|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
75-715 |
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: 685.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 75 EEDFKLAEAEKLLVAQQLKKKATNnlvEPGLNKEFLKHLQMLAKIMIPQAFCYETGLLSVHTFCLISRTFLSIYVAALEG 154
Cdd:TIGR00954 44 RGDKSGKEELTIVGKHSTIEGAKK---KAHVNGVFLGKLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 155 ALVKFIVRKDIKQFALVLLKWFGIAIPATFVNSMIRFLESKLSLAFRTRLVRHSYRLYFKNQNYYRVSNLDGRIENADHR 234
Cdd:TIGR00954 121 QIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 235 LTEDISVFANSVAHLYSSLTKPCFDLMLIGLALMRsskkmkANIITGPALSIGVIALTAHILRIVSPKFGQLVSEEANRY 314
Cdd:TIGR00954 201 LTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLT------ALGSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 315 GYLRHIHSRIITNAEEIAFYGGHKVEMQQLRQAYNRLVNQMTTIFNQKLWFIMLEQFFMKYVWSGTGMIMVSLPILtgsd 394
Cdd:TIGR00954 275 GEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIF---- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 395 vglgTVPNTAISESRVSERTQYLTTARNLLISAADAIERLMSSYKEIVSLAGYTFRVAGMMDVFEETALGVYCKTsvMES 474
Cdd:TIGR00954 351 ----DKTHPAFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRP--RVE 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 475 NQSNGIIEFRNGKPIA-KGRIIYSDdpkNMsISLRAVPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSG 553
Cdd:TIGR00954 425 EIESGREGGRNSNLVPgRGIVEYQD---NG-IKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 554 LWPIYAGELHIPRPVKdvpcMFYIPQRPYMSIGSLCDQIIYPDTREDMKRKHITENELRSILKMVSLEHIAQRD-SFDVV 632
Cdd:TIGR00954 501 LWPVYGGRLTKPAKGK----LFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREgGWSAV 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 633 RDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYEIAKGMGITLLTITHRPTLWKYHTHILEFDGLGN 712
Cdd:TIGR00954 577 QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGG 656
|
...
gi 386763404 713 WQF 715
Cdd:TIGR00954 657 YQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
116-390 |
3.30e-110 |
|
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: 334.96 E-value: 3.30e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 116 LAKIMIPQAFCYETGLLSVHTFCLISRTFLSIYVAALEGALVKFIVRKDIKQFALVLLKWFGIAIPATFVNSMIRFLESK 195
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 196 LSLAFRTRLVRHSYRLYFKNQNYYRVSNLDGRIENADHRLTEDISVFANSVAHLYSSLTKPCFDLMLIGLALMRSSKKMk 275
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWR- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 276 aniitGPALSIGVIALTAHILRIVSPKFGQLVSEEANRYGYLRHIHSRIITNAEEIAFYGGHKVEMQQLRQAYNRLVNQM 355
Cdd:pfam06472 160 -----GPAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHM 234
|
250 260 270
....*....|....*....|....*....|....*
gi 386763404 356 TTIFNQKLWFIMLEQFFMKYVWSGTGMIMVSLPIL 390
Cdd:pfam06472 235 RRILRRRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
144-718 |
7.25e-91 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 295.18 E-value: 7.25e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 144 FLSIYVAALEGALVKFIVR--------------KDIKQFALVLLKWFGIAIPATFVNSMIRFLESKLSLAFRTRLVRHSY 209
Cdd:COG4178 25 GLLALLLLLTLASVGLNVLlnfwnrdfydalqaRDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 210 RLYFKNQNYYRVSNLDGRIENADHRLTEDISVFANSVAHLYSSLTKPCFDLMLIGLALMRSSKKMKANI----ITGP-AL 284
Cdd:COG4178 105 DRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLISFIGILWSLSGSLTFTLggysITIPgYM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 285 SIGVIA------LTAHIL--RIVSPKFGQLVSEeAN-RYGyLRHIHSriitNAEEIAFYGGHKVEMQQLRQAYNRLVNQM 355
Cdd:COG4178 185 VWAALIyaiigtLLTHLIgrPLIRLNFEQQRRE-ADfRFA-LVRVRE----NAESIALYRGEAAERRRLRRRFDAVIANW 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 356 ttifnqklWFIMLEQFFMKYVWSGTGMIMVSLPILTGS------DVGLGTVPNTAISESRVSertqyltTARNLLISaad 429
Cdd:COG4178 259 --------RRLIRRQRNLTFFTTGYGQLAVIFPILVAApryfagEITLGGLMQAASAFGQVQ-------GALSWFVD--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 430 aierlmsSYKEIVSLAGYTFRVAGMMDVFEETAlgvycktsvmesnqsngiiefrnGKPIAKGRIIYSDDPknmSISLRA 509
Cdd:COG4178 321 -------NYQSLAEWRATVDRLAGFEEALEAAD-----------------------ALPEAASRIETSEDG---ALALED 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 510 VPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKdvpcMFYIPQRPYMSIGSLC 589
Cdd:COG4178 368 LTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGAR----VLFLPQRPYLPLGTLR 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 590 DQIIYPDTREDmkrkhITENELRSILKMVSLEHIAQRdsFDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAV 669
Cdd:COG4178 444 EALLYPATAEA-----FSDAELREALEAVGLGHLAER--LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 386763404 670 SIDVESSIYEIAKGM--GITLLTITHRPTLWKYHTHILEFDGLGNWQFRKM 718
Cdd:COG4178 517 DEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPA 567
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
505-713 |
2.22e-82 |
|
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: 258.62 E-value: 2.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 505 ISLRAVPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPvkdvPCMFYIPQRPYMS 584
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG----EDLLFLPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 585 IGSLCDQIIYPdtredmkrkhitenelrsilkmvslehiaqrdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:cd03223 77 LGTLREQLIYP---------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 386763404 665 CTSAVSIDVESSIYEIAKGMGITLLTITHRPTLWKYHTHILEFDGLGNW 713
Cdd:cd03223 118 ATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
505-693 |
4.76e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.99 E-value: 4.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 505 ISLRAVPVVTPNCDIVVPkLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI---PRPVKDVPC----MFYI 577
Cdd:COG4619 1 LELEGLSFRVGGKPILSP-VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdgkPLSAMPPPEwrrqVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 578 PQRPYMSIGSLCDQIIYPDTredMKRKHITENELRSILKMVSL-EHIAQRDsfdVVRdwkdiLSGGEKQRMAIARLFYHR 656
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQ---LRERKFDRERALELLERLGLpPDILDKP---VER-----LSGGERQRLALIRALLLQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 386763404 657 PRYALLDECTSAVSID----VESSIYEIAKGMGITLLTITH 693
Cdd:COG4619 149 PDVLLLDEPTSALDPEntrrVEELLREYLAEEGRAVLWVSH 189
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
504-709 |
1.03e-27 |
|
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: 118.32 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 504 SISLRAVPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVP------CMFY 576
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILInGVDLSDLDpaswrrQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 577 IPQRPYMSIGSLCDQIiypdtreDMKRKHITENELRSILKMVSLEHIAQR--DSFDVVrdwkdI------LSGGEKQRMA 648
Cdd:COG4988 416 VPQNPYLFAGTIRENL-------RLGRPDASDEELEAALEAAGLDEFVAAlpDGLDTP-----LgeggrgLSGGQAQRLA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386763404 649 IARLFYHRPRYALLDECTSavSIDVES------SIYEIAKgmGITLLTITHRPTLWKYHTHILEFDG 709
Cdd:COG4988 484 LARALLRDAPLLLLDEPTA--HLDAETeaeilqALRRLAK--GRTVILITHRLALLAQADRILVLDD 546
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
524-709 |
4.39e-26 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 105.16 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP------CMFYIPQRPYmsigslcdqiIYPD 596
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDgVDLRDLDleslrkNIAYVPQDPF----------LFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 597 TredmkrkhITENelrsilkmvslehiaqrdsfdvvrdwkdILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESS 676
Cdd:cd03228 91 T--------IREN----------------------------ILSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*
gi 386763404 677 IYEI--AKGMGITLLTITHRPTLWKYHTHILEFDG 709
Cdd:cd03228 135 ILEAlrALAKGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
106-694 |
3.27e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.64 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 106 NKEFLKHLQMLAKIMIPQAfcyetGLLSVHTFCLISRTFLSIYVAALEGALV-KFIVRKDIKQFALVLLKWFGIAIPATF 184
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYR-----GLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSALLLLLLLLLGLALLRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 185 VNSMIRFLESKLSLAF----RTRLVRHSYRL---YFKNQNYYRVSNldgrienadhRLTEDISVFANSVAHLYSSLTKPC 257
Cdd:COG1132 77 LSYLQRYLLARLAQRVvadlRRDLFEHLLRLplsFFDRRRTGDLLS----------RLTNDVDAVEQFLAHGLPQLVRSV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 258 FdLMLIGLALMrsskkmkanIITGPALSIGVIA---LTAHILRIVSPKFGQLVSEEANRYGYL-RHIHsRIITNAEEIAF 333
Cdd:COG1132 147 V-TLIGALVVL---------FVIDWRLALIVLLvlpLLLLVLRLFGRRLRKLFRRVQEALAELnGRLQ-ESLSGIRVVKA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 334 YGGHKVEMQQLRQAYNRLVNqmttiFNQKLWFIMLEQFFMKYVWSGTGMIMV----SLPILTGSdVGLGTVpntaisesr 409
Cdd:COG1132 216 FGREERELERFREANEELRR-----ANLRAARLSALFFPLMELLGNLGLALVllvgGLLVLSGS-LTVGDL--------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 410 vserTQYLTTARNLLisaaDAIERLMSSYKEIVSLAGYTFRVAGMMDVFEEtalgVYCKTSVMESNQSNGIIEFRN---G 486
Cdd:COG1132 281 ----VAFILYLLRLF----GPLRQLANVLNQLQRALASAERIFELLDEPPE----IPDPPGAVPLPPVRGEIEFENvsfS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 487 kpiakgriiYSDDPKnmsislravpvvtpncdiVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-P 565
Cdd:COG1132 349 ---------YPGDRP------------------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdG 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 566 RPVKDVP------CMFYIPQRPYMSIGSLCDQIIYPdtredmkRKHITENELRSILKMVSLEHIAQR--DSFD-VVRDWK 636
Cdd:COG1132 402 VDIRDLTleslrrQIGVVPQDTFLFSGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFIEAlpDGYDtVVGERG 474
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 637 DILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYE-IAKGM-GITLLTITHR 694
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEaLERLMkGRTTIVIAHR 534
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
142-697 |
2.38e-24 |
|
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: 108.77 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 142 RTFLSIYVAALEGAL--------VKFIVRKDIKQFALVLLKWFGIAIPATFV-NSMIRFLESKLSLAFRTRL-VRHSYRL 211
Cdd:COG2274 156 RLLLQVLLASLLINLlalatplfTQVVIDRVLPNQDLSTLWVLAIGLLLALLfEGLLRLLRSYLLLRLGQRIdLRLSSRF 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 212 YfknqnyYRVSNLdgRIENADHRLTEDISVFANSVAHLYSSLTKP----CFDL--MLIGLALMrsskkmkanIITGPAL- 284
Cdd:COG2274 236 F------RHLLRL--PLSFFESRSVGDLASRFRDVESIREFLTGSlltaLLDLlfVLIFLIVL---------FFYSPPLa 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 285 --SIGVIALTAHILRIVSPKFGQLVSEEANRYGYLRHIHSRIITNAEEIAFYGGHKVEMQQLRQAYNRLVNQMTTIFNQK 362
Cdd:COG2274 299 lvVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLS 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 363 LWFIMLEQFFMKY-----VWSGTGMIMvslpiltGSDVGLGTvpntaisesrvsertqyLTTARNLLISAADAIERLMSS 437
Cdd:COG2274 379 NLLSTLSGLLQQLatvalLWLGAYLVI-------DGQLTLGQ-----------------LIAFNILSGRFLAPVAQLIGL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 438 YKEIVSLAGYTFRVAGMMDVFEETALGvyckTSVMESNQSNGIIEFRNgkpiakgriiysddpknmsISLRAVPVVTPnc 517
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEG----RSKLSLPRLKGDIELEN-------------------VSFRYPGDSPP-- 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 518 diVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVP------CMFYIPQRPYMSIGSLCD 590
Cdd:COG2274 490 --VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdGIDLRQIDpaslrrQIGVVLQDVFLFSGTIRE 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 591 QIIypdtredMKRKHITENELRSILKMVSLEHIAQR--DSFD-VVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:COG2274 568 NIT-------LGDPDATDEEIIEAARLAGLHDFIEAlpMGYDtVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
570 580 590
....*....|....*....|....*....|....*.
gi 386763404 668 AvsIDVES------SIYEIAKGMgiTLLTITHRPTL 697
Cdd:COG2274 641 A--LDAETeaiileNLRRLLKGR--TVIIIAHRLST 672
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
519-709 |
6.21e-24 |
|
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: 100.30 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPCMF-YIPQRPYMS------------ 584
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEKERKRIgYVPQRRSIDrdfpisvrdvvl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 585 ---IGSLCDQIIYpdTREDMKRkhITEnelrsILKMVSLEHIAQR--DSfdvvrdwkdiLSGGEKQRMAIARLFYHRPRY 659
Cdd:cd03235 93 mglYGHKGLFRRL--SKADKAK--VDE-----ALERVGLSELADRqiGE----------LSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386763404 660 ALLDECTSAVSIDVESSIYEIAKGM---GITLLTITH-RPTLWKYHTHILEFDG 709
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELrreGMTILVVTHdLGLVLEYFDRVLLLNR 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
505-697 |
3.40e-23 |
|
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: 96.90 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 505 ISLRAVPVVTPNCD-IVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDV------PCMFY 576
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDgADISQWdpnelgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 577 IPQrpymsigslcDQIIYPDTredmkrkhITENelrsilkmvslehiaqrdsfdvvrdwkdILSGGEKQRMAIARLFYHR 656
Cdd:cd03246 81 LPQ----------DDELFSGS--------IAEN----------------------------ILSGGQRQRLGLARALYGN 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386763404 657 PRYALLDECTSAVSIDVESSIYEIAKGM---GITLLTITHRPTL 697
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPET 158
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
524-667 |
6.60e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 95.41 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPCMF------YIPQ----RPYMSIGslcDQI 592
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdGQDLTDDERKSlrkeigYVFQdpqlFPRLTVR---ENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386763404 593 IYPDTREDMKRKHITEnELRSILKMVSLEHIAQRdsfdVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:pfam00005 81 RLGLLLKGLSKREKDA-RAEEALEKLGLGDLADR----PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
524-708 |
1.35e-22 |
|
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: 96.38 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPC------MFYIPQRPYmsigslcDQIIYPD 596
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgKDLTKLSLkelrrkVGLVFQNPD-------DQFFGPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 597 TRED---------MKRKHItENELRSILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:cd03225 93 VEEEvafglenlgLPEEEI-EERVEEALELVGLEGLRDRSPFT--------LSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 386763404 668 AVSIDVESSIYEIAKGM---GITLLTITHRPTLWKYH-THILEFD 708
Cdd:cd03225 164 GLDPAGRRELLELLKKLkaeGKTIIIVTHDLDLLLELaDRVIVLE 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
524-697 |
7.62e-22 |
|
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: 92.69 E-value: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIprpvkdvpcmfyipqrpymsigslcdqiiypdtredmKR 603
Cdd:cd00267 18 VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-------------------------------------DG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 604 KHITENELRSILKMVSLehIAQrdsfdvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYEIAKG 683
Cdd:cd00267 61 KDIAKLPLEELRRRIGY--VPQ-------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170
....*....|....*..
gi 386763404 684 M---GITLLTITHRPTL 697
Cdd:cd00267 126 LaeeGRTVIIVTHDPEL 142
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
524-696 |
2.11e-21 |
|
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: 98.68 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP------CMFYIPQRPYmsigslcdqiIYPD 596
Cdd:COG4987 354 LSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgVDLRDLDeddlrrRIAVVPQRPH----------LFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 597 T-REDMK--RKHITENELRSILKMVSLEhiaqrdsfDVVRDWKD-----------ILSGGEKQRMAIARLFYHRPRYALL 662
Cdd:COG4987 424 TlRENLRlaRPDATDEELWAALERVGLG--------DWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 386763404 663 DECTSavSIDVES------SIYEIAKGMgiTLLTITHRPT 696
Cdd:COG4987 496 DEPTE--GLDAATeqallaDLLEALAGR--TVLLITHRLA 531
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
501-693 |
5.50e-21 |
|
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: 91.81 E-value: 5.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 501 KNMSISLRAVPVVTPncdivvpkLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPcmfyiPQ 579
Cdd:cd03259 4 KGLSKTYGSVRALDD--------LSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgRDVTGVP-----PE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 580 R-------------PYMSIGslcDQIIYPDTREDMKRKHITENELRsILKMVSLEHIAQRdsfdvvrdWKDILSGGEKQR 646
Cdd:cd03259 71 RrnigmvfqdyalfPHLTVA---ENIAFGLKLRGVPKAEIRARVRE-LLELVGLEGLLNR--------YPHELSGGQQQR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 386763404 647 MAIARLFYHRPRYALLDECTSAvsIDVESSIY------EIAKGMGITLLTITH 693
Cdd:cd03259 139 VALARALAREPSLLLLDEPLSA--LDAKLREElreelkELQRELGITTIYVTH 189
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
501-697 |
6.67e-21 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 92.80 E-value: 6.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 501 KNMSISLRAVPVVTPncdivvpkLTLCIEPG-VHLLItGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVP------ 572
Cdd:COG1120 5 ENLSVGYGGRPVLDD--------VSLSLPPGeVTALL-GPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLASLSrrelar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 573 CMFYIPQRPYMSIGSLCDQII----YP-------DTREDmkRKHITEnelrsILKMVSLEHIAQRDsfdvVRDwkdiLSG 641
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELValgrYPhlglfgrPSAED--REAVEE-----ALERTGLEHLADRP----VDE----LSG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 642 GEKQRMAIARLFYHRPRYALLDECTSAV----SIDVESSIYEIAKGMGITLLTITHRPTL 697
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLHDLNL 200
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
501-697 |
7.29e-21 |
|
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: 90.57 E-value: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 501 KNMSISLRAVPVVTPncdivvpkLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP------C 573
Cdd:cd03214 3 ENLSVGYGGRTVLDD--------LSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDgKDLASLSpkelarK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 574 MFYIPQrpymsigslcdqiiypdtredmkrkhitenelrsILKMVSLEHIAQRDSfdvvrdwkDILSGGEKQRMAIARLF 653
Cdd:cd03214 75 IAYVPQ----------------------------------ALELLGLAHLADRPF--------NELSGGERQRVLLARAL 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386763404 654 YHRPRYALLDECTSAV----SIDVESSIYEIAKGMGITLLTITHRPTL 697
Cdd:cd03214 113 AQEPPILLLDEPTSHLdiahQIELLELLRRLARERGKTVVMVLHDLNL 160
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
524-693 |
1.11e-20 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 91.63 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI------PRPVKDVPCMF-YIPQRPYmsigslcDQIIYPD 596
Cdd:COG1122 20 VSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkditKKNLRELRRKVgLVFQNPD-------DQLFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 597 TRED----MKRKHITENELR----SILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSA 668
Cdd:COG1122 93 VEEDvafgPENLGLPREEIRerveEALELVGLEHLADRPPHE--------LSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180
....*....|....*....|....*...
gi 386763404 669 VSIDVESSIYEIAKGM---GITLLTITH 693
Cdd:COG1122 165 LDPRGRRELLELLKRLnkeGKTVIIVTH 192
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
501-693 |
1.96e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 91.30 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 501 KNMSISLRAVPVVTPncdivvpkLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPCMF-YIP 578
Cdd:COG1121 10 ENLTVSYGGRPVLED--------VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPRRARRRIgYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 579 QRP------------------YMSIGSLCdqiiyPDTREDmkRKHITEnelrsILKMVSLEHIAQRDsfdvVRDwkdiLS 640
Cdd:COG1121 82 QRAevdwdfpitvrdvvlmgrYGRRGLFR-----RPSRAD--REAVDE-----ALERVGLEDLADRP----IGE----LS 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 386763404 641 GGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYEIAKGM---GITLLTITH 693
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrreGKTILVVTH 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
519-695 |
2.86e-20 |
|
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: 89.46 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP-----CMFYIPQRPymsigslcdqI 592
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgEPIRDARedyrrRLAYLGHAD----------G 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 593 IYPD-T-RE------DMKRKHITENELRSILKMVSLEHIAQRDsfdvVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:COG4133 86 LKPElTvREnlrfwaALYGLRADREAIDEALEAVGLAGLADLP----VRQ----LSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 386763404 665 CTSAvsIDVESS--IYEI-----AKGmGITLLTiTHRP 695
Cdd:COG4133 158 PFTA--LDAAGValLAELiaahlARG-GAVLLT-THQP 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
504-697 |
3.24e-20 |
|
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: 94.66 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 504 SISLRAVPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPCMF------Y 576
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLADADADSwrdqiaW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 577 IPQRPYMSIGSLCDQIIypdtredMKRKHITENELRSILKMVSLEHIAQ--RDSFD-VVRDWKDILSGGEKQRMAIARLF 653
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIR-------LARPDASDAEIREALERAGLDEFVAalPQGLDtPIGEGGAGLSGGQAQRLALARAF 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 386763404 654 YHRPRYALLDECTSAVSIDVESSIYE-IAKGM-GITLLTITHRPTL 697
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEaLRALAqGRTVLLVTHRLAL 519
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
520-693 |
5.36e-20 |
|
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: 89.07 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPCMF-YIPQR----PYMSIGslcDQII 593
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgEPVTGPGPDRgYVFQQdallPWLTVL---DNVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 594 YPDTREDMKRKHITEnELRSILKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSI-- 671
Cdd:cd03293 96 LGLELQGVPKAEARE-RAEELLELVGLSGFENA--------YPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAlt 166
|
170 180
....*....|....*....|....
gi 386763404 672 --DVESSIYEIAKGMGITLLTITH 693
Cdd:cd03293 167 reQLQEELLDIWRETGKTVLLVTH 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
518-693 |
2.82e-19 |
|
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: 87.29 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 518 DIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPcmfyIPQR------------PYMS 584
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgKDITNLP----PHKRpvntvfqnyalfPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 585 IGslcDQIIYPDTREDMKRKHITEnELRSILKMVSLEHIAQRDSfdvvrdwkDILSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:cd03300 89 VF---ENIAFGLRLKKLPKAEIKE-RVAEALDLVQLEGYANRKP--------SQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190
....*....|....*....|....*....|...
gi 386763404 665 CTSAVSI----DVESSIYEIAKGMGITLLTITH 693
Cdd:cd03300 157 PLGALDLklrkDMQLELKRLQKELGITFVFVTH 189
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
504-697 |
3.30e-19 |
|
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: 86.87 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 504 SISLRAVPVVTPNCDI-VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI---------PRPVKDVpc 573
Cdd:cd03245 2 RIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldPADLRRN-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 574 MFYIPQRPYMSIGSLCDQIIypdtredMKRKHITENELRSILKMVSLEHIAQR--DSFDV-VRDWKDILSGGEKQRMAIA 650
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNIT-------LGAPLADDERILRAAELAGVTDFVNKhpNGLDLqIGERGRGLSGGQRQAVALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 386763404 651 RLFYHRPRYALLDECTSAVSIDVESSIYEIAKGM--GITLLTITHRPTL 697
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
525-709 |
3.98e-19 |
|
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: 86.77 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 525 TLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRpvKDVPCMF-------------YIPQR----PYMSIGs 587
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDG--TDISKLSekelaafrrrhigFVFQSfnllPDLTAL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 588 lcDQIIYPDTredMKRKHITENELR--SILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDEC 665
Cdd:cd03255 101 --ENVELPLL---LAGVPKKERRERaeELLERVGLGDRLNHYPSE--------LSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 386763404 666 TSAvsIDVESS------IYEIAKGMGITLLTITHRPTLWKYHTHILEF-DG 709
Cdd:cd03255 168 TGN--LDSETGkevmelLRELNKEAGTTIVVVTHDPELAEYADRIIELrDG 216
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
520-693 |
1.13e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 85.70 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGElhiprPV--------KDVPCMFYIP-----------QR 580
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA-----PDegevlldgKDIYDLDVDVlelrrrvgmvfQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 581 PYMSIGSLCDQIIYPDTREDMKRKHITENELRSILKMVSLehiaqrdsFDVVRDWKDI--LSGGEKQRMAIARLFYHRPR 658
Cdd:cd03260 90 PNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAAL--------WDEVKDRLHAlgLSGGQQQRLCLARALANEPE 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 386763404 659 YALLDECTSAVSI----DVESSIYEIAKGMgiTLLTITH 693
Cdd:cd03260 162 VLLLDEPTSALDPistaKIEELIAELKKEY--TIVIVTH 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
505-694 |
4.57e-18 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 88.04 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 505 ISLRAVPVVTPNCDI-VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPI---YAGELHI-PRPVKDVP------C 573
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLdGRDLLELSealrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 574 MFYIPQRPYMSIGSLC--DQIIYPDTREDMKRKHITEnELRSILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIAR 651
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgDQIAEALENLGLSRAEARA-RVLELLEAVGLERRLDRYPHQ--------LSGGQRQRVAIAM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 386763404 652 LFYHRPRYALLDECTSA----VSIDVESSIYEIAKGMGITLLTITHR 694
Cdd:COG1123 156 ALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHD 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
501-693 |
5.89e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 81.00 E-value: 5.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 501 KNMSISLRAVPVVTPncdiVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI------PRPVKDVPC- 573
Cdd:COG1124 5 RNLSVSYGQGGRRVP----VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtRRRRKAFRRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 574 MFYIPQRPY------MSIgslcDQIIypdtREDMKRKHITENELR--SILKMVSLEHiAQRDSFdvvrdwKDILSGGEKQ 645
Cdd:COG1124 81 VQMVFQDPYaslhprHTV----DRIL----AEPLRIHGLPDREERiaELLEQVGLPP-SFLDRY------PHQLSGGQRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386763404 646 RMAIARLFYHRPRYALLDECTSAVSIDVESSI----YEIAKGMGITLLTITH 693
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEIlnllKDLREERGLTYLFVSH 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
528-693 |
6.02e-17 |
|
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: 84.57 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 528 IEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPC---------MFYIPQRPY------MSIGslcDQ 591
Cdd:COG1123 288 LRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLTKLSRrslrelrrrVQMVFQDPYsslnprMTVG---DI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 592 IIYP-DTREDMKRKHITEnELRSILKMVSL-EHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAv 669
Cdd:COG1123 365 IAEPlRLHGLLSRAERRE-RVAELLERVGLpPDLADRYPHE--------LSGGQRQRVAIARALALEPKLLILDEPTSA- 434
|
170 180 190
....*....|....*....|....*....|..
gi 386763404 670 sIDVesSIY--------EIAKGMGITLLTITH 693
Cdd:COG1123 435 -LDV--SVQaqilnllrDLQRELGLTYLFISH 463
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
520-693 |
2.03e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.30 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPcmfyiPQR-------------PYMSI 585
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdGRDVTGLP-----PEKrnvgmvfqdyalfPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 586 GslcDQIIYPDTREDMKRKHITEnELRSILKMVSLEHIAQRDsfdvVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDEC 665
Cdd:COG3842 95 A---ENVAFGLRMRGVPKAEIRA-RVAELLELVGLEGLADRY----PHQ----LSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190
....*....|....*....|....*....|....
gi 386763404 666 TSAvsIDVE------SSIYEIAKGMGITLLTITH 693
Cdd:COG3842 163 LSA--LDAKlreemrEELRRLQRELGITFIYVTH 194
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
524-693 |
3.43e-16 |
|
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: 77.68 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI---PRPVKD-VPCMFYIPQRPymsigslcDQIIYPDT-- 597
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkPIKAKErRKSIGYVMQDV--------DYQLFTDSvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 ---REDMKRKHITENELRSILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAV---SI 671
Cdd:cd03226 91 eelLLGLKELDAGNEQAETVLKDLDLYALKERHPLS--------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLdykNM 162
|
170 180
....*....|....*....|..
gi 386763404 672 DVESSIYEIAKGMGITLLTITH 693
Cdd:cd03226 163 ERVGELIRELAAQGKAVIVITH 184
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
524-706 |
4.05e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 78.18 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPG-VHLLItGPNGCGKSSLFRILSGLWPIYAGELHI--------PRPVKdvPCMFYIPQR----PYMSIGSLCD 590
Cdd:COG1131 19 VSLTVEPGeIFGLL-GPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardPAEVR--RRIGYVPQEpalyPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 591 QI--IYPDTREDMKRKhiteneLRSILKMVSLEHIAQRdsfdVVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSA 668
Cdd:COG1131 96 FFarLYGLPRKEARER------IDELLELFGLTDAADR----KVGT----LSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 386763404 669 VsiDVESS------IYEIAK-GMGItLLTithrptlwkyhTHILE 706
Cdd:COG1131 162 L--DPEARrelwelLRELAAeGKTV-LLS-----------THYLE 192
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
500-695 |
4.30e-16 |
|
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: 82.02 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 500 PKNMSISLRAVPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP------ 572
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgVPVSSLDqdevrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 573 CMFYIPQRPYMSIGSLCDQIIypdtredMKRKHITENELRSILKMVSLEHIAQR--DSFD-VVRDWKDILSGGEKQRMAI 649
Cdd:TIGR02868 410 RVSVCAQDAHLFDTTVRENLR-------LARPDATDEELWAALERVGLADWLRAlpDGLDtVLGEGGARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386763404 650 ARLFYHRPRYALLDECTSAVSIDVESSIYE-IAKGM-GITLLTITHRP 695
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEdLLAALsGRTVVLITHHL 530
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
524-693 |
6.31e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.21 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDV-PCMFYIPQR----PYMSIgslCDQIIYPdt 597
Cdd:COG1116 30 VSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgKPVTGPgPDRGVVFQEpallPWLTV---LDNVALG-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 redMKRKHITENELRSI----LKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVsiDV 673
Cdd:COG1116 105 ---LELRGVPKAERRERarelLELVGLAGFEDA--------YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGAL--DA 171
|
170 180
....*....|....*....|....*.
gi 386763404 674 ------ESSIYEIAKGMGITLLTITH 693
Cdd:COG1116 172 ltrerlQDELLRLWQETGKTVLFVTH 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
519-709 |
9.37e-16 |
|
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: 77.27 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP-----CMF-YIPQRPYMSIGSLCDQ 591
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDgIDIRDISrkslrSMIgVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 592 IIYpdtredmKRKHITENELRSILKMVSLEHIAQR--DSFD-VVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSA 668
Cdd:cd03254 97 IRL-------GRPNATDEEVIEAAKEAGAHDFIMKlpNGYDtVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386763404 669 VSIDVESSIYE-IAKGM-GITLLTITHRPTLWKYHTHILEFDG 709
Cdd:cd03254 170 IDTETEKLIQEaLEKLMkGRTSIIIAHRLSTIKNADKILVLDD 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
524-694 |
1.21e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP------CMFYIPQRPYMSIGSLCDQIIypd 596
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNgQPIADYSeaalrqAISVVSQRVHLFSATLRDNLL--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 597 tredMKRKHITENELRSILKMVSLEHIAQRDsfDVVRDWkdI------LSGGEKQRMAIARLFYHRPRYALLDECTSAVS 670
Cdd:PRK11160 436 ----LAAPNASDEALIEVLQQVGLEKLLEDD--KGLNAW--LgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
170 180
....*....|....*....|....*...
gi 386763404 671 IDVESSI----YEIAKGMgiTLLTITHR 694
Cdd:PRK11160 508 AETERQIlellAEHAQNK--TVLMITHR 533
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
524-709 |
1.59e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 76.24 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIprpvKDVPC---------MF------YIPQR----PYMS 584
Cdd:COG1136 27 VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI----DGQDIsslserelaRLrrrhigFVFQFfnllPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 585 IgslCDQIIYPDTREDMKRKHITEnELRSILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:COG1136 103 A---LENVALPLLLAGVSRKERRE-RARELLERVGLGDRLDHRPSQ--------LSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386763404 665 CTSAV----SIDVESSIYEIAKGMGITLLTITHRPTLWKYHTHILEF-DG 709
Cdd:COG1136 171 PTGNLdsktGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLrDG 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
520-693 |
2.35e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.45 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL--------HIP---RPVKDV---PCMFyipqrPYMSI 585
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqditHVPaenRHVNTVfqsYALF-----PHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 586 gslCDQIIYpdtreDMKRKHITENELRS----ILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYAL 661
Cdd:PRK09452 104 ---FENVAF-----GLRMQKTPAAEITPrvmeALRMVQLEEFAQRKPHQ--------LSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386763404 662 LDECTSAVSidvessiYEIAKGM-----------GITLLTITH 693
Cdd:PRK09452 168 LDESLSALD-------YKLRKQMqnelkalqrklGITFVFVTH 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
528-705 |
4.56e-15 |
|
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: 74.43 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 528 IEPGVHLLITGPNGCGKSSLfriLSGLwpiyAGELHIPRPVKDVPCMF-YIPQRPYMSIGSLCDQIIYpDTREDMKRkhi 606
Cdd:cd03250 28 VPKGELVAIVGPVGSGKSSL---LSAL----LGELEKLSGSVSVPGSIaYVSQEPWIQNGTIRENILF-GKPFDEER--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 607 teneLRSILKMVSLEhiaqRDsFDVV--RDWKDI------LSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIY 678
Cdd:cd03250 97 ----YEKVIKACALE----PD-LEILpdGDLTEIgekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIF 167
|
170 180 190
....*....|....*....|....*....|.
gi 386763404 679 E---IAKGMGI-TLLTITHRPTLWKYHTHIL 705
Cdd:cd03250 168 EnciLGLLLNNkTRILVTHQLQLLPHADQIV 198
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
524-705 |
4.75e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.00 E-value: 4.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPCMFY------IPQRPYMSIGSLCDQIIYPD 596
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgVPLVQYDHHYLhrqvalVGQEPVLFSGSVRENIAYGL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 597 TREDMkrkhiteNELRSILKMVSLEHIAQRDSFD---VVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDV 673
Cdd:TIGR00958 580 TDTPD-------EEIMAAAKAANAHDFIMEFPNGydtEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190
....*....|....*....|....*....|...
gi 386763404 674 ESSIYEIAKGMGITLLTITHR-PTLWKYHtHIL 705
Cdd:TIGR00958 653 EQLLQESRSRASRTVLLIAHRlSTVERAD-QIL 684
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
524-695 |
5.31e-15 |
|
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: 75.51 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSG-LWPIYAGELHI---PRPVKDVpcmFYIPQRpymsIG----SLCDQIIYP 595
Cdd:COG1119 22 ISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLfgeRRGGEDV---WELRKR----IGlvspALQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 596 DTREDM----------KRKHITENEL---RSILKMVSLEHIAQRdSFDVvrdwkdiLSGGEKQRMAIARLFYHRPRYALL 662
Cdd:COG1119 95 ETVLDVvlsgffdsigLYREPTDEQReraRELLELLGLAHLADR-PFGT-------LSQGEQRRVLIARALVKDPELLIL 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 386763404 663 DECTSavSIDVES------SIYEIAKGMGITLLTITHRP 695
Cdd:COG1119 167 DEPTA--GLDLGArelllaLLDKLAAEGAPTLVLVTHHV 203
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
520-693 |
6.83e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 75.15 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP---------CMfyiPQRPYMSIGSLC 589
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgRPLAAWSpwelarrraVL---PQHSSLAFPFTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 590 DQII----YPDTREDMKRKHIteneLRSILKMVSLEHIAQRDsfdvVRDwkdiLSGGEKQRMAIAR----LFYHR---PR 658
Cdd:COG4559 93 EEVValgrAPHGSSAAQDRQI----VREALALVGLAHLAGRS----YQT----LSGGEQQRVQLARvlaqLWEPVdggPR 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 386763404 659 YALLDECTSAVSIDVESSIYEIAKGM---GITLLTITH 693
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLarrGGGVVAVLH 198
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
519-693 |
8.35e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.37 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPC------MFYIPQRPYMSIGSLCDQ 591
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEgEDISTLKPeiyrqqVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 592 IIYPdtrEDMKRKHITENELRSILKMVSL-EHIAQrdsfdvvrdwKDI--LSGGEKQRMAIARLFYHRPRYALLDECTSA 668
Cdd:PRK10247 101 LIFP---WQIRNQQPDPAIFLDDLERFALpDTILT----------KNIaeLSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180
....*....|....*....|....*....
gi 386763404 669 VS----IDVESSIYEIAKGMGITLLTITH 693
Cdd:PRK10247 168 LDesnkHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
520-693 |
1.08e-14 |
|
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: 73.44 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVP------CMFYipQR----PYMSIgsl 588
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIgGRDVTDLPpkdrdiAMVF--QNyalyPHMTV--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 589 CDQIIYPDTREDMKRKHITEnELRSILKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDECTSA 668
Cdd:cd03301 90 YDNIAFGLKLRKVPKDEIDE-RVREVAELLQIEHLLDR--------KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180
....*....|....*....|....*....
gi 386763404 669 VS----IDVESSIYEIAKGMGITLLTITH 693
Cdd:cd03301 161 LDaklrVQMRAELKRLQQRLGTTTIYVTH 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
528-694 |
1.71e-14 |
|
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: 73.42 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 528 IEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP------CMFYIPQRPYMSIGSLCDQIIY--PD-T 597
Cdd:cd03253 24 IPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgQDIREVTldslrrAIGVVPQDTVLFNDTIGYNIRYgrPDaT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 REDM----KRKHITEnelrSILKMvslehiaqRDSFDVV---RDWKdiLSGGEKQRMAIARLFYHRPRYALLDECTSAVS 670
Cdd:cd03253 104 DEEVieaaKAAQIHD----KIMRF--------PDGYDTIvgeRGLK--LSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
170 180
....*....|....*....|....*...
gi 386763404 671 IDVESSIYE----IAKGMgiTLLTITHR 694
Cdd:cd03253 170 THTEREIQAalrdVSKGR--TTIVIAHR 195
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
515-693 |
2.31e-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: 72.07 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 515 PNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVK-DVPCMFYIPQRPYMSIGSLCDQI 592
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgEPLDySRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 593 IYPDTREDM----KRKHITENELRSI----LKMVSLEHIAQRDSfdvvrdwkDILSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:TIGR01166 82 FAADVDQDVafgpLNLGLSEAEVERRvreaLTAVGASGLRERPT--------HCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 386763404 665 CTSAVSIDVESSIYEIAKGM---GITLLTITH 693
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRLraeGMTVVISTH 185
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
524-693 |
8.27e-14 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 70.12 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPG-VHLLItGPNGCGKSSLFRILSGLWPIYAGELHI------PRPVKDVPCMFYIPQRPYmsigslcdqiIYPD 596
Cdd:cd03230 19 ISLTVEKGeIYGLL-GPNGAGKTTLIKIILGLLKPDSGEIKVlgkdikKEPEEVKRRIGYLPEEPS----------LYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 597 tredmkrkhitenelrsilkMVSLEHIaqrdsfdvvrdwkdILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESS 676
Cdd:cd03230 88 --------------------LTVRENL--------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180
....*....|....*....|
gi 386763404 677 IYEIAKGM---GITLLTITH 693
Cdd:cd03230 134 FWELLRELkkeGKTILLSSH 153
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
519-694 |
1.06e-13 |
|
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: 71.42 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPR-PVKDVPC------MFYIPQRPYMSIGSLCDQ 591
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvDIRDLNLrwlrsqIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 592 IIY--PDTREDMKRKHITENELRSILkmVSLEhiaqrDSFD-VVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSA 668
Cdd:cd03249 97 IRYgkPDATDEEVEEAAKKANIHDFI--MSLP-----DGYDtLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190
....*....|....*....|....*....|.
gi 386763404 669 vsIDVESSiYEIAKG-----MGITLLTITHR 694
Cdd:cd03249 170 --LDAESE-KLVQEAldramKGRTTIVIAHR 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
536-696 |
1.15e-13 |
|
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: 70.79 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 536 ITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKDVPC--MFYIPQR-------------PYMSIGSlcdQIIYPDTRED 600
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkINLPPQQrkiglvfqqyalfPHLNVRE---NLAFGLKRKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 601 MKRKHITENElrsILKMVSLEHIAQRDSfdvvrdwkDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIY-- 678
Cdd:cd03297 105 NREDRISVDE---LLDLLGLDHLLNRYP--------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLpe 173
|
170 180
....*....|....*....|
gi 386763404 679 --EIAKGMGITLLTITHRPT 696
Cdd:cd03297 174 lkQIKKNLNIPVIFVTHDLS 193
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
520-693 |
1.21e-13 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 71.00 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPCMF---------YIPQRPY------M 583
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGKDLLKLSRRLrkirrkeiqMVFQDPMsslnprM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 584 SIGslcDQIIYPDTREDMKRKHiTENELRSILKMVSL---EHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYA 660
Cdd:cd03257 100 TIG---EQIAEPLRIHGKLSKK-EARKEAVLLLLVGVglpEEVLNRYPHE--------LSGGQRQRVAIARALALNPKLL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 386763404 661 LLDECTSAVSIDVESSI----YEIAKGMGITLLTITH 693
Cdd:cd03257 168 IADEPTSALDVSVQAQIldllKKLQEELGLTLLFITH 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
526-693 |
1.30e-13 |
|
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: 70.83 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 526 LCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL--------HIPRPVKDVPcmfYIPQR----PYMSIGslcDQII 593
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkditNLPPEKRDIS---YVPQNyalfPHMTVY---KNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 594 YPDTREDMKRKHItENELRSILKMVSLEHIAQRDSfdvvrdwkDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDV 673
Cdd:cd03299 94 YGLKKRKVDKKEI-ERKVLEIAEMLGIDHLLNRKP--------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180
....*....|....*....|....
gi 386763404 674 ESSIYE----IAKGMGITLLTITH 693
Cdd:cd03299 165 KEKLREelkkIRKEFGVTVLHVTH 188
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
520-664 |
1.68e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 72.41 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPcmfyiPQR-------------PYMSI 585
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIgGRDVTDLP-----PKDrniamvfqsyalyPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 586 GslcDQIIYPDTREDMKRKHITEnELRSILKMVSLEHIAQRdsfdvvrdwK-DILSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:COG3839 93 Y---ENIAFPLKLRKVPKAEIDR-RVREAAELLGLEDLLDR---------KpKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
520-709 |
4.88e-13 |
|
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: 69.04 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPCMFY------IPQRPYMSIGSLCDQI 592
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgKPISQYEHKYLhskvslVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 593 IYPDTREDMKRkhITENELRS-----ILKMvslEHIAQRDsfdvVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:cd03248 109 AYGLQSCSFEC--VKEAAQKAhahsfISEL---ASGYDTE----VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 386763404 668 AVSID----VESSIYEIAKGMgiTLLTITHRPTLWKYHTHILEFDG 709
Cdd:cd03248 180 ALDAEseqqVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDG 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
503-693 |
1.55e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 503 MSISLRAVpvvtpNC----DIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-------PRPV--- 568
Cdd:COG4161 1 MSIQLKNI-----NCfygsHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdfSQKPsek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 569 ------KDVPCMFyipQR----PYMSIgsLCDQIIYPDTREDMKRKHITEnELRSILKMVSLEHIAQRdsfdvvrdWKDI 638
Cdd:COG4161 76 airllrQKVGMVF---QQynlwPHLTV--MENLIEAPCKVLGLSKEQARE-KAMKLLARLRLTDKADR--------FPLH 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386763404 639 LSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYEIAK---GMGITLLTITH 693
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRelsQTGITQVIVTH 199
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
515-708 |
1.59e-12 |
|
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: 67.52 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 515 PNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP------CMFYIPQRPYMSIGS 587
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgVDISKIGlhdlrsRISIIPQDPVLFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 588 LcdqiiypdtRE--DMKRKHiTENELRSILKMVSL-EHI-AQRDSFD-VVRDWKDILSGGEKQRMAIARLFYHRPRYALL 662
Cdd:cd03244 94 I---------RSnlDPFGEY-SDEELWQALERVGLkEFVeSLPGGLDtVVEEGGENLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386763404 663 DECTSAVSIDVESSIYEIAKGM--GITLLTITHRptlwkYHThILEFD 708
Cdd:cd03244 164 DEATASVDPETDALIQKTIREAfkDCTVLTIAHR-----LDT-IIDSD 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
524-697 |
3.60e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 66.61 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI--------PRpvKDVPcmfYIPQRpymsIGslcdqIIYP 595
Cdd:COG2884 21 VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlKR--REIP---YLRRR----IG-----VVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 596 DTR--EDM--------------KRKHITENELRSILKMVSLEHIAqrDSFdvvrdwKDILSGGEKQRMAIARLFYHRPRY 659
Cdd:COG2884 87 DFRllPDRtvyenvalplrvtgKSRKEIRRRVREVLDLVGLSDKA--KAL------PHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386763404 660 ALLDECTSAVsiDVESS------IYEIAKgMGITLLTITHRPTL 697
Cdd:COG2884 159 LLADEPTGNL--DPETSweimelLEEINR-RGTTVLIATHDLEL 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
504-693 |
3.68e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.52 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 504 SISLRAVpvvtpnC----DIVVPK-LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPCMfyi 577
Cdd:PRK11000 3 SVTLRNV------TkaygDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgEKRMNDVPPA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 578 pQRpymSIGSLCDQ-IIYP--DTREDM----KRKHITENELRSILKMVS----LEHIAQRDSfdvvrdwKDiLSGGEKQR 646
Cdd:PRK11000 74 -ER---GVGMVFQSyALYPhlSVAENMsfglKLAGAKKEEINQRVNQVAevlqLAHLLDRKP-------KA-LSGGQRQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 386763404 647 MAIARLFYHRPRYALLDECTS----AVSIDVESSIYEIAKGMGITLLTITH 693
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSnldaALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
525-694 |
3.88e-12 |
|
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: 64.76 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 525 TLCIEPG-VHLLItGPNGCGKSSLFRILSGLWPIYAGELHIprpvkdvpcmfyipqrpymsigslCDQIIYPDTREDMKR 603
Cdd:cd03216 20 SLSVRRGeVHALL-GENGAGKSTLMKILSGLYKPDSGEILV------------------------DGKEVSFASPRDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 604 KHITenelrsilkMVSlehiaQrdsfdvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYEIAKG 683
Cdd:cd03216 75 AGIA---------MVY-----Q-------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR 127
|
170
....*....|....
gi 386763404 684 M---GITLLTITHR 694
Cdd:cd03216 128 LraqGVAVIFISHR 141
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
520-676 |
4.14e-12 |
|
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: 66.80 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPG-VHLLItGPNGCGKSSLFRILSGLWPIYAGELHI--------PRPVKDVpcMFYIPQRPYmsigslcd 590
Cdd:COG4555 16 ALKDVSFTAKDGeITGLL-GPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrkePREARRQ--IGVLPDERG-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 591 qiIYPD-TREDMKRKHITENELRSILKMVSLEHIAQRDSFDVVRD--WKDiLSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:COG4555 85 --LYDRlTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDrrVGE-LSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
....*....
gi 386763404 668 AvsIDVESS 676
Cdd:COG4555 162 G--LDVMAR 168
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
518-695 |
4.27e-12 |
|
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: 65.84 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 518 DIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRpvKDVPCMFYIPQRpymsigslcdQIIYPDT 597
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG--TPLAEQRDEPHE----------NILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 REDMK-RKHITEN----------ELRSI---LKMVSLEHIAQRdsfdVVRDwkdiLSGGEKQRMAIARLFYHRPRYALLD 663
Cdd:TIGR01189 81 LPGLKpELSALENlhfwaaihggAQRTIedaLAAVGLTGFEDL----PAAQ----LSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 386763404 664 ECTsaVSIDVES-----SIYE--IAKGmGITLLTiTHRP 695
Cdd:TIGR01189 153 EPT--TALDKAGvallaGLLRahLARG-GIVLLT-THQD 187
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
512-693 |
4.30e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.21 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 512 VVTPNCDIVVPKLTLciepgVHLLitGPNGCGKSSLFRILSGLWPIYAGELHIPRpvKDVP---------CMFYipQR-- 580
Cdd:PRK11432 20 TVIDNLNLTIKQGTM-----VTLL--GPSGCGKTTVLRLVAGLEKPTEGQIFIDG--EDVThrsiqqrdiCMVF--QSya 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 581 --PYMSIGslcDQIIYpdtreDMKRKHITENELRS----ILKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFY 654
Cdd:PRK11432 89 lfPHMSLG---ENVGY-----GLKMLGVPKEERKQrvkeALELVDLAGFEDR--------YVDQISGGQQQRVALARALI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386763404 655 HRPRYALLDECTSAVSIDVESS----IYEIAKGMGITLLTITH 693
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSmrekIRELQQQFNITSLYVTH 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
536-695 |
4.50e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.99 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 536 ITGPNGCGKSSLFRILSGLWPIYAGELHIPRPV----------------KDVPCMFYIPQR-PYMSIgslCDQIIYPDTR 598
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifqidaiklrKEVGMVFQQPNPfPHLSI---YDNIAYPLKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 599 EDMKRKHITENELRSILKMVSLehiaQRDSFDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSI----DVE 674
Cdd:PRK14246 118 HGIKEKREIKKIVEECLRKVGL----WKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsqAIE 193
|
170 180
....*....|....*....|.
gi 386763404 675 SSIYEIAKGMGITLltITHRP 695
Cdd:PRK14246 194 KLITELKNEIAIVI--VSHNP 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
519-693 |
4.74e-12 |
|
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: 64.90 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGL-WP-----------IYAGELHIPRPVKDVPCMFyipQR----PY 582
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLeEPdsgsilidgedLTDLEDELPPLRRRIGMVF---QDfalfPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 583 MSIGslcDQIIYPdtredmkrkhitenelrsilkmvslehiaqrdsfdvvrdwkdiLSGGEKQRMAIARLFYHRPRYALL 662
Cdd:cd03229 91 LTVL---ENIALG-------------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190
....*....|....*....|....*....|....*
gi 386763404 663 DECTSA----VSIDVESSIYEIAKGMGITLLTITH 693
Cdd:cd03229 125 DEPTSAldpiTRREVRALLKSLQAQLGITVVLVTH 159
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
520-694 |
9.27e-12 |
|
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: 64.99 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI---PRPVKDVPCMFYIPQR----PYMSIGslcDQI 592
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkPLDIAARNRIGYLPEErglyPKMKVI---DQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 593 IYPDTREDMKRKHItENELRSILKMVSLEHIAQRdsfdVVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSA---V 669
Cdd:cd03269 92 VYLAQLKGLKKEEA-RRRIDEWLERLELSEYANK----RVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGldpV 162
|
170 180
....*....|....*....|....*
gi 386763404 670 SIDVESSIYEIAKGMGITLLTITHR 694
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
504-697 |
1.10e-11 |
|
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: 67.85 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 504 SISLRAVPVVTPNCDIVVPK-LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL--------HIPRpvkDV--P 572
Cdd:COG4618 330 RLSVENLTVVPPGSKRPILRgVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQWDR---EElgR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 573 CMFYIPQRPymsigSLcdqiiYPDTredmkrkhITENELRsiLKMVSLEHI---AQR-----------DSFD-VVRDWKD 637
Cdd:COG4618 407 HIGYLPQDV-----EL-----FDGT--------IAENIAR--FGDADPEKVvaaAKLagvhemilrlpDGYDtRIGEGGA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386763404 638 ILSGGEKQRMAIARLFYHRPRYALLDECTSavSIDVESS------IyEIAKGMGITLLTITHRPTL 697
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNS--NLDDEGEaalaaaI-RALKARGATVVVITHRPSL 529
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
514-693 |
1.18e-11 |
|
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: 65.30 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 514 TPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPCMFYIPQRpyMSIG------ 586
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgTDLTLLSGKELRKAR--RRIGmifqhf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 587 ------SLCDQIIYPDTREDMKRKHITE--NELrsiLKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPR 658
Cdd:cd03258 92 nllssrTVFENVALPLEIAGVPKAEIEErvLEL---LELVGLEDKADA--------YPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 386763404 659 YALLDECTSAVSIDVESSI----YEIAKGMGITLLTITH 693
Cdd:cd03258 161 VLLCDEATSALDPETTQSIlallRDINRELGLTIVLITH 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
520-693 |
1.18e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.47 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELhiprpvkdvpcmfyipqrpymsigsLCDQIIYPDTRE 599
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-------------------------LAGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 600 DMKR----------KHITEN-----------ELRSILKMVSLEHIAQrdsfdvvrDWKDILSGGEKQRMAIARLFYHRPR 658
Cdd:PRK11247 82 DTRLmfqdarllpwKKVIDNvglglkgqwrdAALQALAAVGLADRAN--------EWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 386763404 659 YALLDECTSAVS----IDVESSIYEIAKGMGITLLTITH 693
Cdd:PRK11247 154 LLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
515-694 |
1.21e-11 |
|
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: 65.20 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 515 PNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAG-------ELHIPRPVKDVPCMFYIPQRPYMSIGS 587
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghDLALADPAWLRRQVGVVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 588 LCDQIIYPDTREDMKRkhitenelrsILKMVSL----EHIAQ-RDSFD-VVRDWKDILSGGEKQRMAIARLFYHRPRYAL 661
Cdd:cd03252 92 IRDNIALADPGMSMER----------VIEAAKLagahDFISElPEGYDtIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 386763404 662 LDECTSAVSIDVESSI----YEIAKGMgiTLLTITHR 694
Cdd:cd03252 162 FDEATSALDYESEHAImrnmHDICAGR--TVIIIAHR 196
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
536-696 |
1.37e-11 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 66.67 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 536 ITGPNGCGKSSLFRILSGLWPIYAGELHIprpvkDVPCMF----------------YIPQR----PYMSIGSlcdQIIYP 595
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVL-----NGRTLFdsrkgiflppekrrigYVFQEarlfPHLSVRG---NLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 596 DTREDMKRKHITENElrsILKMVSLEHIAQRdsfdVVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAVSidvES 675
Cdd:TIGR02142 100 MKRARPSERRISFER---VIELLGIGHLLGR----LPGR----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALD---DP 165
|
170 180
....*....|....*....|....*...
gi 386763404 676 SIYEI-------AKGMGITLLTITHRPT 696
Cdd:TIGR02142 166 RKYEIlpylerlHAEFGIPILYVSHSLQ 193
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
520-664 |
1.42e-11 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 64.55 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPG-VHLLItGPNGCGKSSLFRILSGLWPIYAGELHI--PRPVKDVPCmfyiPQRpymsIGSLCD-QIIYP 595
Cdd:cd03268 15 VLDDISLHVKKGeIYGFL-GPNGAGKTTTMKIILGLIKPDSGEITFdgKSYQKNIEA----LRR----IGALIEaPGFYP 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386763404 596 D--TREDMKRKH----ITENELRSILKMVSLEHIAQRDsfdvVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:cd03268 86 NltARENLRLLArllgIRKKRIDEVLDVVGLKDSAKKK----VKG----FSLGMKQRLGIALALLGNPDLLILDE 152
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
501-664 |
1.52e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.43 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 501 KNMSISLRAVPVVTPncdivvpkLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWP---IYAGELHI-PRPVKDVPcmfy 576
Cdd:COG4136 5 ENLTITLGGRPLLAP--------LSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLnGRRLTALP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 577 IPQR------------PYMSIGslcDQIIY--PDTREDMKRKHITENELRSIlkmvSLEHIAQRDSfdvvrdwkDILSGG 642
Cdd:COG4136 73 AEQRrigilfqddllfPHLSVG---ENLAFalPPTIGRAQRRARVEQALEEA----GLAGFADRDP--------ATLSGG 137
|
170 180
....*....|....*....|..
gi 386763404 643 EKQRMAIARLFYHRPRYALLDE 664
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDE 159
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
505-677 |
1.61e-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: 64.14 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 505 ISLRAVPVVTPNCDIVVPkLTLCIEPGVHLLItGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPCMF-----YIP 578
Cdd:cd03264 1 LQLENLTKRYGKKRALDG-VSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDgQDVLKQPQKLrrrigYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 579 QRPymsigslcdqIIYPD-TREDMKR-----KHITENELRSILKMVsLEHIaqrDSFDVVRDWKDILSGGEKQRMAIARL 652
Cdd:cd03264 79 QEF----------GVYPNfTVREFLDyiawlKGIPSKEVKARVDEV-LELV---NLGDRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180
....*....|....*....|....*
gi 386763404 653 FYHRPRYALLDECTsaVSIDVESSI 677
Cdd:cd03264 145 LVGDPSILIVDEPT--AGLDPEERI 167
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
526-693 |
1.65e-11 |
|
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: 64.79 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 526 LCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL-----HIPRPVKDVPCMFyipQR----PYMSIG---SLCDQII 593
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVilegkQITEPGPDRMVVF---QNysllPWLTVReniALAVDRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 594 YPDTREDMKRKHITENelrsiLKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDV 673
Cdd:TIGR01184 83 LPDLSKSERRAIVEEH-----IALVGLTEAADK--------RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180
....*....|....*....|....
gi 386763404 674 ESSIYE----IAKGMGITLLTITH 693
Cdd:TIGR01184 150 RGNLQEelmqIWEEHRVTVLMVTH 173
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
520-693 |
2.10e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.40 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL--------HIPRPVKDVPCMFyipQR----PYMSIgs 587
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPYQRPINMMF---QSyalfPHMTV-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 588 lcDQIIYPDTREDMKRKHITENELRSILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:PRK11607 109 --EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ--------LSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190
....*....|....*....|....*....|
gi 386763404 668 AVSIDV----ESSIYEIAKGMGITLLTITH 693
Cdd:PRK11607 179 ALDKKLrdrmQLEVVDILERVGVTCVMVTH 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
515-694 |
2.21e-11 |
|
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: 63.10 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 515 PNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPR-PVKDVPC-----MFYIPQRPYMSIGSL 588
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvPVSDLEKalsslISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 589 cdqiiypdtredmkrkhitenelrsilkmvsLEHIAQRdsfdvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTsa 668
Cdd:cd03247 92 -------------------------------RNNLGRR------------FSGGERQRLALARILLQDAPIVLLDEPT-- 126
|
170 180 190
....*....|....*....|....*....|..
gi 386763404 669 VSIDVE------SSIYEIAKGMgiTLLTITHR 694
Cdd:cd03247 127 VGLDPIterqllSLIFEVLKDK--TLIWITHH 156
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
525-695 |
2.32e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.39 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 525 TLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI---------P--RPVKdvpcM-------FyipqrPYMSIG 586
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltalpPaeRPVS----MlfqennlF-----PHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 587 slcdQIIY----PD---TREDMKRkhiteneLRSILKMVSLEHIAQRdsfdvvrdwK-DILSGGEKQRMAIAR-LFYHRP 657
Cdd:COG3840 90 ----QNIGlglrPGlklTAEQRAQ-------VEQALERVGLAGLLDR---------LpGQLSGGQRQRVALARcLVRKRP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 386763404 658 rYALLDECTSAVSIDVESSIY----EIAKGMGITLLTITHRP 695
Cdd:COG3840 150 -ILLLDEPFSALDPALRQEMLdlvdELCRERGLTVLMVTHDP 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
503-693 |
2.49e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 64.27 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 503 MSISLRAVpvvtpNC---------DIvvpklTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI--------- 564
Cdd:PRK11124 1 MSIQLNGI-----NCfygahqalfDI-----TLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsk 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 565 -PRPV------KDVPCMFyipQR----PYMSIgsLCDQIIYPdtredMKRKHITENELRS----ILKMVSLEHIAQRdsf 629
Cdd:PRK11124 71 tPSDKairelrRNVGMVF---QQynlwPHLTV--QQNLIEAP-----CRVLGLSKDQALAraekLLERLRLKPYADR--- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386763404 630 dvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYEIAK---GMGITLLTITH 693
Cdd:PRK11124 138 -----FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRelaETGITQVIVTH 199
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
505-697 |
3.08e-11 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 64.13 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 505 ISLRAVPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIprpvkdvpcmfyipqrpyms 584
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 585 igSLCDQIIYPDTREDMKRKHI---------------TENEL----------RSILKMVSLEHIAQ-RDSFDVV----RD 634
Cdd:cd03256 61 --DGTDINKLKGKALRQLRRQIgmifqqfnlierlsvLENVLsgrlgrrstwRSLFGLFPKEEKQRaLAALERVglldKA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386763404 635 WK--DILSGGEKQRMAIARLFYHRPRYALLDECTSavSIDVESS------IYEIAKGMGITLLTITHRPTL 697
Cdd:cd03256 139 YQraDQLSGGQQQRVAIARALMQQPKLILADEPVA--SLDPASSrqvmdlLKRINREEGITVIVSLHQVDL 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
518-668 |
3.82e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 518 DIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKDVPcmfyipqrpymsigSLCDQIIYPDT 597
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP--------------DVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 REDMKR-----------KHITENELRSI---LKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLF-YHRPRYaLL 662
Cdd:PRK13539 81 RNAMKPaltvaenlefwAAFLGGEELDIaaaLEAVGLAPLAHLPFGY--------LSAGQKRRVALARLLvSNRPIW-IL 151
|
....*.
gi 386763404 663 DECTSA 668
Cdd:PRK13539 152 DEPTAA 157
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
520-705 |
4.03e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 62.64 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKdvpcMFYIPQRpymsiGSLCDQIiyPDTRE 599
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR----VAYVPQR-----SEVPDSL--PLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 600 D---MKR-------KHITENELRSI---LKMVSLEHIAQRdSFDVvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECT 666
Cdd:NF040873 76 DlvaMGRwarrglwRRLTRDDRAAVddaLERVGLADLAGR-QLGE-------LSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 386763404 667 SAVSIDVESSIYEI---AKGMGITLLTITHRPTLWKYHTHIL 705
Cdd:NF040873 148 TGLDAESRERIIALlaeEHARGATVVVVTHDLELVRRADPCV 189
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
501-668 |
8.21e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.25 E-value: 8.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 501 KNMSISLRAVPVVTpncDIvvpklTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP------- 572
Cdd:PRK13548 6 RNLSVRLGGRTLLD---DV-----SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgRPLADWSpaelarr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 573 --CMfyiPQRPYMSIGSLCDQII----YPDTREDMKRKHITENELRSilkmVSLEHIAQRD--SfdvvrdwkdiLSGGEK 644
Cdd:PRK13548 78 raVL---PQHSSLSFPFTVEEVVamgrAPHGLSRAEDDALVAAALAQ----VDLAHLAGRDypQ----------LSGGEQ 140
|
170 180 190
....*....|....*....|....*....|
gi 386763404 645 QRMAIARLF------YHRPRYALLDECTSA 668
Cdd:PRK13548 141 QRVQLARVLaqlwepDGPPRWLLLDEPTSA 170
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
524-695 |
1.05e-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: 61.74 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPrpvkdvpcmfyiPQRPYMSIGSLCDQIIYPDTREDMKR 603
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN------------GGPLDFQRDSIARGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 604 KHITENELRSILKMVSLEHIaqRDSFDVV--RDWKDI----LSGGEKQRMAIARLFYHRPRYALLDECTsaVSIDVeSSI 677
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQV--EEALARVglNGFEDRpvaqLSAGQQRRVALARLLLSGRPLWILDEPT--TALDK-AGV 161
|
170 180
....*....|....*....|....*
gi 386763404 678 YEIAKGM-------GITLLTiTHRP 695
Cdd:cd03231 162 ARFAEAMaghcargGMVVLT-THQD 185
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
538-689 |
1.50e-10 |
|
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: 61.68 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 538 GPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPCmfyiPQRPYMSIGSLcdqiiyPDTREDMKRKHITENelrsiLK 616
Cdd:cd03224 33 GRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITGLPP----HERARAGIGYV------PEGRRIFPELTVEEN-----LL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 617 MVslEHIAQRDSFDVVRDW--------KDI-------LSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYEIA 681
Cdd:cd03224 98 LG--AYARRRAKRKARLERvyelfprlKERrkqlagtLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAI 175
|
170
....*....|.
gi 386763404 682 KGM---GITLL 689
Cdd:cd03224 176 RELrdeGVTIL 186
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
520-694 |
2.31e-10 |
|
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: 61.48 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPC------MFYIPQRPYMSIGSLCDQI 592
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDgHDVRDYTLaslrrqIGLVSQDVFLFNDTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 593 IYPDTREdmkrkhiTENELRSILKMVSLEHIAQR--DSFDVV---RDWKdiLSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:cd03251 97 AYGRPGA-------TREEVEEAARAANAHEFIMElpEGYDTVigeRGVK--LSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190
....*....|....*....|....*....|...
gi 386763404 668 AvsIDVES------SIYEIAKGMgiTLLTITHR 694
Cdd:cd03251 168 A--LDTESerlvqaALERLMKNR--TTFVIAHR 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
528-715 |
3.63e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 528 IEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKdvpcMFYIPQRPYMSIG-SLCDQII--YPDTREDMKRK 604
Cdd:COG0488 21 INPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR----IGYLPQEPPLDDDlTVLDTVLdgDAELRALEAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 605 HITENEL----RSILKMVSLEH-IAQRDSFDVVRDWKDIL-----------------SGGEKQRMAIARLFYHRPRYALL 662
Cdd:COG0488 97 EELEAKLaepdEDLERLAELQEeFEALGGWEAEARAEEILsglgfpeedldrpvselSGGWRRRVALARALLSEPDLLLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386763404 663 DECTSavSIDVESsiyeIA------KGMGITLLTITH-RptlwkyH------THILEFDG------LGNWQF 715
Cdd:COG0488 177 DEPTN--HLDLES----IEwleeflKNYPGTVLVVSHdR------YfldrvaTRILELDRgkltlyPGNYSA 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
520-693 |
3.83e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 60.24 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL------------HIPRPVKDVPCMFyipQR----PYM 583
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltddkkNINELRQKVGMVF---QQfnlfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 584 SIgslCDQIIYPDTREDMKRKHITENELRSILKMVSLEHIAQrdsfdvvrDWKDILSGGEKQRMAIARLFYHRPRYALLD 663
Cdd:cd03262 92 TV---LENITLAPIKVKGMSKAEAEERALELLEKVGLADKAD--------AYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|....
gi 386763404 664 ECTSA----VSIDVESSIYEIAKGmGITLLTITH 693
Cdd:cd03262 161 EPTSAldpeLVGEVLDVMKDLAEE-GMTMVVVTH 193
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
524-693 |
4.64e-10 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 60.91 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPCMFYIPQRpymsIGSLC----DQIIYPDTR 598
Cdd:TIGR04520 21 VSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgLDTLDEENLWEIRKK----VGMVFqnpdNQFVGATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 599 ED----MKRKHITENELRSI----LKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAVS 670
Cdd:TIGR04520 97 DDvafgLENLGVPREEMRKRvdeaLKLVGMEDFRDREPHL--------LSGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
170 180
....*....|....*....|....*..
gi 386763404 671 ----IDVESSIYEIAKGMGITLLTITH 693
Cdd:TIGR04520 169 pkgrKEVLETIRKLNKEEGITVISITH 195
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
520-694 |
4.71e-10 |
|
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: 60.53 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPG-VHLLItGPNGCGKSSLFRILSGLWPIYAGELH------------------------IPRPVKDvpcm 574
Cdd:cd03219 15 ALDDVSFSVRPGeIHGLI-GPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglppheiarlgigrtfqIPRLFPE---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 575 fyipqrpyMS------IGSLCDQIIYPDTREDMKRKHITENELRSILKMVSLEHIAQRdsfdVVRDwkdiLSGGEKQRMA 648
Cdd:cd03219 90 --------LTvlenvmVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADR----PAGE----LSYGQQRRLE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386763404 649 IARLFYHRPRYALLDECTSAVSI----DVESSIYEIAKGmGITLLTITHR 694
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPeeteELAELIRELRER-GITVLLVEHD 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
523-693 |
5.30e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.77 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 523 KLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKDVPCMFYIPQRpymsIGslcdqIIY--PD---- 596
Cdd:PRK13632 27 NVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK----IG-----IIFqnPDnqfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 597 --TRED-----MKRKHITENELRSIL----KMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDEC 665
Cdd:PRK13632 98 gaTVEDdiafgLENKKVPPKKMKDIIddlaKKVGMEDYLDKEPQN--------LSGGQKQRVAIASVLALNPEIIIFDES 169
|
170 180 190
....*....|....*....|....*....|..
gi 386763404 666 TSAV----SIDVESSIYEIAKGMGITLLTITH 693
Cdd:PRK13632 170 TSMLdpkgKREIKKIMVDLRKTRKKTLISITH 201
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
524-695 |
1.18e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVP-----CMFYIPQRP--------------YM 583
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgEPIRRQRdeyhqDLLYLGHQPgikteltalenlrfYQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 584 SIGSLCDqiiypdtredmkrkhitENELRSILKMVSL---EHIAQRdsfdvvrdwkdILSGGEKQRMAIARLFYHRPRYA 660
Cdd:PRK13538 100 RLHGPGD-----------------DEALWEALAQVGLagfEDVPVR-----------QLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 386763404 661 LLDECTSAvsIDV------ESSIYEIAKGMGITLLTiTHRP 695
Cdd:PRK13538 152 ILDEPFTA--IDKqgvarlEALLAQHAEQGGMVILT-THQD 189
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
524-693 |
1.45e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.89 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKdvpcmfYIPQRPYMSIGSLCDQIIYPdtredmkr 603
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA------YVPQQAWIQNDSLRENILFG-------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 604 KHITENELRSILK----MVSLEHIAQRDSFDVVRdwKDI-LSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIY 678
Cdd:TIGR00957 723 KALNEKYYQQVLEacalLPDLEILPSGDRTEIGE--KGVnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180
....*....|....*....|
gi 386763404 679 EIAKG-MGI----TLLTITH 693
Cdd:TIGR00957 801 EHVIGpEGVlknkTRILVTH 820
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
524-695 |
1.86e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGlwpiyageLHIPRPVKdvpCMFYIPQRPYMSIGSLCDQI-IYPDTREDMK 602
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------ALKGTPVA---GCVDVPDNQFGREASLIDAIgRKGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 603 rkhitenelrsILKMVSLEhiaqrDSFDVVRDWKDiLSGGEKQRMAIARLFYHRPRYALLDECTSAVSID----VESSIY 678
Cdd:COG2401 118 -----------LLNAVGLS-----DAVLWLRRFKE-LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrVARNLQ 180
|
170
....*....|....*..
gi 386763404 679 EIAKGMGITLLTITHRP 695
Cdd:COG2401 181 KLARRAGITLVVATHHY 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
520-693 |
2.07e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.57 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL-----HIPRPVKDVPCM----------FYIpqRPYMS 584
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdglKVNDPKVDERLIrqeagmvfqqFYL--FPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 585 IgslCDQIIYPDTREDMKRKHITENELRSILKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:PRK09493 94 A---LENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHH--------YPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 386763404 665 CTSAvsIDVESSiYEIAKGM------GITLLTITH 693
Cdd:PRK09493 163 PTSA--LDPELR-HEVLKVMqdlaeeGMTMVIVTH 194
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
515-694 |
2.93e-09 |
|
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: 57.42 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 515 PNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPC------MFYIPQRPYMSIGS 587
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgIDISTIPLedlrssLTIIPQDPTLFSGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 588 LcdqiiypdtREDMKR-KHITENELRSILKmvslehiaqrdsfdvVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECT 666
Cdd:cd03369 98 I---------RSNLDPfDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190
....*....|....*....|....*....|
gi 386763404 667 SAVSIDVESSIYEIAKGM--GITLLTITHR 694
Cdd:cd03369 154 ASIDYATDALIQKTIREEftNSTILTIAHR 183
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
524-693 |
4.08e-09 |
|
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: 58.13 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPG-VHLLItGPNGCGKSSLFRILSGLWPIYAGELH------------------------IPRPVKD-------- 570
Cdd:COG0411 23 VSLEVERGeIVGLI-GPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphriarlgiartfqNPRLFPEltvlenvl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 571 VPCMFyipQRPYMSIGSLCDQIIYPDTREDMKRkhitenELRSILKMVSLEHIAQRdsfdVVRDwkdiLSGGEKQRMAIA 650
Cdd:COG0411 102 VAAHA---RLGRGLLAALLRLPRARREEREARE------RAEELLERVGLADRADE----PAGN----LSYGQQRRLEIA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386763404 651 RLFYHRPRYALLDECTSAVSiDVESS-----IYEIAKGMGITLLTITH 693
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLN-PEETEelaelIRRLRDERGITILLIEH 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
524-693 |
4.43e-09 |
|
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: 57.73 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPG--VHLLitGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPcmfyIPQR------------PYMSIgsl 588
Cdd:cd03296 21 VSLDIPSGelVALL--GPSGSGKTTLLRLIAGLERPDSGTILFGgEDATDVP----VQERnvgfvfqhyalfRHMTV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 589 CDQIIYpDTREDMKRKHITENELR----SILKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:cd03296 92 FDNVAF-GLRVKPRSERPPEAEIRakvhELLKLVQLDWLADR--------YPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190
....*....|....*....|....*....|...
gi 386763404 665 CTSA----VSIDVESSIYEIAKGMGITLLTITH 693
Cdd:cd03296 163 PFGAldakVRKELRRWLRRLHDELHVTTVFVTH 195
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
521-693 |
5.03e-09 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 56.99 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 521 VPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI--------PRPVKDVpcMFYIPQRPymsigSLCDQI 592
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvrePREVRRR--IGIVFQDL-----SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 593 -----------IYPDTREDMKRKhiteneLRSILKMVSLEHIAQRdsfdVVRDWkdilSGGEKQRMAIARLFYHRPRYAL 661
Cdd:cd03265 89 tgwenlyiharLYGVPGAERRER------IDELLDFVGLLEAADR----LVKTY----SGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 386763404 662 LDECTSAVSIDVESSIYEIAKGM----GITLLTITH 693
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLkeefGMTILLTTH 190
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
283-694 |
6.00e-09 |
|
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: 59.34 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 283 ALSIGVIA---LTAHILRIVSPKFGQLVSEEANRYGYLRHIHSRIITNAEEIAFYGGHKVEMQQLRQAYNRLVNQ---MT 356
Cdd:TIGR02203 155 QLTLIVVVmlpVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLamkMT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 357 TifnqklwfimleqffmkyvwsgTGMIMVSLPILTGSdVGLGTVPNTAISESRVSERTQYLTTArnlLISAADAIerlms 436
Cdd:TIGR02203 235 S----------------------AGSISSPITQLIAS-LALAVVLFIALFQAQAGSLTAGDFTA---FITAMIAL----- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 437 sYKEIVSLAgytfRVAGMMDVFEETALGVYcktSVMESNQsngiiEFRNGK---PIAKGRIiysddpknmsiSLRAVPVV 513
Cdd:TIGR02203 284 -IRPLKSLT----NVNAPMQRGLAAAESLF---TLLDSPP-----EKDTGTraiERARGDV-----------EFRNVTFR 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 514 TPNCDI-VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIprpvKDVPCMFY-----------IPQRP 581
Cdd:TIGR02203 340 YPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL----DGHDLADYtlaslrrqvalVSQDV 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 582 YMSIGSLCDQIIYPDTREdmkrkhITENELRSILKMVSLEHIAQR--DSFD-VVRDWKDILSGGEKQRMAIARLFYHRPR 658
Cdd:TIGR02203 416 VLFNDTIANNIAYGRTEQ------ADRAEIERALAAAYAQDFVDKlpLGLDtPIGENGVLLSGGQRQRLAIARALLKDAP 489
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 386763404 659 YALLDECTSAvsIDVES------SIYEIAKGMgiTLLTITHR 694
Cdd:TIGR02203 490 ILILDEATSA--LDNESerlvqaALERLMQGR--TTLVIAHR 527
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
520-664 |
6.69e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.92 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKdvpcMFYIPQ-RPYMSIG-SLCDQIIypDT 597
Cdd:COG0488 330 LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK----IGYFDQhQEELDPDkTVLDELR--DG 403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386763404 598 REDMKRKHItenelRSILkmvslehiaQR------DSFDVVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:COG0488 404 APGGTEQEV-----RGYL---------GRflfsgdDAFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
495-694 |
7.84e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.70 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 495 IYSDDPknMSISLRAVPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPiYAGELHIP-RPVKDVPC 573
Cdd:PRK11174 342 LASNDP--VTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINgIELRELDP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 574 MFY------IPQRPYMSIGSLCDQIIypdtredMKRKHITENELRSILKMvslehiAQRDSF---------DVVRDWKDI 638
Cdd:PRK11174 419 ESWrkhlswVGQNPQLPHGTLRDNVL-------LGNPDASDEQLQQALEN------AWVSEFlpllpqgldTPIGDQAAG 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386763404 639 LSGGEKQRMAIARLFYHRPRYALLDECTSavSID------VESSIYEIAKGMgiTLLTITHR 694
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTA--SLDahseqlVMQALNAASRRQ--TTLMVTHQ 543
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
524-696 |
9.54e-09 |
|
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: 55.63 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGL--WPIYAGELHI---PRPVKDVPCMF-YIPQrpymsigslcDQIIYPdt 597
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLIngrPLDKRSFRKIIgYVPQ----------DDILHP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 redmkrkHITENElrsilkmvSLEHIAQRDSfdvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTS----AVSIDV 673
Cdd:cd03213 96 -------TLTVRE--------TLMFAAKLRG----------LSGGERKRVSIALELVSNPSLLFLDEPTSgldsSSALQV 150
|
170 180
....*....|....*....|...
gi 386763404 674 ESSIYEIAKgMGITLLTITHRPT 696
Cdd:cd03213 151 MSLLRRLAD-TGRTIICSIHQPS 172
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
524-693 |
9.90e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.95 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI------PRPVKDVPCM----FYIPQRPYmsIGS-LCDQI 592
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmvlsEETVWDVRRQvgmvFQNPDNQF--VGAtVQDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 593 IY-------PdtREDMKRKhiteneLRSILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDEC 665
Cdd:PRK13635 104 AFglenigvP--REEMVER------VDQALRQVGMEDFLNREPHR--------LSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190
....*....|....*....|....*....|..
gi 386763404 666 TSAVS----IDVESSIYEIAKGMGITLLTITH 693
Cdd:PRK13635 168 TSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
524-697 |
1.11e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 56.29 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLwpiyagelhiprpvkDVPcmfyipqrpymSIGS--LCDQIIYP---DTR 598
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGL---------------DRP-----------TSGTvrLAGQDLFAldeDAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 599 EDMKRKHI-------------T--ENelrsilKMVSLEHIAQRDSFDVVRDWKDI-------------LSGGEKQRMAIA 650
Cdd:COG4181 85 ARLRARHVgfvfqsfqllptlTalEN------VMLPLELAGRRDARARARALLERvglghrldhypaqLSGGEQQRVALA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386763404 651 RLFYHRPRYAL-------LDECTSAVSIDVessIYEIAKGMGITLLTITHRPTL 697
Cdd:COG4181 159 RAFATEPAILFadeptgnLDAATGEQIIDL---LFELNRERGTTLVLVTHDPAL 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
517-708 |
1.24e-08 |
|
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: 58.21 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 517 CDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVP------CMFYIPQRPYMSIGSLC 589
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLnGFSLKDIDrhtlrqFINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 590 DQIIY---PDTREDMKRKHITENELRSILKMVSLEHIAQ--RDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:TIGR01193 566 ENLLLgakENVSQDEIWAACEIAEIKDDIENMPLGYQTElsEEGSS--------ISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 386763404 665 CTSAVSIDVESSIyeIAKGMGI---TLLTITHRPTLWKYHTHILEFD 708
Cdd:TIGR01193 638 STSNLDTITEKKI--VNNLLNLqdkTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
528-694 |
1.26e-08 |
|
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: 58.29 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 528 IEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPcmfyipQRpymsigSLCDQI-IYP-DT------- 597
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDgQDIRDVT------QA------SLRAAIgIVPqDTvlfndti 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 -------REDmkrkhITENELRSILKMVSLEHIAQR--DSFDVV---RDWKdiLSGGEKQRMAIARLFYHRPRYALLDEC 665
Cdd:COG5265 449 ayniaygRPD-----ASEEEVEAAARAAQIHDFIESlpDGYDTRvgeRGLK--LSGGEKQRVAIARTLLKNPPILIFDEA 521
|
170 180 190
....*....|....*....|....*....|....*
gi 386763404 666 TSAvsID------VESSIYEIAKGMgiTLLTITHR 694
Cdd:COG5265 522 TSA--LDsrteraIQAALREVARGR--TTLVIAHR 552
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
524-705 |
1.31e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 55.61 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPG-VHLLItGPNGCGKSSLFRILSGLwPIYagelhipRPVKdvpcmfyipqrpymsiGSlcdqIIYPDtrEDMK 602
Cdd:cd03217 19 VNLTIKKGeVHALM-GPNGSGKSTLAKTIMGH-PKY-------EVTE----------------GE----ILFKG--EDIT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 603 RKHITENELRSI---------LKMVSLEhiaqrdsfDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDV 673
Cdd:cd03217 68 DLPPEERARLGIflafqyppeIPGVKNA--------DFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 386763404 674 ESSIYEIAKGM---GITLLTITHRPTLWKY----HTHIL 705
Cdd:cd03217 140 LRLVAEVINKLreeGKSVLIITHYQRLLDYikpdRVHVL 178
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
519-693 |
1.39e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.63 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPR-PVKDVPCMFYIPQRPYMSIGSLCDQIIYPDT 597
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWDIRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 REDM----KRKHITENELRS----ILKMVSLehiaqrdsFDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAV 669
Cdd:PRK13633 104 EEDVafgpENLGIPPEEIRErvdeSLKKVGM--------YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180
....*....|....*....|....*...
gi 386763404 670 S----IDVESSIYEIAKGMGITLLTITH 693
Cdd:PRK13633 176 DpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
520-680 |
1.39e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.28 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKdvpcMFYIPQRPYMSIgslcdqiIYPDT-- 597
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR----IGYVPQKLYLDT-------TLPLTvn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 REDMKRKHITENELRSILKMVSLEHIAQRDsfdvvrdwKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSI 677
Cdd:PRK09544 88 RFLRLRPGTKKEDILPALKRVQAGHLIDAP--------MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
...
gi 386763404 678 YEI 680
Cdd:PRK09544 160 YDL 162
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
524-688 |
1.46e-08 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 55.99 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPCmfyiPQRPYMSIGslcdqiiY-PDTREDM 601
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDgEDITKLPP----HERARAGIA-------YvPQGREIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 602 KRKHITENelrsiLKMV------SLEHIAQR--DSFDVVRDWKD----ILSGGEKQRMAIARLFYHRPRYALLDECTSAV 669
Cdd:TIGR03410 88 PRLTVEEN-----LLTGlaalprRSRKIPDEiyELFPVLKEMLGrrggDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180
....*....|....*....|....*
gi 386763404 670 --SI--DVESSIYEIAK--GMGITL 688
Cdd:TIGR03410 163 qpSIikDIGRVIRRLRAegGMAILL 187
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-695 |
1.72e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.07 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIY-----AGELHI------PRPV----KDVPCMFYIPQR-PYM 583
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLdgqdifKMDVielrRRVQMVFQIPNPiPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 584 SIGSlcDQIIYPDTREDMKRKHITENELRSILKMVSLehiaqrdsFDVVRDWKDI----LSGGEKQRMAIARLFYHRPRY 659
Cdd:PRK14247 98 SIFE--NVALGLKLNRLVKSKKELQERVRWALEKAQL--------WDEVKDRLDApagkLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 386763404 660 ALLDECTSAV----SIDVESSIYEIAKGMGITLltITHRP 695
Cdd:PRK14247 168 LLADEPTANLdpenTAKIESLFLELKKDMTIVL--VTHFP 205
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
524-708 |
2.80e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.58 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYA---GELHIP-RPVKDvpcMFYIPQRpymsigslcdQIIYpDTRE 599
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNgIPYKE---FAEKYPG----------EIIY-VSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 600 DMKRKHITENELrsilkmvsLEHIAQRDSFDVVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDECT----SAVSIDVES 675
Cdd:cd03233 92 DVHFPTLTVRET--------LDFALRCKGNEFVRG----ISGGERKRVSIAEALVSRASVLCWDNSTrgldSSTALEILK 159
|
170 180 190
....*....|....*....|....*....|...
gi 386763404 676 SIYEIAKGMGITLLTITHRPTLWKYHThileFD 708
Cdd:cd03233 160 CIRTMADVLKTTTFVSLYQASDEIYDL----FD 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
501-693 |
2.81e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 501 KNMSISLRAVPVVTPncdiVVPKLTLCIEPGVHLLITGPNGCGKS----SLFRILSG---LWP----IYAGE--LHIP-- 565
Cdd:PRK15134 9 ENLSVAFRQQQTVRT----VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYPsgdiRFHGEslLHASeq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 566 --RPVK-DVPCMfyIPQRPYMSIGSLcdQIIYPDTREDMK-----RKHITENELRSILKMVSLEHIAQRdsfdvVRDWKD 637
Cdd:PRK15134 85 tlRGVRgNKIAM--IFQEPMVSLNPL--HTLEKQLYEVLSlhrgmRREAARGEILNCLDRVGIRQAAKR-----LTDYPH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 638 ILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIY----EIAKGMGITLLTITH 693
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILqllrELQQELNMGLLFITH 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
520-664 |
3.33e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.25 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRpvKDVPCMF------------YIPQRpYMSIgs 587
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG--TDVSRLHardrkvgfvfqhYALFR-HMTV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 588 lCDQIIYPDT---REDMKRKHITENELRSILKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:PRK10851 92 -FDNIAFGLTvlpRRERPNAAAIKAKVTQLLEMVQLAHLADR--------YPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
523-709 |
3.41e-08 |
|
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: 52.84 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 523 KLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKdvpcMFYIPQrpymsigslcdqiiypdtredmk 602
Cdd:cd03221 18 DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK----IGYFEQ----------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 603 rkhitenelrsilkmvslehiaqrdsfdvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSavSIDVES--SIYEI 680
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN--HLDLESieALEEA 112
|
170 180 190
....*....|....*....|....*....|
gi 386763404 681 AKGMGITLLTITH-RPTLWKYHTHILEFDG 709
Cdd:cd03221 113 LKEYPGTVILVSHdRYFLDQVATKIIELED 142
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
524-693 |
3.72e-08 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 54.82 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRpvKDVPCM---FYIPQRPYMSI--------GSL--CD 590
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG--EDISGLseaELYRLRRRMGMlfqsgalfDSLtvFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 591 QIIYPdTRE--DMKRKHITEnELRSILKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDECTS- 667
Cdd:cd03261 97 NVAFP-LREhtRLSEEEIRE-IVLEKLEAVGLRGAEDL--------YPAELSGGMKKRVALARALALDPELLLYDEPTAg 166
|
170 180
....*....|....*....|....*....
gi 386763404 668 ---AVSIDVESSIYEIAKGMGITLLTITH 693
Cdd:cd03261 167 ldpIASGVIDDLIRSLKKELGLTSIMVTH 195
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
525-693 |
4.86e-08 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 54.61 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 525 TLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL-----HIPRPVKDVP------CM-FyipQR----PYMSIGsl 588
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTItvdgeDLTDSKKDINklrrkvGMvF---QQfnlfPHLTVL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 589 cDQIIYPDtredMKRKHITENELRSI----LKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:COG1126 96 -ENVTLAP----IKVKKMSKAEAEERamelLERVGLADKADA--------YPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 386763404 665 CTSA-----VSiDVESSIYEIAKGmGITLLTITH 693
Cdd:COG1126 163 PTSAldpelVG-EVLDVMRDLAKE-GMTMVVVTH 194
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
568-708 |
5.27e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 568 VKDVPCMFYI-PQRPYMSIGSLCDQIIYPD---TREDMKRkhitenelrsILKMVSLEHIAQR--DSFDV-VRDWKDILS 640
Cdd:PTZ00265 1291 LKDLRNLFSIvSQEPMLFNMSIYENIKFGKedaTREDVKR----------ACKFAAIDEFIESlpNKYDTnVGPYGKSLS 1360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386763404 641 GGEKQRMAIARLFYHRPRYALLDECTSAVSID----VESSIYEIAKGMGITLLTITHRPTLWKYHTHILEFD 708
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFN 1432
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
538-693 |
5.42e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.40 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 538 GPNGCGKSSLFRIL---SGLWP--------IYAG-ELHIPRP-----VKDVPCMFYIPQRPYMSIgslCDQIIYPDTRED 600
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPevtitgsiVYNGhNIYSPRTdtvdlRKEIGMVFQQPNPFPMSI---YENVVYGLRLKG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 601 MKRKHITENELRSILKMVSLEHIAQrdsfDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAV----SIDVESS 676
Cdd:PRK14239 115 IKDKQVLDEAVEKSLKGASIWDEVK----DRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALdpisAGKIEET 190
|
170
....*....|....*..
gi 386763404 677 IYEIAKGMgiTLLTITH 693
Cdd:PRK14239 191 LLGLKDDY--TMLLVTR 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
520-694 |
6.70e-08 |
|
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: 53.91 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP--RPVKDvpcmfyiPQRPYMSIGSLCDQI-IYP- 595
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKE-------PAEARRRLGFVSDSTgLYDr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 596 -DTRED---------MKRKHITE--NELRSILKMvslEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLD 663
Cdd:cd03266 93 lTARENleyfaglygLKGDELTArlEELADRLGM---EELLDRRVGG--------FSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190
....*....|....*....|....*....|....
gi 386763404 664 ECTSAVSIDVESSIYEIA---KGMGITLLTITHR 694
Cdd:cd03266 162 EPTTGLDVMATRALREFIrqlRALGKCILFSTHI 195
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
528-671 |
7.21e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.97 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 528 IEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-------PRPV------KDVPCMFyipQRPYMS------IGSL 588
Cdd:PRK11308 38 LERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqgqdllkADPEaqkllrQKIQIVF---QNPYGSlnprkkVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 589 CD---QIIYPDTREDMKRKhiteneLRSILKMVSL--EHiAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLD 663
Cdd:PRK11308 115 LEeplLINTSLSAAERREK------ALAMMAKVGLrpEH-YDR--------YPHMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170
....*....|
gi 386763404 664 ECTSA--VSI 671
Cdd:PRK11308 180 EPVSAldVSV 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
525-694 |
7.53e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.41 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 525 TLCIEPG-VHLLItGPNGCGKSSLFRILSGLWPIYAGELHIprpvKDVPCMF------------YIPQR----PYMSIGs 587
Cdd:COG1129 24 SLELRPGeVHALL-GENGAGKSTLMKILSGVYQPDSGEILL----DGEPVRFrsprdaqaagiaIIHQElnlvPNLSVA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 588 lcdQIIYPDtREDMKRKHITENELRS----ILKMVSLEhiaqrdsFDV---VRDwkdiLSGGEKQRMAIARLFYHRPRYA 660
Cdd:COG1129 98 ---ENIFLG-REPRRGGLIDWRAMRRrareLLARLGLD-------IDPdtpVGD----LSVAQQQLVEIARALSRDARVL 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 386763404 661 LLDECTSAVSiDVESSI-YEIA---KGMGITLLTITHR 694
Cdd:COG1129 163 ILDEPTASLT-EREVERlFRIIrrlKAQGVAIIYISHR 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
505-703 |
7.66e-08 |
|
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: 53.57 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 505 ISLRAVPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPCMfyipQRPYM 583
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgQDVSDLRGR----AIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 584 --SIGslcdqIIYPDTREDMKRK---------HITENELRSILKMVSlEHIAQRDSFDVVRDWKDILSGGEKQRMAIARL 652
Cdd:cd03292 77 rrKIG-----VVFQDFRLLPDRNvyenvafalEVTGVPPREIRKRVP-AALELVGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386763404 653 FYHRPRYALLDECTSAVSIDVESSIYEIAKG---MGITLLTITHRPTLWKYHTH 703
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKinkAGTTVVVATHAKELVDTTRH 204
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
520-693 |
9.50e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 54.04 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPV------------KDVPCMF---YIPQRPYM 583
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgQDLyqldrkqrrafrRDVQLVFqdsPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 584 SIGslcdQIIYPDTR--EDMKRkhiTENELR--SILKMVSLehiaqRDsfDVVRDWKDILSGGEKQRMAIARLFYHRPRY 659
Cdd:TIGR02769 106 TVR----QIIGEPLRhlTSLDE---SEQKARiaELLDMVGL-----RS--EDADKLPRQLSGGQLQRINIARALAVKPKL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 386763404 660 ALLDECTSAVSIDVESSIYEIAKGM----GITLLTITH 693
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKLqqafGTAYLFITH 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
520-694 |
9.75e-08 |
|
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: 53.32 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPG--VHLLitGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPcMF--------YIPQRPymSIG-- 586
Cdd:cd03218 15 VVNGVSLSVKQGeiVGLL--GPNGAGKTTTFYMIVGLVKPDSGKILLDgQDITKLP-MHkrarlgigYLPQEA--SIFrk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 587 -------SLCDQIIYPDTREDMKRkhiteneLRSILKMVSLEHIAQRDSfdvvrdwkDILSGGEKQRMAIARLFYHRPRY 659
Cdd:cd03218 90 ltveeniLAVLEIRGLSKKEREEK-------LEELLEEFHITHLRKSKA--------SSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386763404 660 ALLDECTSAVS----IDVESSIYEI-AKGMG--IT------LLTITHR 694
Cdd:cd03218 155 LLLDEPFAGVDpiavQDIQKIIKILkDRGIGvlITdhnvreTLSITDR 202
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
520-697 |
1.14e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.36 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI--------PRPVKDVPCMFYIPQRPymSIG---SL 588
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllPLHARARRGIGYLPQEA--SIFrrlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 589 CDQII-YPDTREDMKRKHiTENELRSILKMVSLEHIaqRDSFDvvrdwkDILSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:PRK10895 96 YDNLMaVLQIRDDLSAEQ-REDRANELMEEFHIEHL--RDSMG------QSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 386763404 668 AVS----IDVEsSIYEIAKGMGITLLTITH--RPTL 697
Cdd:PRK10895 167 GVDpisvIDIK-RIIEHLRDSGLGVLITDHnvRETL 201
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
520-693 |
1.27e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.28 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELhiprpvkdvpcMFYIPQRPYMSIGSLCD------QII 593
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-----------IFNGQPMSKLSSAAKAElrnqklGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 594 Y------PD--TRED---------MKRKHITENElRSILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHR 656
Cdd:PRK11629 93 YqfhhllPDftALENvamplligkKKPAEINSRA-LEMLAAVGLEHRANHRPSE--------LSGGERQRVAIARALVNN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 386763404 657 PRYALLDECTSAVSIDVESSIY----EIAKGMGITLLTITH 693
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFqllgELNRLQGTAFLVVTH 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
524-693 |
1.33e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.56 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKDVPCMFYIPQRPYMSIGSLCDQIIYPDTRED--- 600
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 601 -MKRKHITENELrsiLKMVSlEHIAQRDSFDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVS----IDVES 675
Cdd:PRK13642 106 gMENQGIPREEM---IKRVD-EALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMR 181
|
170
....*....|....*...
gi 386763404 676 SIYEIAKGMGITLLTITH 693
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITH 199
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-695 |
1.49e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.31 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWP-----------------IYAGELHIPRPVKDVPCMFYIPQR-P 581
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearvegevrlfgrnIYSPDVDPIEVRREVGMVFQYPNPfP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 582 YMSIgslcdqiiYPDTREDMKRKHI--TENELRSILKMvSLEHIAQRDSF-DVVRDWKDILSGGEKQRMAIARLFYHRPR 658
Cdd:PRK14267 99 HLTI--------YDNVAIGVKLNGLvkSKKELDERVEW-ALKKAALWDEVkDRLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 386763404 659 YALLDECTSAV----SIDVESSIYEIAKGMGITLltITHRP 695
Cdd:PRK14267 170 ILLMDEPTANIdpvgTAKIEELLFELKKEYTIVL--VTHSP 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
530-675 |
1.78e-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: 54.56 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 530 PGVHLLITGPNGCGKSSLFRILSGLWPIYAGElhiPRPVKDVPCMfYIPQRPY------------MSIGSLCDQI----- 592
Cdd:TIGR03719 30 PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE---ARPQPGIKVG-YLPQEPQldptktvrenveEGVAEIKDALdrfne 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 593 ---IYPDTREDMKRKHITENELRSILKMVSLEHIAQR--DSFDVVR----DWK-DILSGGEKQRMAIARLFYHRPRYALL 662
Cdd:TIGR03719 106 isaKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQleIAMDALRcppwDADvTKLSGGERRRVALCRLLLSKPDMLLL 185
|
170
....*....|...
gi 386763404 663 DECTSavSIDVES 675
Cdd:TIGR03719 186 DEPTN--HLDAES 196
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
524-693 |
2.30e-07 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 52.29 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHiprpV--KDVPCM-----FYIPQRpymsIG---------- 586
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL----VdgQDITGLsekelYELRRR----IGmlfqggalfd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 587 SLC--DQIIYPdTREdmkRKHITENELRSI----LKMVSLEHIAQR---DsfdvvrdwkdiLSGGEKQRMAIARLFYHRP 657
Cdd:COG1127 96 SLTvfENVAFP-LRE---HTDLSEAEIRELvlekLELVGLPGAADKmpsE-----------LSGGMRKRVALARALALDP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 386763404 658 RYALLDECTS----AVSIDVESSIYEIAKGMGITLLTITH 693
Cdd:COG1127 161 EILLYDEPTAgldpITSAVIDELIRELRDELGLTSVVVTH 200
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
524-664 |
2.53e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.39 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDvP-----CMF----YIPQRPYMSIGSLCDQII 593
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgKPVEG-PgaergVVFqnegLLPWRNVQDNVAFGLQLA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386763404 594 YPDTREdmkRKHITenelRSILKMVSLEHIAQRdsfdvvRDWKdiLSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:PRK11248 99 GVEKMQ---RLEIA----HQMLKKVGLEGAEKR------YIWQ--LSGGQRQRVGIARALAANPQLLLLDE 154
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
524-705 |
2.59e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 52.38 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPG-VHLlITGPNGCGKSSLFRILSGLwPIY---AGELHI------------------------PRPVKDVPCMF 575
Cdd:COG0396 19 VNLTIKPGeVHA-IMGPNGSGKSTLAKVLMGH-PKYevtSGSILLdgedilelspderaragiflafqyPVEIPGVSVSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 576 YIpqrpYMSIGSLCDQIIypDTREDMKrkhitenELRSILKMVSL-EHIAQRD---SFdvvrdwkdilSGGEKQRMAIAR 651
Cdd:COG0396 97 FL----RTALNARRGEEL--SAREFLK-------LLKEKMKELGLdEDFLDRYvneGF----------SGGEKKRNEILQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386763404 652 LFYHRPRYALLDECTSAVSID----VESSIYEIA-KGMGItlLTITHRPTLWKY----HTHIL 705
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDalriVAEGVNKLRsPDRGI--LIITHYQRILDYikpdFVHVL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
519-693 |
3.39e-07 |
|
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: 51.74 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIprpvkdvpCMFYI---PQRPYMSIGsLCDQ--II 593
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI--------NGYSIrtdRKAARQSLG-YCPQfdAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 594 YPD-TREDMKR-----KHITENELRS----ILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLD 663
Cdd:cd03263 87 FDElTVREHLRfyarlKGLPKSEIKEevelLLRVLGLTDKANKRART--------LSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 386763404 664 ECTSavSIDVES------SIYEIAKGMGItLLTiTH 693
Cdd:cd03263 159 EPTS--GLDPASrraiwdLILEVRKGRSI-ILT-TH 190
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
528-693 |
3.60e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.39 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 528 IEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVK-DVPCMFYIPQRPYMSIGSLCDQIIYPDTREDMK--- 602
Cdd:PRK13639 25 AEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgEPIKyDKKSLLEVRKTVGIVFQNPDDQLFAPTVEEDVAfgp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 603 -----RKHITENELRSILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSI 677
Cdd:PRK13639 105 lnlglSKEEVEKRVKEALKAVGMEGFENKPPHH--------LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQI 176
|
170 180
....*....|....*....|
gi 386763404 678 ----YEIAKgMGITLLTITH 693
Cdd:PRK13639 177 mkllYDLNK-EGITIIISTH 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
504-693 |
4.20e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.10 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 504 SISLRAVPVVTPNCDIVVPkLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-------------PRPVKD 570
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHP-LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLdaqpleswsskafARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 571 VPCMfyIPQRPYMSIGSLCDQIIYP-------DTREDmkRKHITEnelrsILKMVSLEHIAQRdsfdVVrdwkDILSGGE 643
Cdd:PRK10575 90 LPQQ--LPAAEGMTVRELVAIGRYPwhgalgrFGAAD--REKVEE-----AISLVGLKPLAHR----LV----DSLSGGE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386763404 644 KQRMAIARLFYHRPRYALLDECTSAVSI----DVESSIYEIAKGMGITLLTITH 693
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLH 206
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
541-693 |
5.22e-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: 52.36 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 541 GCGKSSLFRILSGLWP---------IYAGE--LHIP----RPV--KDvpcMFYIPQRPY------MSIGslcDQIIYP-D 596
Cdd:COG0444 41 GSGKSTLARAILGLLPppgitsgeiLFDGEdlLKLSekelRKIrgRE---IQMIFQDPMtslnpvMTVG---DQIAEPlR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 597 TREDMKRKHITEnELRSILKMVSLehiaqRDSFDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSA--VSI--D 672
Cdd:COG0444 115 IHGGLSKAEARE-RAIELLERVGL-----PDPERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTAldVTIqaQ 188
|
170 180
....*....|....*....|.
gi 386763404 673 VESSIYEIAKGMGITLLTITH 693
Cdd:COG0444 189 ILNLLKDLQRELGLAILFITH 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
534-693 |
5.84e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 534 LLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKDVPCMFYIPQRPYMSIGSLCDQIIYPDTRED----MKRKHITEN 609
Cdd:PRK13650 36 LSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQFVGATVEDDvafgLENKGIPHE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 610 ELRS----ILKMVSLEHIAQRDSfdvVRdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAVS----IDVESSIYEIA 681
Cdd:PRK13650 116 EMKErvneALELVGMQDFKEREP---AR-----LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIR 187
|
170
....*....|..
gi 386763404 682 KGMGITLLTITH 693
Cdd:PRK13650 188 DDYQMTVISITH 199
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
524-693 |
7.26e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.39 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGE-LHIPRPV-----------KDVPCMFYIPQRPYMSiGSLCDQ 591
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRiLFDGKPIdysrkglmklrESVGMVFQDPDNQLFS-ASVYQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 592 IIYPDTREDMKRKHITEnELRSILKMVSLEHIAQRDSfdvvrdwkDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSI 671
Cdd:PRK13636 104 VSFGAVNLKLPEDEVRK-RVDNALKRTGIEHLKDKPT--------HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180
....*....|....*....|....*.
gi 386763404 672 DVESSIY----EIAKGMGITLLTITH 693
Cdd:PRK13636 175 MGVSEIMkllvEMQKELGLTIIIATH 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
528-697 |
7.97e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.64 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 528 IEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL----HIPRPVKDVPCMFYIPQrpymsIGslcdqIIYPDTREDMKR 603
Cdd:PRK10908 25 MRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsgHDITRLKNREVPFLRRQ-----IG-----MIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 604 KHITENELRSILKMVSLEHIAQRDS--------FDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVES 675
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSaaldkvglLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180
....*....|....*....|....*
gi 386763404 676 SI---YEIAKGMGITLLTITHRPTL 697
Cdd:PRK10908 175 GIlrlFEEFNRVGVTVLMATHDIGL 199
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
521-693 |
8.20e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.63 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 521 VPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGE---------------LHIPRpvKDVPCMFYIPQ---RPY 582
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEvawlgkdllgmkddeWRAVR--SDIQMIFQDPLaslNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 583 MSIGslcdQII-------YPD-TREDMKRKhiteneLRSILKMVSLEHiaqrdsfDVVRDWKDILSGGEKQRMAIARLFY 654
Cdd:PRK15079 115 MTIG----EIIaeplrtyHPKlSRQEVKDR------VKAMMLKVGLLP-------NLINRYPHEFSGGQCQRIGIARALI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386763404 655 HRPRYALLDECTSA--VSI--DVESSIYEIAKGMGITLLTITH 693
Cdd:PRK15079 178 LEPKLIICDEPVSAldVSIqaQVVNLLQQLQREMGLSLIFIAH 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
520-664 |
8.59e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.80 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPG--VHLLitGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPcMF--------YIPQRPymSIG-- 586
Cdd:COG1137 18 VVKDVSLEVNQGeiVGLL--GPNGAGKTTTFYMIVGLVKPDSGRIFLDgEDITHLP-MHkrarlgigYLPQEA--SIFrk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 587 -SLCDQI-----IYPDTREDMKRKhiteneLRSILKMVSLEHIaqrdsfdvvRDWKDI-LSGGEKQRMAIARLFYHRPRY 659
Cdd:COG1137 93 lTVEDNIlavleLRKLSKKEREER------LEELLEEFGITHL---------RKSKAYsLSGGERRRVEIARALATNPKF 157
|
....*
gi 386763404 660 ALLDE 664
Cdd:COG1137 158 ILLDE 162
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
639-693 |
8.61e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 51.73 E-value: 8.61e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386763404 639 LSGGEKQRMAIARLFYHRPRYALLDECTSAvsIDVES--SIYEIAKG----MGITLLTITH 693
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSA--LDPATtrSILELLKDinreLGLTIVLITH 199
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
536-697 |
8.92e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.96 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 536 ITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPV---------KDVPCMFYIPQrpymsigslcDQIIYPDTREDMKRKH 605
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRgEPItkenirevrKFVGLVFQNPD----------DQIFSPTVEQDIAFGP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 606 IT--------ENELRSILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAVS----IDV 673
Cdd:PRK13652 105 INlgldeetvAHRVSSALHMLGLEELRDRVPHH--------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKEL 176
|
170 180
....*....|....*....|....
gi 386763404 674 ESSIYEIAKGMGITLLTITHRPTL 697
Cdd:PRK13652 177 IDFLNDLPETYGMTVIFSTHQLDL 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
639-693 |
1.08e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 51.23 E-value: 1.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386763404 639 LSGGEKQRMAIARLFYHRPRYALLDECTSAVsiDVES--SIYE----IAKGMGITLLTITH 693
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSAL--DPETtrSILDllkdINRELGLTIVLITH 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
513-679 |
1.16e-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: 52.22 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 513 VTPncdiVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSG-LWPIYAGELHIPRpvkdvpcMFYIPQRPYMSIGSLCDQ 591
Cdd:TIGR01271 438 VTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKIKHSGR-------ISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 592 IIYPDTREdmkrkhitENELRSILKMVSLEH----IAQRDSFdVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:TIGR01271 507 IIFGLSYD--------EYRYTSVIKACQLEEdialFPEKDKT-VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170
....*....|..
gi 386763404 668 AVSIDVESSIYE 679
Cdd:TIGR01271 578 HLDVVTEKEIFE 589
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
520-693 |
1.27e-06 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 50.13 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRIlsglwpIYAGelhiprpvkdvpcmfYIPQRP---YMSIGSLCD------ 590
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKC------IYGN---------------YLPDSGsilVRHDGGWVDlaqasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 591 -QIIYpdtredMKRKHI--TENELRSILKMVSLEHIAQR---------DSFDVVRDWKDIL--------------SGGEK 644
Cdd:COG4778 85 rEILA------LRRRTIgyVSQFLRVIPRVSALDVVAEPllergvdreEARARARELLARLnlperlwdlppatfSGGEQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386763404 645 QRMAIARLFYHRPRYALLDECTSavSIDVESS------IYEiAKGMGITLLTITH 693
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTA--SLDAANRavvvelIEE-AKARGTAIIGIFH 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
520-669 |
1.53e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGE-LHIPRPV-----------KDVPCMFYIPQRpymsigs 587
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAvLWQGKPLdyskrgllalrQQVATVFQDPEQ------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 588 lcdQIIYPDTRED----MKRKHITENEL-RSI---LKMVSLEHIAQRDSfdvvrdwkDILSGGEKQRMAIARLFYHRPRY 659
Cdd:PRK13638 89 ---QIFYTDIDSDiafsLRNLGVPEAEItRRVdeaLTLVDAQHFRHQPI--------QCLSHGQKKRVAIAGALVLQARY 157
|
170
....*....|
gi 386763404 660 ALLDECTSAV 669
Cdd:PRK13638 158 LLLDEPTAGL 167
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
536-693 |
1.85e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 50.96 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 536 ITGPNGCGKSSLFRILSGLWPIYAGELHI-----------PRPVKDVPCMFYI----------PQRPYmsIGSLCDQII- 593
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkPGPDGRGRAKRYIgilhqeydlyPHRTV--LDNLTEAIGl 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 594 -YPDTREDMKRKHItenelrsiLKMVSLEhiaQRDSFDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVS-- 670
Cdd:TIGR03269 393 eLPDELARMKAVIT--------LKMVGFD---EEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpi 461
|
170 180
....*....|....*....|....*
gi 386763404 671 --IDVESSIYEIAKGMGITLLTITH 693
Cdd:TIGR03269 462 tkVDVTHSILKAREEMEQTFIIVSH 486
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
504-664 |
1.99e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.61 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 504 SISLRAVPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPV--------KDVPCMF 575
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 576 -----YipqrPYMSIgslcdqiiypdtREDMK-----RKhitenelrsilkmVSLEHIAQRdsfdvVRDWKDI------- 638
Cdd:PRK11650 83 qnyalY----PHMSV------------RENMAyglkiRG-------------MPKAEIEER-----VAEAARIlelepll 128
|
170 180 190
....*....|....*....|....*....|..
gi 386763404 639 ------LSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:PRK11650 129 drkpreLSGGQRQRVAMGRAIVREPAVFLFDE 160
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
536-693 |
2.53e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.65 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 536 ITGPNGCGKSSLFRILSGL-----------------WPIYAGELHIPRPVKDVPCMFYIPQRPYMSIgslCDQIIYP--- 595
Cdd:PRK14258 38 IIGPSGCGKSTFLKCLNRMnelesevrvegrveffnQNIYERRVNLNRLRRQVSMVHPKPNLFPMSV---YDNVAYGvki 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 596 -DTREDMKRKHITENELRSILKMVSLEHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDE-CTS---AVS 670
Cdd:PRK14258 115 vGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALD--------LSGGQQQRLCIARALAVKPKVLLMDEpCFGldpIAS 186
|
170 180
....*....|....*....|...
gi 386763404 671 IDVESSIYEIAKGMGITLLTITH 693
Cdd:PRK14258 187 MKVESLIQSLRLRSELTMVIVSH 209
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
503-697 |
2.97e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 503 MSISLRAVPVVTPncdivvpkLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPCMFYIpqrP 581
Cdd:PRK13543 17 LAFSRNEEPVFGP--------LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDRSRFM---A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 582 YMS-IGSLCDQIiypDTREDM--------KRKHITENelrSILKMVSLEHIAQrdsfDVVRDwkdiLSGGEKQRMAIARL 652
Cdd:PRK13543 86 YLGhLPGLKADL---STLENLhflcglhgRRAKQMPG---SALAIVGLAGYED----TLVRQ----LSAGQKKRLALARL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 386763404 653 FYHRPRYALLDECTSAVSID----VESSIYEIAKGMGITLLTiTH--RPTL 697
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLDLEgitlVNRMISAHLRGGGAALVT-THgaYAAP 201
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
521-692 |
3.76e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.02 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 521 VPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIprpvKDVPCMF----YIPQR-------------PYM 583
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI----DDHPLHFgdysYRSQRirmifqdpstslnPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 584 SIGSLCDQIIYPDTREDMKRKhitENELRSILKMVSLEHiaqrdsfDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLD 663
Cdd:PRK15112 105 RISQILDFPLRLNTDLEPEQR---EKQIIETLRQVGLLP-------DHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190
....*....|....*....|....*....|...
gi 386763404 664 ECTSAVSIDVESSI----YEIAKGMGITLLTIT 692
Cdd:PRK15112 175 EALASLDMSMRSQLinlmLELQEKQGISYIYVT 207
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
503-664 |
6.46e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 48.32 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 503 MS-ISLRAVPVVTPNCDIVVPKL---TLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVK----DVPC 573
Cdd:COG4525 1 MSmLTVRHVSVRYPGGGQPQPALqdvSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDgVPVTgpgaDRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 574 MFyipQR----PYMSIGslcDQIIYPDTREDMKRKHITENELRsILKMVSLEHIAQRdsfdvvRDWKdiLSGGEKQRMAI 649
Cdd:COG4525 81 VF---QKdallPWLNVL---DNVAFGLRLRGVPKAERRARAEE-LLALVGLADFARR------RIWQ--LSGGMRQRVGI 145
|
170
....*....|....*
gi 386763404 650 ARLFYHRPRYALLDE 664
Cdd:COG4525 146 ARALAADPRFLLMDE 160
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
538-664 |
8.57e-06 |
|
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: 48.56 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 538 GPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPCMFYIP--QR------------PYMSI-GSLCdqiiYPDTREDM 601
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGRIRLgGEVLQDSARGIFLPphRRrigyvfqearlfPHLSVrGNLL----YGRKRAPR 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386763404 602 KRKHItenELRSILKMVSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:COG4148 108 AERRI---SFDEVVELLGIGHLLDR--------RPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
525-674 |
8.81e-06 |
|
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: 47.79 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 525 TLCIEPGVH-----LLITGPNGCGKSSLFRILSGLWPIYAGElhiprPVKDVPCMFYIPQrpYMSIGslcdqiiYPDTRE 599
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGD-----IEIELDTVSYKPQ--YIKAD-------YEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 600 DMKRK----HITENELRS-ILKMVSLEHIAQRDsfdvVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDEcTSAvSIDVE 674
Cdd:cd03237 80 DLLSSitkdFYTHPYFKTeIAKPLQIEQILDRE----VPE----LSGGELQRVAIAACLSKDADIYLLDE-PSA-YLDVE 149
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
475-694 |
8.94e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 475 NQSNGIIEfrNGKPIA----KGRIIYSDdpknmsISLRAVPVVTPncdiVVPKLTLCIEPGVHLLITGPNGCGKSSLFRI 550
Cdd:PLN03232 1214 SEATAIIE--NNRPVSgwpsRGSIKFED------VHLRYRPGLPP----VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNA 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 551 LSGLWPIYAGELHIPR------PVKDVP-CMFYIPQRPYMSIGSLCDQIiypdtreDMKRKHiTENELRSILKMVSLEHI 623
Cdd:PLN03232 1282 LFRIVELEKGRIMIDDcdvakfGLTDLRrVLSIIPQSPVLFSGTVRFNI-------DPFSEH-NDADLWEALERAHIKDV 1353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386763404 624 AQRDSFDV---VRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYEIAKG--MGITLLTITHR 694
Cdd:PLN03232 1354 IDRNPFGLdaeVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAHR 1429
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
521-693 |
9.86e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 521 VPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP------------RPVK-DVPCMFyipQRPYMSIG- 586
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridtlspgklQALRrDIQFIF---QDPYASLDp 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 587 --SLCDQIIYPDTREDMKRKHITENELRSILKMVSL--EHiAQRdsfdvvrdWKDILSGGEKQRMAIARLFYHRPRYALL 662
Cdd:PRK10261 417 rqTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlpEH-AWR--------YPHEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190
....*....|....*....|....*....|....*
gi 386763404 663 DECTSAVSIDVESSI----YEIAKGMGITLLTITH 693
Cdd:PRK10261 488 DEAVSALDVSIRGQIinllLDLQRDFGIAYLFISH 522
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
524-700 |
1.04e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPG-VHLlITGPNGCGKSSLFRILSG--LWPIYAGELHiprpVKDVPCMFYIP-QRPYMSIgSLCDQiiYP---- 595
Cdd:CHL00131 26 LNLSINKGeIHA-IMGPNGSGKSTLSKVIAGhpAYKILEGDIL----FKGESILDLEPeERAHLGI-FLAFQ--YPieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 596 -DTREDM-------KRKHITENEL---------RSILKMVSLEhiaqrDSFdVVRDWKDILSGGEKQRMAIARLFYHRPR 658
Cdd:CHL00131 98 gVSNADFlrlaynsKRKFQGLPELdplefleiiNEKLKLVGMD-----PSF-LSRNVNEGFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386763404 659 YALLDECTSAVSIDvesSIYEIAKGMGI------TLLTITHRPTLWKY 700
Cdd:CHL00131 172 LAILDETDSGLDID---ALKIIAEGINKlmtsenSIILITHYQRLLDY 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
526-697 |
1.09e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.47 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 526 LCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELH-IPRPV-------------KDVPCMFyipqRPYMSIGSLcdq 591
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlVGQPLhqmdeearaklraKHVGFVF----QSFMLIPTL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 592 iiypDTREDMK--------RKHITENELRSILKMVSL----EHI-AQrdsfdvvrdwkdiLSGGEKQRMAIARLFYHRPR 658
Cdd:PRK10584 104 ----NALENVElpallrgeSSRQSRNGAKALLEQLGLgkrlDHLpAQ-------------LSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386763404 659 YALLDECTSAVSIDVESSI----YEIAKGMGITLLTITHRPTL 697
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIadllFSLNREHGTTLILVTHDLQL 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
525-650 |
1.47e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 525 TLCIEPG-VH----LLITGPNGCGKSSLFRILsglwpiyAGELH-----IPRPVKdvpcMFYIPQrpYMSIGslcdqiiY 594
Cdd:COG1245 355 SLEVEGGeIRegevLGIVGPNGIGKTTFAKIL-------AGVLKpdegeVDEDLK----ISYKPQ--YISPD-------Y 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386763404 595 PDTREDMKRKHITENeLRS------ILKMVSLEHIAQRDsfdvVRDwkdiLSGGEKQRMAIA 650
Cdd:COG1245 415 DGTVEEFLRSANTDD-FGSsyykteIIKPLGLEKLLDKN----VKD----LSGGELQRVAIA 467
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
528-693 |
1.50e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 47.80 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 528 IEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI---------PRPVKDV-PCMFYIPQRPY------MSIGslcdQ 591
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFdgqditglsGRELRPLrRRMQMVFQDPYaslnprMTVG----D 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 592 IIY--PDTREDMKRKHITEnELRSILKMVSL--EHiAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:COG4608 117 IIAepLRIHGLASKAERRE-RVAELLELVGLrpEH-ADRYPHE--------FSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190
....*....|....*....|....*....|..
gi 386763404 668 A--VSIdvESSIY----EIAKGMGITLLTITH 693
Cdd:COG4608 187 AldVSI--QAQVLnlleDLQDELGLTYLFISH 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
500-693 |
1.75e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.10 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 500 PKNMSISLRAVPVVTPNCDI-VVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSG-LWPIYAGELHI--------PRPVK 569
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNSKItvdgitltAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 570 D----VPCMFYIPQRPYMSiGSLCDQIIYpdtreDMKRKHITENELRSILKMVslehIAQRDSFDVVRDWKDILSGGEKQ 645
Cdd:PRK13640 81 DirekVGIVFQNPDNQFVG-ATVGDDVAF-----GLENRAVPRPEMIKIVRDV----LADVGMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386763404 646 RMAIARLFYHRPRYALLDECTSAVS----IDVESSIYEIAKGMGITLLTITH 693
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKKNNLTVISITH 202
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
524-705 |
2.10e-05 |
|
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: 46.50 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGL---WPIYAGELHI---PRPVKDVP-CMFYIPQR-------------PYM 583
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFngqPRKPDQFQkCVAYVRQDdillpgltvretlTYT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 584 SIGSLcdqiiyPDTREDMKRKHITENELrsiLKMVSLEHIAQRdsfdVVRDwkdiLSGGEKQRMAIARLFYHRPRYALLD 663
Cdd:cd03234 106 AILRL------PRKSSDAIRKKRVEDVL---LRDLALTRIGGN----LVKG----ISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386763404 664 ECTSAV----SIDVESSIYEIAKGMGITLLTItHRPT--LWKYHTHIL 705
Cdd:cd03234 169 EPTSGLdsftALNLVSTLSQLARRNRIVILTI-HQPRsdLFRLFDRIL 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
536-693 |
2.31e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 46.67 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 536 ITGPNGCGKSSLFRILSGLWPIYAGELhiprpvkdvpcmFYipqrpymsigslCDQIIYPDTREDMkRKHI--------- 606
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGEI------------FY------------NNQAITDDNFEKL-RKHIgivfqnpdn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 607 --------------TENELRSILKMVSL--EHIAQRDSFDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVS 670
Cdd:PRK13648 95 qfvgsivkydvafgLENHAVPYDEMHRRvsEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180
....*....|....*....|....*..
gi 386763404 671 IDVESSIYEIAKGM----GITLLTITH 693
Cdd:PRK13648 175 PDARQNLLDLVRKVksehNITIISITH 201
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
483-679 |
2.70e-05 |
|
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: 46.77 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 483 FRNGKPIAKGRIIYSDDPkNMSISLRAVpVVTPncdiVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL 562
Cdd:cd03291 21 LEKAKQENNDRKHSSDDN-NLFFSNLCL-VGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 563 -HIPRpvkdvpcMFYIPQRPYMSIGSLCDQIIYPDTREdmkrkhitENELRSILKMVSLEH----IAQRDSfDVVRDWKD 637
Cdd:cd03291 95 kHSGR-------ISFSSQFSWIMPGTIKENIIFGVSYD--------EYRYKSVVKACQLEEditkFPEKDN-TVLGEGGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 386763404 638 ILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYE 679
Cdd:cd03291 159 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
607-708 |
2.95e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.26 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 607 TENELRSILKMVS-LEHIAQR-DSFD-VVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAvsIDVES------SI 677
Cdd:PRK13657 437 TDEEMRAAAERAQaHDFIERKpDGYDtVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA--LDVETeakvkaAL 514
|
90 100 110
....*....|....*....|....*....|.
gi 386763404 678 YEIAKGMgiTLLTITHRPTLWKYHTHILEFD 708
Cdd:PRK13657 515 DELMKGR--TTFIIAHRLSTVRNADRILVFD 543
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
524-715 |
3.23e-05 |
|
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: 47.24 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKdvpcMFYIpqrpymsigslcDQIiypdtredmkR 603
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK----LAYV------------DQS----------R 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 604 KHITENelRSILKMVS--LEHI------------AQRDSFDVVRDWKDI--LSGGEKQRMAIARLFYHRPRYALLDECTS 667
Cdd:TIGR03719 395 DALDPN--KTVWEEISggLDIIklgkreipsrayVGRFNFKGSDQQKKVgqLSGGERNRVHLAKTLKSGGNVLLLDEPTN 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 386763404 668 AVSID----VESSIYEIAkgmGITLLtITH-RPTLWKYHTHILEFDGLGNWQF 715
Cdd:TIGR03719 473 DLDVEtlraLEEALLNFA---GCAVV-ISHdRWFLDRIATHILAFEGDSHVEW 521
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
530-688 |
1.01e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 530 PGVH-----------LLITGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPcmfyiPQRpymsigSLCDQIIYpdT 597
Cdd:PRK10762 266 PGVNdvsftlrkgeiLGVSGLMGAGRTELMKVLYGALPRTSGYVTLDgHEVVTRS-----PQD------GLANGIVY--I 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 REDMKRK------HITEN----ELRSILK-MVSLEHIAQRDsfdVVRDWKDI--------------LSGGEKQRMAIARL 652
Cdd:PRK10762 333 SEDRKRDglvlgmSVKENmsltALRYFSRaGGSLKHADEQQ---AVSDFIRLfniktpsmeqaiglLSGGNQQKVAIARG 409
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 386763404 653 FYHRPRYALLDECTSAVSIDVESSIYEI-----AKGMGITL 688
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLinqfkAEGLSIIL 450
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
524-695 |
1.02e-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: 44.02 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGEL------HIPRPVKDVPCMFYIPQR---PYMSIGSLCDQIIY 594
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdVTAAPPADRPVSMLFQENnlfAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 595 PDTR---EDMKRKHitenelrSILKMVSLEHIAQRDSfdvvrdwkDILSGGEKQRMAIAR-LFYHRPrYALLDECTSAVS 670
Cdd:cd03298 97 PGLKltaEDRQAIE-------VALARVGLAGLEKRLP--------GELSGGERQRVALARvLVRDKP-VLLLDEPFAALD 160
|
170 180
....*....|....*....|....*....
gi 386763404 671 ----IDVESSIYEIAKGMGITLLTITHRP 695
Cdd:cd03298 161 palrAEMLDLVLDLHAETKMTVLMVTHQP 189
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
520-664 |
1.05e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 44.69 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 520 VVPKLTLCIEPG-VHLLItGPNGCGKSSLFRILSGLWPIYAGELHIP-RPVKDVPCMFY------------IPQR----- 580
Cdd:COG4604 16 VLDDVSLTIPKGgITALI-GPNGAGKSTLLSMISRLLPPDSGEVLVDgLDVATTPSRELakrlailrqenhINSRltvre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 581 -------PYmSIGSLcdqiiypdTREDmkRKHITEnelrSILKMvSLEHIAQRdsfdvvrdWKDILSGGEKQRMAIARLF 653
Cdd:COG4604 95 lvafgrfPY-SKGRL--------TAED--REIIDE----AIAYL-DLEDLADR--------YLDELSGGQRQRAFIAMVL 150
|
170
....*....|.
gi 386763404 654 YHRPRYALLDE 664
Cdd:COG4604 151 AQDTDYVLLDE 161
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
614-695 |
1.08e-04 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 45.56 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 614 ILKMVSLEHIAQRdsfdVVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSavSID------VESSIYEIAKGMGIT 687
Cdd:TIGR03269 152 LIEMVQLSHRITH----IARD----LSGGEKQRVVLARQLAKEPFLFLADEPTG--TLDpqtaklVHNALEEAVKASGIS 221
|
....*...
gi 386763404 688 LLTITHRP 695
Cdd:TIGR03269 222 MVLTSHWP 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
639-694 |
2.28e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.62 E-value: 2.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 639 LSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIY----EIAKGMgiTLLTITHR 694
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQaaldELQKNR--TSLVIAHR 538
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
519-669 |
2.95e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 43.20 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLT-------------LCIEPGVHLLITGPNGCGKSSLFRILSGL-----WPIYAGELHI--PRPV---------- 568
Cdd:PRK11264 4 IEVKNLVkkfhgqtvlhgidLEVKPGEVVAIIGPSGSGKTTLLRCINLLeqpeaGTIRVGDITIdtARSLsqqkglirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 569 -KDVPCMF----YIPQRpymsigSLCDQIIY-PDTREDMKRKHITENElRSILKMVSLEhiAQRDSFdvvrdwKDILSGG 642
Cdd:PRK11264 84 rQHVGFVFqnfnLFPHR------TVLENIIEgPVIVKGEPKEEATARA-RELLAKVGLA--GKETSY------PRRLSGG 148
|
170 180
....*....|....*....|....*..
gi 386763404 643 EKQRMAIARLFYHRPRYALLDECTSAV 669
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSAL 175
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
524-705 |
3.11e-04 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 43.02 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPG-VHLlITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKDVPCM----------FYIPQRP--------YMS 584
Cdd:TIGR01978 19 VNLTVKKGeIHA-IMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLELepderaraglFLAFQYPeeipgvsnLEF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 585 IGSLCDQIIYPDTREDMK----RKHITENelRSILKMvslehiaqrDSFDVVRDWKDILSGGEKQRMAIARLFYHRPRYA 660
Cdd:TIGR01978 98 LRSALNARRSARGEEPLDlldfEKLLKEK--LALLDM---------DEEFLNRSVNEGFSGGEKKRNEILQMALLEPKLA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386763404 661 LLDECTSAVSID----VESSIYEIA-KGMGitLLTITHRPTLWKY----HTHIL 705
Cdd:TIGR01978 167 ILDEIDSGLDIDalkiVAEGINRLRePDRS--FLIITHYQRLLNYikpdYVHVL 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
524-664 |
3.28e-04 |
|
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: 42.66 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPG--VHLLitGPNGCGKSSLFRILSGLWPIYAGELHI-PRPVKDVPC-------MFYIPQR----PYMSigslc 589
Cdd:COG0410 22 VSLEVEEGeiVALL--GRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITGLPPhriarlgIGYVPEGrrifPSLT----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 590 dqiiypdtredmkrkhITENelrsiLKMVSlehIAQRDSFDVVRDWKDI-----------------LSGGEKQRMAIARL 652
Cdd:COG0410 95 ----------------VEEN-----LLLGA---YARRDRAEVRADLERVyelfprlkerrrqragtLSGGEQQMLAIGRA 150
|
170
....*....|..
gi 386763404 653 FYHRPRYALLDE 664
Cdd:COG0410 151 LMSRPKLLLLDE 162
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
524-572 |
3.99e-04 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 42.91 E-value: 3.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPiYAGELHIP-RPVKDVP 572
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNgRPLSDWS 63
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
524-705 |
5.48e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHI--PRPVKDVPCMFY------IPQRPYMSIGSLCDQIIYP 595
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndSHNLKDINLKWWrskigvVSQDPLLFSNSIKNNIKYS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 596 -------------------DTREDMKRKHITE----NELRSILK-MVSLEHIAQRDSFDVVRDWKDI------------- 638
Cdd:PTZ00265 484 lyslkdlealsnyynedgnDSQENKNKRNSCRakcaGDLNDMSNtTDSNELIEMRKNYQTIKDSEVVdvskkvlihdfvs 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 639 ----------------LSGGEKQRMAIARLFYHRPRYALLDECTSavSIDVESSiYEIAKGMG--------ITLLtITHR 694
Cdd:PTZ00265 564 alpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATS--SLDNKSE-YLVQKTINnlkgnenrITII-IAHR 639
|
250
....*....|.
gi 386763404 695 PTLWKYHTHIL 705
Cdd:PTZ00265 640 LSTIRYANTIF 650
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
530-696 |
8.47e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 530 PGVHLLITGPNGCGKSSLFRILsglwpiyAGELhiprpvkdvpcmfyipQRPYMSIGSLCDQIIYPDTREDMKRKHITEN 609
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL-------AREL----------------GPPGGGVIYIDGEDILEEVLDQLLLIIVGGK 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 610 ELRsilkmvslehiaqrdsfdvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSI---------YEI 680
Cdd:smart00382 58 KAS--------------------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleelrllLLL 111
|
170
....*....|....*.
gi 386763404 681 AKGMGITLLTITHRPT 696
Cdd:smart00382 112 KSEKNLTVILTTNDEK 127
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
639-693 |
9.30e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 41.88 E-value: 9.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 386763404 639 LSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYEIAKGM---GITLLTITH 693
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTH 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
524-693 |
1.00e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 41.64 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 524 LTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIP-------------RPV-KDVPCMFYIPQrpymsiGSLC 589
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeiKPVrKKVGVVFQFPE------SQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 590 DQIIYPDTREDMKRKHITENELRSI----LKMVSL-EHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEKAEKIaaekLEMVGLaDEFWEKSPFE--------LSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190
....*....|....*....|....*....|..
gi 386763404 665 CTSAVSIDVE---SSIYEIAKGMGITLLTITH 693
Cdd:PRK13643 171 PTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
532-704 |
1.09e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 532 VHLLITGpNGCGKSSLFRILSGLWPIYAGELHIprpvKDVPC------------MFYIPQRPymsigslcdqIIYPD--T 597
Cdd:PRK15439 39 VHALLGG-NGAGKSTLMKIIAGIVPPDSGTLEI----GGNPCarltpakahqlgIYLVPQEP----------LLFPNlsV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 RED----MKRKHITENELRSILKM--VSLEHIAQRDSFDVvrdwkdilsgGEKQRMAIARLFYHRPRYALLDECTSAVS- 670
Cdd:PRK15439 104 KENilfgLPKRQASMQKMKQLLAAlgCQLDLDSSAGSLEV----------ADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 386763404 671 IDVESSIYEI----AKGMGITLltITHR-PTLWKYHTHI 704
Cdd:PRK15439 174 AETERLFSRIrellAQGVGIVF--ISHKlPEIRQLADRI 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
535-693 |
1.25e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 41.18 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 535 LItGPNGCGKSSLFRILSGLWPIYAG-------ELH---IPRPVKDVP------CMfyIPQRP---YMSIGslcDQIIYP 595
Cdd:COG1117 42 LI-GPSGCGKSTLLRCLNRMNDLIPGarvegeiLLDgedIYDPDVDVVelrrrvGM--VFQKPnpfPKSIY---DNVAYG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 596 DTREDMKRKHITENELRSILKMVSLehiaqrdsfdvvrdW---KDIL-------SGGEKQRMAIARLFYHRPRYALLDEC 665
Cdd:COG1117 116 LRLHGIKSKSELDEIVEESLRKAAL--------------WdevKDRLkksalglSGGQQQRLCIARALAVEPEVLLMDEP 181
|
170 180 190
....*....|....*....|....*....|....
gi 386763404 666 TSAvsID------VESSIYEIAKGMgiTLLTITH 693
Cdd:COG1117 182 TSA--LDpistakIEELILELKKDY--TIVIVTH 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
519-684 |
1.57e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 41.61 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLTLCIEPGVHLLITGPNGCGKSS----LFRILSGLWPI-YAGE-LHIPRPVKDVPC---MFYIPQRPYMSIGSLC 589
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIwFDGQpLHNLNRRQLLPVrhrIQVVFQDPNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 590 D--QIIYPDTREDMKRKHITENELRSILKM--VSLEHiAQRDSFDVVrdwkdiLSGGEKQRMAIARLFYHRPRYALLDEC 665
Cdd:PRK15134 380 NvlQIIEEGLRVHQPTLSAAQREQQVIAVMeeVGLDP-ETRHRYPAE------FSGGQRQRIAIARALILKPSLIILDEP 452
|
170
....*....|....*....
gi 386763404 666 TSAVSIDVESSIYEIAKGM 684
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSL 471
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
519-664 |
1.95e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 40.86 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 519 IVVPKLTLCIEPGVhllIT---GPNGCGKSSLFRILSGLWPIYAGELHI---PRPVKDVPCMFYIPQ----RPYMSIGsl 588
Cdd:COG4152 15 TAVDDVSFTVPKGE---IFgllGPNGAGKTTTIRIILGILAPDSGEVLWdgePLDPEDRRRIGYLPEerglYPKMKVG-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 589 cDQIIYPDTREDMKRKHIteneLRSILKMVslehiaqrDSFDVVrDWKD--I--LSGGEKQRMAIARLFYHRPRYALLDE 664
Cdd:COG4152 90 -EQLVYLARLKGLSKAEA----KRRADEWL--------ERLGLG-DRANkkVeeLSKGNQQKVQLIAALLHDPELLILDE 155
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
534-690 |
2.27e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.93 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 534 LLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKDVPCMFYIPQ----------RPYMSIGSLCdqiiYPDTREDMKR 603
Cdd:PRK13540 30 LHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQlcfvghrsgiNPYLTLRENC----LYDIHFSPGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 604 KHITEnelrsILKMVSLEHIAqrdsfdvvrDWK-DILSGGEKQRMAIARLFYHRPRYALLDEctSAVSID------VESS 676
Cdd:PRK13540 106 VGITE-----LCRLFSLEHLI---------DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDE--PLVALDelslltIITK 169
|
170
....*....|....
gi 386763404 677 IYEIAKGMGITLLT 690
Cdd:PRK13540 170 IQEHRAKGGAVLLT 183
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
639-693 |
2.92e-03 |
|
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: 40.82 E-value: 2.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386763404 639 LSGGEKQRMAIARLFYHRPRYALLDECTSA--VSIDVEssIYEIAKGM----GITLLTITH 693
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSAldVSVQAQ--ILDLLRDLqrehGLAYLFISH 484
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
522-679 |
2.96e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 522 PKLT---LCIEPGVHLLITGPNGCGKSSLFRILSG-LWPIYAGELHIPRPVKdvpcmfYIPQRPYMSIGSLCDQIIYPDT 597
Cdd:PLN03232 631 PTLSdinLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVA------YVPQVSWIFNATVRENILFGSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 598 REdmkrkhiTENELRSIlKMVSLEH----IAQRDSFDVVRDWKDIlSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDV 673
Cdd:PLN03232 705 FE-------SERYWRAI-DVTALQHdldlLPGRDLTEIGERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
....*.
gi 386763404 674 ESSIYE 679
Cdd:PLN03232 776 AHQVFD 781
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
536-686 |
4.47e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.39 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 536 ITGPNGCGKSSLFRILSGLWPIYAGELHI---PRPVKDVPC-----MFYIPQ-R------PYMSIGslcDQIIYPDTRED 600
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLdgkPVRIRSPRDairagIAYVPEdRkgeglvLDLSIR---ENITLASLDRL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 601 MKRKHITENELRSIL-KMVSLEHIAQRDSFDVVRDwkdiLSGGEKQRMAIARLFYHRPRYALLDECTsaVSIDVES--SI 677
Cdd:COG1129 360 SRGGLLDRRRERALAeEYIKRLRIKTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPT--RGIDVGAkaEI 433
|
170
....*....|....
gi 386763404 678 YEI-----AKGMGI 686
Cdd:COG1129 434 YRLirelaAEGKAV 447
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
612-693 |
7.42e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 39.30 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 612 RSILKMVSL-EHIAQRDSFDvvrdwkdiLSGGEKQRMAIARLFYHRPRYALLDECTSAV----SIDVESSIYEIAKgMGI 686
Cdd:PRK13651 146 AKYIELVGLdESYLQRSPFE--------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLdpqgVKEILEIFDNLNK-QGK 216
|
....*..
gi 386763404 687 TLLTITH 693
Cdd:PRK13651 217 TIILVTH 223
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
536-569 |
7.75e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 7.75e-03
10 20 30
....*....|....*....|....*....|....
gi 386763404 536 ITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVK 569
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK 388
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
505-553 |
8.87e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.23 E-value: 8.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 386763404 505 ISLRAVpVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSG 553
Cdd:PRK10938 261 IVLNNG-VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
534-692 |
9.69e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 39.04 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 534 LLITGPNGCGKSSLFRILSGLWP-IYAGELHIP-RPVKDVPCMFYIPQRPYMsigslcdqiiypdTREDMKR-------- 603
Cdd:TIGR02633 289 LGVAGLVGAGRTELVQALFGAYPgKFEGNVFINgKPVDIRNPAQAIRAGIAM-------------VPEDRKRhgivpilg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763404 604 --KHITENELRSILKMVSLEHIAQRDSFD-------VVRDWKDI----LSGGEKQRMAIARLFYHRPRYALLDECTSAVS 670
Cdd:TIGR02633 356 vgKNITLSVLKSFCFKMRIDAAAELQIIGsaiqrlkVKTASPFLpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180
....*....|....*....|....*
gi 386763404 671 IDVESSIYEIAKGM---GITLLTIT 692
Cdd:TIGR02633 436 VGAKYEIYKLINQLaqeGVAIIVVS 460
|
|
| |
