590
Cdd:PRK03695 95 -------PDKtRTEAVASALNEVA-----EALGLDDKLGR-----SVNQ----LSGGEWQRVRLAAVVLQvwpdiNPagQ 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 966918915 591 FAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSH 625
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSH 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
456-602 |
1.18e-03 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 40.95 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPERGKLF----YVPQ-RPYMTLGTLRDQV- 523
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLtGELRPtsgtaYINGYSIRTDRKAARqslgYCPQfDALFDELTVREHLr 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966918915 524 IYpdGREDQKRKGISDLVLKEYLDNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVS 602
Cdd:cd03263 98 FY--ARLKGLPKSEIKEEVELLLRVLGLTDKANKR-----ART----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
456-601 |
1.18e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.94 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 456 IRDLNFEVQSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLFYvpqrPYMTLGTLRDQVIypdgrEDQKRK 535
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN--------RLIEPTRGQVLI----DGVDIAKISDAEL-----REVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 536 GISdLVLKEY--------LDNVQLGHIL-------EREGGWDSVQD---------WMDVLSGGEKQRMAMARLFYHKPQF 591
Cdd:PRK10070 107 KIA-MVFQSFalmphmtvLDNTAFGMELaginaeeRREKALDALRQvglenyahsYPDELSGGMRQRVGLARALAINPDI 185
|
170
....*....|
gi 966918915 592 AILDECTSAV 601
Cdd:PRK10070 186 LLMDEAFSAL 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
546-629 |
1.31e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.92 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 546 LDNVQLGHILEREGGWDSVQDWMDVL----------------SGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYI 609
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLeqlglgkrldhlpaqlSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
90 100
....*....|....*....|....
gi 966918915 610 ----YSHCRKVGITLFTVSHRKSL 629
Cdd:PRK10584 186 adllFSLNREHGTTLILVTHDLQL 209
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
471-615 |
1.92e-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: 40.63 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 471 ICGPNGCGKSSL-----FrVLGE---------LWPL-FGGRLTKPergklfyVPQRPYMTLgtlrdQVIYPDGREDQKRK 535
Cdd:cd03275 27 IIGPNGSGKSNLmdaisF-VLGEksshlrsknLKDLiYRARVGKP-------DSNSAYVTA-----VYEDDDGEEKTFRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966918915 536 GISDLV-----------LKEYLDNVQLGHILER-------EGGWDSV----------QDwMDVLSGGEKQRMAMARLF-- 585
Cdd:cd03275 94 IITGGSssyringkvvsLKEYNEELEKINILVKarnflvfQGDVESIasknppgkrfRD-MDNLSGGEKTMAALALLFai 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 966918915 586 --YHKPQFAILDECTSA---VSVD-VEGYIYSHCRK 615
Cdd:cd03275 173 hsYQPAPFFVLDEVDAAldnTNVGkVASYIREQAGP 208
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
456-483 |
6.07e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 6.07e-03
10 20
....*....|....*....|....*...
gi 966918915 456 IRDLNFEVQSGANvLICGPNGCGKSSLF 483
Cdd:pfam13476 9 FRDQTIDFSKGLT-LITGPNGSGKTTIL 35
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
456-486 |
7.00e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.22 E-value: 7.00e-03
10 20 30
....*....|....*....|....*....|.
gi 966918915 456 IRDLNFEVQSGANVLIcGPNGCGKSSLFRVL 486
Cdd:COG3593 14 IKDLSIELSDDLTVLV-GENNSGKSSILEAL 43
|
|
| |
