|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-532 |
1.43e-173 |
|
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: 500.97 E-value: 1.43e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MT--IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaiKGEVTGSLEINGKNISDFSM 78
Cdd:COG1123 1 MTplLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPH--GGRISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 79 HDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILV 158
Cdd:COG1123 79 ALRGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILASelle 238
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEI-ADRVVVMDDGRIVEDGPPEEILAA---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 239 thgirePLYLSAlkaakapltsedklsnlkaldykrfRPAVQAWFAERPTPVAEKQyqPLLEVHGLTYSYD----GEKNA 314
Cdd:COG1123 234 ------PQALAA-------------------------VPRLGAARGRAAPAAAAAE--PLLEVRNLSKRYPvrgkGGVRA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS---IFERSQKVGVVMQNPNHMISHHM- 390
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYSSLNPRMt 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 391 IFDEVAFGLRNRGVA-EQEIKEKVENVLELCGLS-KFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNY 468
Cdd:COG1123 361 VGDIIAEPLRLHGLLsRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQ 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 469 TSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP-SLLERANL 532
Cdd:COG1123 441 AQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPqHPYTRALL 505
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
299-529 |
1.53e-93 |
|
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: 285.77 E-value: 1.53e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:COG1122 81 FQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 459 PTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLER 529
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
300-510 |
3.45e-92 |
|
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: 281.28 E-value: 3.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 300 EVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515631642 459 PTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-221 |
7.27e-88 |
|
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: 270.11 E-value: 7.27e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 5 FSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEINGKNISDFSMHDYTEQ 84
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL-----GPTSGEVLVDGKDLTKLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 85 VGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:cd03225 77 VGLVFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLhRDIDRVILMERGE 221
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLL-ELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-238 |
2.68e-83 |
|
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: 259.19 E-value: 2.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikgeVTGSLEINGKNISDFSMHDYT 82
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP-----TSGEVLVDGKDITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:COG1122 75 RKVGLVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILA-SELLE 238
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVA-ELADRVIVLDDGRIVADGTPREVFSdYELLE 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-245 |
5.64e-76 |
|
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: 241.57 E-value: 5.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISDFS-MHDY 81
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLL-PTSGKVT----VDGLDTLDEEnLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:TIGR04520 76 RKKVGMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTPDEILA-SELLETH 240
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV--LADRVIVMNKGKIVAEGTPREIFSqVELLKEI 233
|
....*
gi 515631642 241 GIREP 245
Cdd:TIGR04520 234 GLDVP 238
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
299-545 |
5.86e-70 |
|
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: 226.16 E-value: 5.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGED-LSELSIFERSQKVG 376
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLIL 456
Cdd:TIGR04520 81 MVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 457 DEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCTTS 536
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVELLKEIGLDVPF 239
|
....*....
gi 515631642 537 IYELATMMK 545
Cdd:TIGR04520 240 ITELAKALK 248
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
299-545 |
3.92e-63 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 208.46 E-value: 3.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS-- 372
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 -QKVGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVL 449
Cdd:TIGR04521 81 rKKVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeyLERSPFE-LSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 450 EPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLER 529
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDELEK 239
|
250
....*....|....*.
gi 515631642 530 ANLCTTSIYELATMMK 545
Cdd:TIGR04521 240 IGLDVPEITELARKLK 255
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-262 |
4.00e-62 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 205.76 E-value: 4.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYE---SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PhaikgeVTGSLEINGKNIS---D 75
Cdd:TIGR04521 1 IKLKNVSYIYQpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLkP------TSGTVTIDGRDITakkK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 76 FSMHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDL-ADMLDRSPHDLSGGQKQRVSLA 154
Cdd:TIGR04521 75 KKLKDLRKKVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILA- 233
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEY-ADRVIVMHKGKIVLDGTPREVFSd 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 515631642 234 SELLETHGIREP--LYL-SALKAA-----KAPLTSED 262
Cdd:TIGR04521 234 VDELEKIGLDVPeiTELaRKLKEKglpvpKDPLTVEE 270
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-235 |
4.38e-62 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 205.61 E-value: 4.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDFSMHDY 81
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQS------GEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK13632 82 RKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTPDEILASE 235
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI--LADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-238 |
4.01e-61 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 203.32 E-value: 4.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYT 82
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-----AGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK13635 81 RQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdiDRVILMERGEIVADMTPDEI--LASELLE 238
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQA--DRVIVMNKGEILEEGTPEEIfkSGHMLQE 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
298-561 |
1.81e-57 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 193.37 E-value: 1.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--SELSIFERSQKV 375
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCTT 535
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLRLP 239
|
250 260
....*....|....*....|....*..
gi 515631642 536 SIYELATMM-KIDDTNAFMQYFIDYER 561
Cdd:PRK13639 240 RVAHLIEILnKEDNLPIKMGYTIGEAR 266
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
296-545 |
2.73e-57 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 193.31 E-value: 2.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK 374
Cdd:PRK13635 3 EEIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13635 83 VGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCT 534
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQEIGLDV 241
|
250
....*....|.
gi 515631642 535 TSIYELATMMK 545
Cdd:PRK13635 242 PFSVKLKELLK 252
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
298-530 |
3.04e-56 |
|
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: 189.48 E-value: 3.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:COG1120 1 MLEAENLSVGYGG-RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPNhmISHHM-IFDEVAFG----LRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPE 452
Cdd:COG1120 80 VPQEPP--APFGLtVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 453 LLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSqPSLLERA 530
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT-PELLEEV 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
298-552 |
7.78e-56 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 189.67 E-value: 7.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE--DLSELSIFERSQKV 375
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK13636 85 GMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCTT 535
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNLRLP 244
|
250
....*....|....*..
gi 515631642 536 SIYELATMMKIDDTNAF 552
Cdd:PRK13636 245 RIGHLMEILKEKDGFVF 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
296-521 |
2.01e-55 |
|
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: 186.72 E-value: 2.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS--- 372
Cdd:COG1127 3 EPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 QKVGVVMQNP---NHMishhMIFDEVAFGLR-NRGVAEQEIKEKVENVLELCGLSKFRH-WPIEaLSYGQKKRVTIASIL 447
Cdd:COG1127 82 RRIGMLFQGGalfDSL----TVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADkMPSE-LSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 448 VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVF 521
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
296-524 |
1.36e-54 |
|
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: 185.24 E-value: 1.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKv 375
Cdd:COG0411 2 DPLLEVRGLTKRFGGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVM--QNP----------NHMISHHM----IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKK 439
Cdd:COG0411 80 GIARtfQNPrlfpeltvleNVLVAAHArlgrGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
....*
gi 515631642 520 VFSQP 524
Cdd:COG0411 240 VRADP 244
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
308-495 |
1.75e-52 |
|
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: 177.23 E-value: 1.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 308 YDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE--DLSELSIFERSQKVGVVMQNPNHM 385
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRKGLLERRQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 386 ISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDY 465
Cdd:TIGR01166 81 LFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 515631642 466 RNYTSMLAFIQKLnRELGITVVIISHDMHL 495
Cdd:TIGR01166 161 AGREQMLAILRRL-RAEGMTVVISTHDVDL 189
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
296-528 |
2.24e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 178.74 E-value: 2.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSelsifERSQKV 375
Cdd:COG1121 4 MPAIELENLTVSYGG-RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQnpNHMISHHM---IFDEVAFGLRNR----GVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:COG1121 78 GYVPQ--RAEVDWDFpitVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADsKLIANAAMTEVFSQPSLLE 528
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEEVLTPENLSR 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
299-545 |
3.12e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 179.86 E-value: 3.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSE--LSIFERS 372
Cdd:PRK13637 3 IKIENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 QKVGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLS--KFR-HWPIEaLSYGQKKRVTIASILVL 449
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKdKSPFE-LSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 450 EPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLER 529
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLES 241
|
250
....*....|....*.
gi 515631642 530 ANLCTTSIYELATMMK 545
Cdd:PRK13637 242 IGLAVPQVTYLVRKLR 257
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
299-521 |
3.71e-52 |
|
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: 178.08 E-value: 3.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQ---KV 375
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNpNHMISHHMIFDEVAFGLR-NRGVAEQEIKEKVENVLELCGLSKFRH-WPIEaLSYGQKKRVTIASILVLEPEL 453
Cdd:cd03261 80 GMLFQS-GALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDlYPAE-LSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 454 LILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVF 521
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-233 |
8.14e-52 |
|
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: 188.50 E-value: 8.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYT 82
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT-----SGRILIDGIDLRQIDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDtDSQFVGlSIGEDIAFALEnqlvsNIDMYPLVKStAKMVDLADMLDRSPH-----------DLSGGQKQRV 151
Cdd:COG2274 549 RQIGVVLQD-VFLFSG-TIRENITLGDP-----DATDEEIIEA-ARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDEI 231
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI--RLADRIIVLDKGRIVEDGTHEEL 696
|
..
gi 515631642 232 LA 233
Cdd:COG2274 697 LA 698
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
300-513 |
8.66e-52 |
|
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: 176.18 E-value: 8.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 300 EVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSElsifeRSQKVGVVM 379
Cdd:cd03235 1 EVEDLTVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 380 QNPNhmISHHM---IFDEVAFGLRNRGVAEQEI----KEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPE 452
Cdd:cd03235 75 QRRS--IDRDFpisVRDVVLMGLYGHKGLFRRLskadKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 453 LLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIaDSKLIA 513
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVA 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
299-513 |
1.22e-51 |
|
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: 175.79 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR--NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNHMisHHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03259 78 FQDYALF--PHLtVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
296-524 |
2.51e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 179.52 E-value: 2.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKV 375
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR--NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQN----PnhmishHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLE 450
Cdd:COG3842 80 GMVFQDyalfP------HLtVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 451 PELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERP 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
299-524 |
2.51e-51 |
|
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: 175.70 E-value: 2.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKvGVV 378
Cdd:cd03219 1 LEVRGLTKRFGGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARL-GIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 M--QNP----------NHMISHHMIFDEVAFGLRNRGvAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:cd03219 79 RtfQIPrlfpeltvleNVMVAAQARTGSGLLLARARR-EEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-245 |
3.17e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 177.10 E-value: 3.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDFS-MHD 80
Cdd:PRK13644 2 IRLENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQK------GKVLVSGIDTGDFSkLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDD 160
Cdd:PRK13644 75 IRKLVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 161 VDILLFDEPLASLDPKTGKATIEIIDQLHkETNKTIVIIEHRLEDvLHrDIDRVILMERGEIVADMTPDEILASELLETH 240
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEE-LH-DADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
....*
gi 515631642 241 GIREP 245
Cdd:PRK13644 232 GLTPP 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
295-545 |
8.10e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 176.05 E-value: 8.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 295 YQPLLEVHGLTYSY-----DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS-I 368
Cdd:PRK13633 1 MNEMIKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 369 FERSQKVGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQPSLLE 528
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMK 239
|
250
....*....|....*..
gi 515631642 529 RANLCTTSIYELATMMK 545
Cdd:PRK13633 240 KIGLDVPQVTELAYELK 256
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
299-512 |
1.77e-50 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 172.93 E-value: 1.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSifeRSQ----- 373
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK---RREipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 374 -KVGVVMQNpNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPE 452
Cdd:COG2884 79 rRIGVVFQD-FRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 453 LLILDEPTAGQDYRNYTSMLAFIQKLNReLGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-245 |
2.30e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 174.85 E-value: 2.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRY---ESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHaikgevTGSLEINGKNISD- 75
Cdd:PRK13637 1 MSIKIENLTHIYmegTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPT------SGKIIIDGVDITDk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 76 -FSMHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMV--DLADMLDRSPHDLSGGQKQRVS 152
Cdd:PRK13637 75 kVKLSDIRKKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEIL 232
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVA-KLADRIIVMNKGKCELQGTPREVF 233
|
250
....*....|....
gi 515631642 233 AS-ELLETHGIREP 245
Cdd:PRK13637 234 KEvETLESIGLAVP 247
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
300-513 |
2.62e-50 |
|
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: 171.08 E-value: 2.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 300 EVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVM 379
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 380 QnpnhmishhmifdevafglrnrgvaeqeikekvenVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:cd03214 80 Q-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515631642 460 TAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
299-511 |
3.08e-50 |
|
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: 172.29 E-value: 3.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKN---ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS----IFER 371
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 372 SQKVGVVMQNPNhMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:cd03255 81 RRHIGFVFQSFN-LLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVlEYTTRSIVIADSKL 511
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
296-516 |
3.08e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 172.54 E-value: 3.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS 372
Cdd:COG1136 2 SPLLELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 ----QKVGVVMQNPNhMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:COG1136 82 rlrrRHIGFVFQFFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLvLEYTTRSIVIADSKLIANAA 516
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLRDGRIVSDER 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
296-549 |
3.19e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 174.02 E-value: 3.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK 374
Cdd:PRK13632 5 SVMIKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13632 85 IGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCT 534
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEILEKAKIDS 243
|
250
....*....|....*.
gi 515631642 535 TSIYELATMMK-IDDT 549
Cdd:PRK13632 244 PFIYKLSKKLKgIDPT 259
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
299-520 |
5.43e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.17 E-value: 5.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsQKVGVV 378
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNhmishhmiFDE-------VAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:COG1131 79 PQEPA--------LYPdltvrenLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-247 |
5.57e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 173.83 E-value: 5.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAIKgevTGSLEINGKNISDFSMHDY 81
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNP---NSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK13640 83 REKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHrdIDRVILMERGEIVADMTPDEILA-SELLETH 240
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM--ADQVLVLDDGKLLAQGSPVEIFSkVEMLKEI 240
|
....*..
gi 515631642 241 GIREPLY 247
Cdd:PRK13640 241 GLDIPFV 247
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
298-532 |
7.48e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 173.38 E-value: 7.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDG--EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKV 375
Cdd:PRK13650 4 IIEVKNLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVlEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANL 532
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDLLQLGL 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-524 |
8.27e-50 |
|
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: 179.88 E-value: 8.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 9 SFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIkGEVTGSLEINGKNIsdfsmhdyteqvgtv 88
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPA-AHPSGSILFDGQDL--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 89 LQDTDSQFVGLSiGEDIAF-------AL------ENQLVSnidmyPLV--------KSTAKMVDL---------ADMLDR 138
Cdd:COG4172 79 LGLSERELRRIR-GNRIAMifqepmtSLnplhtiGKQIAE-----VLRlhrglsgaAARARALELlervgipdpERRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 139 SPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPkTGKATI-EIIDQLHKETNKTIVIIEHRLEDVlhRDI-DRVIL 216
Cdd:COG4172 153 YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQAQIlDLLKDLQRELGMALLLITHDLGVV--RRFaDRVAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 217 MERGEIVADMTPDEILASEllethgiREPlYLSALKAAkapltsedklsnlkaldykrfRPAVqawfaeRPTPVAEKQyQ 296
Cdd:COG4172 230 MRQGEIVEQGPTAELFAAP-------QHP-YTRKLLAA---------------------EPRG------DPRPVPPDA-P 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYD----------GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAdSGSSYLNGEDLSEL 366
Cdd:COG4172 274 PLLEARDLKVWFPikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 367 SifeRSQ------KVGVVMQNPNHMISHHM-IFDEVAFGLR--NRGVAEQEIKEKVENVLELCGLSK-FRH-WPIEaLSY 435
Cdd:COG4172 353 S---RRAlrplrrRMQVVFQDPFGSLSPRMtVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPaARHrYPHE-FSG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 436 GQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANA 515
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQG 508
|
....*....
gi 515631642 516 AMTEVFSQP 524
Cdd:COG4172 509 PTEQVFDAP 517
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
299-532 |
3.13e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 171.46 E-value: 3.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:PRK13647 85 FQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 459 PTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAmTEVFSQPSLLERANL 532
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KSLLTDEDIVEQAGL 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
310-525 |
3.54e-49 |
|
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: 170.07 E-value: 3.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE---RSQKVGVVMQNPNhMI 386
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkARRRIGMIFQHFN-LL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 387 SHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYR 466
Cdd:cd03258 95 SSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 467 NYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:cd03258 175 TTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
299-545 |
4.24e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 171.52 E-value: 4.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVI---DADSGSSYLNGEDLSELSIFERSQK 374
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13640 86 VGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVlEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCT 534
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDI 244
|
250
....*....|.
gi 515631642 535 TSIYELATMMK 545
Cdd:PRK13640 245 PFVYKLKNKLK 255
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
16-224 |
6.79e-49 |
|
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: 168.47 E-value: 6.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDytEQVGTVLQDtDSQ 95
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-----SGEILIDGRDVTGVPPER--RNIGMVFQD-YAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:cd03259 84 FPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515631642 176 KTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVA 224
Cdd:cd03259 164 KLREELREELKELQRELGITTIYVTHDQEEAL-ALADRIAVMNEGRIVQ 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-523 |
1.23e-48 |
|
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: 176.53 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL----------IPHAIKGEVTGSLEINGK-------------- 71
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriIYHVALCEKCGYVERPSKvgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 72 ------NISDFSMHDYTEQVGTVLQDTDSQFvglsiGEDIAfaLENQLVSNIDM-YPLVKSTAKMVDLADMLD---RSPH 141
Cdd:TIGR03269 92 eevdfwNLSDKLRRRIRKRIAIMLQRTFALY-----GDDTV--LDNVLEALEEIgYEGKEAVGRAVDLIEMVQlshRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 142 ---DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEdVLHRDIDRVILME 218
Cdd:TIGR03269 165 iarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE-VIEDLSDKAIWLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 219 RGEIVADMTPDEILAsELLEThgireplyLSALKAAKAPLTSED--KLSNLKaldykrfrpavqawfaerptpvaeKQYq 296
Cdd:TIGR03269 244 NGEIKEEGTPDEVVA-VFMEG--------VSEVEKECEVEVGEPiiKVRNVS------------------------KRY- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 pllevhgltYSYD-GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLN-GE---DLSELSIFER 371
Cdd:TIGR03269 290 ---------ISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvDMTKPGPDGR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 372 ---SQKVGVVMQNPNhMISHHMIFDEV--AFGL-------RNRGVAEQEI----KEKVENVLElcglskfrHWPIEaLSY 435
Cdd:TIGR03269 361 graKRYIGILHQEYD-LYPHRTVLDNLteAIGLelpdelaRMKAVITLKMvgfdEEKAEEILD--------KYPDE-LSE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 436 GQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANA 515
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*...
gi 515631642 516 AMTEVFSQ 523
Cdd:TIGR03269 511 DPEEIVEE 518
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-270 |
2.91e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 169.43 E-value: 2.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYES---LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVT-GSLEI-NGKNISD 75
Cdd:PRK13634 1 MDITFQKVEHRYQYktpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL-QPTSGTVTiGERVItAGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 76 fsMHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDL-ADMLDRSPHDLSGGQKQRVSLA 154
Cdd:PRK13634 80 --LKPLRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILA- 233
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAA-RYADQIVVMHKGTVFLQGTPREIFAd 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 515631642 234 SELLETHGIREP---LYLSALKAA------KAPLTSEDKLSNLKAL 270
Cdd:PRK13634 237 PDELEAIGLDLPetvKFKRALEEKfgisfpKPCLTLEELAHEVVQL 282
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-235 |
4.41e-48 |
|
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: 167.46 E-value: 4.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVtgslEINGKNISDFSMHDYT 82
Cdd:COG1127 6 IEVRNLTKSFG--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR-PDSGEI----LVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 E---QVGTVLQDT---DSqfvgLSIGEDIAFAL-ENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAG 155
Cdd:COG1127 79 ElrrRIGMLFQGGalfDS----LTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEILAS 234
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSA--FAIaDRVAVLADGKIIAEGTPEELLAS 232
|
.
gi 515631642 235 E 235
Cdd:COG1127 233 D 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
299-492 |
4.51e-48 |
|
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: 167.03 E-value: 4.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR--PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNpnHMISHHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03300 78 FQN--YALFPHLtVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190
....*....|....*....|....*....|....*
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHD 492
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHD 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
298-555 |
4.99e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 168.44 E-value: 4.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:PRK13652 83 VFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCTTSI 537
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLPSL 242
|
250
....*....|....*...
gi 515631642 538 YELATMMKIDDTNAFMQY 555
Cdd:PRK13652 243 PKLIRSLQAQGIAIDMAY 260
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
299-494 |
9.22e-48 |
|
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: 165.72 E-value: 9.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSelsifERSQKV 375
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNhMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKF-RHWPIEaLSYGQKKRVTIASILVLEPELL 454
Cdd:cd03293 76 GYVFQQDA-LLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFeNAYPHQ-LSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMH 494
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDID 193
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-242 |
4.20e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 173.43 E-value: 4.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISDFSMHD 80
Cdd:COG1132 339 EIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY------DPTsGRILIDGVDIRDLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQDTdSQFVGlSIGEDIAFALENqlVSNIDmyplVKSTAKMVDLADMLDRSPH-----------DLSGGQKQ 149
Cdd:COG1132 412 LRRQIGVVPQDT-FLFSG-TIRENIRYGRPD--ATDEE----VEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 150 RVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPD 229
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTI--RNADRILVLDDGRIVEQGTHE 559
|
250
....*....|...
gi 515631642 230 eilasELLETHGI 242
Cdd:COG1132 560 -----ELLARGGL 567
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-238 |
5.22e-47 |
|
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: 164.83 E-value: 5.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYT 82
Cdd:COG1120 2 LEAENLSVGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-----SGEVLLDGRDLASLSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTDSQFvGLSIGEDIA---------FALENQlvsniDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSL 153
Cdd:COG1120 75 RRIAYVPQEPPAPF-GLTVRELVAlgryphlglFGRPSA-----EDREAVEEALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 154 AGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIiehrledVLHrDI-------DRVILMERGEIVADM 226
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVM-------VLH-DLnlaaryaDRLVLLKDGRIVAQG 220
|
250
....*....|..
gi 515631642 227 TPDEILASELLE 238
Cdd:COG1120 221 PPEEVLTPELLE 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-235 |
6.49e-47 |
|
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: 172.64 E-value: 6.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDY 81
Cdd:COG4988 336 SIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDtdSQFVGLSIGEDIAFALENqlVSNIDMyplvKSTAKMVDLADMLDRSPHD-----------LSGGQKQR 150
Cdd:COG4988 410 RRQIAWVPQN--PYLFAGTIRENLRLGRPD--ASDEEL----EAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDE 230
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL--AQADRILVLDDGRIVEQGTHEE 557
|
....*
gi 515631642 231 ILASE 235
Cdd:COG4988 558 LLAKN 562
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
298-512 |
8.07e-47 |
|
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: 163.45 E-value: 8.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS---IFER 371
Cdd:cd03257 1 LLEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 372 SQKVGVVMQNPNHMISHHM-IFDEVAFGLRNRGV--AEQEIKEKVENVLELCGLSK--FRHWPIEaLSYGQKKRVTIASI 446
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMtIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLPEevLNRYPHE-LSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-221 |
8.16e-47 |
|
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: 161.40 E-value: 8.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikgeVTGSLEINGKNISDFSMHDYT 82
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP-----TSGEILIDGVDLRDLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTdsQFVGLSIGEdiafalenqlvsNIdmyplvkstakmvdladmldrsphdLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03228 76 KNIAYVPQDP--FLFSGTIRE------------NI-------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGE 221
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI--RDADRIIVLDDGR 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
298-520 |
8.77e-47 |
|
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: 163.88 E-value: 8.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVGV 377
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNpNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:COG4555 79 LPDE-RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG4555 158 EPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
296-492 |
2.15e-46 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 163.34 E-value: 2.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELsiferS 372
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 QKVGVVMQNPNHMisHHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFR-HWPIEaLSYGQKKRVTIASILVLE 450
Cdd:COG1116 80 PDRGVVFQEPALL--PWLtVLDNVALGLELRGVPKAERRERARELLELVGLAGFEdAYPHQ-LSGGMRQRVAIARALAND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515631642 451 PELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHD 492
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-235 |
1.37e-45 |
|
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: 160.36 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVtgslEINGKNISDFSMHDYT 82
Cdd:cd03261 1 IELRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR-PDSGEV----LIDGEDISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 E---QVGTVLQDTdSQFVGLSIGEDIAFAL-ENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILV 158
Cdd:cd03261 74 RlrrRMGMLFQSG-ALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEILASE 235
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTA-FAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-222 |
2.08e-45 |
|
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: 159.58 E-value: 2.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgeVT-GSLEINGKNISDFSMH 79
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR------PTsGEVRVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYT----EQVGTVLQdtdsQF---VGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVS 152
Cdd:cd03255 75 ELAafrrRHIGFVFQ----SFnllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHrlEDVLHRDIDRVILMERGEI 222
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTH--DPELAEYADRIIELRDGKI 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-231 |
2.30e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 163.35 E-value: 2.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDFSMHDy 81
Cdd:COG3842 6 LELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFEtPDS------GRILLDGRDVTGLPPEK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 tEQVGTVLQDtDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:COG3842 77 -RNVGMVFQD-YALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhrdiDRVILMERGEIVADMTPDEI 231
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALal-aDRIAVMNDGRIEQVGTPEEI 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
5.24e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 159.92 E-value: 5.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaIKGEVTGSLEINGKNISDFSMHDYT 82
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-----IEKVKSGEIFYNNQAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK13648 83 KHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdiDRVILMERGEIVADMTPDEIL--ASELLE 238
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA--DHVIVMNKGTVYKEGTPTEIFdhAEELTR 238
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
298-544 |
1.93e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 158.63 E-value: 1.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE--DLSELSIFERSQKV 375
Cdd:PRK13638 1 MLATSDLWFRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK13638 80 ATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCTT 535
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQP 238
|
....*....
gi 515631642 536 SIYELATMM 544
Cdd:PRK13638 239 WLVKLHTQL 247
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-233 |
3.25e-44 |
|
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: 165.32 E-value: 3.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDFSMHD 80
Cdd:COG4987 333 SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLdPQS------GSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQDT---DSqfvglSIGEDIAFALENqlVSNIDMYplvkSTAKMVDLADMLDRSPHDL-----------SGG 146
Cdd:COG4987 407 LRRRIAVVPQRPhlfDT-----TLRENLRLARPD--ATDEELW----AALERVGLGDWLAALPDGLdtwlgeggrrlSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 147 QKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADM 226
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL--ERMDRILVLEDGRIVEQG 551
|
....*..
gi 515631642 227 TPDEILA 233
Cdd:COG4987 552 THEELLA 558
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-524 |
3.77e-44 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 165.80 E-value: 3.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 7 NFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEV-TGSLEINGKNisdfsmhdytEQV 85
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQA-GGLVqCDKMLLRRRS----------RQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 86 GTVLQDTDSQFVGLSiGEDIA-------------FALENQLVSNIDMYPLVKSTAKMVDLADMLD------------RSP 140
Cdd:PRK10261 88 IELSEQSAAQMRHVR-GADMAmifqepmtslnpvFTVGEQIAESIRLHQGASREEAMVEAKRMLDqvripeaqtilsRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 141 HDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERG 220
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDM-GVVAEIADRVLVMYQG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 221 EIVADMTPDEILaselletHGIREPlYLSALKAAkAPltsedKLSNLKALDYKRFRPAVQAWFAERPTPVAEKQY----Q 296
Cdd:PRK10261 246 EAVETGSVEQIF-------HAPQHP-YTRALLAA-VP-----QLGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTvvdgE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSY----------DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSEL 366
Cdd:PRK10261 312 PILQVRNLVTRFplrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 367 SIFERS---QKVGVVMQNPNHMIS-HHMIFDEVAFGLRNRGVAE-QEIKEKVENVLELCGLSKFRHW--PIEaLSYGQKK 439
Cdd:PRK10261 392 SPGKLQalrRDIQFIFQDPYASLDpRQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAWryPHE-FSGGQRQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
|
....*
gi 515631642 520 VFSQP 524
Cdd:PRK10261 551 VFENP 555
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-512 |
4.11e-44 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 164.08 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 5 FSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTGSleiNGKNISDFSMHDYTEQ 84
Cdd:COG0488 1 LENLSKSFG--GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGEL-EPDSGEVSIP---KGLRIGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 85 VGTVLQDTDSQFVGL-SIGEDIAFALENQLVSNIDMYPLVKSTAKMVDL-------------------ADMLDRSPHDLS 144
Cdd:COG0488 75 DLTVLDTVLDGDAELrALEAELEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsglgfpEEDLDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDpktgkatIEIIDQLH---KETNKTIVIIEH-R--LEDVlhrdIDRVILME 218
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEWLEeflKNYPGTVLVVSHdRyfLDRV----ATRILELD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 219 RGEIvadmTP------------DEILASELL-----------ETHGIREPLYlSALKAAKAplTS-EDKLSNLKALDYKR 274
Cdd:COG0488 224 RGKL----TLypgnysayleqrAERLEQEAAayakqqkkiakEEEFIRRFRA-KARKAKQA--QSrIKALEKLEREEPPR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 275 FRPAVQAWFaerptPVAEKQYQPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSG 354
Cdd:COG0488 297 RDKTVEIRF-----PPPERLGKKVLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 355 SSYLnGEDLselsifersqKVGVVMQNPNHMISHHMIFDEVafglrnRGVAEQEIKEKVENVLELCGLSKFRHW-PIEAL 433
Cdd:COG0488 371 TVKL-GETV----------KIGYFDQHQEELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSGDDAFkPVGVL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 434 SYGQKKRVTIASILVLEPELLILDEPTagqdyrNY--TSML-AFIQKLNRELGiTVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPT------NHldIETLeALEEALDDFPG-TVLLVSHDRYFLDRVATRILEFEDGG 506
|
..
gi 515631642 511 LI 512
Cdd:COG0488 507 VR 508
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-236 |
4.33e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 156.76 E-value: 4.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFS---MH 79
Cdd:COG3638 3 LELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGEILVDGQDVTALRgraLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYTEQVGTVLQdtdsQF--VG-LSigediafALENQLVSNIDMYPLVKSTAKM---------------VDLADMLDRSPH 141
Cdd:COG3638 77 RLRRRIGMIFQ----QFnlVPrLS-------VLTNVLAGRLGRTSTWRSLLGLfppedreralealerVGLADKAYQRAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 142 DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERGE 221
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQV-DLARRYADRIIGLRDGR 224
|
250
....*....|....*
gi 515631642 222 IVADMTPDEILASEL 236
Cdd:COG3638 225 VVFDGPPAELTDAVL 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
7-231 |
1.16e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 156.79 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 7 NFSFRYESLD----KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAIKGEVTGSLEINGKNISDFSmhdy 81
Cdd:PRK13633 9 NVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlIPSEGKVYVDGLDTSDEENLWDIR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 tEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK13633 85 -NKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTPDEI 231
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV--EADRIIVMDSGKVVMEGTPKEI 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
298-525 |
1.28e-43 |
|
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: 155.73 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYD---GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK 374
Cdd:COG1124 1 MLEVRNLSVSYGqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNPnhMIS---HHMIFDEVAFGLRNRGVAEQEikEKVENVLELCGLSK-FRHWPIEALSYGQKKRVTIASILVLE 450
Cdd:COG1124 81 VQMVFQDP--YASlhpRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 451 PELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-222 |
2.81e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.43 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYT 82
Cdd:COG4619 1 LELEGLSFRVG--GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPLSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDtdSQFVGLSIGEDIAFALenQLVSNIDMYPLVKSTAKMVDL-ADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:COG4619 74 RQVAYVPQE--PALWGGTVRDNLPFPF--QLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHrLEDVLHRDIDRVILMERGEI 222
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSH-DPEQIERVADRVLTLEAGRL 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
299-525 |
5.84e-43 |
|
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: 153.65 E-value: 5.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQnpNHMISHHM-IFDEVAFGLRNRGVA----EQEIKEKVENVLELCGLSKF-RHWPIEaLSYGQKKRVTIASILVLEPE 452
Cdd:cd03296 80 FQ--HYALFRHMtVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLaDRYPAQ-LSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 453 LLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-238 |
5.99e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 153.71 E-value: 5.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikgeVTGSLEINGKNIsdfsmHDYT 82
Cdd:COG1121 7 IELENLTVSYG--GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-----TSGTVRLFGKPP-----RRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQ--DTDSQF-------VGL----SIG----------EDIAFALEnqlvsnidmyplvkstakMVDLADMLDRS 139
Cdd:COG1121 75 RRIGYVPQraEVDWDFpitvrdvVLMgrygRRGlfrrpsradrEAVDEALE------------------RVGLEDLADRP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 140 PHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHRdIDRVILMER 219
Cdd:COG1121 137 IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREY-FDRVLLLNR 214
|
250
....*....|....*....
gi 515631642 220 GeIVADMTPDEILASELLE 238
Cdd:COG1121 215 G-LVAHGPPEEVLTPENLS 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
299-525 |
9.57e-43 |
|
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: 152.87 E-value: 9.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLtySYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:cd03299 1 LKVENL--SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR--DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNpnHMISHHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03299 77 PQN--YALFPHMtVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
299-511 |
1.09e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.89 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:COG4619 1 LELEGLSFRVGG-KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNP---NHMISHHMIFdevAFGLRNRGVAEqeikEKVENVLELCGLSK-FRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:COG4619 80 PQEPalwGGTVRDNLPF---PFQLRERKFDR----ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-235 |
1.37e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 152.22 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLdkptLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDyt 82
Cdd:COG3840 2 LRLDDLTYRYGDF----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLP-----PDSGRILWNGQDLTALPPAE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTDsQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:COG3840 71 RPVSMLFQENN-LFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIVADMTPDEILASE 235
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAAR--IaDRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
300-512 |
2.11e-42 |
|
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: 150.87 E-value: 2.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 300 EVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELsifERSQKVGVVM 379
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 380 QNPNHMISHHMIFDEVAFGLRNRGvaeqEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:cd03226 78 QDVDYQLFTDSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515631642 460 TAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
297-560 |
2.24e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 152.98 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYDGEKN-ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKV 375
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNP-NHMISHHMIFDeVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13648 86 GIVFQNPdNQFVGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQPSLLERANLct 534
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGL-- 241
|
250 260
....*....|....*....|....*.
gi 515631642 535 tsiyELATMMKIDDTNAFMQYFIDYE 560
Cdd:PRK13648 242 ----DLPFPIKINQMLGHQTSFLTYE 263
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-225 |
2.24e-42 |
|
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: 149.89 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 6 SNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISDFSMHDYTEQV 85
Cdd:cd03214 3 ENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK-PSSGEIL----LDGKDLASLSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 86 GTVLQdtdsqfvglsigediafALEnqlvsnidmyplvkstakMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:cd03214 76 AYVPQ-----------------ALE------------------LLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLHKETNKTIVIiehrledVLHrDI-------DRVILMERGEIVAD 225
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVM-------VLH-DLnlaaryaDRVILLKDGRIVAQ 179
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-238 |
2.41e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 153.35 E-value: 2.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRY-ESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaiKGEvTGSLEINGKNISDFSMHDY 81
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL----EAE-SGQIIIDGDLLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK13650 80 RHKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdiDRVILMERGEIVADMTPDEILA--SELLE 238
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALS--DRVLVMKNGQVESTSTPRELFSrgNDLLQ 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
299-524 |
2.45e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 154.85 E-value: 2.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSifERS--- 372
Cdd:COG1135 2 IELENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALS--ERElra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 --QKVGVVMQNPNhMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRH-WPIEaLSYGQKKRVTIASILVL 449
Cdd:COG1135 80 arRKIGMIFQHFN-LLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADaYPSQ-LSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 450 EPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVleyttRSI-----VIADSKLIANAAMTEVFSQP 524
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVV-----RRIcdrvaVLENGRIVEQGPVLDVFANP 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-231 |
3.50e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 154.85 E-value: 3.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNIS------ 74
Cdd:COG3839 3 SLELENVSKSYG--GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLE------DPTsGEILIGGRDVTdlppkd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 75 -DFSMhdyteqvgtVLQdtdsQFV---GLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQR 150
Cdd:COG3839 75 rNIAM---------VFQ----SYAlypHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhrdiDRVILMERGEIVADMTPDE 230
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMtl-aDRIAVMNDGRIQQVGTPEE 220
|
.
gi 515631642 231 I 231
Cdd:COG3839 221 L 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
299-510 |
4.78e-42 |
|
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: 148.87 E-value: 4.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIF--ERSQKVG 376
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQNPNhMISHHMIFDEVAFGlrnrgvaeqeikekvenvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLIL 456
Cdd:cd03229 80 MVFQDFA-LFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515631642 457 DEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-233 |
5.13e-42 |
|
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: 150.81 E-value: 5.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAikgevtGSLEINGKNISDFS---MHDYTEQVGTVLQdtd 93
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTS------GSVLVDGTDLTLLSgkeLRKARRRIGMIFQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 94 sQFVGLS---IGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:cd03258 90 -HFNLLSsrtVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 171 ASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEILA 233
Cdd:cd03258 169 SALDPETTQSILALLRDINRELGLTIVLITHEMEVV--KRIcDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-231 |
5.37e-42 |
|
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: 150.41 E-value: 5.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEINGKNISDFSMHDYT 82
Cdd:cd03260 1 IELRDLNVYYG--DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 --EQVGTVLQDTdSQFVGlSIGEDIAFALENQLVSNID-MYPLVKSTAKMVDLADMLDRSPH--DLSGGQKQRVSLAGIL 157
Cdd:cd03260 79 lrRRVGMVFQKP-NPFPG-SIYDNVAYGLRLHGIKLKEeLDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 158 VDDVDILLFDEPLASLDPkTGKATIE-IIDQLHKETnkTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEI 231
Cdd:cd03260 157 ANEPEVLLLDEPTSALDP-ISTAKIEeLIAELKKEY--TIVIVTHNMQQAA-RVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-223 |
6.00e-42 |
|
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: 150.35 E-value: 6.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 9 SFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFS---MHDYTEQV 85
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-----PTSGSIIFDGKDLLKLSrrlRKIRRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 86 GTVLQDTDSQF-VGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDL---ADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:cd03257 85 QMVFQDPMSSLnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEdvLHRDI-DRVILMERGEIV 223
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLG--VVAKIaDRVAVMYAGKIV 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-234 |
6.33e-42 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (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: 213262 [Multi-domain] Cd Length: 242 Bit Score: 150.91 E-value: 6.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTgsleINGKNISDFSMHDYT 82
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPT-SGEIF----IDGEDIREQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDtdsqfVGL----SIGEDIAfalenqLVSNIDMYP------LVKSTAKMVDL--ADMLDRSPHDLSGGQKQR 150
Cdd:cd03295 75 RKIGYVIQQ-----IGLfphmTVEENIA------LVPKLLKWPkekireRADELLALVGLdpAEFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDE 230
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAF-RLADRIAIMKNGEIVQVGTPDE 222
|
....
gi 515631642 231 ILAS 234
Cdd:cd03295 223 ILRS 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-225 |
1.15e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.42 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgeVT-GSLEINGKNISDFSMH 79
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDR------PTsGEVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYT----EQVGTVLQdtDSQFV-GLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLA 154
Cdd:COG1136 79 ELArlrrRHIGFVFQ--FFNLLpELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHrlEDVLHRDIDRVILMERGEIVAD 225
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH--DPELAARADRVIRLRDGRIVSD 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.54e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 151.78 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYESlDKPT----LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHaikgevTGSLEINGKNISD 75
Cdd:PRK13651 1 MQIKVKNIVKIFNK-KLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALlLPD------TGTIEWIFKDEKN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 76 FSMHDYTE------------------------QVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVD 131
Cdd:PRK13651 74 KKKTKEKEkvleklviqktrfkkikkikeirrRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 132 L-ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHRd 210
Cdd:PRK13651 154 LdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEW- 231
|
250 260
....*....|....*....|....*
gi 515631642 211 IDRVILMERGEIVADMTPDEILASE 235
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDILSDN 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-270 |
2.09e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 150.66 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlIPHAIKGEVTgsleINGKNISDFSMHDYT 82
Cdd:PRK13647 5 IEVEDLHFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG-IYLPQRGRVK----VMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK13647 79 SKVGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 163 ILLFDEPLASLDPKtGKATI-EIIDQLHKEtNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILASELLETHG 241
Cdd:PRK13647 159 VIVLDEPMAYLDPR-GQETLmEILDRLHNQ-GKTVIVATHDV-DLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAG 235
|
250 260 270
....*....|....*....|....*....|....*
gi 515631642 242 IREPL------YLSALKAAKAPLTSEDKLSNLKAL 270
Cdd:PRK13647 236 LRLPLvaqifeDLPELGQSKLPLTVKEAVQIIRKL 270
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-519 |
2.17e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 155.95 E-value: 2.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQ-VGTVLQDTdSQFVG 98
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD-----SGEILLDGEPVRFRSPRDAQAAgIAIIHQEL-NLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 LSIGEDIAFALENQLVSNIDMYPLVKSTAKMvdLADM-LDRSPH----DLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:COG1129 94 LSVAENIFLGREPRRGGLIDWRAMRRRAREL--LARLgLDIDPDtpvgDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 174 DPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEilasellethgireplylsalk 252
Cdd:COG1129 172 TEREVERLFRIIRRL-KAQGVAIIYISHRLDEV--FEIaDRVTVLRDGRLVGTGPVAE---------------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 253 aakaplTSEDKLSNL---KALDYKrfrpavqawFAERPTPVAEkqyqPLLEVHGLTysydgEKNALEDVSFKIGKGEFVS 329
Cdd:COG1129 227 ------LTEDELVRLmvgRELEDL---------FPKRAAAPGE----VVLEVEGLS-----VGGVVRDVSFSVRAGEILG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 330 ILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE-------------RSQkvGVVmqnPNHMISHHMI---FD 393
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayvpedrKGE--GLV---LDLSIRENITlasLD 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 394 EVA-FGLRNRG----VAEQEIKE---KVENVLElcglskfrhwPIEALSYG--QKkrVTIASILVLEPELLILDEPTAGQ 463
Cdd:COG1129 358 RLSrGGLLDRRreraLAEEYIKRlriKTPSPEQ----------PVGNLSGGnqQK--VVLAKWLATDPKVLILDEPTRGI 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 464 D-------YRnytsmlaFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIA---NAAMTE 519
Cdd:COG1129 426 DvgakaeiYR-------LIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGeldREEATE 483
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-231 |
2.63e-41 |
|
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: 149.26 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNI---SDFSMH 79
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-----PTSGSVLIDGTDInklKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYTEQVGTVLQDTdsQFVG-LSigediafALENQLVSNIDMYPLVKSTAKM---------------VDLADMLDRSPHDL 143
Cdd:cd03256 75 QLRRQIGMIFQQF--NLIErLS-------VLENVLSGRLGRRSTWRSLFGLfpkeekqralaalerVGLLDKAYQRADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 144 SGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEdvLHRDI-DRVILMERGEI 222
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVD--LAREYaDRIVGLKDGRI 223
|
....*....
gi 515631642 223 VADMTPDEI 231
Cdd:cd03256 224 VFDGPPAEL 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
299-492 |
2.81e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.15 E-value: 2.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:COG3839 4 LELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR--NIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQN----PnhmishHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPEL 453
Cdd:COG3839 81 FQSyalyP------HMtVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 515631642 454 LILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHD 492
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-229 |
3.30e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.47 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSmhd 80
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT-----SGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 ytEQVGTVLQDtDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDD 160
Cdd:COG1116 80 --PDRGVVFQE-PALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 161 VDILLFDEPLASLDPKTgKATI-EIIDQLHKETNKTIVIIEHrledvlhrDI-------DRVILMER--GEIVADMTPD 229
Cdd:COG1116 157 PEVLLMDEPFGALDALT-RERLqDELLRLWQETGKTVLFVTH--------DVdeavflaDRVVVLSArpGRIVEEIDVD 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
299-511 |
4.79e-41 |
|
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: 147.40 E-value: 4.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGVV 378
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNpnHMISHHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03301 78 FQN--YALYPHMtVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-234 |
1.14e-40 |
|
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: 147.64 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 9 SFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQVGTV 88
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW-----SGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 89 LQDTDSQF-----VGLSIGEdiafALENQLVSNIDMYplVKSTAKMVDL-ADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:COG1124 85 FQDPYASLhprhtVDRILAE----PLRIHGLPDREER--IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILAS 234
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHL-CDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-224 |
1.19e-40 |
|
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: 146.52 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 5 FSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSmhdytEQ 84
Cdd:cd03235 2 VEDLTVSYG--GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT-----SGSIRVFGKPLEKER-----KR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 85 VGTVLQ----DTDS-----QFVGLSIGEDIAFAlenQLVSNIDmYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAG 155
Cdd:cd03235 70 IGYVPQrrsiDRDFpisvrDVVLMGLYGHKGLF---RRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHRdIDRVILMERgEIVA 224
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEY-FDRVLLLNR-TVVA 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-229 |
1.26e-40 |
|
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: 146.46 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSmhd 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT-----SGEVLVDGEPVTGPG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 ytEQVGTVLQDtDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDD 160
Cdd:cd03293 73 --PDRGYVFQQ-DALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 161 VDILLFDEPLASLDPKTgKATI--EIIDQLHkETNKTIVIIEHRLEDVLHRDiDRVILMER--GEIVADMTPD 229
Cdd:cd03293 150 PDVLLLDEPFSALDALT-REQLqeELLDIWR-ETGKTVLLVTHDIDEAVFLA-DRVVVLSArpGRIVAEVEVD 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-525 |
1.63e-40 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 154.09 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 10 FRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEINGKnisdfsmhdyteqvgTVL 89
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGE---------------SLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 90 QDTDSQFVGLSiGEDIAF-------------ALENQLVSNIDMYPLVKSTAKMVDLADMLDRS------------PHDLS 144
Cdd:PRK15134 80 HASEQTLRGVR-GNKIAMifqepmvslnplhTLEKQLYEVLSLHRGMRREAARGEILNCLDRVgirqaakrltdyPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVA 224
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNL-SIVRKLADRVAVMQNGRCVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 225 DMTPDEILAsellethgireplylsalkAAKAPLTsedklsnlkaldykrfRPAVQAWFAERPTPVAEkQYQPLLEVHGL 304
Cdd:PRK15134 238 QNRAATLFS-------------------APTHPYT----------------QKLLNSEPSGDPVPLPE-PASPLLDVEQL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 305 TYSYD----------GEKNALEDVSFKIGKGEFVSILGKNGSGKSTiTKLIMGVIDADSGSSYLNGEDLSELSifeRSQ- 373
Cdd:PRK15134 282 QVAFPirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKST-TGLALLRLINSQGEIWFDGQPLHNLN---RRQl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 374 -----KVGVVMQNPNHMISHHM-IFDEVAFGLR--NRGVAEQEIKEKVENVLELCGLS-KFRH-WPIEaLSYGQKKRVTI 443
Cdd:PRK15134 358 lpvrhRIQVVFQDPNSSLNPRLnVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDpETRHrYPAE-FSGGQRQRIAI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 444 ASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQ 523
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAA 516
|
..
gi 515631642 524 PS 525
Cdd:PRK15134 517 PQ 518
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
299-524 |
1.66e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 149.91 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL-SELSIFERsqKVGV 377
Cdd:COG1118 3 IEVRNISKRFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER--RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQN----PnhmishHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKF-RHWPIEaLSYGQKKRVTIASILVLEP 451
Cdd:COG1118 80 VFQHyalfP------HMtVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLaDRYPSQ-LSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 452 ELLILDEPTAGQDyrnytsmlAFIQK--------LNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQ 523
Cdd:COG1118 153 EVLLLDEPFGALD--------AKVRKelrrwlrrLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
.
gi 515631642 524 P 524
Cdd:COG1118 225 P 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-234 |
2.30e-40 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. 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: 213261 [Multi-domain] Cd Length: 269 Bit Score: 147.40 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISDFSMHDYTE----QVGTVLQDTdS 94
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI------EPTsGKVLIDGQDIAAMSRKELRElrrkKISMVFQSF-A 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 QFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLD 174
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 175 PKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEAL-RLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-223 |
3.03e-40 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.07 E-value: 3.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEkIV-IIGPSGSGKSTLGQCLNGLiphaikgEV--TGSLEINGKNISDFS 77
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGE-IFgIIGYSGAGKSTLIRCINLL-------ERptSGSVLVDGVDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 78 MHDYTE---QVGTVLQdtdsQFVGLS---IGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRV 151
Cdd:COG1135 74 ERELRAarrKIGMIFQ----HFNLLSsrtVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIV 223
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVV--RRIcDRVAVLENGRIV 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-235 |
3.42e-40 |
|
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: 145.84 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNgLIPHAIkgEVT-GSLEINGKNISDFSMHDY 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTL---VN-LIPRFY--DVDsGRILIDGHDVRDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTdSQFVGlSIGEDIAFALENqlVSNIDmyplVKSTAKMVDLADMLDRSPH-----------DLSGGQKQR 150
Cdd:cd03251 75 RRQIGLVSQDV-FLFND-TVAENIAYGRPG--ATREE----VEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDE 230
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTI--ENADRIVVLEDGKIVERGTHEE 222
|
....*
gi 515631642 231 ILASE 235
Cdd:cd03251 223 LLAQG 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
296-532 |
6.32e-40 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 149.33 E-value: 6.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKV 375
Cdd:PRK09452 12 SPLVELRGISKSFDG-KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR--HV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNpnHMISHHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK09452 89 NTVFQS--YALFPHMtVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPsllerANL 532
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP-----KNL 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-234 |
1.04e-39 |
|
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: 144.29 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTgsleINGKNISDFSMHDYT 82
Cdd:cd03254 3 IEFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-KGQIL----IDGIDIRDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTdSQFVGlSIGEDIAFAlenqlvSNIDMYPLVKSTAKMVDLADMLDRSP-----------HDLSGGQKQRV 151
Cdd:cd03254 77 SMIGVVLQDT-FLFSG-TIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDEI 231
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTI--KNADKILVLDDGKIIEEGTHDEL 224
|
...
gi 515631642 232 LAS 234
Cdd:cd03254 225 LAK 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
300-510 |
1.04e-39 |
|
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: 142.00 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 300 EVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVM 379
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 380 QnpnhmishhmifdevafglrnrgvaeqeikekvenvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515631642 460 TAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-231 |
1.43e-39 |
|
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: 144.30 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISDFSMHDy 81
Cdd:cd03300 1 IELENVSKFYG--GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE------TPTsGEILLDGKDITNLPPHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 tEQVGTVLQDTdSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:cd03300 72 -RPVNTVFQNY-ALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEI 231
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMS-DRIAVMNKGKIQQIGTPEEI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-236 |
1.86e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.05 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDFSmHDY 81
Cdd:COG1131 1 IEVRGLTKRYG--DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTS------GEVRVLGEDVARDP-AEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDtDSQFVGLSIGEDIAFALenqlvsniDMYPLVKSTAK--------MVDLADMLDRSPHDLSGGQKQRVSL 153
Cdd:COG1131 72 RRRIGYVPQE-PALYPDLTVRENLRFFA--------RLYGLPRKEAReridelleLFGLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 154 AGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEILA 233
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEA-ERLCDRVAIIDKGRIVADGTPDELKA 220
|
...
gi 515631642 234 SEL 236
Cdd:COG1131 221 RLL 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
299-512 |
1.86e-39 |
|
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: 144.25 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE-RSQ--KV 375
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlRQLrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNhMISHHMIFDEVAFGLRNR---------GVAEQEIKEKVENvLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:cd03256 81 GMIFQQFN-LIERLSVLENVLSGRLGRrstwrslfgLFPKEEKQRALAA-LERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
299-511 |
2.47e-39 |
|
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: 141.38 E-value: 2.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVGVV 378
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPnhMISHHMifdevafglrnrgvaeqeikeKVENVLElcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILDE 458
Cdd:cd03230 79 PEEP--SLYENL---------------------TVRENLK--------------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515631642 459 PTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-232 |
3.01e-39 |
|
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: 143.24 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDytEQVGTVLQDTdSQFVGL 99
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK-----PDSGKILLNGKDITNLPPEK--RDISYVPQNY-ALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGK 179
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515631642 180 ATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEIL 232
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWALA-DKVAIMLNGKLIQVGKPEEVF 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
16-234 |
3.70e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 143.21 E-value: 3.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNI--SDFSMHDYTEQVGTVLQdtd 93
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPD-----SGTITVDGEDLtdSKKDINKLRRKVGMVFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 94 sQFvGLsigediaF----ALENqlVsnidMYPLV------KSTAK--------MVDLADMLDRSPHDLSGGQKQRVSLAG 155
Cdd:COG1126 85 -QF-NL-------FphltVLEN--V----TLAPIkvkkmsKAEAEeramelleRVGLADKADAYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIiehrledVLH-----RDI-DRVILMERGEIVADMTPD 229
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVV-------VTHemgfaREVaDRVVFMDGGRIVEEGPPE 221
|
....*
gi 515631642 230 EILAS 234
Cdd:COG1126 222 EFFEN 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
298-524 |
4.71e-39 |
|
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: 145.20 E-value: 4.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKN---ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDA---DSGSSYLNGEDLSELSIFE- 370
Cdd:COG0444 1 LLEVRNLKVYFPTRRGvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 371 ---RSQKVGVVMQ------NPNHMISHHMIfdEVAfgLRNRGVAEQEIKEKVENVLELCGLSK----FRHWPIEaLSYGQ 437
Cdd:COG0444 81 rkiRGREIQMIFQdpmtslNPVMTVGDQIA--EPL--RIHGGLSKAEARERAIELLERVGLPDperrLDRYPHE-LSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 438 KKRVTIASILVLEPELLILDEPTAGQDyrnyTSM----LAFIQKLNRELGITVVIISHDMHLVLEYTTRSIV-------- 505
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALD----VTIqaqiLNLLKDLQRELGLAILFITHDLGVVAEIADRVAVmyagrive 231
|
250
....*....|....*....
gi 515631642 506 IADSKlianaamtEVFSQP 524
Cdd:COG0444 232 EGPVE--------ELFENP 242
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
311-528 |
1.15e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 143.62 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYL---------NGEDLSELSifersQKVGVVMQN 381
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkKNKKLKPLR-----KKVGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 382 PNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:PRK13634 94 PEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEelLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 460 TAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLE 528
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELE 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-223 |
2.39e-38 |
|
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: 139.70 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 7 NFSFRYESLDKpTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDfsmHDYTEQVG 86
Cdd:cd03226 4 NISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPIKA---KERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 87 TVLQDTDSQFVGLSIGEDIAFALENqlvsnIDMYPLVKSTA-KMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:cd03226 75 YVMQDVDYQLFTDSVREELLLGLKE-----LDAGNEQAETVlKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLHKETnKTIVIIEHRLEdVLHRDIDRVILMERGEIV 223
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQG-KAVIVITHDYE-FLAKVCDRVLLLANGAIV 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-225 |
2.67e-38 |
|
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: 140.42 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAikgevtGSLEINGKNISDFSMHDY 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTS------GSVLLDGTDIRQLDPADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTdSQFVGlSIGEDIAFAleNQLVSNIDMYplvkSTAKMVDLADMLDRSPH-----------DLSGGQKQR 150
Cdd:cd03245 77 RRNIGYVPQDV-TLFYG-TLRDNITLG--APLADDERIL----RAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtnKTIVIIEHRLedVLHRDIDRVILMERGEIVAD 225
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRP--SLLDLVDRIIVMDSGRIVAD 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
298-522 |
2.74e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 142.15 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEK--NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKV 375
Cdd:PRK13642 4 ILEVENLVFKYEKESdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFS 522
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
299-511 |
3.23e-38 |
|
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: 139.85 E-value: 3.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSEL---SIFERSQKV 375
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNpNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLS-KFRHWPIEaLSYGQKKRVTIASILVLEPELL 454
Cdd:cd03292 81 GVVFQD-FRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLShKHRALPAE-LSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
297-520 |
6.50e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 140.25 E-value: 6.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-V 375
Cdd:COG4674 9 PILYVEDLTVSFDGFK-ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLgI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNhMISHHMIFD--EVAFGlRNRGVAE-------QEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:COG4674 88 GRKFQKPT-VFEELTVFEnlELALK-GDRGVFAslfarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGML 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 447 LVLEPELLILDEPTAG--QDYRNYTSMLafIQKLNRELgiTVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG4674 166 LAQDPKLLLLDEPVAGmtDAETERTAEL--LKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEV 237
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
300-524 |
9.95e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 142.25 E-value: 9.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 300 EVHGLTYSYDG---EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS----IFERs 372
Cdd:PRK11153 3 ELKNISKVFPQggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelRKAR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 QKVGVVMQNPNhMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRH-WPIEaLSYGQKKRVTIASILVLEP 451
Cdd:PRK11153 82 RQIGMIFQHFN-LLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADrYPAQ-LSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-222 |
1.26e-37 |
|
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: 136.96 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDYT 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR-----PTSGRVRLDGADISQWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDtDSQFVGlSIGEDIafalenqlvsnidmyplvkstakmvdladmldrsphdLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03246 76 DHVGYLPQD-DELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEdvLHRDIDRVILMERGEI 222
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPE--TLASADRILVLEDGRV 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
299-513 |
1.57e-37 |
|
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: 138.02 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSElSIFERSQKVGV 377
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQnpnhmisHHMIFDE------VAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:cd03263 80 CPQ-------FDALFDEltvrehLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRELgiTVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-231 |
1.77e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 142.39 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEVTgsleINGKNISDFSMHDyt 82
Cdd:PRK09452 15 VELRGISKSFD--GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-ETPDSGRIM----LDGQDITHVPAEN-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTdSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK09452 86 RHVNTVFQSY-ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEI 231
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMS-DRIVVMRDGRIEQDGTPREI 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-268 |
2.16e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 139.96 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYE---SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNI---- 73
Cdd:PRK13641 1 MSIKFENVDYIYSpgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS-----SGTITIAGYHItpet 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 74 SDFSMHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLA-DMLDRSPHDLSGGQKQRVS 152
Cdd:PRK13641 76 GNKNLKKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNkTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEIL 232
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEY-ADDVLVLEHGKLIKHASPKEIF 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 515631642 233 A-SELLETHGIREP--------LYLSALKAAKAPLTSEDKLSNLK 268
Cdd:PRK13641 234 SdKEWLKKHYLDEPatsrfaskLEKGGFKFSEMPLTIDELVDGIK 278
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
299-513 |
2.25e-37 |
|
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: 137.72 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKN-ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03245 3 IEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnhmishHMIF----DEVAFGLRNrgVAEQEIkekvENVLELCGLSKF--RH-----WPI----EALSYGQKKRVT 442
Cdd:cd03245 83 VPQDV------TLFYgtlrDNITLGAPL--ADDERI----LRAAELAGVTDFvnKHpngldLQIgergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 443 IASILVLEPELLILDEPTAGQDYRnytSMLAFIQKLNREL-GITVVIISHDMHLvLEYTTRSIVIADSKLIA 513
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMN---SEERLKERLRQLLgDKTLIIITHRPSL-LDLVDRIIVMDSGRIVA 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
315-461 |
2.32e-37 |
|
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: 135.47 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPNHmISHHMIFDE 394
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQL-FPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 395 VAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEA----LSYGQKKRVTIASILVLEPELLILDEPTA 461
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-238 |
2.51e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 139.49 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYES---LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPhaikgeVTGSLEINGKNISDF 76
Cdd:PRK13649 1 MGINLQNVSYTYQAgtpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVP------TQGSVRVDDTLITST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 77 S----MHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLA-DMLDRSPHDLSGGQKQRV 151
Cdd:PRK13649 75 SknkdIKQIRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHkETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEI 231
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANY-ADFVYVLEKGKLVLSGKPKDI 232
|
....*...
gi 515631642 232 LAS-ELLE 238
Cdd:PRK13649 233 FQDvDFLE 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
299-513 |
3.53e-37 |
|
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: 146.52 E-value: 3.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:COG2274 474 IELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnhMISHHMIFDEVAFGlrNRGVAEQEIKEkvenVLELCGLSKFrhwpIEA---------------LSYGQKKRVT 442
Cdd:COG2274 554 VLQDV--FLFSGTIRENITLG--DPDATDEEIIE----AARLAGLHDF----IEAlpmgydtvvgeggsnLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 443 IASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRelGITVVIISHDMHLVlEYTTRSIVIADSKLIA 513
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVE 689
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
296-531 |
5.60e-37 |
|
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: 137.52 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSS-YLNGEDLSELSIFERSQK 374
Cdd:COG1119 1 DPLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVV---MQN--PNHMISHHMI----FDevAFGLRNRGVAEQEikEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIAS 445
Cdd:COG1119 80 IGLVspaLQLrfPRDETVLDVVlsgfFD--SIGLYREPTDEQR--ERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 446 ILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIA---------NAA 516
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAagpkeevltSEN 235
|
250
....*....|....*
gi 515631642 517 MTEVFSQPSLLERAN 531
Cdd:COG1119 236 LSEAFGLPVEVERRD 250
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-201 |
5.85e-37 |
|
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: 135.63 E-value: 5.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHaikgevTGSLEINGKNIsDFSMHDYTE---QVGTVLQDTDSQ 95
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLrPQ------SGAVLIDGEPL-DYSRKGLLErrqRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:TIGR01166 81 LFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*.
gi 515631642 176 KTGKATIEIIDQLhKETNKTIVIIEH 201
Cdd:TIGR01166 161 AGREQMLAILRRL-RAEGMTVVISTH 185
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
311-532 |
7.90e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 138.42 E-value: 7.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL----SELSIFERSQKVGVVMQNPNHMI 386
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 387 SHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVLEPELLILDEPTAGQD 464
Cdd:PRK13641 99 FENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdlISKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 465 YRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANL 532
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYL 244
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-231 |
8.25e-37 |
|
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: 136.70 E-value: 8.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYESLdkPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEVTgsleINGKNISDFSMHD 80
Cdd:cd03296 1 MSIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-ERPDSGTIL----FGGEDATDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 ytEQVGTVLQDTdSQFVGLSIGEDIAFALE----NQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGI 156
Cdd:cd03296 74 --RNVGFVFQHY-ALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEI 231
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEV-ADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
16-222 |
8.88e-37 |
|
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: 135.74 E-value: 8.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFS--MHDYTEQVGTVLQDTD 93
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD-----SGTIIIDGLKLTDDKknINELRQKVGMVFQQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 94 sQFVGLSIGEDIAFALenQLVSNIDmyplvKSTA--------KMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:cd03262 87 -LFPHLTVLENITLAP--IKVKGMS-----KAEAeeralellEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEdvLHRDI-DRVILMERGEI 222
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMG--FAREVaDRVIFMDDGRI 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
298-545 |
1.02e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 137.81 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VG 376
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLIL 456
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 457 DEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHlVLEYTTRSIVIADSKLIANAAMTEVFSQPSlLERANLCTTS 536
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVS-LQTLGLTPPS 237
|
....*....
gi 515631642 537 IYELATMMK 545
Cdd:PRK13644 238 LIELAENLK 246
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-221 |
1.07e-36 |
|
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: 134.62 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYT 82
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-----SGSILIDGEDLTDLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQ--VGTVLQDTdSQFVGLSIGEDIAFALenqlvsnidmyplvkstakmvdladmldrsphdlSGGQKQRVSLAGILVDD 160
Cdd:cd03229 74 LRrrIGMVFQDF-ALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 161 VDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGE 221
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAA-RLADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-234 |
2.41e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 138.74 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNI-SDFSM 78
Cdd:COG1118 1 MSIEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLEtPDS------GRIVLNGRDLfTNLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 79 HDytEQVGTVLQDTDsQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILV 158
Cdd:COG1118 73 RE--RRVGFVFQHYA-LFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 159 DDVDILLFDEPLASLDPKTgKATIEI-IDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKV-RKELRRwLRRLHDELGGTTVFVTHDQEEAL-ELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-221 |
2.95e-36 |
|
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: 132.37 E-value: 2.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 5 FSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQ 84
Cdd:cd00267 2 IENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 85 VGTVLQdtdsqfvglsigediafalenqlvsnidmyplvkstakmvdladmldrsphdLSGGQKQRVSLAGILVDDVDIL 164
Cdd:cd00267 75 IGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLhRDIDRVILMERGE 221
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAE-LAADRVIVLKDGK 157
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-231 |
4.19e-36 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 135.12 E-value: 4.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEINGKNISDFSMHDYT 82
Cdd:TIGR02315 2 LEVENLSKVYPN-GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLV-----EPSSGSILLEGTDITKLRGKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 E---QVGTVLQDTdsQFVG-LSIGEDI---AFALENQLVSNIDMYP-----LVKSTAKMVDLADMLDRSPHDLSGGQKQR 150
Cdd:TIGR02315 76 KlrrRIGMIFQHY--NLIErLTVLENVlhgRLGYKPTWRSLLGRFSeedkeRALSALERVGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDE 230
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQV-DLAKKYADRIVGLKAGEIVFDGAPSE 232
|
.
gi 515631642 231 I 231
Cdd:TIGR02315 233 L 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-225 |
4.51e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.02 E-value: 4.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISDFSMHD-- 80
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER-PTSGQVL----VNGQDLSRLKRREip 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 -YTEQVGTVLQD----TDsqfvgLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAG 155
Cdd:COG2884 76 yLRRRIGVVFQDfrllPD-----RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKeTNKTIVIIEHRLEDVLHRDIdRVILMERGEIVAD 225
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPK-RVLELEDGRLVRD 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
299-532 |
4.63e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 136.75 E-value: 4.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGS---SYLNGEDLSELSIFE- 370
Cdd:PRK13651 3 IKVKNIVKIFNKklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 371 ----------RSQK----------VGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGL--SKFRHW 428
Cdd:PRK13651 83 vleklviqktRFKKikkikeirrrVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdeSYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 429 PIEaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIAD 508
Cdd:PRK13651 163 PFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250 260
....*....|....*....|....
gi 515631642 509 SKLIANAAMTEVFSQPSLLERANL 532
Cdd:PRK13651 241 GKIIKDGDTYDILSDNKFLIENNM 264
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-269 |
4.74e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 135.99 E-value: 4.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 7 NFSFRYE-SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDYTEQV 85
Cdd:PRK13642 9 NLVFKYEkESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-----EFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 86 GTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdiDRVILMERGEIVADMTPDEILA-SELLETHGIRE 244
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASS--DRILVMKAGEIIKEAAPSELFAtSEDMVEIGLDV 241
|
250 260 270
....*....|....*....|....*....|..
gi 515631642 245 PLYLSALKAAKA-------PLTSEDKLSNLKA 269
Cdd:PRK13642 242 PFSSNLMKDLRKngfdlpeKYLSEDELVELLA 273
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
299-512 |
6.39e-36 |
|
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: 133.85 E-value: 6.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDA-----DSGSSYLNGEDLSELSIF--ER 371
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 372 SQKVGVVMQNPNhMIshHM-IFDEVAFGLRNRGVAE-QEIKEKVENVLELCGLSKF--RHWPIEALSYGQKKRVTIASIL 447
Cdd:cd03260 80 RRRVGMVFQKPN-PF--PGsIYDNVAYGLRLHGIKLkEELDERVEEALRKAALWDEvkDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 448 VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElgITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-258 |
1.01e-35 |
|
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: 133.83 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHdYT 82
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD-----SGSILIDGEDVRKEPRE-AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTDSqFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:COG4555 74 RQIGVLPDERGL-YDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHrDIDRVILMERGEIVADMTPDEILASELLEThgi 242
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEA-LCDRVVILHKGKVVAQGSLDELREEIGEEN--- 227
|
250
....*....|....*.
gi 515631642 243 REPLYLSALKAAKAPL 258
Cdd:COG4555 228 LEDAFVALIGSEEGEA 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
299-496 |
1.20e-35 |
|
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: 131.35 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKN-ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnhmishhMIFDE-VAfglrnrgvaeqeikekvENVlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLIL 456
Cdd:cd03228 81 VPQDP-------FLFSGtIR-----------------ENI----------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515631642 457 DEPTAGQDYRNYTSMLAFIQKLNRelGITVVIISHDMHLV 496
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI 158
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
311-514 |
2.30e-35 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; 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 to 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 the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 132.84 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVGVVMQNPNHMISHHM 390
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK-KFLRRIGVVFGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 391 IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTS 470
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515631642 471 MLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIAN 514
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-233 |
3.08e-35 |
|
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: 132.35 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISDFSMHDY 81
Cdd:cd03253 1 IEFENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFY------DVSsGSILIDGQDIREVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDT----DsqfvglSIGEDIAFALENqlVSNIDMYplvkSTAKMVDLADMLDRSPHD-----------LSGG 146
Cdd:cd03253 74 RRAIGVVPQDTvlfnD------TIGYNIRYGRPD--ATDEEVI----EAAKAAQIHDKIMRFPDGydtivgerglkLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 147 QKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADM 226
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV--NADKIIVLKDGRIVERG 217
|
....*..
gi 515631642 227 TPDEILA 233
Cdd:cd03253 218 THEELLA 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-237 |
4.46e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 133.39 E-value: 4.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 7 NFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDYTEQVG 86
Cdd:PRK13652 8 DLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK-----PTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 87 TVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PRK13652 82 LVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 167 DEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILASELL 237
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQL-DLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
284-513 |
4.60e-35 |
|
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: 139.12 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 284 AERPTPVAEkqyQPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL 363
Cdd:COG4988 325 GTAPLPAAG---PPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 364 SELSIFERSQKVGVVMQNPnhmishhMIF-----DEVAFGlrNRGVAEQEIKEkvenVLELCGLSKFrhwpIEA------ 432
Cdd:COG4988 402 SDLDPASWRRQIAWVPQNP-------YLFagtirENLRLG--RPDASDEELEA----ALEAAGLDEF----VAAlpdgld 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 433 ---------LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRelGITVVIISHDMHLVLEYtTRS 503
Cdd:COG4988 465 tplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRI 541
|
250
....*....|
gi 515631642 504 IVIADSKLIA 513
Cdd:COG4988 542 LVLDDGRIVE 551
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
299-515 |
6.34e-35 |
|
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: 130.41 E-value: 6.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSifERSQKVGVV 378
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNP---NHMISHHmifdevafGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:cd03268 78 IEAPgfyPNLTARE--------NLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANA 515
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
304-541 |
7.37e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 132.56 E-value: 7.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 304 LTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS----IFERSQKV 375
Cdd:PRK13649 8 VSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVLEPEL 453
Cdd:PRK13649 88 GLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKNPFE-LSGGQMRRVAIAGILAMEPKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 454 LILDEPTAGQDYRNYTSMLAFIQKLNrELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLC 533
Cdd:PRK13649 167 LVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLEEKQLG 245
|
....*...
gi 515631642 534 TTSIYELA 541
Cdd:PRK13649 246 VPKITKFA 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-247 |
1.01e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 132.44 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYES---LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEI--NGKNISDfs 77
Cdd:PRK13645 7 IILDNVSYTYAKktpFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 78 MHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLA-DMLDRSPHDLSGGQKQRVSLAGI 156
Cdd:PRK13645 85 VKRLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS-E 235
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVL-RIADEVIVMHEGKVISIGSPFEIFSNqE 243
|
250
....*....|...
gi 515631642 236 LLETHGIREP-LY 247
Cdd:PRK13645 244 LLTKIEIDPPkLY 256
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-234 |
1.01e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 132.60 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYES---LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNIS--- 74
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLK-----PTTGTVTVDDITIThkt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 75 -DFSMHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENqLVSNIDMyplVKSTAK--MVDLA---DMLDRSPHDLSGGQK 148
Cdd:PRK13646 76 kDKYIRPVRKRIGMVFQFPESQLFEDTVEREIIFGPKN-FKMNLDE---VKNYAHrlLMDLGfsrDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTP 228
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVA-RYADEVIVMKEGSIVSQTSP 230
|
....*.
gi 515631642 229 DEILAS 234
Cdd:PRK13646 231 KELFKD 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-245 |
1.06e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 132.12 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 7 NFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaIKGEVTGSLEINGKNI--SDFSMHDYTEQ 84
Cdd:PRK13639 6 DLKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNG-----ILKPTSGEVLIKGEPIkyDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 85 VGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:PRK13639 80 VGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILA-SELLETHGIR 243
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDV-DLVPVYADKVYVMSDGKIIKEGTPKEVFSdIETIRKANLR 237
|
..
gi 515631642 244 EP 245
Cdd:PRK13639 238 LP 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-513 |
1.26e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 137.08 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVtgslEINGKNISDFSMHDYTEQ-VGTVLQ-----DTd 93
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLY-QPDSGEI----LIDGKPVRIRSPRDAIALgIGMVHQhfmlvPN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 94 sqfvgLSIGEDIAFALENQLVSNIDMyplvKSTAKMV-DLADM------LDRSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:COG3845 95 -----LTVAENIVLGLEPTKGGRLDR----KAARARIrELSERygldvdPDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 167 DEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEilasellethgirep 245
Cdd:COG3845 166 DEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREV--MAIaDRVTVLRRGKVVGTVDTAE--------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 246 lylsalkaakaplTSEDKLSNL---KALDYKRFRPAVQawfaerPTPvaekqyqPLLEVHGLTYSYDGEKNALEDVSFKI 322
Cdd:COG3845 228 -------------TSEEELAELmvgREVLLRVEKAPAE------PGE-------VVLEVENLSVRDDRGVPALKDVSLEV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 323 GKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VGVVMQNPNHM-------ISHHMIFDE 394
Cdd:COG3845 282 RAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRglvpdmsVAENLILGR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 395 ------VAFGLRNRGVAEQEIKEKVEnvlelcglsKFR------HWPIEALSYG--QKkrVTIASILVLEPELLILDEPT 460
Cdd:COG3845 362 yrrppfSRGGFLDRKAIRAFAEELIE---------EFDvrtpgpDTPARSLSGGnqQK--VILARELSRDPKLLIAAQPT 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 461 AGQDYRNytsmLAFIQKLNREL---GITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:COG3845 431 RGLDVGA----IEFIHQRLLELrdaGAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
299-524 |
2.02e-34 |
|
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: 129.97 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VGV 377
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPNhmishhmIF------DEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:cd03218 80 LPQEAS-------IFrkltveENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 452 ELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
296-519 |
2.35e-34 |
|
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: 129.86 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSifE-- 370
Cdd:COG4181 6 APIIELRGLTKTVgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD--Eda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 371 ----RSQKVGVVMQNpNHMISHHMIFDEVAFGLRNRGVAeqEIKEKVENVLELCGLSK-FRHWPIEaLSYGQKKRVTIAS 445
Cdd:COG4181 84 rarlRARHVGFVFQS-FQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHrLDHYPAQ-LSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 446 ILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLvLEYTTRSIVIADSKLIANAAMTE 519
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL-AARCDRVLRLRAGRLVEDTAATA 232
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-234 |
2.81e-34 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 133.69 E-value: 2.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISDFSMHDYTE----QVGTVLQdtds 94
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLI------EPTaGEVLIDGEDITKLSKKELRElrrkKMSMVFQ---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 QFvGL----SIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:COG4175 113 HF-ALlphrTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAF 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 171 ASLDPktgkatieII-----DQ---LHKETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIVADMTPDEILAS 234
Cdd:COG4175 192 SALDP--------LIrremqDElleLQAKLKKTIVFITHDLDEALR--LgDRIAIMKDGRIVQIGTPEEILTN 254
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
297-530 |
3.05e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 130.28 E-value: 3.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVG 376
Cdd:PRK13548 1 AMLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQnpnhmiSHHMIFD----E-VAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILV--- 448
Cdd:PRK13548 80 VLPQ------HSSLSFPftveEvVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 449 ---LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFsQPS 525
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL-TPE 232
|
....*
gi 515631642 526 LLERA 530
Cdd:PRK13548 233 TLRRV 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
314-493 |
4.39e-34 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. 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: 213261 [Multi-domain] Cd Length: 269 Bit Score: 130.07 E-value: 4.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE----RSQKVGVVMQNPNHMiSHH 389
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelRRKKISMVFQSFALL-PHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 390 MIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYT 469
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180
....*....|....*....|....
gi 515631642 470 SMLAFIQKLNRELGITVVIISHDM 493
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHDL 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
276-513 |
5.40e-34 |
|
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: 136.05 E-value: 5.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 276 RPAVQawFAERPTPVAEkqyQPLLEVHGLTYSYDGE-KNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSG 354
Cdd:COG4987 316 PPAVT--EPAEPAPAPG---GPSLELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 355 SSYLNGEDLSELSIFERSQKVGVVMQNPnHmishhmIFDE-VAFGLR--NRGVAEQEIKEkvenVLELCGLSKF-RHWPI 430
Cdd:COG4987 391 SITLGGVDLRDLDEDDLRRRIAVVPQRP-H------LFDTtLRENLRlaRPDATDEELWA----ALERVGLGDWlAALPD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 431 ----------EALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRelGITVVIISHDMHLvLEYT 500
Cdd:COG4987 460 gldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAG-LERM 536
|
250
....*....|...
gi 515631642 501 TRSIVIADSKLIA 513
Cdd:COG4987 537 DRILVLEDGRIVE 549
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
286-525 |
6.11e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 132.65 E-value: 6.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 286 RPTPVAEKQYQPLLEVHGLTYSYDGEkNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSE 365
Cdd:PRK11607 7 RPQAKTRKALTPLLEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 366 LSIFERSqkvgVVMQNPNHMISHHMIFDE-VAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIA 444
Cdd:PRK11607 86 VPPYQRP----INMMFQSYALFPHMTVEQnIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 445 SILVLEPELLILDEPTAGQDYRNYTSM-LAFIQKLNReLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQ 523
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
..
gi 515631642 524 PS 525
Cdd:PRK11607 241 PT 242
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-217 |
6.30e-34 |
|
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: 135.11 E-value: 6.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESLDkPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDY 81
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDtdSQFVGLSIGEDIAFALENQLVSNID-------MYPLVKSTAKMVDLadMLDRSPHDLSGGQKQRVSLA 154
Cdd:TIGR02857 395 RDQIAWVPQH--PFLFAGTIAENIRLARPDASDAEIRealeragLDEFVAALPQGLDT--PIGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILM 217
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA--ALADRIVVL 529
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-233 |
7.46e-34 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 136.53 E-value: 7.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISDFSMHDYT 82
Cdd:TIGR03375 464 IEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQ-PTEGSVL----LDGVDIRQIDPADLR 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTdSQFVGlSIGEDIAFAleNQLVSNIDMYplvkSTAKMVDLADMLDRSPH-----------DLSGGQKQRV 151
Cdd:TIGR03375 539 RNIGYVPQDP-RLFYG-TLRDNIALG--APYADDEEIL----RAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAV 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 152 SLAGILVDDVDILLFDEPLASLDPKTGKatiEIIDQLHKET-NKTIVIIEHRLEdvLHRDIDRVILMERGEIVADMTPDE 230
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEE---RFKDRLKRWLaGKTLVLVTHRTS--LLDLVDRIIVMDNGRIVADGPKDQ 685
|
...
gi 515631642 231 ILA 233
Cdd:TIGR03375 686 VLE 688
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
299-519 |
1.08e-33 |
|
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: 127.49 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsQKVGVV 378
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR-RRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPnhmishhmIFDEVAFGLRN-------RGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:cd03265 79 FQDL--------SVDDELTGWENlyiharlYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-237 |
1.80e-33 |
|
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: 127.89 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHA------IKGEVTGsleinGKNISDF 76
Cdd:COG1119 4 LELRNVTVRRG--GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTygndvrLFGERRG-----GEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 77 ---------SMHDYTEQVGTVLQDTDSQFVGlSIG-------EDIAFALEnqlvsnidmyplvksTAKMVDLADMLDRSP 140
Cdd:COG1119 77 rkriglvspALQLRFPRDETVLDVVLSGFFD-SIGlyreptdEQRERARE---------------LLELLGLAHLADRPF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 141 HDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERG 220
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIP-PGITHVLLLKDG 219
|
250
....*....|....*..
gi 515631642 221 EIVADMTPDEILASELL 237
Cdd:COG1119 220 RVVAAGPKEEVLTSENL 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
16-223 |
1.86e-33 |
|
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: 126.60 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISDFSMHDytEQVGTVLQDTdS 94
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE------EPTsGRIYIGGRDVTDLPPKD--RDIAMVFQNY-A 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 QFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLD 174
Cdd:cd03301 83 LYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515631642 175 PKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIV 223
Cdd:cd03301 163 AKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMA-DRIAVMNDGQIQ 210
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-235 |
1.96e-33 |
|
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: 127.60 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISDFSMHDYT 82
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV-PENGRVL----VDGHDLALADPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQdtDSQFVGLSIGEDIAFALEnqlvsNIDMYPLVKStAKMVDLADMLDRSPH-----------DLSGGQKQRV 151
Cdd:cd03252 76 RQVGVVLQ--ENVLFNRSIRDNIALADP-----GMSMERVIEA-AKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 152 SLAGILVDDVDILLFDEPLASLDPKTGKAtieIIDQLHK-ETNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDE 230
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHA---IMRNMHDiCAGRTVIIIAHRLSTV--KNADRIIVMEKGRIVEQGSHDE 222
|
....*
gi 515631642 231 ILASE 235
Cdd:cd03252 223 LLAEN 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-242 |
2.37e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 127.01 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLdkPTlkNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNisdfsmHDYT 82
Cdd:PRK10771 2 LKLTDITWLYHHL--PM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA-----SGSLTLNGQD------HTTT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 ----EQVGTVLQDtDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILV 158
Cdd:PRK10771 67 ppsrRPVSMLFQE-NNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEILASELLE 238
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDA-ARIAPRSLVVADGRIAWDGPTDELLSGKASA 224
|
....*.
gi 515631642 239 TH--GI 242
Cdd:PRK10771 225 SAllGI 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
296-496 |
2.72e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 129.47 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKN----------ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSE 365
Cdd:COG4608 5 EPLLEVRDLKKHFPVRGGlfgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 366 LS---IFERSQKVGVVMQNP----NhmiSHHMIFDEVAFGLRNRGVA-EQEIKEKVENVLELCGLSK--FRHWPIEaLSY 435
Cdd:COG4608 85 LSgreLRPLRRRMQMVFQDPyaslN---PRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLRPehADRYPHE-FSG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 436 GQKKRVTIASILVLEPELLILDEPTAGQDYrnytSMLAfiQKLN------RELGITVVIISHDMHLV 496
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDV----SIQA--QVLNlledlqDELGLTYLFISHDLSVV 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-245 |
3.90e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 128.81 E-value: 3.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTGSLEINGKNISDFSMHDYTEQ------------VGT 87
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK-YGTIQVGDIYIGDKKNNHELITNPYSkkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 88 VLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDL-ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PRK13631 121 VFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 167 DEPLASLDPKTGKATIEIIDQlHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEILASE-LLETHGIREP 245
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVA-DEVIVMDKGKILKTGTPYEIFTDQhIINSTSIQVP 278
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
299-506 |
4.16e-33 |
|
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: 126.01 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VGV 377
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPNhmISHHM-IFDEVAFGLRNRGvaEQEIKEKVENVLELC-GLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:cd03224 80 VPEGRR--IFPELtVEENLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 456 LDEPTAG------QDyrnytsMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVI 506
Cdd:cd03224 156 LDEPSEGlapkivEE------IFEAIRELRDE-GVTILLVEQNARFALEIADRAYVL 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-235 |
6.28e-33 |
|
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: 126.01 E-value: 6.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVtgslEINGKNISDFSMHDYTEQ-VGTVLQDTdSQFVG 98
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR-PTSGSV----LFDGEDITGLPPHEIARLgIGRTFQIP-RLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 LSIGEDIAFALENQLVSNIDMYPLVKS----------TAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:cd03219 90 LTVLENVMVAAQARTGSGLLLARARREereareraeeLLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 169 PLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEILASE 235
Cdd:cd03219 170 PAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVV--MSLaDRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-228 |
6.94e-33 |
|
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: 125.30 E-value: 6.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDYT 82
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE-----LSSGSILIDGVDISKIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQD------------------TDsqfvglsigEDIAFALENqlVSNIDmypLVKSTAKMVDLadMLDRSPHDLS 144
Cdd:cd03244 78 SRISIIPQDpvlfsgtirsnldpfgeySD---------EELWQALER--VGLKE---FVESLPGGLDT--VVEEGGENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDPktgkATIEIIDQLHKE--TNKTIVIIEHRLEDVLhrDIDRVILMERGEI 222
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDP----ETDALIQKTIREafKDCTVLTIAHRLDTII--DSDRILVLDKGRV 215
|
....*.
gi 515631642 223 VADMTP 228
Cdd:cd03244 216 VEFDSP 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
304-545 |
1.39e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 126.66 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 304 LTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSS----YLNGEDLSELSIFERSQK- 374
Cdd:PRK13645 12 VSYTYAKktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIKEVKRLRKe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVLEPE 452
Cdd:PRK13645 92 IGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdyVKRSPFE-LSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 453 LLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANL 532
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEI 250
|
250
....*....|...
gi 515631642 533 CTTSIYELATMMK 545
Cdd:PRK13645 251 DPPKLYQLMYKLK 263
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
299-524 |
1.62e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.48 E-value: 1.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGE-KNAledvSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGV 377
Cdd:COG3840 2 LRLDDLTYRYGDFpLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER--PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNpNHMISHHMIFDEVAFGLRNRG--VAEQeiKEKVENVLELCGLSKF--RHwPiEALSYGQKKRVTIASILVLEPEL 453
Cdd:COG3840 76 LFQE-NNLFPHLTVAQNIGLGLRPGLklTAEQ--RAQVEQALERVGLAGLldRL-P-GQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 454 LILDEPTAGQD--YRNytSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:COG3840 151 LLLDEPFSALDpaLRQ--EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-225 |
1.66e-32 |
|
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: 122.81 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTgsleINGKNISDfsmhdyt 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL-KPQQGEIT----LDGVPVSD------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 eqvgtvLQDTDSQFVGLsigediafalenqlvsnIDMYPLVKSTAKMVDLAdmldrspHDLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03247 69 ------LEKALSSLISV-----------------LNQRPYLFDTTLRNNLG-------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVLHrdIDRVILMERGEIVAD 225
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEH--MDKILFLENGKIIMQ 177
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-225 |
2.41e-32 |
|
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: 123.76 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKptlkNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHaikgevTGSLEINGKnisDFSMHDY 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQ------SGRVLINGV---DVTAAPP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQ-VGTVLQDtDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDD 160
Cdd:cd03298 68 ADRpVSMLFQE-NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 161 VDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVAD 225
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLA-QRVVFLDNGRIAAQ 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
299-512 |
2.58e-32 |
|
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: 123.46 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVsILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsQKVGVV 378
Cdd:cd03264 1 LQLENLTKRYGK-KRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNhMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:cd03264 78 PQEFG-VYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 459 PTAGQD------YRNytsmlafiqkLNRELGIT-VVIIS-HDMHLVLEYTTRSIVIADSKLI 512
Cdd:cd03264 157 PTAGLDpeerirFRN----------LLSELGEDrIVILStHIVEDVESLCNQVAVLNKGKLV 208
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-223 |
3.04e-32 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 123.59 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRY--ESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISDFSMH 79
Cdd:TIGR02982 1 VISIRNLNHYYghGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGL-----RSVQEGSLKVLGQELHGASKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYTE---QVGTVLQdTDSQFVGLSIGEDIAFALE-NQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAG 155
Cdd:TIGR02982 76 QLVQlrrRIGYIFQ-AHNLLGFLTARQNVQMALElQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEH--RLEDVlhrdIDRVILMERGEIV 223
Cdd:TIGR02982 155 ALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHdnRILDV----ADRILQMEDGKLL 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-245 |
3.36e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 125.35 E-value: 3.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNIsDFS---MHDYTEQVGTVLQDTDSQF 96
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK-----PSSGRILFDGKPI-DYSrkgLMKLRESVGMVFQDPDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 97 VGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPK 176
Cdd:PRK13636 96 FSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 177 TGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILAS-ELLETHGIREP 245
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDI-DIVPLYCDNVFVMKEGRVILQGNPKEVFAEkEMLRKVNLRLP 244
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-223 |
3.57e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.97 E-value: 3.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYESLdkPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPhaikgeVTGSLEINGKNIsDFSMH 79
Cdd:COG4161 1 MSIQLKNINCFYGSH--QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLeTP------DSGQLNIAGHQF-DFSQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYTEQ-------VGTVLQdtdsQF---VGLSIgediafaLENQLVSNIDMYPLVKSTA--------KMVDLADMLDRSPH 141
Cdd:COG4161 72 PSEKAirllrqkVGMVFQ----QYnlwPHLTV-------MENLIEAPCKVLGLSKEQArekamkllARLRLTDKADRFPL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 142 DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEdVLHRDIDRVILMERGE 221
Cdd:COG4161 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVE-FARKVASQVVYMEKGR 218
|
..
gi 515631642 222 IV 223
Cdd:COG4161 219 II 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
299-513 |
4.25e-32 |
|
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: 122.77 E-value: 4.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSelsiFERSQKVGVV 378
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQN----PNHMISHHMIFdevaFGlRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:cd03269 76 PEErglyPKMKVIDQLVY----LA-QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-222 |
4.70e-32 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 123.05 E-value: 4.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 24 NLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISdfSMHDYTEQVGTVLQDtDSQFVGLSIGE 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPA-----SGSIKVNDQSHT--GLAPYQRPVSMLFQE-NNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 104 DIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIE 183
Cdd:TIGR01277 90 NIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 515631642 184 IIDQLHKETNKTIVIIEHRLEDvLHRDIDRVILMERGEI 222
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSD-ARAIASQIAVVSQGKI 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
299-520 |
4.78e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.22 E-value: 4.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIF-------ER 371
Cdd:COG4152 2 LELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpeER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 372 ----SQKVGvvmqnpnhmisHHMIFdevaFGlRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASIL 447
Cdd:COG4152 81 glypKMKVG-----------EQLVY----LA-RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 448 VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-245 |
4.83e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 124.73 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHaiKGEVTGsleiNGK--NISDFSMH 79
Cdd:PRK13638 2 LATSDLWFRYQ--DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ--KGAVLW----QGKplDYSKRGLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVD 159
Cdd:PRK13638 74 ALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 160 DVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKtIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILA-SELLE 238
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDI-DLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAME 231
|
....*..
gi 515631642 239 THGIREP 245
Cdd:PRK13638 232 QAGLTQP 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-223 |
5.41e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.99 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG---LIPHAikgEVTGSLEINGKNISDFSMh 79
Cdd:COG1117 12 IEVRNLNVYYG--DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGA---RVEGEILLDGEDIYDPDV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYTE---QVGTVLQdtdsQ---FVgLSIGEDIAFALE-NQLVSNIDMYPLVKSTAKMVDL----ADMLDRSPHDLSGGQK 148
Cdd:COG1117 86 DVVElrrRVGMVFQ----KpnpFP-KSIYDNVAYGLRlHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETnkTIVIIEHRLEDVLhRDIDRVILMERGEIV 223
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAA-RVSDYTAFFYLGELV 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-519 |
1.00e-31 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 128.75 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQ-VGTVLQDtdsqfvg 98
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT-----KGTITINNINYNKLDHKLAAQLgIGIIYQE------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 LSIGEDIAfALENQLVS----------NIDMYPLVKSTAKM----VDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:PRK09700 89 LSVIDELT-VLENLYIGrhltkkvcgvNIIDWREMRVRAAMmllrVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASELLETHGIRE 244
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIR-RICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 245 plylsalkaakapltsedklsnlkaldykrfrpaVQAWFAERPTPVAEKQYQPLLEVHGLTySYDGEKnaLEDVSFKIGK 324
Cdd:PRK09700 246 ----------------------------------LQNRFNAMKENVSNLAHETVFEVRNVT-SRDRKK--VRDISFSVCR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 325 GEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VGVVMQN-------PNHMISHHMIFDEV- 395
Cdd:PRK09700 289 GEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYITESrrdngffPNFSIAQNMAISRSl 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 396 -------AFGLRNRgVAEQEIKEKVENVLELCGLSKFRHwpIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNY 468
Cdd:PRK09700 369 kdggykgAMGLFHE-VDEQRTAENQRELLALKCHSVNQN--ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAK 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 469 TSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSK----LIANAAMTE 519
Cdd:PRK09700 446 AEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRltqiLTNRDDMSE 499
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
296-524 |
1.02e-31 |
|
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: 129.03 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKStITKL-IMGVIDAD----SGSSYLNGEDLSELS 367
Cdd:COG4172 4 MPLLSVEDLSVAFgqgGGTVEAVKGVSFDIAAGETLALVGESGSGKS-VTALsILRLLPDPaahpSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 368 IFE----RSQKVGVVMQNPnhMIS---HHMIFDEVAFGLR-NRGVAEQEIKEKVENVLELCGL----SKFRHWPIEaLSY 435
Cdd:COG4172 83 ERElrriRGNRIAMIFQEP--MTSlnpLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIpdpeRRLDAYPHQ-LSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 436 GQKKRVTIASILVLEPELLILDEPT-------AGQdyrnytsMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIAD 508
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTtaldvtvQAQ-------ILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQ 232
|
250
....*....|....*.
gi 515631642 509 SKLIANAAMTEVFSQP 524
Cdd:COG4172 233 GEIVEQGPTAELFAAP 248
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-235 |
1.37e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 129.69 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPhaikgeVTGSLEINGKNISDFSMHDY 81
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFeTP------ESGSVFYDGQDLAGLDVQAV 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDtdSQFVGLSIGEDIAFAleNQLvsNIDmypLVKSTAKMVDLADMLDRSP---H--------DLSGGQKQR 150
Cdd:TIGR03797 526 RRQLGVVLQN--GRLMSGSIFENIAGG--APL--TLD---EAWEAARMAGLAEDIRAMPmgmHtvisegggTLSGGQRQR 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhketNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDE 230
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTI--RNADRIYVLDAGRVVQQGTYDE 670
|
....*
gi 515631642 231 ILASE 235
Cdd:TIGR03797 671 LMARE 675
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
299-514 |
2.41e-31 |
|
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: 119.07 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE-RSQKVGV 377
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQnpnhmishhmifdevafglrnrgvaeqeikekvenvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIAN 514
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-222 |
2.43e-31 |
|
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: 119.42 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISDfSMHDYT 82
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-PDSGEIK----VLGKDIKK-EPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDtDSQFVGLSIGEdiafalenqlvsNIDmyplvkstakmvdladmldrsphdLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03230 73 RRIGYLPEE-PSLYENLTVRE------------NLK------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHRdIDRVILMERGEI 222
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERL-CDRVAILNNGRI 173
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-231 |
2.72e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 124.43 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISdfSMHDYTEQVGTVLQDTdSQFVGL 99
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT-----SGHIRFHGTDVS--RLHARDRKVGFVFQHY-ALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAFAL----ENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:PRK10851 90 TVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 176 KTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEI 231
Cdd:PRK10851 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEV-ADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
299-525 |
2.83e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 124.43 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR--KVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNpnHMISHHM-IFDEVAFGL-----RNRGVAEqEIKEKVENVLELCGLSKF-RHWPIEaLSYGQKKRVTIASILVLEP 451
Cdd:PRK10851 80 FQH--YALFRHMtVFDNIAFGLtvlprRERPNAA-AIKAKVTQLLEMVQLAHLaDRYPAQ-LSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
284-491 |
2.94e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.97 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 284 AERPTPVAEKQYQPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL 363
Cdd:COG1132 325 PDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 364 SELSIFERSQKVGVVMQNPnhmishhMIFDE-----VAFGlrNRGVAEQEIKEkvenVLELCGLSKFrhwpIEA------ 432
Cdd:COG1132 405 RDLTLESLRRQIGVVPQDT-------FLFSGtirenIRYG--RPDATDEEVEE----AAKAAQAHEF----IEAlpdgyd 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 433 ---------LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYtsmlAFIQK-LNREL-GITVVIISH 491
Cdd:COG1132 468 tvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETE----ALIQEaLERLMkGRTTIVIAH 533
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-215 |
3.11e-31 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 120.41 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNglIPHAIKGEVTGSLEINGKNI----SDFSMHDYTEQVGTVLQD 91
Cdd:TIGR03608 10 DKVILDDLNLTIEKGKMYAIIGESGSGKSTL---LN--IIGLLEKFDSGQVYLNGQETpplnSKKASKFRREKLGYLFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 92 ---TDSQfvglSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:TIGR03608 85 falIENE----TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515631642 169 PLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEdvLHRDIDRVI 215
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPE--VAKQADRVI 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-235 |
4.74e-31 |
|
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: 120.72 E-value: 4.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESL-DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQclngLI-----PhaikgeVTGSLEINGKNISDF 76
Cdd:cd03249 1 IEFKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVS----LLerfydP------TSGEILLDGVDIRDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 77 SMHDYTEQVGTVLQDtdSQFVGLSIGEDIAFALENQLVSnidmypLVKSTAKMVDLADMLDRSPH-----------DLSG 145
Cdd:cd03249 71 NLRWLRSQIGLVSQE--PVLFDGTIAENIRYGKPDATDE------EVEEAAKKANIHDFIMSLPDgydtlvgergsQLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVAD 225
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTI--RNADLIAVLQNGQVVEQ 218
|
250
....*....|
gi 515631642 226 MTPDEILASE 235
Cdd:cd03249 219 GTHDELMAQK 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-229 |
5.82e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 121.12 E-value: 5.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYESL--DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSm 78
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS-----SGEITLDGVPVTGPG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 79 hdyTEQvGTVLQDtDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILV 158
Cdd:COG4525 76 ---ADR-GVVFQK-DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMER--GEIVADMTPD 229
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLA-TRLVVMSPgpGRIVERLELD 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
299-493 |
5.93e-31 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (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: 213262 [Multi-domain] Cd Length: 242 Bit Score: 120.48 E-value: 5.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNhMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGL--SKFRH-WPIEaLSYGQKKRVTIASILVLEPELLI 455
Cdd:cd03295 81 IQQIG-LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADrYPHE-LSGGQQQRVGVARALAADPPLLL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDM 493
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDI 196
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-238 |
7.20e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 120.99 E-value: 7.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAikGEVTgsleINGKNISDFSMHDYTEQVGTVLQDTDSQ 95
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSS--GEVR----LNGRPLAAWSPWELARRRAVLPQHSSLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FvGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILV---DDVD----ILLFDE 168
Cdd:COG4559 88 F-PFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwEPVDggprWLFLDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 169 PLASLDPKTGKATIEIIDQLHKEtnKTIVIIehrledVLHrDI-------DRVILMERGEIVADMTPDEILASELLE 238
Cdd:COG4559 167 PTSALDLAHQHAVLRLARQLARR--GGGVVA------VLH-DLnlaaqyaDRILLLHQGRLVAQGTPEEVLTDELLE 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
299-508 |
9.99e-31 |
|
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: 119.17 E-value: 9.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--SELSIFERSQKVG 376
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQNPNhMISHHMIFDEVAFGLRN-RGVAEQEIKEKVENVLELCGLSKFRH-WPIEaLSYGQKKRVTIASILVLEPELL 454
Cdd:cd03262 80 MVFQQFN-LFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADaYPAQ-LSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIAD 508
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
299-531 |
1.01e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 122.91 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGVV 378
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD--ICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNpnHMISHHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:PRK11432 84 FQS--YALFPHMsLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERAN 531
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMAS 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
314-532 |
1.08e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 121.38 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS----IFERSQKVGVVMQNPNHMISHH 389
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 390 MIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRN 467
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADefWEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 468 YTSMLAFIQKLNrELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANL 532
Cdd:PRK13643 180 RIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHEL 243
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
296-524 |
1.11e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 120.09 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSiferSQKV 375
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLL-AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP----GHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 ---GVV--MQN----------PNHMISHHM---------IFDEVAFglRNrgvAEQEIKEKVENVLELCGLSKFRHWPIE 431
Cdd:PRK11300 78 armGVVrtFQHvrlfremtviENLLVAQHQqlktglfsgLLKTPAF--RR---AESEALDRAATWLERVGLLEHANRQAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 432 ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
250
....*....|...
gi 515631642 512 IANAAMTEVFSQP 524
Cdd:PRK11300 233 LANGTPEEIRNNP 245
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-245 |
1.11e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 121.38 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKP----TLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEV-TGSLEINGKNISDfS 77
Cdd:PRK13643 2 IKFEKVNYTYQP-NSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL-QPTEGKVtVGDIVVSSTSKQK-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 78 MHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLA-DMLDRSPHDLSGGQKQRVSLAGI 156
Cdd:PRK13643 79 IKPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHkETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILAS-E 235
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADY-ADYVYLLEKGHIISCGTPSDVFQEvD 236
|
250
....*....|
gi 515631642 236 LLETHGIREP 245
Cdd:PRK13643 237 FLKAHELGVP 246
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
298-513 |
1.42e-30 |
|
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: 119.01 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKN---ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSElSIFERSQK 374
Cdd:cd03266 1 MITADALTKRFRDVKKtvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVmqNPNHMISHHMIFDE-VAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPEL 453
Cdd:cd03266 80 LGFV--SDSTGLYDRLTAREnLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 454 LILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-223 |
1.62e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 122.22 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaikgE--VTGSLEINGKNISDFSM 78
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL-------ErpTSGRVLVDGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 79 HDYTE---QVGTVLQdtdsQFVGLS---IGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVS 152
Cdd:PRK11153 75 KELRKarrQIGMIFQ----HFNLLSsrtVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERGEIV 223
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEM-DVVKRICDRVAVIDAGRLV 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-232 |
1.80e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.43 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLipHAIKGevtGSLEINGKNISD--FSMHD 80
Cdd:PRK09493 2 IEFKNVSKHFG--PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL--EEITS---GDLIVDGLKVNDpkVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQdtdsQFV---GLSIGEDIAFA-LENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGI 156
Cdd:PRK09493 75 IRQEAGMVFQ----QFYlfpHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEdvLHRDI-DRVILMERGEIVADMTPDEIL 232
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIG--FAEKVaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
296-495 |
2.49e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 118.76 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEK---NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE-- 370
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 371 --RSQKVGVVMQNpNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSK-FRHWPIEaLSYGQKKRVTIASIL 447
Cdd:PRK11629 83 elRNQKLGFIYQF-HHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHrANHRPSE-LSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515631642 448 VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHL 495
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-171 |
2.49e-30 |
|
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: 115.82 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTgsleINGKNISDFSMHDYTEQVGTVLQDtDSQFVGL 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL-SPTEGTIL----LDGQDLTDDERKSLRKEIGYVFQD-PQLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 100 SIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDR----SPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
297-529 |
2.71e-30 |
|
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: 118.55 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-V 375
Cdd:COG0410 2 PMLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNpnhmishHMIFDE--V-------AFGLRNRGvaeqEIKEKVENVLELcglskF------RHWPIEALSYGQKKR 440
Cdd:COG0410 81 GYVPEG-------RRIFPSltVeenlllgAYARRDRA----EVRADLERVYEL-----FprlkerRRQRAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 441 VTIASILVLEPELLILDEPTAG------QDyrnytsMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIAN 514
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGlaplivEE------IFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
250
....*....|....*
gi 515631642 515 AAMTEVFSQPSLLER 529
Cdd:COG0410 218 GTAAELLADPEVREA 232
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-221 |
2.81e-30 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 117.73 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAikgevtGSLEINGKNISDFSMHD- 80
Cdd:TIGR02673 2 IEFHNVSKAYPG-GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGaLTPSR------GQVRIAGEDVNRLRGRQl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 --YTEQVGTVLQDtdSQFVG-LSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGIL 157
Cdd:TIGR02673 75 plLRRRIGVVFQD--FRLLPdRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 158 VDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEdVLHRDIDRVILMERGE 221
Cdd:TIGR02673 153 VNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLS-LVDRVAHRVIILDDGR 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-234 |
3.19e-30 |
|
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: 124.86 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISDFSMHDYT 82
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP-PTAGSVR----LDGADLSQWDREELG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDtdsqfVGL---SIGEDIA-FAlenqlvsNIDMYpLVKSTAKMVDLADMLDRSPH--D---------LSGGQ 147
Cdd:COG4618 406 RHIGYLPQD-----VELfdgTIAENIArFG-------DADPE-KVVAAAKLAGVHEMILRLPDgyDtrigeggarLSGGQ 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHR---LEDVlhrdiDRVILMERGEIVA 224
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRpslLAAV-----DKLLVLRDGRVQA 546
|
250
....*....|
gi 515631642 225 DMTPDEILAS 234
Cdd:COG4618 547 FGPRDEVLAR 556
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-235 |
3.89e-30 |
|
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: 118.60 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTE-------QVGTVlqdt 92
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT-----SGRILFDGRDITGLPPHRIARlgiartfQNPRL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 93 dsqFVGLSIGEDIAFALENQLVSNIDMYPL---------------VKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGIL 157
Cdd:COG0411 91 ---FPELTVLENVLVAAHARLGRGLLAALLrlprarreerearerAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 158 VDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILASE 235
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDM-DLVMGLADRIVVLDFGRVIAEGTPAEVRADP 244
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-234 |
4.04e-30 |
|
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: 124.93 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISDFSMHD 80
Cdd:COG5265 357 EVRFENVSFGYDP-ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY------DVTsGRILIDGQDIRDVTQAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQDT----DSqfvglsIGEDIAF----ALENQlvsnidmyplVKSTAKMVDLADMLDRSPH----------- 141
Cdd:COG5265 430 LRAAIGIVPQDTvlfnDT------IAYNIAYgrpdASEEE----------VEAAARAAQIHDFIESLPDgydtrvgergl 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 142 DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGE 221
Cdd:COG5265 494 KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTI--VDADEILVLEAGR 569
|
250
....*....|...
gi 515631642 222 IVADMTPDEILAS 234
Cdd:COG5265 570 IVERGTHAELLAQ 582
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-238 |
4.59e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 118.26 E-value: 4.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISDFSMHDYT 82
Cdd:COG4604 2 IEIKNVSKRYG--GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLP-PDSGEVL----VDGLDVATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQdtdsqfvglsigediafalENQLVSNIDMYPLV----------KSTA---KMVD-------LADMLDRSPHD 142
Cdd:COG4604 75 KRLAILRQ-------------------ENHINSRLTVRELVafgrfpyskgRLTAedrEIIDeaiayldLEDLADRYLDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 143 LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIiehrledVLHrDI-------DRVI 215
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVI-------VLH-DInfascyaDHIV 207
|
250 260
....*....|....*....|...
gi 515631642 216 LMERGEIVADMTPDEILASELLE 238
Cdd:COG4604 208 AMKDGRVVAQGTPEEIITPEVLS 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
298-524 |
5.78e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 118.71 E-value: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSyDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS---IFERSQK 374
Cdd:PRK11831 7 LVDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNpNHMISHHMIFDEVAFGLRNRG-VAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPEL 453
Cdd:PRK11831 86 MSMLFQS-GALFTDMNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 454 LILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-222 |
9.66e-30 |
|
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: 116.35 E-value: 9.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLnglipHAIKGEVTGSLEINGKNISDF---SMH 79
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLI-----YKEELPTSGTIRVNGQDVSDLrgrAIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYTEQVGTVLQDTdSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVD 159
Cdd:cd03292 75 YLRRKIGVVFQDF-RLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 160 DVDILLFDEPLASLDPKTGKATIEIIDQLHKeTNKTIVIIEHRlEDVLHRDIDRVILMERGEI 222
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHA-KELVDTTRHRVIALERGKL 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
311-512 |
9.77e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 119.42 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDlselsIFERSQK----VGVVMQNPNHMI 386
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKRRKEfarrIGVVFGQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 387 SHHMIFDevAFGLrNR---GVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQ 463
Cdd:COG4586 109 WDLPAID--SFRL-LKaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515631642 464 DYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
297-492 |
1.19e-29 |
|
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: 116.04 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQkvg 376
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 vvMqnpnHMISHH-MIFDE------VAFGLRNRGVAEQEikEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVL 449
Cdd:COG4133 77 --L----AYLGHAdGLKPEltvrenLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515631642 450 EPELLILDEPTAGQDYRnytSMLAFIQKLNREL--GITVVIISHD 492
Cdd:COG4133 149 PAPLWLLDEPFTALDAA---GVALLAELIAAHLarGGAVLLTTHQ 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
278-499 |
1.29e-29 |
|
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: 122.78 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 278 AVQAWFAERPTPVAEKQ-----YQPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD 352
Cdd:TIGR02857 296 ALFAVLDAAPRPLAGKApvtaaPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 353 SGSSYLNGEDLSELSIFERSQKVGVVMQNPnhmishHMIFDEVAFGLR--NRGVAEQEIKEkvenVLELCGLSKF----- 425
Cdd:TIGR02857 376 EGSIAVNGVPLADADADSWRDQIAWVPQHP------FLFAGTIAENIRlaRPDASDAEIRE----ALERAGLDEFvaalp 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 426 --RHWPI----EALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRelGITVVIISHDMHLVLEY 499
Cdd:TIGR02857 446 qgLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA 523
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-221 |
1.50e-29 |
|
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: 115.64 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYES---LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIphaikGEVT---GSLEINGKnISdf 76
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSL---LSALL-----GELEklsGSVSVPGS-IA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 77 smhdYTEQVGTVLQDTdsqfvglsIGEDIAFALEnqlvSNIDMYPLV-KSTAKMVDLADMLDrspHD----------LSG 145
Cdd:cd03250 70 ----YVSQEPWIQNGT--------IRENILFGKP----FDEERYEKViKACALEPDLEILPD---GDlteigekginLSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKAtieIIDQL---HKETNKTIVIIEHRLEDVLHrdIDRVILMERGE 221
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH---IFENCilgLLLNNKTRILVTHQLQLLPH--ADQIVVLDNGR 204
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-233 |
1.65e-29 |
|
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: 122.90 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQclngLIPHAIKGEvTGSLEINGKNISDFSMHDYT 82
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVN----LIPRFYEPD-SGQILLDGHDLADYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDtdsqfVGL---SIGEDIAFALENQLVSnidmyPLVKSTAKMVDLADMLDRSPH-----------DLSGGQK 148
Cdd:TIGR02203 406 RQVALVSQD-----VVLfndTIANNIAYGRTEQADR-----AEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVLHrdIDRVILMERGEIVADMTP 228
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK--ADRIVVMDDGRIVERGTH 551
|
....*
gi 515631642 229 DEILA 233
Cdd:TIGR02203 552 NELLA 556
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
298-493 |
1.75e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 116.72 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERsqkvGV 377
Cdd:PRK11248 1 MLQISHLYADYGG-KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ER----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNpNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:PRK11248 75 VFQN-EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDM 493
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
298-522 |
1.89e-29 |
|
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: 117.21 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSY--------DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELsif 369
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 370 ERSQK------VGVVMQNPNHMISHHMIFDE-VAFGLRN-RGVAEQEIKEKVENVLELCGL--SKFRHWPIEaLSYGQKK 439
Cdd:TIGR02769 79 DRKQRrafrrdVQLVFQDSPSAVNPRMTVRQiIGEPLRHlTSLDESEQKARIAELLDMVGLrsEDADKLPRQ-LSGGQLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQ 237
|
...
gi 515631642 520 VFS 522
Cdd:TIGR02769 238 LLS 240
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-231 |
2.16e-29 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 118.37 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 35 IIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDFSMHdyTEQVGTVLQDTdSQFVGLSIGEDIAFALENQL 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEqPDS------GSIMLDGEDVTNVPPH--LRHINMVFQSY-ALFPHMTVEENVAFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 114 VSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETN 193
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 515631642 194 KTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEI 231
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMS-DRIAIMRKGKIAQIGTPEEI 188
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-223 |
2.64e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 115.88 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHaikgevTGSLEINGKNIsDFSMH 79
Cdd:PRK11124 1 MSIQLNGINCFYGA--HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLeMPR------SGTLNIAGNHF-DFSKT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYTEQ-------VGTVLQdtdsQF---VGLSIgediafaLENQLVSNIDMYPLVKSTAK--------MVDLADMLDRSPH 141
Cdd:PRK11124 72 PSDKAirelrrnVGMVFQ----QYnlwPHLTV-------QQNLIEAPCRVLGLSKDQALaraeklleRLRLKPYADRFPL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 142 DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEdVLHRDIDRVILMERGE 221
Cdd:PRK11124 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVE-VARKTASRVVYMENGH 218
|
..
gi 515631642 222 IV 223
Cdd:PRK11124 219 IV 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
296-520 |
3.64e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.89 E-value: 3.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFErSQKV 375
Cdd:COG1129 2 EPLLEMRGISKSFGGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVM--QNPNhmishhmIFDE--VA----FG--LRNRG-VAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIA 444
Cdd:COG1129 80 GIAIihQELN-------LVPNlsVAenifLGrePRRGGlIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 445 SILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-493 |
3.72e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 122.93 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLgqcLnGLIP--HAIKgevTGSLEINGKNISDfsmHDYTEQV-----------G 86
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSL---L-SLIAgaRKIQ---QGRVEVLGGDMAD---ARHRRAVcpriaympqglG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 87 TVLQDTdsqfvgLSIGEDIAF--------ALENQlvSNIDMypLVKSTakmvDLADMLDRSPHDLSGGQKQRVSLAGILV 158
Cdd:NF033858 87 KNLYPT------LSVFENLDFfgrlfgqdAAERR--RRIDE--LLRAT----GLAPFADRPAGKLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVII--------EHrledvlhrdIDRVILMERGEIVADMTPDE 230
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVataymeeaER---------FDWLVAMDAGRVLATGTPAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 231 ILAsellETHGireplylSALKAAKAPLTSEDKLSNLKALdykrfrpavqawfaERPTPVAEKQYQPLLEVHGLTYSYdG 310
Cdd:NF033858 224 LLA----RTGA-------DTLEAAFIALLPEEKRRGHQPV--------------VIPPRPADDDDEPAIEARGLTMRF-G 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE--DLSELSIFERsqkVG------------ 376
Cdd:NF033858 278 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIATRRR---VGymsqafslygel 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQNpnhMISHHMIFDevafglrnrgVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLIL 456
Cdd:NF033858 355 TVRQN---LELHARLFH----------LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 515631642 457 DEPTAGQD--YRNytsmlAFIQ---KLNRELGITVVIISHDM 493
Cdd:NF033858 422 DEPTSGVDpvARD-----MFWRlliELSREDGVTIFISTHFM 458
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
280-537 |
4.08e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 117.64 E-value: 4.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 280 QAWFAER---PTPVAEKQyqpLLEVHGLTYSYDGEKN----ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD 352
Cdd:PRK13631 3 DYFMKKKlkvPNPLSDDI---ILRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 353 SGSS-----YLNGEDLSELSIFERSQK-----------VGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENV 416
Cdd:PRK13631 80 YGTIqvgdiYIGDKKNNHELITNPYSKkiknfkelrrrVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 417 LELCGL--SKFRHWPIEaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMH 494
Cdd:PRK13631 160 LNKMGLddSYLERSPFG-LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTME 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 515631642 495 LVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLEranlcTTSI 537
Cdd:PRK13631 238 HVLEVADEVIVMDKGKILKTGTPYEIFTDQHIIN-----STSI 275
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
5.45e-29 |
|
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: 120.93 E-value: 5.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISDFSMHDY 81
Cdd:TIGR02868 334 TLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-PLQGEVT----LDGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDtdSQFVGLSIGEDIAFALENqlVSNIDMYPLVKStakmVDLADMLDRSPHDL-----------SGGQKQR 150
Cdd:TIGR02868 408 RRRVSVCAQD--AHLFDTTVRENLRLARPD--ATDEELWAALER----VGLADWLRALPDGLdtvlgeggarlSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEiiDQLHKETNKTIVIIEHRL 203
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLE--DLLAALSGRTVVLITHHL 530
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-234 |
5.46e-29 |
|
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: 117.89 E-value: 5.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFsNFSFRYESLdkpTLkNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHD 80
Cdd:COG4148 1 MMLEV-DFRLRRGGF---TL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD-----SGRIRLGGEVLQDSARGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 Y--TEQ--VGTVLQDtDSQFVGLSIGEDIAFALENQLVSNidMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGI 156
Cdd:COG4148 71 FlpPHRrrIGYVFQE-ARLFPHLSVRGNLLYGRKRAPRAE--RRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 157 LVDDVDILLFDEPLASLDPKTgKATI-EIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:COG4148 148 LLSSPRLLLMDEPLAALDLAR-KAEIlPYLERLRDELDIPILYVSHSLDEVA-RLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-235 |
6.90e-29 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 121.39 E-value: 6.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHaikgevTGSLEINGKNISDFSMHDY 81
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLyTPQ------HGQVLVDGVDLAIADPAWL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDtdSQFVGLSIGEDIAFALENQLVSNidmyplVKSTAKMVDLADMLDRSPH-----------DLSGGQKQR 150
Cdd:TIGR01846 530 RRQMGVVLQE--NVLFSRSIRDNIALCNPGAPFEH------VIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKAtieIIDQLHKET-NKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPD 229
Cdd:TIGR01846 602 IAIARALVGNPRILIFDEATSALDYESEAL---IMRNMREICrGRTVIIIAHRLSTV--RACDRIIVLEKGQIAESGRHE 676
|
....*.
gi 515631642 230 EILASE 235
Cdd:TIGR01846 677 ELLALQ 682
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
296-544 |
9.68e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.75 E-value: 9.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDlselsifersqkv 375
Cdd:COG3845 3 PPALELRGITKRFGGVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 gVVMQNPNH-------MISHH-MIFDE------VAFGLRNRGVAEQEIKEKVENVLELCGLSKFR---HWPIEALSYGQK 438
Cdd:COG3845 69 -VRIRSPRDaialgigMVHQHfMLVPNltvaenIVLGLEPTKGGRLDRKAARARIRELSERYGLDvdpDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 439 KRVTIASILVLEPELLILDEPTAG---QDYRnytSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANA 515
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVltpQEAD---ELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTV 223
|
250 260
....*....|....*....|....*....
gi 515631642 516 AMTEvfsqpslleranlctTSIYELATMM 544
Cdd:COG3845 224 DTAE---------------TSEEELAELM 237
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
304-548 |
9.94e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 115.08 E-value: 9.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 304 LTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQN-- 381
Cdd:PRK10253 13 LTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNat 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 382 -PNHMISHHMifdeVAFG------LRNRGVAEQEikEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK10253 92 tPGDITVQEL----VARGryphqpLFTRWRKEDE--EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSqPSLLERanlct 534
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT-AELIER----- 239
|
250
....*....|....
gi 515631642 535 tsIYELATMMkIDD 548
Cdd:PRK10253 240 --IYGLRCMI-IDD 250
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
317-513 |
1.41e-28 |
|
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: 113.16 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 317 DVSFKIgKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--SELSIFERSQ--KVGVVMQNpNHMISHHMIF 392
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKINLPPQqrKIGLVFQQ-YALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 393 DEVAFGLRnrGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSML 472
Cdd:cd03297 94 ENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515631642 473 AFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
311-512 |
1.50e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 114.41 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPnhMI--SH 388
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDP--MMgtAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 389 HM-IFDEVA--------FGLRnRGVAEQEI---KEKVEnVLELcGLSKFRHWPIEALSYGQKKRVT--IASIlvLEPELL 454
Cdd:COG1101 96 SMtIEENLAlayrrgkrRGLR-RGLTKKRRelfRELLA-TLGL-GLENRLDTKVGLLSGGQRQALSllMATL--TKPKLL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:COG1101 171 LLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
307-520 |
1.70e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 113.64 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 307 SYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEdLSelSIFErsqkVGVVMqnpnhmi 386
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VS--ALLE----LGAGF------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 387 shHMIF---DEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQ 463
Cdd:COG1134 100 --HPELtgrENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 464 DyrnytsmLAFIQKLNREL------GITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG1134 178 D-------AAFQKKCLARIrelresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
309-513 |
2.47e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 112.63 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 309 DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSI---FERSQkvgVVMQNpnhm 385
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgggFNPEL---TGREN---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 386 ishhmifdeVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDY 465
Cdd:cd03220 105 ---------IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515631642 466 RNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03220 176 AFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-530 |
3.02e-28 |
|
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: 118.39 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikGEVTGSLEINGKNISDFSMHDyTEQVGTVLQDTDSQFV-G 98
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPH---GTWDGEIYWSGSPLKASNIRD-TERAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 LSIGEDIAFALENQLVSNIDMYPLV----KSTAKMVDLADMLDRSP-HDLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRMAYNAMylraKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 174 DPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVA-----DMTPDEILASELLethgiREplyl 248
Cdd:TIGR02633 173 TEKETEILLDIIRDL-KAHGVACVYISHKLNEV-KAVCDTICVIRDGQHVAtkdmsTMSEDDIITMMVG-----RE---- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 249 salkaakapltsedkLSNLkaldykrfrpavqawFAERPTPVAEKqyqpLLEVHGLT--YSYDGEKNALEDVSFKIGKGE 326
Cdd:TIGR02633 242 ---------------ITSL---------------YPHEPHEIGDV----ILEARNLTcwDVINPHRKRVDDVSFSLRRGE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 327 FVSILGKNGSGKSTITKLIMGVID-ADSGSSYLNGEDLSELS-----------IFERSQKVGVVmqnPNHMISHHM---I 391
Cdd:TIGR02633 288 ILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpaqairagiamVPEDRKRHGIV---PILGVGKNItlsV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 392 FDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFrhWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSM 471
Cdd:TIGR02633 365 LKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF--LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEI 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 472 LAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVfSQPSLLERA 530
Cdd:TIGR02633 443 YKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL-TQEQVLAAA 499
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
297-532 |
7.01e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 112.86 E-value: 7.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSY--------DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSi 368
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 369 feRSQK------VGVVMQ------NPNHMISHhmIFDEVAFGLRNRGVAEQEikEKVENVLELCGL--SKFRHWPiEALS 434
Cdd:PRK10419 81 --RAQRkafrrdIQMVFQdsisavNPRKTVRE--IIREPLRHLLSLDKAERL--ARASEMLRAVDLddSVLDKRP-PQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 435 YGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIAN 514
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
250 260
....*....|....*....|..
gi 515631642 515 AAMTEV--FSQPS--LLERANL 532
Cdd:PRK10419 234 QPVGDKltFSSPAgrVLQNAVL 255
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-201 |
8.62e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 114.74 E-value: 8.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 21 KNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaikGEVT-GSLEINGKNISDFSMHDytEQVGTVLQdTDSQFVGL 99
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL------EDITsGDLFIGEKRMNDVPPAE--RGVGMVFQ-SYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDpktgk 179
Cdd:PRK11000 91 SVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD----- 165
|
170 180
....*....|....*....|....*..
gi 515631642 180 ATIEI-----IDQLHKETNKTIVIIEH 201
Cdd:PRK11000 166 AALRVqmrieISRLHKRLGRTMIYVTH 192
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
307-511 |
9.14e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 111.12 E-value: 9.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 307 SYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS----IFERSQkVGVVMQNp 382
Cdd:PRK10908 10 AYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrevPFLRRQ-IGMIFQD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 383 NHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCG-LSKFRHWPIEaLSYGQKKRVTIASILVLEPELLILDEPTA 461
Cdd:PRK10908 88 HHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGlLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515631642 462 GQDYRNYTSMLAFIQKLNReLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-292 |
1.19e-27 |
|
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: 114.05 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 23 INLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDFSMHDYT----EQVGTVLQDTdSQFV 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDE------GEIVLNGRTLFDSRKGIFLppekRRIGYVFQEA-RLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 98 GLSIGEDIAFALENQLVSNIDMYPlvKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKT 177
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 178 GKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASELLETHGIREPLYLsaLKAAKAP 257
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVL-RLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSL--IEGVVAE 243
|
250 260 270
....*....|....*....|....*....|....*
gi 515631642 258 LTSEDKLSNLKAldykrfrPAVQAWFAERPTPVAE 292
Cdd:TIGR02142 244 HDQHYGLTALRL-------GGGHLWVPENLGPTGA 271
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
300-493 |
1.84e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 112.49 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 300 EVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVM 379
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 380 QN----PnhmishHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGL--SKFRH-WPIEaLSYGQKKRVTIASILVLEP 451
Cdd:COG1125 83 QQiglfP------HMtVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDrYPHE-LSGGQQQRVGVARALAADP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515631642 452 ELLILDEP---------TAGQDyrnytsmlaFIQKLNRELGITVVIISHDM 493
Cdd:COG1125 156 PILLMDEPfgaldpitrEQLQD---------ELLRLQRELGKTIVFVTHDI 197
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-247 |
2.87e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 115.89 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISDFSMHDY 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY------DIDeGEILLDGHDLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVlqdtdSQFVGL---SIGEDIAFALENQLvSNIDmyplVKSTAKMVDLADMLDRSPHD-----------LSGGQ 147
Cdd:PRK11176 416 RNQVALV-----SQNVHLfndTIANNIAYARTEQY-SREQ----IEEAARMAYAMDFINKMDNGldtvigengvlLSGGQ 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMT 227
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI--EKADEILVVEDGEIVERGT 561
|
250 260
....*....|....*....|
gi 515631642 228 pdeilASELLETHGIREPLY 247
Cdd:PRK11176 562 -----HAELLAQNGVYAQLH 576
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-238 |
3.63e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.25 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHD 80
Cdd:PRK13548 1 AMLEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-----SGEVRLNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQDTDSQFvGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILV-- 158
Cdd:PRK13548 74 LARRRAVLPQHSSLSF-PFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 159 ----DDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIiehrledVLHrDI-------DRVILMERGEIVADMT 227
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIV-------VLH-DLnlaaryaDRIVLLHQGRLVADGT 224
|
250
....*....|.
gi 515631642 228 PDEILASELLE 238
Cdd:PRK13548 225 PAEVLTPETLR 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
298-524 |
5.01e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.41 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS--QKV 375
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNhMISHHMIFDEVAFG-LRNRGVAEQEIKEKVENVLELCGLS-KFRHWPIEaLSYGQKKRVTIASILVLEPEL 453
Cdd:PRK09493 80 GMVFQQFY-LFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAeRAHHYPSE-LSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 454 LILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
308-513 |
6.08e-27 |
|
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: 108.35 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 308 YDGEKNALEDVSFKigKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGVVMQNpNHMIS 387
Cdd:cd03298 9 SYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQE-NNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 388 HHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRN 467
Cdd:cd03298 84 HLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515631642 468 YTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
317-526 |
1.31e-26 |
|
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: 110.97 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 317 DVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSE------LSIFERsqKVGVVMQNPNhMISHHM 390
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKR--RIGYVFQEAR-LFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 391 IFDEVAFGLRNRGVAEQEIKEkvENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTS 470
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 471 MLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSL 526
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
304-540 |
1.46e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 304 LTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNgedlsELSIFERS------- 372
Cdd:PRK13646 8 VSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-----DITITHKTkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 --QKVGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILV 448
Cdd:PRK13646 83 vrKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdvMSQSPFQ-MSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLE 528
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLA 241
|
250
....*....|..
gi 515631642 529 RANLCTTSIYEL 540
Cdd:PRK13646 242 DWHIGLPEIVQL 253
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-223 |
1.81e-26 |
|
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: 109.76 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaiKGEVTGSLEINGKNISDFSMHDYTE----QVGTVLQDTDSQF- 96
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPP--PGITSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDPMTSLn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 97 -VgLSIGEDIAFALE-NQLVSNIDMYPLVKSTAKMVDL---ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:COG0444 101 pV-MTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 172 SLDpktgkATI--EIID---QLHKETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIV 223
Cdd:COG0444 180 ALD-----VTIqaQILNllkDLQRELGLAILFITHDLGVVAE--IaDRVAVMYAGRIV 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-231 |
1.95e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.58 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISDFSMHDytEQVGTVLQdTDSQFVGLSI 101
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL-----EKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQ-SYALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 102 GEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKAT 181
Cdd:PRK11432 96 GENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515631642 182 IEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEI 231
Cdd:PRK11432 176 REKIRELQQQFNITSLYVTHDQSEAFAVS-DTVIVMNKGKIMQIGSPQEL 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
299-491 |
2.31e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 107.85 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID--ADSGSSYLNGEDLSELSIFERSQK-V 375
Cdd:COG0396 1 LEIKNLHVSVEG-KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERARAgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPnhmishhmifdeVAF-GLRNR--------GVAEQEIK-----EKVENVLELCGLSK-FRHWPI-EALSYGQKK 439
Cdd:COG0396 80 FLAFQYP------------VEIpGVSVSnflrtalnARRGEELSareflKLLKEKMKELGLDEdFLDRYVnEGFSGGEKK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515631642 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISH 491
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITH 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-223 |
2.35e-26 |
|
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: 106.10 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSF----RYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAIKGEVTgsleINGKNISD 75
Cdd:cd03213 2 VTLSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVSGEVL----INGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 76 FSmhdYTEQVGTVLQDtDSQFVGLSIGEDIAFAlenqlvsnidmyplvkstAKMvdladmldRSphdLSGGQKQRVSLAG 155
Cdd:cd03213 78 RS---FRKIIGYVPQD-DILHPTLTVRETLMFA------------------AKL--------RG---LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKeTNKTIVIIEHRLEDVLHRDIDRVILMERGEIV 223
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSSEIFELFDKLLLLSQGRVI 191
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-219 |
2.55e-26 |
|
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: 106.41 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDfSMHD 80
Cdd:COG4133 1 MMLEAENLSCRRG--ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS-----AGEVLWNGEPIRD-ARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQDtDSQFVGLSIGEDIAF--ALENQLVSNIDmyplVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILV 158
Cdd:COG4133 73 YRRRLAYLGHA-DGLKPELTVRENLRFwaALYGLRADREA----IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 159 DDVDILLFDEPLASLDpktgKATIEIIDQL---HKETNKTIVIIEHRLEDVLHrdiDRVILMER 219
Cdd:COG4133 148 SPAPLWLLDEPFTALD----AAGVALLAELiaaHLARGGAVLLTTHQPLELAA---ARVLDLGD 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
306-524 |
3.62e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 107.44 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 306 YSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDA-DS-----GSSYLNGEDLSELSIFERSQKVGVVM 379
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSkikvdGKVLYFGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 380 QNPNHMiSHHMIFDEVAFGLRNRGVAEQ-EIKEKVENVLELCGLSKFRH----WPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK14246 97 QQPNPF-PHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVYdrlnSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNRElgITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
298-522 |
3.84e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.90 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VG 376
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQNPNhMISHHMIFDEVAFGLRNR-GVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK10895 82 YLPQEAS-IFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFS 522
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
317-492 |
4.14e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 110.12 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 317 DVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGVVMQnpNHMISHHM-IFDEV 395
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VGMVFQ--SYALYPHLsVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 396 AFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFI 475
Cdd:PRK11000 97 SFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEI 176
|
170
....*....|....*..
gi 515631642 476 QKLNRELGITVVIISHD 492
Cdd:PRK11000 177 SRLHKRLGRTMIYVTHD 193
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-514 |
4.90e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 111.56 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikGEVTGSLEING-----KNISDfsmhdyTEQVGTVLQDTDS 94
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPH---GTYEGEIIFEGeelqaSNIRD------TERAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 QFV-GLSIGEDIaFaLENQLVSNIDM-YPLVKSTAKMVdLADM-LDRSPH----DLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:PRK13549 92 ALVkELSVLENI-F-LGNEITPGGIMdYDAMYLRAQKL-LAQLkLDINPAtpvgNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 168 EPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIV-----ADMTPDEILASELlethG 241
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEV--KAIsDTICVIRDGRHIgtrpaAGMTEDDIITMMV----G 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 242 iREplylsalkaakapltsedkLSNLkaldykrfrpavqawFAERPTPVAEKqyqpLLEVHGLTySYDGE---KNALEDV 318
Cdd:PRK13549 242 -RE-------------------LTAL---------------YPREPHTIGEV----ILEVRNLT-AWDPVnphIKRVDDV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 319 SFKIGKGEFVSILGKNGSGKSTITKLIMGVID-ADSGSSYLNGEDLSelsifersqkvgvvMQNPNHMISHHM------- 390
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVK--------------IRNPQQAIAQGIamvpedr 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 391 ------------------IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRhwPIEALSYGQKKRVTIASILVLEPE 452
Cdd:PRK13549 348 krdgivpvmgvgknitlaALDRFTGGSRIDDAAELKTILESIQRLKVKTASPEL--AIARLSGGNQQKAVLAKCLLLNPK 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 453 LLILDEPTAGQD----YRNYTSMLAFIQKlnrelGITVVIISHDMHLVLEYTTRSIVIADSKLIAN 514
Cdd:PRK13549 426 ILILDEPTRGIDvgakYEIYKLINQLVQQ-----GVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-511 |
5.37e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 111.68 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSmHDYTEQVGTVLQDTDSQ-F 96
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD-----SGTLEIGGNPCARLT-PAKAHQLGIYLVPQEPLlF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 97 VGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLadmlDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPK 176
Cdd:PRK15439 99 PNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDL----DSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 177 TGKATIEIIDQLHKEtNKTIVIIEHRLEDVlhRDI-DRVILMERGEIV-----ADMTPDEILAsellethgireplylsa 250
Cdd:PRK15439 175 ETERLFSRIRELLAQ-GVGIVFISHKLPEI--RQLaDRISVMRDGTIAlsgktADLSTDDIIQ----------------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 251 lkaAKAPLTSEDKLSNLKALdykrfrpavqaWFAERPTPVAEKQYQPLLEVHGLTysydGEknALEDVSFKIGKGEFVSI 330
Cdd:PRK15439 235 ---AITPAAREKSLSASQKL-----------WLELPGNRRQQAAGAPVLTVEDLT----GE--GFRNISLEVRAGEILGL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 331 LGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFER-----------SQKVGVVMQNPNHMISHHMIFDEVAFGL 399
Cdd:PRK15439 295 AGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarglvylpedRQSSGLYLDAPLAWNVCALTHNRRGFWI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 400 rnRGVAEQEIKEKVENVLELcglsKFRH--WPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDyrnyTSMLAFIQK 477
Cdd:PRK15439 375 --KPARENAVLERYRRALNI----KFNHaeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD----VSARNDIYQ 444
|
490 500 510
....*....|....*....|....*....|....*..
gi 515631642 478 LNREL---GITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK15439 445 LIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-231 |
7.00e-26 |
|
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: 105.66 E-value: 7.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 11 RYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISDfSMHDYTEQVGTVLQ 90
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR-PTSGTAY----INGYSIRT-DRKAARQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 91 DtDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:cd03263 83 F-DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 171 ASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhrDI--DRVILMERGEIVADMTPDEI 231
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEA---EAlcDRIAIMSDGKLRCIGSPQEL 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-239 |
8.44e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.25 E-value: 8.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPhaikgeVTGSLEINGKNISDFSMH 79
Cdd:PRK11231 1 MTLRTENLTVGYG--TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARlLTP------QSGTVFLGDKPISMLSSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYTEQVGTVLQdtdsQFV---GLSIGEDIAF------ALENQLVSNIDMypLVKSTAKMVDLADMLDRSPHDLSGGQKQR 150
Cdd:PRK11231 73 QLARRLALLPQ----HHLtpeGITVRELVAYgrspwlSLWGRLSAEDNA--RVNQAMEQTRINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDE 230
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQA-SRYCDHLVVLANGHVMAQGTPEE 224
|
....*....
gi 515631642 231 ILASELLET 239
Cdd:PRK11231 225 VMTPGLLRT 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-235 |
1.00e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.46 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQclngLIPHA---IKGEVTgsleINGKNISDFSMH 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ----LLTRAwdpQQGEIL----LNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYTEQVGTVlqdtdSQFVGL---SIGEDIAFALEN----QLvsnIDMypLVKstakmVDLADMLD-RSPHD--------- 142
Cdd:PRK11160 411 ALRQAISVV-----SQRVHLfsaTLRDNLLLAAPNasdeAL---IEV--LQQ-----VGLEKLLEdDKGLNawlgeggrq 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 143 LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKatiEIIDQLHKE-TNKTIVIIEHRLEDVLHrdIDRVILMERGE 221
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETER---QILELLAEHaQNKTVLMITHRLTGLEQ--FDRICVMDNGQ 550
|
250
....*....|....
gi 515631642 222 IVADMTPDEILASE 235
Cdd:PRK11160 551 IIEQGTHQELLAQQ 564
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
299-529 |
1.20e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.87 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQnpnhmisHHM------IFDEVAFG----LRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:PRK11231 82 PQ-------HHLtpegitVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFsQPSLLE 528
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM-TPGLLR 232
|
.
gi 515631642 529 R 529
Cdd:PRK11231 233 T 233
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
314-524 |
1.52e-25 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 105.14 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD----SGSSYLNGEDLSELSIfeRSQKVGVVMQNPN------ 383
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSI--RGRHIATIMQNPRtafnpl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 384 HMISHHMIfdEVafgLRNRGVAEQEIKEKVENVLELCGLSK----FRHWPIEaLSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:TIGR02770 79 FTMGNHAI--ET---LRSLGKLSKQARALILEALEAVGLPDpeevLKKYPFQ-LSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 460 TAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
248-492 |
1.58e-25 |
|
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: 110.53 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 248 LSALKAAKAPLT----SEDKLSNLkaLDYKRFRPAVQAwfaerPTPVAEKQYQPLLEVHGLTYSYDGEKNALEDVSFKIG 323
Cdd:TIGR02868 287 FAALPAAAQQLTrvraAAERIVEV--LDAAGPVAEGSA-----PAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 324 KGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPnHMIsHHMIFDEVAFGlrNRG 403
Cdd:TIGR02868 360 PGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDA-HLF-DTTVRENLRLA--RPD 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 404 VAEQEIKEkvenVLELCGLSKfrhWPIE--------------ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYT 469
Cdd:TIGR02868 436 ATDEELWA----ALERVGLAD---WLRAlpdgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD 508
|
250 260
....*....|....*....|...
gi 515631642 470 SMLAFIqkLNRELGITVVIISHD 492
Cdd:TIGR02868 509 ELLEDL--LAALSGRTVVLITHH 529
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-239 |
1.77e-25 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 105.31 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevtGSLEINGKNISDFSMHDYTEQVGTVLQDTDSQFVgL 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ------GEILLNGRPLSDWSAAELARHRAYLSQQQSPPFA-M 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAFALENQLVSnidmyPLVKSTAKMV----DLADMLDRSPHDLSGGQKQRVSLAGIL--VDDVD-----ILLFDE 168
Cdd:COG4138 85 PVFQYLALHQPAGASS-----EAVEQLLAQLaealGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWPTInpegqLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 169 PLASLDPKTGKATIEIIDQLHkETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASELLET 239
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTL-RHADRVWLLKQGKLVASGETAEVMTPENLSE 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-223 |
1.80e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.22 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNgLIPHAIKGEVT-GSLEING-KNISDFS--MHDYTEQVGTVLQDTDsQ 95
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCIN-LLEQPEAGTIRvGDITIDTaRSLSQQKglIRQLRQHVGFVFQNFN-L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGEDIafaLENQLVsnidmyplVKSTAK------------MVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDI 163
Cdd:PRK11264 97 FPHRTVLENI---IEGPVI--------VKGEPKeeatararellaKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 164 LLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHrlEDVLHRDI-DRVILMERGEIV 223
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTH--EMSFARDVaDRAIFMDQGRIV 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-492 |
1.86e-25 |
|
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: 110.41 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlIPHAIKGEVTGSLEINgknisdfsmhdyteqVGTVLQD---- 91
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDFNGEARPQPGIK---------------VGYLPQEpqld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 92 ---TDSQFVGLSIGEdIAFALE--NQLVSNI-----DMYPLVKSTAKMVDLADMLD---------------RSP------ 140
Cdd:TIGR03719 81 ptkTVRENVEEGVAE-IKDALDrfNEISAKYaepdaDFDKLAAEQAELQEIIDAADawdldsqleiamdalRCPpwdadv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 141 HDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTgkatIEIIDQLHKETNKTIVIIEHrledvlhrdiDRVILmerg 220
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTH----------DRYFL---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 221 eivaDMTPDEILasELLETHGIR-EPLYLSALKAAKAPLTSEDK----------------LSNLKALDYK------RFRP 277
Cdd:TIGR03719 222 ----DNVAGWIL--ELDRGRGIPwEGNYSSWLEQKQKRLEQEEKeesarqktlkrelewvRQSPKGRQAKskarlaRYEE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 278 AVQAWFAERP------TPVAEKQYQPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDA 351
Cdd:TIGR03719 296 LLSQEFQKRNetaeiyIPPGPRLGDKVIEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 352 DSGSsylngedlseLSIFErSQKVGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVenvleLCGLSKFR----H 427
Cdd:TIGR03719 375 DSGT----------IEIGE-TVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRFNFKgsdqQ 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 428 WPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRnytSMLAFIQKLnRELGITVVIISHD 492
Cdd:TIGR03719 439 KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE---TLRALEEAL-LNFAGCAVVISHD 499
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-233 |
1.87e-25 |
|
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: 104.44 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVtgslEINGKNISDFSMHDYTEQ-VGTVLQDTDSqF 96
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-PRSGSI----RFDGRDITGLPPHERARAgIGYVPEGRRI-F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 97 VGLSIGEDIAFALENQLVSNI--------DMYPlvkstakmvDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:cd03224 88 PELTVEENLLLGAYARRRAKRkarlervyELFP---------RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 169 PLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILA 233
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEI-ADRAYVLERGRVVLEGTAAELLA 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
297-526 |
2.05e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.39 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVG 376
Cdd:PRK09536 2 PMIDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQNPNhmishhmifdeVAFGLRNRGVAE--------------QEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVT 442
Cdd:PRK09536 81 SVPQDTS-----------LSFEFDVRQVVEmgrtphrsrfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 443 IASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFS 522
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
....
gi 515631642 523 QPSL 526
Cdd:PRK09536 229 ADTL 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
299-498 |
2.14e-25 |
|
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: 104.62 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnhMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLEL-CGLSKFRHWPIE----ALSYGQKKRVTIASILVLEPE 452
Cdd:cd03251 81 VSQDV--FLFNDTVAENIAYGRPGATREEVEEAARAANAHEFiMELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 453 LLILDEPTAGQDyrNYTSMLafIQKLNREL--GITVVIISH--------DMHLVLE 498
Cdd:cd03251 159 ILILDEATSALD--TESERL--VQAALERLmkNRTTFVIAHrlstienaDRIVVLE 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-230 |
2.20e-25 |
|
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: 104.44 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaikgEV--TGSLEINGKNISDFSmhdytE---------QVGTV 88
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-------DRptSGTVRLAGQDLFALD-----EdararlrarHVGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 89 LQDtdSQFVG-LSigediafALENqlVsnidMYPL-------VKSTAK----MVDLADMLDRSPHDLSGGQKQRVSLAGI 156
Cdd:COG4181 96 FQS--FQLLPtLT-------ALEN--V----MLPLelagrrdARARARalleRVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEdvLHRDIDRVILMERGEIVADMTPDE 230
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA--LAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
299-511 |
2.35e-25 |
|
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: 102.68 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNA-LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNpnhmishhmifDEVAFGlrnrGVAeqeikekvENVlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03246 81 LPQD-----------DELFSG----SIA--------ENI----------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLvLEYTTRSIVIADSKL 511
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPET-LASADRILVLEDGRV 173
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-223 |
2.56e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 109.93 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikgevTGSLEINGKNISDFSMHDYTEQVGTVLQdtDSQ 95
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY------QGSLKINGIELRELDPESWRKHLSWVGQ--NPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGEDIAFAleNQLVSNIDMYPLVKSTakmvDLADMLDRSPHDL-----------SGGQKQRVSLAGILVDDVDIL 164
Cdd:PRK11174 434 LPHGTLRDNVLLG--NPDASDEQLQQALENA----WVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGEIV 223
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDL--AQWDQIWVMQDGQIV 562
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-233 |
2.63e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 109.74 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDY 81
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP-----PTSGSVRLDGADLKQWDRETF 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTDsQFVGlSIGEDIAfalenQLVSNIDMYPLVKStAKMVDLADMLDRSP--HD---------LSGGQKQR 150
Cdd:TIGR01842 391 GKHIGYLPQDVE-LFPG-TVAENIA-----RFGENADPEKIIEA-AKLAGVHELILRLPdgYDtvigpggatLSGGQRQR 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEdvLHRDIDRVILMERGEIVADMTPDE 230
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS--LLGCVDKILVLQDGRIARFGERDE 539
|
...
gi 515631642 231 ILA 233
Cdd:TIGR01842 540 VLA 542
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
297-516 |
3.06e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.04 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsQKVG 376
Cdd:PRK13537 6 APIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-QRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQ----NPNHMISHHMIFdevaFGlRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPE 452
Cdd:PRK13537 84 VVPQfdnlDPDFTVRENLLV----FG-RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 453 LLILDEPTAGQD-------YRNYTSMLAfiqklnreLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAA 516
Cdd:PRK13537 159 VLVLDEPTTGLDpqarhlmWERLRSLLA--------RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-233 |
3.52e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.78 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNgliphAIKGEV---TGSLEINGKNISDFSMHDYTEQVGTVLQD-- 91
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTL---LN-----AIAGSLppdSGSILIDGKDVTKLPEYKRAKYIGRVFQDpm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 92 --TDSqfvGLSIGEDIA------------FALENQlvsNIDMYplvKSTAKMVD--LADMLDRSPHDLSGGQKQRVSLAG 155
Cdd:COG1101 91 mgTAP---SMTIEENLAlayrrgkrrglrRGLTKK---RRELF---RELLATLGlgLENRLDTKVGLLSGGQRQALSLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVAD--------MT 227
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYG-NRLIMMHEGRIILDvsgeekkkLT 240
|
....*.
gi 515631642 228 PDEILA 233
Cdd:COG1101 241 VEDLLE 246
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
299-491 |
4.60e-25 |
|
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: 102.61 E-value: 4.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSyDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID--ADSGSSYLNGEDLSELSIFERSQK-V 375
Cdd:cd03217 1 LEIKDLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPnhmishhmifdevafgLRNRGVaeqeikeKVENVLELCGlskfrhwpiEALSYGQKKRVTIASILVLEPELLI 455
Cdd:cd03217 80 FLAFQYP----------------PEIPGV-------KNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190
....*....|....*....|....*....|....*.
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISH 491
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITH 162
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-175 |
5.70e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.95 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKgeVTGSLEINGKNISDFSMHDytEQVGTVLQDtDSQ 95
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFS--ASGEVLLNGRRLTALPAEQ--RRIGILFQD-DLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGEDIAFALENQlVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:COG4136 88 FPHLSVGENLAFALPPT-IGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-233 |
6.41e-25 |
|
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: 109.44 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYeSLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDYT 82
Cdd:TIGR01193 474 IVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ-----ARSGEILLNGFSLKDIDRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQD----TDSQFVGLSIG-------EDIAFALE-NQLVSNIDMYPLVKSTAkmvdladmLDRSPHDLSGGQKQR 150
Cdd:TIGR01193 548 QFINYLPQEpyifSGSILENLLLGakenvsqDEIWAACEiAEIKDDIENMPLGYQTE--------LSEEGSSISGGQKQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGKatiEIIDQLHKETNKTIVIIEHRLEdvLHRDIDRVILMERGEIVADMTPDE 230
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEK---KIVNNLLNLQDKTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQGSHDE 694
|
...
gi 515631642 231 ILA 233
Cdd:TIGR01193 695 LLD 697
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
304-512 |
8.88e-25 |
|
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: 102.69 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 304 LTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPn 383
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 384 hMISHHMIFDEVAFGlrnRGVAEQeikEKVENVLELCGLSKF-RHWPI----------EALSYGQKKRVTIASILVLEPE 452
Cdd:cd03254 87 -FLFSGTIMENIRLG---RPNATD---EEVIEAAKEAGAHDFiMKLPNgydtvlgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 453 LLILDEPTAGQDyrnyTSMLAFIQKLNREL--GITVVIISHdmHL-VLEYTTRSIVIADSKLI 512
Cdd:cd03254 160 ILILDEATSNID----TETEKLIQEALEKLmkGRTSIIIAH--RLsTIKNADKILVLDDGKII 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
299-492 |
1.25e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.79 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD---SGSSYLNGEDLSELSIFERsqKV 375
Cdd:COG4136 2 LSLENLTITLGG-RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR--RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPnHMISHHMIFDEVAFGLRNrGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:COG4136 79 GILFQDD-LLFPHLSVGENLAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 515631642 456 LDEPTAG--QDYRNYTSMLAFIQKlnRELGITVVIISHD 492
Cdd:COG4136 157 LDEPFSKldAALRAQFREFVFEQI--RQRGIPALLVTHD 193
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-229 |
2.28e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.47 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 6 SNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSmhdytEQV 85
Cdd:PRK11248 5 SHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-----HGSITLDGKPVEGPG-----AER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 86 GTVLQDtDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK11248 73 GVVFQN-EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDIDRVILMER-GEIVADMTPD 229
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGpGRVVERLPLN 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
299-492 |
2.44e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 104.54 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGVV 378
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD--IAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQN----PnhmishHM-IFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPEL 453
Cdd:PRK11650 82 FQNyalyP------HMsVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 515631642 454 LILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHD 492
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD 194
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-228 |
2.49e-24 |
|
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: 100.95 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYT 82
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE-----EGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTdSQFVGlsigediafalenQLVSNIDmyPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03369 82 SSLTIIPQDP-TLFSG-------------TIRSNLD--PFDEYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIdqlHKE-TNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTP 228
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTI---REEfTNSTILTIAHRLRTII--DYDKILVMDAGEVKEYDHP 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-496 |
3.06e-24 |
|
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: 106.79 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 28 EKGEKIVIIGPSGSGKSTLGQCLNG-LIPhaikgevtgsleingkNISDFSMHDYTEQV-----GTVLQDtdsQFVGLSI 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGeLKP----------------NLGDYDEEPSWDEVlkrfrGTELQD---YFKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 102 GEdIAFALENQLVSNIDMYplVKST-----------------AKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:COG1245 158 GE-IKVAHKPQYVDLIPKV--FKGTvrellekvdergkldelAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRL------EDVLHrdidrVILMERGE--IVADMTPDEIlasel 236
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLaildylADYVH-----ILYGEPGVygVVSKPKSVRV----- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 237 lethGIREplYLsalkaaKAPLTSEdklsNLkaldykRFRP-AVQawFAERPtPVAEKQYQPLLEVHGLTYSYDGEKnaL 315
Cdd:COG1245 304 ----GINQ--YL------DGYLPEE----NV------RIRDePIE--FEVHA-PRREKEEETLVEYPDLTKSYGGFS--L 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 316 EDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYlngedlSELSIFERSQKVGvvmqnpnhmishHMIFDEV 395
Cdd:COG1245 357 EVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD------EDLKISYKPQYIS------------PDYDGTV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 396 AFGLRNrgvaeqEIKEKVEN------VLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYT 469
Cdd:COG1245 419 EEFLRS------ANTDDFGSsyykteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
490 500
....*....|....*....|....*..
gi 515631642 470 SMLAFIQKLNRELGITVVIISHDMHLV 496
Cdd:COG1245 493 AVAKAIRRFAENRGKTAMVVDHDIYLI 519
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-217 |
5.31e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.62 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 11 RYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIkgevtgsleingknisdfsmhdyteqvGTVLQ 90
Cdd:NF040873 1 GYGG--RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS---------------------------GTVRR 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 91 DTdsqfvglsiGEDIAFALenQLVSNIDMYPL-VKSTAKM--------------------------VDLADMLDRSPHDL 143
Cdd:NF040873 52 AG---------GARVAYVP--QRSEVPDSLPLtVRDLVAMgrwarrglwrrltrddraavddalerVGLADLAGRQLGEL 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 144 SGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHkETNKTIVIIEHRLEDVlhRDIDRVILM 217
Cdd:NF040873 121 SGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEH-ARGATVVVVTHDLELV--RRADPCVLL 191
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
317-527 |
5.94e-24 |
|
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: 103.26 E-value: 5.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 317 DVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--SELSIFERSQK--VGVVMQNPnHMISHHMIF 392
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPHRrrIGYVFQEA-RLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 393 DEVAFGLRNRGVAEQEIKekVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSML 472
Cdd:COG4148 96 GNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 473 AFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLL 527
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-242 |
5.94e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.81 E-value: 5.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLipHAIKGEVTGSLEINGKNISDFSMHDY 81
Cdd:PRK13657 334 AVEFDDVSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLL--QRVFDPQSGRILIDGTDIRTVTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTdsqfvGL---SIGEDIAFALENqlVSNIDMYplvkSTAKMVDLADMLDRSPH-----------DLSGGQ 147
Cdd:PRK13657 408 RRNIAVVFQDA-----GLfnrSIEDNIRVGRPD--ATDEEMR----AAAERAQAHDFIERKPDgydtvvgergrQLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMT 227
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTV--RNADRILVFDNGRVVESGS 552
|
250 260
....*....|....*....|
gi 515631642 228 PDEILA-----SELLETHGI 242
Cdd:PRK13657 553 FDELVArggrfAALLRAQGM 572
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-522 |
7.02e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 105.66 E-value: 7.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 27 IEKGEKIVIIGPSGSGKSTLGQCLNG-LIPhaikgevtgsleingkNISDFSMHDYTEQV-----GTVLQDtdsQFVGLS 100
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGeLIP----------------NLGDYEEEPSWDEVlkrfrGTELQN---YFKKLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 101 IGEdIAFALENQLVSNIDMY------PLVKST---------AKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK13409 157 NGE-IKVVHKPQYVDLIPKVfkgkvrELLKKVdergkldevVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLHKetNKTIVIIEHRLedvlhrdidrvilmergeIVADMTPDEI-----------LAS 234
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL------------------AVLDYLADNVhiaygepgaygVVS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 235 ELLETH-GIREplYLSALkaakapLTSEdklsNLkaldykRFRP-AVQawFAERPtPVAEKQYQPLLEVHGLTYSYDGEK 312
Cdd:PRK13409 296 KPKGVRvGINE--YLKGY------LPEE----NM------RIRPePIE--FEERP-PRDESERETLVEYPDLTKKLGDFS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 313 naLEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSgssylnGEDLSELSIFERSQ--------KVGVVMQNPNH 384
Cdd:PRK13409 355 --LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDE------GEVDPELKISYKPQyikpdydgTVEDLLRSITD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 385 MISHHMIFDEVAFGLRnrgvaeqeikekVENVLELcglskfrhwPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQD 464
Cdd:PRK13409 427 DLGSSYYKSEIIKPLQ------------LERLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 465 YRNYTSMLAFIQKLNRELGITVVIISHDmhlvleyttrsIVIADskLIANAAMteVFS 522
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEREATALVVDHD-----------IYMID--YISDRLM--VFE 528
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
299-513 |
7.14e-24 |
|
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: 98.54 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVGV 377
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPNhmishhmIFDEVafgLRNrGVAEQeikekvenvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03247 80 LNQRPY-------LFDTT---LRN-NLGRR-------------------------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLNRELgiTVVIISHdmHLV-LEYTTRSIVIADSKLIA 513
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDK--TLIWITH--HLTgIEHMDKILFLENGKIIM 176
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
276-523 |
8.10e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.29 E-value: 8.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 276 RPAVQawFAERPTPVAEkqyQPLLEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSG 354
Cdd:PRK11160 321 KPEVT--FPTTSTAAAD---QVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 355 SSYLNGEDLSELSifERS--QKVGVVMQNPnHMISHhmifdevafGLRN--RGVAEQEIKEKVENVLELCGLSK------ 424
Cdd:PRK11160 396 EILLNGQPIADYS--EAAlrQAISVVSQRV-HLFSA---------TLRDnlLLAAPNASDEALIEVLQQVGLEKlleddk 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 425 -FRHWPIE---ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRelGITVVIISHDMHLvLEYT 500
Cdd:PRK11160 464 gLNAWLGEggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTG-LEQF 540
|
250 260
....*....|....*....|...
gi 515631642 501 TRSIVIADSKLIANAAMTEVFSQ 523
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-225 |
9.92e-24 |
|
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: 99.29 E-value: 9.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEK--------------GEKIVIIGPSGSGKSTLGQCLNGLI-PHAIKGEVTGSLEINGKNISDFSMHDytEQVG 86
Cdd:cd03297 1 MLCVDIEKrlpdftlkidfdlnEEVTGIFGASGAGKSTLLRCIAGLEkPDGGTIVLNGTVLFDSRKKINLPPQQ--RKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 87 TVLQDTdSQFVGLSIGEDIAFALENQlvSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:cd03297 79 LVFQQY-ALFPHLNVRENLAFGLKRK--RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 167 DEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDvLHRDIDRVILMERGEIVAD 225
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSE-AEYLADRIVVMEDGRLQYI 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
315-530 |
1.22e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 99.91 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAdSGSSYLNGEDLSELSIFERSQKVGVVMQN---PNHMISHHMI 391
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQqspPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 392 fdevAFGLRnRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILV-------LEPELLILDEPTAGQD 464
Cdd:COG4138 91 ----ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 465 YRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFsQPSLLERA 530
Cdd:COG4138 166 VAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPENLSEV 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
20-240 |
1.28e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 100.30 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDYTEQVGTVLQDTDSQF-VG 98
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIE-----PTSGEILINGHKLEYGDYKYRCKHIRMIFQDPNTSLnPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 LSIGEdiafALENQLVSNIDMYP-----LVKSTAKMVDL-ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLAS 172
Cdd:COG4167 104 LNIGQ----ILEEPLRLNTDLTAeereeRIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 173 LDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIVADMTPDEILAS-------ELLETH 240
Cdd:COG4167 180 LDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKH--IsDKVLVMHQGEVVEYGKTAEVFANpqhevtkRLIESH 253
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
296-493 |
1.39e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.00 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGS-SYLNGE----DLSELSIFE 370
Cdd:PRK11701 4 QPLLSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvHYRMRDgqlrDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 371 RSQKV----GVVMQNPnhmishhmifdevAFGLRNRGVAEQEIKEKVENVLElcglskfRH----------W--PIE--- 431
Cdd:PRK11701 83 RRRLLrtewGFVHQHP-------------RDGLRMQVSAGGNIGERLMAVGA-------RHygdiratagdWleRVEida 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 432 --------ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDM 493
Cdd:PRK11701 143 ariddlptTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDL 212
|
|
| DUF3744 |
pfam12558 |
ATP-binding cassette cobalt transporter; This domain family is found in bacteria, and is ... |
234-305 |
1.52e-23 |
|
ATP-binding cassette cobalt transporter; This domain family is found in bacteria, and is approximately 70 amino acids in length. The family is found in association with pfam00005. There is a conserved REP sequence motif. There is a single completely conserved residue P that may be functionally important. The proteins in this family are frequently annotated as ABC Cobalt transporters however there is little accompanying literature to confirm this.
Pssm-ID: 432635 [Multi-domain] Cd Length: 72 Bit Score: 94.15 E-value: 1.52e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 234 SELLETHGIREPLYLSALKAAKAPLTSEDKLSNLKALDYKRFRPAVQAWFAERPTPVAEKQYQPLLEVHGLT 305
Cdd:pfam12558 1 SDLLEQNGIREPLYLTALKYAGCDLTKEDHLSNLETLNLSEDKEKLKSWFEKQEEPKKEPEKEPLLEVKNLS 72
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
299-524 |
1.55e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.99 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID-----ADSGSSYLNGEDLSELSIFERSQ 373
Cdd:PRK14247 4 IEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 374 KVGVVMQNPNHmISHHMIFDEVAFGLR-NRGV-AEQEIKEKVENVLElcglsKFRHW---------PIEALSYGQKKRVT 442
Cdd:PRK14247 83 RVQMVFQIPNP-IPNLSIFENVALGLKlNRLVkSKKELQERVRWALE-----KAQLWdevkdrldaPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 443 IASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELgiTVVIISHdmhlvleYTTRSIVIAD-------SKLIANA 515
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTH-------FPQQAARISDyvaflykGQIVEWG 227
|
....*....
gi 515631642 516 AMTEVFSQP 524
Cdd:PRK14247 228 PTREVFTNP 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-238 |
1.85e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.61 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFryESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHD 80
Cdd:PRK09536 2 PMIDVSDLSV--EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-----AGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQDTDsqfvglsigedIAFALENQLVSNIDMYP--------------LVKSTAKMVDLADMLDRSPHDLSGG 146
Cdd:PRK09536 75 ASRRVASVPQDTS-----------LSFEFDVRQVVEMGRTPhrsrfdtwtetdraAVERAMERTGVAQFADRPVTSLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 147 QKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADM 226
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDL-DLAARYCDELVLLADGRVRAAG 221
|
250
....*....|..
gi 515631642 227 TPDEILASELLE 238
Cdd:PRK09536 222 PPADVLTADTLR 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
310-524 |
3.34e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.89 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLS-------ELSIFERSQ------KVG 376
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADKNQlrllrtRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQNPNhMISHHMIFDEVAFG-LRNRGVAEQEIKEKVENVLELCGLSKFRH--WPIEaLSYGQKKRVTIASILVLEPEL 453
Cdd:PRK10619 96 MVFQHFN-LWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQgkYPVH-LSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 454 LILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
17-231 |
3.54e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.45 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISDfsMHDYTEQVGTVLQdTDSQF 96
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDGVDLSH--VPPYQRPINMMFQ-SYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 97 VGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPK 176
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 177 -TGKATIEIIDQLHKeTNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEI 231
Cdd:PRK11607 184 lRDRMQLEVVDILER-VGVTCVMVTHDQEEAMTM-AGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
299-493 |
3.60e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.68 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqKVGVV 378
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA-RIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNHMISHHMIFDEVAFGlRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515631642 459 PTAGQD-------YRNYTSMLAfiqklnreLGITVVIISHDM 493
Cdd:PRK13536 199 PTTGLDpharhliWERLRSLLA--------RGKTILLTTHFM 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
298-511 |
4.31e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.12 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKNALedvSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGV 377
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP--VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNpNHMISHHMIFDEVAFGLrNRGV---AEQeiKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK10771 76 LFQE-NNLFSHLTVAQNIGLGL-NPGLklnAAQ--REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 455 ILDEPTAGQD--YRNytSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK10771 152 LLDEPFSALDpaLRQ--EMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-235 |
4.79e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 103.26 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVtgslEINGKNISDFSMHDY 81
Cdd:PRK10790 340 RIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT-EGEI----RLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQD----TDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKStakMVD-LADMLDRSPHDLSGGQKQRVSLAGI 156
Cdd:PRK10790 414 RQGVAMVQQDpvvlADTFLANVTLGRDISEEQVWQALETVQLAELARS---LPDgLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETnkTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTPDEILASE 235
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIV--EADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
296-494 |
5.08e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.57 E-value: 5.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKST-------ITKLIMGV-IdadSGSSYLNGEDlsels 367
Cdd:COG1117 9 EPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTllrclnrMNDLIPGArV---EGEILLDGED----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 368 IFERS-------QKVGVVMQNPN--HMiShhmIFDEVAFGLRNRGVA-EQEIKEKVENVLELCGLskfrhW--------- 428
Cdd:COG1117 80 IYDPDvdvvelrRRVGMVFQKPNpfPK-S---IYDNVAYGLRLHGIKsKSELDEIVEESLRKAAL-----Wdevkdrlkk 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 429 PIEALSYGQKKRVTIASILVLEPELLILDEPtagqdyrnyTSML-----AFIQKLNRELG--ITVVIISHDMH 494
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEP---------TSALdpistAKIEELILELKkdYTIVIVTHNMQ 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
314-525 |
5.67e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.26 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE----RSQKVGVVMQNpNHMISHH 389
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQS-FALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 390 MIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYT 469
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 470 SMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-240 |
5.69e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.26 E-value: 5.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESL-DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPhaikgeVTGSLEINGKNISDFSMHD 80
Cdd:TIGR00958 479 IEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQP------TGGQVLLDGVPLVQYDHHY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQdtDSQFVGLSIGEDIAFALenqlvsniDMYPL--VKSTAKMVDLADMLDRSPHD-----------LSGGQ 147
Cdd:TIGR00958 553 LHRQVALVGQ--EPVLFSGSVRENIAYGL--------TDTPDeeIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQ 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKAtieiIDQLHKETNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMT 227
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAECEQL----LQESRSRASRTVLLIAHRLSTV--ERADQILVLKKGSVVEMGT 696
|
250
....*....|...
gi 515631642 228 PDEILASELLETH 240
Cdd:TIGR00958 697 HKQLMEDQGCYKH 709
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-234 |
5.71e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.50 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISDFSMHDyteqvGTVLQDTDSQFVGL 99
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSIVVNGQTINLVRDKD-----GQLKVADKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAF----------ALENQLVSNIDMYPLVKSTA-----KMVDLADMLDRS----PHDLSGGQKQRVSLAGILVDD 160
Cdd:PRK10619 91 RTRLTMVFqhfnlwshmtVLENVMEAPIQVLGLSKQEAreravKYLAKVGIDERAqgkyPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 161 VDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVS-SHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
299-524 |
6.28e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE--DLS----ELSIFERS 372
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSktpsDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 QKVGVVMQNPN---HM-ISHHMIfdEVAfgLRNRGVAEQEIKEKVENVLELCGLSKFRH-WPIEaLSYGQKKRVTIASIL 447
Cdd:PRK11124 82 RNVGMVFQQYNlwpHLtVQQNLI--EAP--CRVLGLSKDQALARAEKLLERLRLKPYADrFPLH-LSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 448 VLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAmTEVFSQP 524
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQP 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-238 |
6.32e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.83 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlIPhaiKGEVT-GSLEINGKNISDFSMHD-----------YTE 83
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HP---KYEVTsGSILLDGEDILELSPDEraragiflafqYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 84 QVGTVlqdTDSQFVGLSIGediafALENQLVSNIDMYPLVKSTAKMVDLA-DMLDRSPHD-LSGGQKQRVSLAGILVDDV 161
Cdd:COG0396 88 EIPGV---SVSNFLRTALN-----ARRGEELSAREFLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEH--RLEDVLHrdIDRVILMERGEIVAdmTPDEILASELLE 238
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHyqRILDYIK--PDFVHVLVDGRIVK--SGGKELALELEE 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
299-496 |
6.98e-23 |
|
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: 97.56 E-value: 6.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQnpNHMISHHMIFDEVAFGlrNRGVAeqeiKEKVENVLELCGLSKF-RHWPI----------EALSYGQKKRVTIASI 446
Cdd:cd03252 81 VLQ--ENVLFNRSIRDNIALA--DPGMS----MERVIEAAKLAGAHDFiSELPEgydtivgeqgAGLSGGQRQRIAIARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515631642 447 LVLEPELLILDEPTAGQDYRnytSMLAFIQKLNREL-GITVVIISHDMHLV 496
Cdd:cd03252 153 LIHNPRILIFDEATSALDYE---SEHAIMRNMHDICaGRTVIIIAHRLSTV 200
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
16-261 |
1.02e-22 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 98.62 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAIKGEVTGsleingknisdfsmHDYTEQVGTVLQDTDS 94
Cdd:TIGR01188 5 DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLrPTSGTARVAG--------------YDVVREPRKVRRSIGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 QFVGLSIGEDIAfALENqLVSNIDMYPLVKSTA--------KMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:TIGR01188 71 VPQYASVDEDLT-GREN-LEMMGRLYGLPKDEAeeraeellELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 167 DEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEiLASELLETHGIREPL 246
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEA-DKLCDRIAIIDHGRIIAEGTPEE-LKRRLGKDTLESRPR 225
|
250
....*....|....*
gi 515631642 247 YLSALKAAKAPLTSE 261
Cdd:TIGR01188 226 DIQSLKVEVSMLIAE 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
287-511 |
1.67e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.06 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 287 PTPVAEKQYQPLLeVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGvIDADSGSSYLNGE-DLSE 365
Cdd:PRK11247 2 MNTARLNQGTPLL-LNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTaPLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 366 LSIFERsqkvgvVMQNPNHMISHHMIFDEVAFGLRNrgvaeqEIKEKVENVLELCGLS-KFRHWPiEALSYGQKKRVTIA 444
Cdd:PRK11247 79 AREDTR------LMFQDARLLPWKKVIDNVGLGLKG------QWRDAALQALAAVGLAdRANEWP-AALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 445 SILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
304-496 |
2.04e-22 |
|
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: 96.15 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 304 LTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPn 383
Cdd:cd03253 6 VTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 384 hMISHHMIFDEVAFGlrNRGVAEQEIKE--KVENVlelcglskfrHWPIEA---------------LSYGQKKRVTIASI 446
Cdd:cd03253 85 -VLFNDTIGYNIRYG--RPDATDEEVIEaaKAAQI----------HDKIMRfpdgydtivgerglkLSGGEKQRVAIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515631642 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRelGITVVIISHDMHLV 496
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI 199
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
296-506 |
2.37e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 98.24 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKN------------ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL 363
Cdd:PRK15079 6 KVLLEVADLKVHFDIKDGkqwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 364 SELSIFERSQK---VGVVMQNPNHMISHHM-IFDEVAFGLRNR--GVAEQEIKEKVENVLELCGL--SKFRHWPIEaLSY 435
Cdd:PRK15079 86 LGMKDDEWRAVrsdIQMIFQDPLASLNPRMtIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlpNLINRYPHE-FSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 436 GQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVI 506
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
315-493 |
2.92e-22 |
|
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: 95.61 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSqkvgVVMQNPNhMISHHMIFDE 394
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRM----VVFQNYS-LLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 395 VAFGLR--NRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSML 472
Cdd:TIGR01184 75 IALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180
....*....|....*....|.
gi 515631642 473 AFIQKLNRELGITVVIISHDM 493
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDV 175
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
296-512 |
7.91e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 99.41 E-value: 7.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPL----LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFER 371
Cdd:PRK10790 334 RPLqsgrIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 372 SQKVGVVMQNPnhMISHHMIFDEVAFGlrnRGVAEqeikEKVENVLELCGLSKF-RHWP--IEA--------LSYGQKKR 440
Cdd:PRK10790 414 RQGVAMVQQDP--VVLADTFLANVTLG---RDISE----EQVWQALETVQLAELaRSLPdgLYTplgeqgnnLSVGQKQL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 441 VTIASILVLEPELLILDEPTAGQDYRNYTSmlafIQKLNREL--GITVVIISHDMhlvleyttRSIVIADSKLI 512
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQA----IQQALAAVreHTTLVVIAHRL--------STIVEADTILV 546
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
307-498 |
8.16e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.07 E-value: 8.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 307 SYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGED----LSELSIFERSQKVGVVmqnp 382
Cdd:NF040873 1 GYGG-RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayVPQRSEVPDSLPLTVR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 383 nhmishhmifDEVAFGL-RNRGVAEQ---EIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:NF040873 76 ----------DLVAMGRwARRGLWRRltrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515631642 459 PTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLE 498
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
300-491 |
9.92e-22 |
|
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: 94.14 E-value: 9.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 300 EVHGLTYSYDGEKN--ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03249 2 EFKNVSFRYPSRPDvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnhMISHHMIFDEVAFGLRNRGVAEqeikekVENVLELCGLSKFrhwpIEA---------------LSYGQKKRVT 442
Cdd:cd03249 82 VSQEP--VLFDGTIAENIRYGKPDATDEE------VEEAAKKANIHDF----IMSlpdgydtlvgergsqLSGGQKQRIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515631642 443 IASILVLEPELLILDEPTAGQDYRnytSMLAFIQKLNR-ELGITVVIISH 491
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAE---SEKLVQEALDRaMKGRTTIVIAH 196
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-235 |
9.98e-22 |
|
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: 94.28 E-value: 9.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQ-VGTVLQDTDSqFVG 98
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR-----SGSIRFDGEDITGLPPHRIARLgIGYVPEGRRI-FPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 LSIGE-------------DIAFALENQLvsniDMYPlvkstakmvDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:COG0410 93 LTVEEnlllgayarrdraEVRADLERVY----ELFP---------RLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEILASE 235
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFAL--EIaDRAYVLERGRIVLEGTAAELLADP 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
293-492 |
1.08e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.01 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 293 KQYQPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS 372
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 QKVGVVMQNPnhMISHHMIFDEVAF--GLRNRGVAEQEIKEKVENV-LELCGLSKfrhwPIEALSYGQKKRVTIASILVL 449
Cdd:PRK10247 81 QQVSYCAQTP--TLFGDTVYDNLIFpwQIRNQQPDPAIFLDDLERFaLPDTILTK----NIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515631642 450 EPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHD 492
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
297-514 |
1.41e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKlIMGVID-ADSGSSYLNGEDLSELSIFE-- 370
Cdd:PRK10535 3 ALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDkPTSGTYRVAGQDVATLDADAla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 371 --RSQKVGVVMQNpNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:PRK10535 82 qlRREHFGFIFQR-YHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHlVLEYTTRSIVIADSKLIAN 514
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRN 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-491 |
1.72e-21 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 97.78 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTG--------SLEINGKNI 73
Cdd:PRK10938 3 SLQISQGTFRLS--DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELP-LLSGERQSqfshitrlSFEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 74 SDFSMHDYTEQVGTVLQDTdsqfvGLSIGEDIAFALENQlvsnidmyPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSL 153
Cdd:PRK10938 80 SDEWQRNNTDMLSPGEDDT-----GRTTAEIIQDEVKDP--------ARCEQLAQQFGITALLDRRFKYLSTGETRKTLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 154 AGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVlhRD-IDRVILMERGEIVADMTPDEIL 232
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEI--PDfVQFAGVLADCTLAETGEREEIL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 233 ASELLETHGIREPLYLSALKAAKAPLTsedklsnlkaldykrfrpavqawfaeRPTPVAEkqyQPLLEVHGLTYSYdGEK 312
Cdd:PRK10938 224 QQALVAQLAHSEQLEGVQLPEPDEPSA--------------------------RHALPAN---EPRIVLNNGVVSY-NDR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 313 NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGvidaDSGSSYLNgeDL--------SELSIFERSQKVGVVMQnpnh 384
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQGYSN--DLtlfgrrrgSGETIWDIKKHIGYVSS---- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 385 miSHHMIFdEVAFGLRN-------------RGVAEQEiKEKVENVLELCGLSK-FRHWPIEALSYGQKKRVTIASILVLE 450
Cdd:PRK10938 344 --SLHLDY-RVSTSVRNvilsgffdsigiyQAVSDRQ-QKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKH 419
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 515631642 451 PELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISH 491
Cdd:PRK10938 420 PTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-232 |
2.17e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDYTE----QVGTVLQdTDSQ 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQ-SFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 176 KTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEIL 232
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-231 |
2.35e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaikGEVT-GSLEINGKNIS-------DFSMhdyteqvgtVL 89
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL------ERITsGEIWIGGRVVNelepadrDIAM---------VF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 90 QDtdsqfVGL----SIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK11650 83 QN-----YALyphmSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 166 FDEPLASLDPKTGKAT-IEiIDQLHKETNKTIVIIEH-RLEDV-LhrdIDRVILMERGEIVADMTPDEI 231
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMrLE-IQRLHRRLKTTSLYVTHdQVEAMtL---ADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-223 |
2.35e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.44 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEINGKNISDFSMHDYTEQVGTVLQdTDSQFVGL 99
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQ-IPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAFALE-NQLV-SNIDMYPLVKSTAKMVDL----ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:PRK14247 98 SIFENVALGLKlNRLVkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515631642 174 DPKTGKATIEIIDQLHKETnkTIVIIEHRLEDVLhRDIDRVILMERGEIV 223
Cdd:PRK14247 178 DPENTAKIESLFLELKKDM--TIVLVTHFPQQAA-RISDYVAFLYKGQIV 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
296-508 |
2.74e-21 |
|
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: 92.88 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSY-----DGEK-NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE----DLSE 365
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 366 LSIFE----RSQKVGVVMQnpnhmishhmiF----------DEVAFGLRNRGVAEQEIKEKVENVLELCGLSKfRHWPIE 431
Cdd:COG4778 82 ASPREilalRRRTIGYVSQ-----------FlrviprvsalDVVAEPLLERGVDREEARARARELLARLNLPE-RLWDLP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 432 AL--SYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIAD 508
Cdd:COG4778 150 PAtfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-238 |
2.88e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 93.07 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 27 IEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaiKGEVTgsleINGKNISDFSMHDYTEQVGTVLQDTDS-------QFVGL 99
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQ----FAGQPLEAWSAAELARHRAYLSQQQTPpfampvfQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAFALENQLVSNIdmyplvkstAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVD-------DVDILLFDEPLAS 172
Cdd:PRK03695 93 HQPDKTRTEAVASALNEV---------AEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 173 LDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILASELLE 238
Cdd:PRK03695 164 LDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRH-ADRVWLLKQGKLLASGRRDEVLTPENLA 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-225 |
2.91e-21 |
|
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: 90.57 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikgeVTGSLEINGKNISdfsmhdyteqvgtVLQDTDSQFVGL 99
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKP-----DSGEILVDGKEVS-------------FASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SigediafalenqlvsnidmyplvkstakMVdladmldrspHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGK 179
Cdd:cd03216 78 A----------------------------MV----------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515631642 180 ATIEIIDQLhKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVAD 225
Cdd:cd03216 120 RLFKVIRRL-RAQGVAVIFISHRLDEV--FEIaDRVTVLRDGRVVGT 163
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-225 |
3.54e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; 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 to 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 the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 92.78 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 10 FRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTGSLEINGKNISDFsmhdyTEQVGTVL 89
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL-QPTSGEVRVAGLVPWKRRKKF-----LRRIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 90 QDTDSQFVGLSIGEDIAFalenqlvsNIDMYPLVKSTAK--------MVDLADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:cd03267 101 GQKTQLWWDLPVIDSFYL--------LAAIYDLPPARFKkrldelseLLDLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVAD 225
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDI-EALARRVLVIDKGRLLYD 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-225 |
3.73e-21 |
|
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: 91.87 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESldKPTLKNINLRIEKGeKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDfSMHDYT 82
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP-----PSSGTIRIDGQDVLK-QPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQD--TDSQFVGLSIGEDIAFALEnqlVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDD 160
Cdd:cd03264 72 RRIGYLPQEfgVYPNFTVREFLDYIAWLKG---IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 161 VDILLFDEPLASLDPKTGKATIEIIDQLhkETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVAD 225
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVE--SLcNQVAVLNKGKLVFE 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-206 |
3.99e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.18 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLipHAIKGEV--TGSLEINGKNISD--FSM 78
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM--NELESEVrvEGRVEFFNQNIYErrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 79 HDYTEQVGTVLQDTDsqFVGLSIGEDIAFALenQLVS---NIDMYPLVKSTAKMVDLAD----MLDRSPHDLSGGQKQRV 151
Cdd:PRK14258 84 NRLRRQVSMVHPKPN--LFPMSVYDNVAYGV--KIVGwrpKLEIDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDV 206
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQV 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
299-464 |
3.99e-21 |
|
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: 91.27 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSyDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVgvv 378
Cdd:TIGR01189 1 LAARNLACS-RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 mqnpnHMISHhmifdevAFGLRNR-GVAE---------QEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:TIGR01189 76 -----LYLGH-------LPGLKPElSALEnlhfwaaihGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWL 143
|
170
....*....|....*.
gi 515631642 449 LEPELLILDEPTAGQD 464
Cdd:TIGR01189 144 SRRPLWILDEPTTALD 159
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-201 |
4.03e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.98 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEINGKNI--SDFSMHDYTEQVGTVLQdTDSQFV 97
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIysPDVDPIEVRREVGMVFQ-YPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 98 GLSIGEDIAFALE-NQLVSNIDMYP-----LVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:PRK14267 99 HLTIYDNVAIGVKlNGLVKSKKELDervewALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190
....*....|....*....|....*....|
gi 515631642 172 SLDPKTGKATIEIIDQLHKETnkTIVIIEH 201
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
310-526 |
4.39e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 92.69 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAdSGSSYLNGEDLSELSIFERSQKVGVVMQNPN------ 383
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTppfamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 384 --HMISHHmifdevafglRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASIL-----VLEPE--LL 454
Cdd:PRK03695 86 vfQYLTLH----------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLNReLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSL 526
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
299-491 |
4.53e-21 |
|
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: 91.07 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYD-----GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID--ADSGSSYLNGEDLSELSIfer 371
Cdd:cd03213 4 LSFRNLTVTVKsspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 372 SQKVGVVMQnpnhmishhmifDEVAFGlrnrgvaEQEIKEKVENVLELCGLSKfrhwpiealsyGQKKRVTIASILVLEP 451
Cdd:cd03213 81 RKIIGYVPQ------------DDILHP-------TLTVRETLMFAAKLRGLSG-----------GERKRVSIALELVSNP 130
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515631642 452 ELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISH 491
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-242 |
5.74e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.42 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIP-HAIKGEVTGSLEINGKNISDFSMHDYTEQVGTVLQDTDS 94
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 qFVGLSIGEDIAFALENQLVSNI-DMYPLVKSTAKMVDL----ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEP 169
Cdd:PRK14246 102 -FPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 170 LASLDPKTGKATIEIIDQLHKETnkTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS---ELLETHGI 242
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVA-RVADYVAFLYNGELVEWGSSNEIFTSpknELTEKYVI 253
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
314-528 |
6.87e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.54 E-value: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 314 ALEDVSFKI-GK------------GEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQ 380
Cdd:PRK10575 13 ALRNVSFRVpGRtllhplsltfpaGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 381 N-PNhmiSHHMIFDE-VAFG-------LRNRGVAEqeiKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:PRK10575 93 QlPA---AEGMTVRElVAIGrypwhgaLGRFGAAD---REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFsQPSLLE 528
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM-RGETLE 242
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
298-524 |
1.10e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.27 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEK---NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID------ADSGSsyLNGEDLSELSI 368
Cdd:PRK11022 3 LLNVDKLSVHFGDESapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvmAEKLE--FNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 369 FERSQKVG----VVMQNPnhMISHHMIFdEVAFGLR-----NRGVAEQEIKEKVENVLELCGL----SKFRHWPiEALSY 435
Cdd:PRK11022 81 KERRNLVGaevaMIFQDP--MTSLNPCY-TVGFQIMeaikvHQGGNKKTRRQRAIDLLNQVGIpdpaSRLDVYP-HQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 436 GQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANA 515
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
....*....
gi 515631642 516 AMTEVFSQP 524
Cdd:PRK11022 237 KAHDIFRAP 245
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
242-494 |
1.14e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 95.42 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 242 IREPLyLSALKAAKAPLTSE---DKLSNLKALDYKrfrpavqawfAERPTPVAEKQYQPLlEVHGLTYSYDGEKNALEDV 318
Cdd:PRK10522 275 LRTPL-LSAVGALPTLLSAQvafNKLNKLALAPYK----------AEFPRPQAFPDWQTL-ELRNVTFAYQDNGFSVGPI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 319 SFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMqnpnhmiSHHMIFDEVafg 398
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVF-------TDFHLFDQL--- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 399 LRNRGvaEQEIKEKVENVLELCGLS---KFRHWPIE--ALSYGQKKRVTIASILVLEPELLILDEPTAGQD--YRNYtsm 471
Cdd:PRK10522 413 LGPEG--KPANPALVEKWLERLKMAhklELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDphFRRE--- 487
|
250 260
....*....|....*....|....*.
gi 515631642 472 laFIQKL---NRELGITVVIISHDMH 494
Cdd:PRK10522 488 --FYQVLlplLQEMGKTIFAISHDDH 511
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-227 |
1.16e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.77 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQC---LNGLIPHAikgEVTGSLEINGKNI--SDFSMHDYTEQVGTVLQDTDS 94
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGF---RVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 qfVGLSIGEDIAF-ALENQLVSNIDmyPLVKSTAKMVDL----ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEP 169
Cdd:PRK14243 103 --FPKSIYDNIAYgARINGYKGDMD--ELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 170 LASLDPKTGKATIEIIDQLHKETnkTIVIIEHRledvlhrdidrvilMERGEIVADMT 227
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQY--TIIIVTHN--------------MQQAARVSDMT 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-236 |
1.67e-20 |
|
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: 90.68 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVtgslEINGKNISDFSMHdYTEQVG-TVLQDTDSQ 95
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK-PDSGKI----LLDGQDITKLPMH-KRARLGiGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:cd03218 87 FRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 176 KTGKATIEIIDQLhKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASEL 236
Cdd:cd03218 167 IAVQDIQKIIKIL-KDRGIGVLITDHNVRETL-SITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-223 |
1.83e-20 |
|
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: 90.41 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaiKGEVTGSLEINGKNISdfsMHDYTEQVGTVLQDtDSQFVGL 99
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG--GGTTSGQILFNGQPRK---PDQFQKCVAYVRQD-DILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAFALENQLvsnidMYPLVKSTAKMVDlADMLDRSPHD----------LSGGQKQRVSLAGILVDDVDILLFDEP 169
Cdd:cd03234 97 TVRETLTYTAILRL-----PRKSSDAIRKKRV-EDVLLRDLALtriggnlvkgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515631642 170 LASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHRDIDRVILMERGEIV 223
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
299-512 |
1.84e-20 |
|
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: 90.25 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnhmishHMIFDEVAFGLRNRGVAEQeikEKVENVLELCGLSKFrhwpIEA---------------LSYGQKKRVT 442
Cdd:cd03244 83 IPQDP------VLFSGTIRSNLDPFGEYSD---EELWQALERVGLKEF----VESlpggldtvveeggenLSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 443 IASILVLEPELLILDEPTAGQDYRnyTSMLafIQKLNREL--GITVVIISHDMHLVLEYtTRSIVIADSKLI 512
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPE--TDAL--IQKTIREAfkDCTVLTIAHRLDTIIDS-DRILVLDKGRVV 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
299-510 |
2.83e-20 |
|
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: 87.12 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSsylngedlselsifersqkvgvV 378
Cdd:cd03221 1 IELENLSKTYGG-KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI----------------------V 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNHMISHhmifdevafglrnrgvaeqeikekvenvlelcglskfrhwpIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:cd03221 58 TWGSTVKIGY-----------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515631642 459 PTAGQDYRNYTSMLAFIQKLNRelgiTVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-222 |
2.86e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 89.84 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESL-DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTgsleINGKNISDFSMHDY 81
Cdd:cd03248 12 VKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-GGQVL----LDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQdtDSQFVGLSIGEDIAFALenQLVSnidmYPLVKSTAKMVDLADMLDRSPHD-----------LSGGQKQR 150
Cdd:cd03248 87 HSKVSLVGQ--EPVLFARSLQDNIAYGL--QSCS----FECVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPKTGkatiEIIDQLHKE--TNKTIVIIEHRLEDVLHrdIDRVILMERGEI 222
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESE----QQVQQALYDwpERRTVLVIAHRLSTVER--ADQILVLDGGRI 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-231 |
3.58e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.05 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDFSMHDYTEQvGTV--LQDTdSQFVG 98
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTG------GTILLRGQHIEGLPGHQIARM-GVVrtFQHV-RLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 LSIGEDIAFALENQLVSNIdMYPLVKSTA----------------KMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK11300 95 MTVIENLLVAQHQQLKTGL-FSGLLKTPAfrraesealdraatwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEI 231
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVM--GIsDRIYVVNQGTPLANGTPEEI 241
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-220 |
3.78e-20 |
|
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: 89.42 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaikgevtgsleingknisdfsmhDYTEQVGTVLQDTDSQFV 97
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG---------------------------NYLPDSGSILVRHDGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 98 glsigeDIAFALENQL--------------------VSNID--MYPLV-----KSTAKmVDLADMLDR----------SP 140
Cdd:COG4778 78 ------DLAQASPREIlalrrrtigyvsqflrviprVSALDvvAEPLLergvdREEAR-ARARELLARlnlperlwdlPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 141 HDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRlEDVLHRDIDRVILMERG 220
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHD-EEVREAVADRVVDVTPF 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
310-500 |
4.21e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.79 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSsylngedlselsiFERSQK--VGVVMQNPNhmIS 387
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------------IKRNGKlrIGYVPQKLY--LD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 388 HHMIFDEVAFGLRNRGVAEQEIKEKVENVlelcGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRN 467
Cdd:PRK09544 80 TTLPLTVNRFLRLRPGTKKEDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190
....*....|....*....|....*....|...
gi 515631642 468 YTSMLAFIQKLNRELGITVVIISHDMHLVLEYT 500
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDLHLVMAKT 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-243 |
5.69e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.05 E-value: 5.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 21 KNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDYTEQVGTVLQDTDSQfvgls 100
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT-----PAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 101 igEDIAFaleNQLVSNiDMYP--------------LVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PRK10253 94 --GDITV---QELVAR-GRYPhqplftrwrkedeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 167 DEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASELLE-THGIR 243
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAC-RYASHLIALREGKIVAQGAPKEIVTAELIErIYGLR 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-492 |
7.00e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 93.48 E-value: 7.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI----------------------PHAIKGEV-----TGSLEI 68
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVllddgriiyeqdlivarlqqdpPRNVEGTVydfvaEGIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 69 NGK-----NISDFSMHDYTEQVGTVLQdtdsqfvglsigediafalenQLVSNIDMYPLVKSTAKMVDLADMLDRSPH-- 141
Cdd:PRK11147 95 AEYlkryhDISHLVETDPSEKNLNELA---------------------KLQEQLDHHNLWQLENRINEVLAQLGLDPDaa 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 142 --DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDpktgKATIEIIDQLHKETNKTIVIIEHRlEDVLHRDIDRVILMER 219
Cdd:PRK11147 154 lsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHD-RSFIRNMATRIVDLDR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 220 GEIVAdmTP---DEILASEllethgiREPLYLSALKAA-----------------KAPLT-SEDKLSNLKALDYKRF-RP 277
Cdd:PRK11147 229 GKLVS--YPgnyDQYLLEK-------EEALRVEELQNAefdrklaqeevwirqgiKARRTrNEGRVRALKALRRERSeRR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 278 AVQAwFAERPTPVAEKQYQPLLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSY 357
Cdd:PRK11147 300 EVMG-TAKMQVEEASRSGKIVFEMENVNYQIDG-KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 358 LnGEDLsELSIF---------ERSqkvgvVMQNpnhmishhmifdevafglrnrgVAE--QEIkekvenvlELCGLSkfR 426
Cdd:PRK11147 378 C-GTKL-EVAYFdqhraeldpEKT-----VMDN----------------------LAEgkQEV--------MVNGRP--R 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 427 H----------------WPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDyrnyTSMLAFIQKLNRELGITVVIIS 490
Cdd:PRK11147 419 HvlgylqdflfhpkramTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVS 494
|
..
gi 515631642 491 HD 492
Cdd:PRK11147 495 HD 496
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-233 |
7.73e-20 |
|
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: 92.94 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLK---NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTGSLeinGKNISDFSmh 79
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT-SGEVNVRV---GDEWVDMT-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 dyteQVGTVLQDTDSQFVGL-----------SIGEDIAFALENQLVSNIDMYPLVkSTAKMVDLAD-----MLDRSPHDL 143
Cdd:TIGR03269 354 ----KPGPDGRGRAKRYIGIlhqeydlyphrTVLDNLTEAIGLELPDELARMKAV-ITLKMVGFDEekaeeILDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 144 SGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhrDI-DRVILMERGEI 222
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVL--DVcDRAALMRDGKI 506
|
250
....*....|.
gi 515631642 223 VADMTPDEILA 233
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-249 |
8.02e-20 |
|
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: 88.35 E-value: 8.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaIKGevtGSLEINGKNISDFSMHDYTEQ-VGTVLQDTDSqFVG 98
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLP--VKS---GSIRLDGEDITKLPPHERARAgIAYVPQGREI-FPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 LSIGEDIAFALENQLVSN-------IDMYPLVKstakmvdlaDMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:TIGR03410 90 LTVEENLLTGLAALPRRSrkipdeiYELFPVLK---------EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 172 SLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEilaselLETHGIREplYLS 249
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELA-DRYYVMERGRVVASGAGDE------LDEDKVRR--YLA 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-231 |
8.61e-20 |
|
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: 88.20 E-value: 8.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMhDYTEQVGTVLQDtdsqfvgl 99
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK-----PTSGRATVAGHDVVREPR-EVRRRIGIVFQD-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAFALENQL-------VSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLAS 172
Cdd:cd03265 82 LSVDDELTGWENLYiharlygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 173 LDPKTGKATIEIIDQLHKETNKTIVIIEHRLE--DVLhrdIDRVILMERGEIVADMTPDEI 231
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEeaEQL---CDRVAIIDHGRIIAEGTPEEL 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
287-525 |
1.22e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 90.17 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 287 PTPVAEKQYQPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD---SGSSYLNG 360
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFstpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 361 EDLSELSIFE----RSQKVGVVMQNPNHMISHHM-IFDEVAFGLR-NRGVAEQEIKEKVENVLELCGL----SKFRHWPI 430
Cdd:PRK09473 81 REILNLPEKElnklRAEQISMIFQDPMTSLNPYMrVGEQLMEVLMlHKGMSKAEAFEESVRMLDAVKMpearKRMKMYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 431 EaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:PRK09473 161 E-FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
250
....*....|....*
gi 515631642 511 LIANAAMTEVFSQPS 525
Cdd:PRK09473 240 TMEYGNARDVFYQPS 254
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
297-524 |
1.34e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.96 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYD---GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID------ADSGSsyLNGEDLSELS 367
Cdd:COG4170 2 PLLDIRNLTIEIDtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtADRFR--WNGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 368 IFERSQKVG----VVMQNPN-HMISHHMIFD---EVAFGLRNRGVAEQEIKEKVENVLELcgLSK---------FRHWPI 430
Cdd:COG4170 80 PRERRKIIGreiaMIFQEPSsCLDPSAKIGDqliEAIPSWTFKGKWWQRFKWRKKRAIEL--LHRvgikdhkdiMNSYPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 431 EaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:COG4170 158 E-LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQ 236
|
250
....*....|....
gi 515631642 511 LIANAAMTEVFSQP 524
Cdd:COG4170 237 TVESGPTEQILKSP 250
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
296-530 |
1.42e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.79 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSifeRSQKV 375
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMISHHMIFDEVAF-------GLRNRgvAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:PRK15056 81 AYVPQSEEVDWSFPVLVEDVVMmgryghmGWLRR--AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAamTEVFSQPSLLE 528
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGP--TETTFTAENLE 235
|
..
gi 515631642 529 RA 530
Cdd:PRK15056 236 LA 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-207 |
1.85e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 87.32 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 6 SNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaiKGEVTGSLEINGKNISdfsmhdyteQV 85
Cdd:COG2401 32 EAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---GTPVAGCVDVPDNQFG---------RE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 86 GTVLQDtdsqfvgLSIGEDIAFALEnqlvsnidmyplVKSTAKMVDLADMLdRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:COG2401 100 ASLIDA-------IGRKGDFKDAVE------------LLNAVGLSDAVLWL-RRFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRlEDVL 207
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHH-YDVI 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-242 |
2.32e-19 |
|
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: 92.70 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRY-ESLDKpTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNgLIPHAIKGEVTgsleINGKNISDFSMHDY 81
Cdd:TIGR00957 1285 VEFRNYCLRYrEDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF-RINESAEGEII----IDGLNIAKIGLHDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQD----TDSQFVGLS-----IGEDIAFALEnqlVSNIDMYplvkstakMVDLADMLD----RSPHDLSGGQK 148
Cdd:TIGR00957 1359 RFKITIIPQDpvlfSGSLRMNLDpfsqySDEEVWWALE---LAHLKTF--------VSALPDKLDhecaEGGENLSVGQR 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 149 QRVSLAGILVDDVDILLFDEPLASLDPKTgkatieiiDQLHKETNK------TIVIIEHRLEDVLhrDIDRVILMERGEI 222
Cdd:TIGR00957 1428 QLVCLARALLRKTKILVLDEATAAVDLET--------DNLIQSTIRtqfedcTVLTIAHRLNTIM--DYTRVIVLDKGEV 1497
|
250 260
....*....|....*....|
gi 515631642 223 VADMTPdeilaSELLETHGI 242
Cdd:TIGR00957 1498 AEFGAP-----SNLLQQRGI 1512
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-223 |
2.63e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.02 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISDFS---MHDYTEQVGTVLQDTdsqFV 97
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLE------EPTsGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 98 GL----SIGEDIAFALENQ-LVSNIDMYPLVKSTAKMVDL-ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:COG4608 107 SLnprmTVGDIIAEPLRIHgLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 172 SLDpktgkATIE--II---DQLHKETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIV 223
Cdd:COG4608 187 ALD-----VSIQaqVLnllEDLQDELGLTYLFISHDLSVVRH--IsDRVAVMYLGKIV 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
16-224 |
2.69e-19 |
|
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: 86.57 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISDFSMHDY-----------TEQ 84
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL-----PDSGEVLFDGKPLDIAARNRIgylpeerglypKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 85 VGTVLQDTdSQFVGLSIgEDIAfalenqlvSNIDMYplvkstAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:cd03269 87 VIDQLVYL-AQLKGLKK-EEAR--------RRIDEW------LERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVA 224
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELV-EELCDRVLLLNKGRAVL 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-220 |
2.76e-19 |
|
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: 87.14 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFS---MhdyteqvgTVLQDTdSQF 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPT-----SGGVILEGKQITEPGpdrM--------VVFQNY-SLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 97 VGLSIGEDIAFALENQL--VSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLD 174
Cdd:TIGR01184 67 PWLTVRENIALAVDRVLpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515631642 175 PKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERG 220
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLS-DRVVMLTNG 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
11-225 |
2.79e-19 |
|
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: 86.65 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 11 RYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDfSMHDYTEQVGt 87
Cdd:cd03266 10 RFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDA------GFATVDGFDVVK-EPAEARRRLG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 88 VLQDTDSQFVGLSIGEDIA-FAlenqlvsniDMYPL--------VKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILV 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEyFA---------GLYGLkgdeltarLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVAD 225
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEV-ERLCDRVVVLHRGRVVYE 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
298-495 |
2.90e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.76 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSY-DGEK--NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE---- 370
Cdd:PRK10584 6 IVEVHHLKKSVgQGEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 371 RSQKVGVVMQNpNHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSK-FRHWPIEaLSYGQKKRVTIASILVL 449
Cdd:PRK10584 86 RAKHVGFVFQS-FMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKrLDHLPAQ-LSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515631642 450 EPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHL 495
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-231 |
3.03e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.90 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTE--QVGTVLQDTD 93
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-----HGEILFDGENIPAMSRSRLYTvrKRMSMLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 94 SQFVGLSIGEDIAFALE--NQLVSnidmyPLVKSTAKM----VDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:PRK11831 94 ALFTDMNVFDNVAYPLRehTQLPA-----PLLHSTVMMkleaVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 168 EPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEI 231
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVL-SIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
297-496 |
3.16e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.78 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS---- 372
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRvnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 ---QKVGVVMQNPNhmISHHMIFDEVAFGLRNRGVAEQ-EIKEKVENVLELCGL-----SKFRHWPIEaLSYGQKKRVTI 443
Cdd:PRK14258 85 rlrRQVSMVHPKPN--LFPMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeikHKIHKSALD-LSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515631642 444 ASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLV 496
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQV 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
299-524 |
3.18e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.50 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLI------------MGVIDADSGSSYLNGEDLsel 366
Cdd:PRK11264 4 IEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 367 sIFERSQKVGVVMQNPNhMISHHMIFDEVAFG-LRNRGVAEQEIKEKVENVLELCGLS-KFRHWPiEALSYGQKKRVTIA 444
Cdd:PRK11264 80 -IRQLRQHVGFVFQNFN-LFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAgKETSYP-RRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 445 SILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
296-496 |
3.61e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.87 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEK---------NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--- 363
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 364 SELSIFERSQKVGVVMQ------NPNHMISHhmIFDEVAfgLRNRGVAEQEIKEKVENVLELCGLsKFRH---WPiEALS 434
Cdd:PRK11308 83 DPEAQKLLRQKIQIVFQnpygslNPRKKVGQ--ILEEPL--LINTSLSAAERREKALAMMAKVGL-RPEHydrYP-HMFS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 435 YGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLV 496
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVV 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-241 |
3.91e-19 |
|
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: 85.66 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 11 RYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlipHAiKGEVT-GSLEINGKNISDFSMHDYTeQVGtvl 89
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---HP-KYEVTeGEILFKGEDITDLPPEERA-RLG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 90 qdtdsqfVGLSIGEDIAFAlenqlvsnidmyplvkstakMVDLADMLdRSPHD-LSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:cd03217 79 -------IFLAFQYPPEIP--------------------GVKNADFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 169 PLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHRDIDRVILMERGEIVadMTPDEILASElLETHG 241
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIKPDRVHVLYDGRIV--KSGDKELALE-IEKKG 199
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-201 |
4.71e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.70 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDfsmHDYTEQvgtvlqdtdSQ 95
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPA-----AGTIKLDGGDIDD---PDVAEA---------CH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVG--------LSIGEDIAF--ALENQLVSNIDmyplvkSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK13539 77 YLGhrnamkpaLTVAENLEFwaAFLGGEELDIA------AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 515631642 166 FDEPLASLDPKTGKATIEIIdQLHKETNKTIVIIEH 201
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELI-RAHLAQGGIVIAATH 185
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
16-226 |
4.79e-19 |
|
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: 85.73 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTgsleINGKNISDfsMHDYTEQVGTVLqDTDSQ 95
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI-KPDSGEIT----FDGKSYQK--NIEALRRIGALI-EAPGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGEDI-AFALENQLVSNIdmyplVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLD 174
Cdd:cd03268 84 YPNLTARENLrLLARLLGIRKKR-----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515631642 175 PKTGKATIEIIdQLHKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADM 226
Cdd:cd03268 159 PDGIKELRELI-LSLRDQGITVLISSHLLSEI-QKVADRIGIINKGKLIEEG 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
296-524 |
8.13e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.37 E-value: 8.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLI--MGVIDAD---SGSSYLNGEDL--SELSI 368
Cdd:PRK14239 3 EPILQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 369 FERSQKVGVVMQNPNHMisHHMIFDEVAFGLRNRGVAEQEI-KEKVENVLElcGLS-----KFR-HWPIEALSYGQKKRV 441
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPF--PMSIYENVVYGLRLKGIKDKQVlDEAVEKSLK--GASiwdevKDRlHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 442 TIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELgiTVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVF 521
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
...
gi 515631642 522 SQP 524
Cdd:PRK14239 236 MNP 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
309-474 |
8.17e-19 |
|
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: 85.40 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 309 DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD---SGSSYLNGEdlsELSIFERSQKVGVVMQNpNHM 385
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQ---PRKPDQFQKCVAYVRQD-DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 386 ISHHMIFDEVAFGLRNRGVAEQ--EIKEKVENVLEL--CGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTA 461
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSsdAIRKKRVEDVLLrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170
....*....|...
gi 515631642 462 GQDyrnytSMLAF 474
Cdd:cd03234 173 GLD-----SFTAL 180
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
16-223 |
1.02e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.98 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLN---GLIPHAIkgeVTGSLEINGKNIsdFSMH----DYTEQVGTV 88
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPEVT---ITGSIVYNGHNI--YSPRtdtvDLRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 89 LQDTDSqfVGLSIGEDIAFALE-NQLVSNIDMYPLVKSTAKMVDLADMLDRSPHD----LSGGQKQRVSLAGILVDDVDI 163
Cdd:PRK14239 92 FQQPNP--FPMSIYENVVYGLRlKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 164 LLFDEPLASLDP-KTGKatieIIDQLHKETNK-TIVIIEHRLEDVlHRDIDRVILMERGEIV 223
Cdd:PRK14239 170 ILLDEPTSALDPiSAGK----IEETLLGLKDDyTMLLVTRSMQQA-SRISDRTGFFLDGDLI 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
296-524 |
1.05e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.53 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEK---NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE----------D 362
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 363 LSELSIFE----RSQKVGVVMQNPnhMISHHMIF---DEVAFGLR-NRGVAEQEIKEKVENVLELCG-------LSKFRH 427
Cdd:PRK10261 90 LSEQSAAQmrhvRGADMAMIFQEP--MTSLNPVFtvgEQIAESIRlHQGASREEAMVEAKRMLDQVRipeaqtiLSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 428 wpieALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIA 507
Cdd:PRK10261 168 ----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMY 243
|
250
....*....|....*..
gi 515631642 508 DSKLIANAAMTEVFSQP 524
Cdd:PRK10261 244 QGEAVETGSVEQIFHAP 260
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
16-229 |
1.14e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.88 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEV-TGSLeingknisdfSMHDYTEQVGTVLQDT-- 92
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-ETPSAGELlAGTA----------PLAEAREDTRLMFQDArl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 93 -------DSqfVGLSIGEDIAFALENQLVSnidmyplvkstakmVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK11247 93 lpwkkviDN--VGLGLKGQWRDAALQALAA--------------VGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPD 229
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAM-ADRVLLIEEGKIGLDLTVD 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
299-464 |
1.38e-18 |
|
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: 84.08 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSElsifersqkVGVV 378
Cdd:cd03231 1 LEADELTCERDGRA-LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF---------QRDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNHMISHhmifdevAFGLRNRGVAEQEIK--------EKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLE 450
Cdd:cd03231 71 IARGLLYLGH-------APGIKTTLSVLENLRfwhadhsdEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSG 143
|
170
....*....|....
gi 515631642 451 PELLILDEPTAGQD 464
Cdd:cd03231 144 RPLWILDEPTTALD 157
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-227 |
1.76e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.51 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEVTgsleINGKNISDFS---MHDYTEQVGTVLQDTDSQF 96
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGNVS----WRGEPLAKLNraqRKAFRRDIQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 97 -----VGLSIGEDIAFALEnqlVSNIDMYPLVKSTAKMVDLAD-MLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:PRK10419 103 nprktVREIIREPLRHLLS---LDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 171 ASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMT 227
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLV-ERFCQRVMVMDNGQIVETQP 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
299-512 |
1.97e-18 |
|
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: 84.00 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGE-KNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03369 7 IEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNP--------NHMISHHMIFDEVAFG-LRnrgvaeqeIKEKVENvlelcglskfrhwpieaLSYGQKKRVTIASILV 448
Cdd:cd03369 87 IPQDPtlfsgtirSNLDPFDEYSDEEIYGaLR--------VSEGGLN-----------------LSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 449 LEPELLILDEPTAGQDYrnytSMLAFIQKLNREL--GITVVIISHDMHLVLEYtTRSIVIADSKLI 512
Cdd:cd03369 142 KRPRVLVLDEATASIDY----ATDALIQKTIREEftNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
299-498 |
2.05e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.54 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:PRK11176 342 IEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnhmishHMIFDEVAfglRNRGVAEQEI--KEKVENVLELCGLSKFrhwpIE---------------ALSYGQKKR 440
Cdd:PRK11176 422 VSQNV------HLFNDTIA---NNIAYARTEQysREQIEEAARMAYAMDF----INkmdngldtvigengvLLSGGQRQR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 441 VTIASILVLEPELLILDEPTAGQDY---RNYTSMLAFIQKlNRelgiTVVIISH--------DMHLVLE 498
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTeseRAIQAALDELQK-NR----TSLVIAHrlstiekaDEILVVE 552
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
298-524 |
2.28e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.23 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGL--TYSYDG------EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIF 369
Cdd:PRK15112 4 LLEVRNLskTFRYRTgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 370 ERSQKVGVVMQ------NPNHMISHhmIFDevaFGLR-NRGVAEQEIKEKVENVLELCGL--SKFRHWPiEALSYGQKKR 440
Cdd:PRK15112 84 YRSQRIRMIFQdpstslNPRQRISQ--ILD---FPLRlNTDLEPEQREKQIIETLRQVGLlpDHASYYP-HMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 441 VTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
....
gi 515631642 521 FSQP 524
Cdd:PRK15112 238 LASP 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
297-530 |
2.54e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIF------E 370
Cdd:PRK14271 20 PAMAAVNLTLGFAG-KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFnyrdvlE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 371 RSQKVGVVMQNPNHMISHhmIFDEVAFGLRN---------RGVAEQEIKEK--VENVLELCGLSKFRhwpieaLSYGQKK 439
Cdd:PRK14271 99 FRRRVGMLFQRPNPFPMS--IMDNVLAGVRAhklvprkefRGVAQARLTEVglWDAVKDRLSDSPFR------LSGGQQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELgiTVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
250
....*....|.
gi 515631642 520 VFSQPSLLERA 530
Cdd:PRK14271 249 LFSSPKHAETA 259
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-225 |
2.67e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.06 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 11 RYESLDKP-----TLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-----PHAIKGEVTGSLEINGKNISDfsMHD 80
Cdd:PRK09984 6 RVEKLAKTfnqhqALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksAGSHIELLGRTVQREGRLARD--IRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQdtdsQFV---GLSIgediafaLENQLVSNIDMYPLVKSTAKM---------------VDLADMLDRSPHD 142
Cdd:PRK09984 84 SRANTGYIFQ----QFNlvnRLSV-------LENVLIGALGSTPFWRTCFSWftreqkqralqaltrVGMVHFAHQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 143 LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLhRDIDRVILMERGEI 222
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAL-RYCERIVALRQGHV 231
|
...
gi 515631642 223 VAD 225
Cdd:PRK09984 232 FYD 234
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
297-464 |
2.80e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTySYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVG 376
Cdd:PRK13539 1 MMLEGEDLA-CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 vvmqNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEkvenVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLIL 456
Cdd:PRK13539 80 ----HRNAMKPALTVAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
....*...
gi 515631642 457 DEPTAGQD 464
Cdd:PRK13539 152 DEPTAALD 159
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
298-491 |
2.88e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.85 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSyDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSylngedlselsifersqkVGV 377
Cdd:COG2401 30 VLEAFGVELR-VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAG------------------CVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnhmishhmiFDEVAFGLRNRGvAEQEIKEKVEnVLELCGLS-------KFRHwpieaLSYGQKKRVTIASILVLE 450
Cdd:COG2401 91 VPDNQ---------FGREASLIDAIG-RKGDFKDAVE-LLNAVGLSdavlwlrRFKE-----LSTGQKFRFRLALLLAER 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515631642 451 PELLILDEPTAGQDYRnyTSM-LAF-IQKLNRELGITVVIISH 491
Cdd:COG2401 155 PKLLVIDEFCSHLDRQ--TAKrVARnLQKLARRAGITLVVATH 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
297-519 |
3.58e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVG 376
Cdd:PRK15439 10 PLLCARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 V--VMQNPnHMISHHMIFDEVAFGLRNRgvaeQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK15439 88 IylVPQEP-LLFPNLSVKENILFGLPKR----QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-231 |
3.97e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.53 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 19 TLK---NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNI---SDFSMHDYTEQVGTVLQDT 92
Cdd:PRK15079 33 TLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK-ATDGEVA----WLGKDLlgmKDDEWRAVRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 93 -DSQFVGLSIGEDIAFALENQL--VSNIDMYPLVKSTAKMVDL-ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:PRK15079 108 lASLNPRMTIGEIIAEPLRTYHpkLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 169 PLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEI 231
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHIS-DRVLVMYLGHAVELGTYDEV 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-236 |
3.98e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 17 KPTLKNINLRIEKGEkIV-IIGPSGSGKSTLGQCLNGLIPHAiKGEVTgsleINGKNISDFSMHdyteQ-----VGTVLQ 90
Cdd:COG1137 16 RTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPD-SGRIF----LDGEDITHLPMH----KrarlgIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 91 DTdSQFVGLSIGEDIAFALEnqlvsnidMYPLVKS--TAKMVDLADMLD-----RSP-HDLSGGQKQRVSLAGILVDDVD 162
Cdd:COG1137 86 EA-SIFRKLTVEDNILAVLE--------LRKLSKKerEERLEELLEEFGithlrKSKaYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 163 ILLFDEPLASLDPktgKATIEI---IDQLhKETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEILASEL 236
Cdd:COG1137 157 FILLDEPFAGVDP---IAVADIqkiIRHL-KERGIGVLITDHNVRETL--GIcDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
315-496 |
4.86e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.86 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPNHMisHHMIFDE 394
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLF--SGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 395 VAFGLRnrgvaeQEIKEKVENVLELCGLSKF-----RHWPIEA------LSYGQKKRVTIASILVLEPELLILDEPTAGQ 463
Cdd:TIGR00958 575 IAYGLT------DTPDEEIMAAAKAANAHDFimefpNGYDTEVgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190
....*....|....*....|....*....|....
gi 515631642 464 DYR-NYTsmlafIQKLNRELGITVVIISHDMHLV 496
Cdd:TIGR00958 649 DAEcEQL-----LQESRSRASRTVLLIAHRLSTV 677
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-201 |
1.02e-17 |
|
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: 79.80 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleingknisdfsmHDYT 82
Cdd:cd03221 1 IELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE-PDEGIVT---------------WGST 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQdtdsqfvglsigediafalenqlvsnidmyplvkstakmvdladmldrsphdLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03221 63 VKIGYFEQ----------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*....
gi 515631642 163 ILLFDEPLASLDPKtgkaTIEIIDQLHKETNKTIVIIEH 201
Cdd:cd03221 91 LLLLDEPTNHLDLE----SIEALEEALKEYPGTVILVSH 125
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
299-512 |
1.59e-17 |
|
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: 86.33 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPnhMISHHMIFDEVAFGlRNRGVAEQEIKEKVENV---LELCGLSKFRHWPIEA----LSYGQKKRVTIASILVLEP 451
Cdd:TIGR01193 554 PQEP--YIFSGSILENLLLG-AKENVSQDEIWAACEIAeikDDIENMPLGYQTELSEegssISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRElgiTVVIISHDMHlVLEYTTRSIVIADSKLI 512
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKII 687
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
296-519 |
2.60e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.98 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADS--GSSYLNGEDLSELSIFErSQ 373
Cdd:PRK13549 3 EYLLEMKNITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRD-TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 374 KVGVVMQNPNHMISHHM-----IF---DEVAFGLRNrgvaEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIAS 445
Cdd:PRK13549 81 RAGIAIIHQELALVKELsvlenIFlgnEITPGGIMD----YDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 446 ILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAG 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
298-529 |
3.19e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.80 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD--------SGSSYLNGEDLSELSIF 369
Cdd:PRK13547 1 MLTADHLHVARRH-RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 370 ERSQKVGVVMQ--NPNHMISHHMIfdeVAFG----LRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTI 443
Cdd:PRK13547 80 RLARLRAVLPQaaQPAFAFSAREI---VLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 444 ASIL---------VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIAN 514
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
250
....*....|....*
gi 515631642 515 AAMTEVFsQPSLLER 529
Cdd:PRK13547 237 GAPADVL-TPAHIAR 250
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-234 |
3.59e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 84.64 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPhaikgeVTGSLEINGKNISDFSMHD 80
Cdd:PRK10522 322 TLELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQP------QSGEILLDGKPVTAEQPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQDtdsqfvglsigediaFALENQLVSNIDMYP---LVKSTAKMVDLADMLDRSPH-----DLSGGQKQRVS 152
Cdd:PRK10522 395 YRKLFSAVFTD---------------FHLFDQLLGPEGKPAnpaLVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHrlEDVLHRDIDRVILMERGEIvADMTPDEI- 231
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH--DDHYFIHADRLLEMRNGQL-SELTGEERd 536
|
...
gi 515631642 232 LAS 234
Cdd:PRK10522 537 AAS 539
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-532 |
4.32e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.01 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaIKGEVTGSLEINGKNISDFSMHDYTEQ-VGTVLQDTDsQFVG 98
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG-----IYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELN-LVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 LSIGEDI---AFALENQLVSNIDMYplvKSTAKMVDLADmLDRSPHD----LSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:PRK10982 88 RSVMDNMwlgRYPTKGMFVDQDKMY---RDTKAIFDELD-IDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 172 SLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVA-----DMTPDEILASELLethgiREpl 246
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIF-QLCDEITILRDGQWIAtqplaGLTMDKIIAMMVG-----RS-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 247 ylsalkaakapLTsedklsnlkaldyKRFrpavqawfaerptpvAEKQYQP---LLEVHGLTysyDGEKNALEDVSFKIG 323
Cdd:PRK10982 235 -----------LT-------------QRF---------------PDKENKPgevILEVRNLT---SLRQPSIRDVSFDLH 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 324 KGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIF-----------ERSQKVGVVMQNP---NHMIShH 389
Cdd:PRK10982 273 KGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfalvtEERRSTGIYAYLDigfNSLIS-N 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 390 MIFDEVAFGLrnrgVAEQEIKEKVENVLELCGLSKFRHW-PIEALSYGQKKRVTIASILVLEPELLILDEPTAGQD---- 464
Cdd:PRK10982 352 IRNYKNKVGL----LDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgak 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 465 YRNYTSMLAFIQKlnrELGItvVIISHDMHLVLEYTTRSIVIADSKL--IANAAMTevfSQPSLLERANL 532
Cdd:PRK10982 428 FEIYQLIAELAKK---DKGI--IIISSEMPELLGITDRILVMSNGLVagIVDTKTT---TQNEILRLASL 489
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
297-511 |
5.49e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 79.01 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYsydgeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFER-SQKV 375
Cdd:cd03215 3 PVLEVRGLSV-----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMishhmifdevafGLrnrgVAEQEIKekvENVLelcgLSKFrhwpieaLSYGQKKRVTIASILVLEPELLI 455
Cdd:cd03215 78 AYVPEDRKRE------------GL----VLDLSVA---ENIA----LSSL-------LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 456 LDEPTAGQDYRNytsmLAFIQKLNREL---GITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:cd03215 128 LDEPTRGVDVGA----KAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
296-506 |
6.24e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSylngedlSELSIFERS-QK 374
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQ-ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAG-------SHIELLGRTvQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNPNHMISHH-MIFDEvaFGLRNR-GVAE---------------------QEIKEKVENVLELCGLSKFRHWPIE 431
Cdd:PRK09984 74 EGRLARDIRKSRANTgYIFQQ--FNLVNRlSVLEnvligalgstpfwrtcfswftREQKQRALQALTRVGMVHFAHQRVS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 432 ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVI 506
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
308-524 |
6.70e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.66 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 308 YDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD-----SGSSYLNGEDL--SELSIFERSQKVGVVMQ 380
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 381 NPNHMiSHHMIFDEVAFGLRNRGVA--EQEIKEKVENVLELCGL-----SKFRHWPiEALSYGQKKRVTIASILVLEPEL 453
Cdd:PRK14267 93 YPNPF-PHLTIYDNVAIGVKLNGLVksKKELDERVEWALKKAALwdevkDRLNDYP-SNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 454 LILDEPTAGQDYRNYTSMLAFIQKLNRELgiTVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-493 |
6.93e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 83.69 E-value: 6.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikGEVTGSLEING-----KNISDfsmhdyTEQVGTVLQDTDS 94
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH---GSYEGEILFDGevcrfKDIRD------SEALGIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 QFV-GLSIGEDIaFaLENQLVSN--IDMYPLVKSTAKMvdLADM-LDRSPH----DLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:NF040905 88 ALIpYLSIAENI-F-LGNERAKRgvIDWNETNRRAREL--LAKVgLDESPDtlvtDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 167 DEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVA--DMTPDEIlasellethgire 244
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIR-RVADSITVLRDGRTIEtlDCRADEV------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 245 plylsalkaakapltSEDK---------LSNLkaldykrfrpavqawFAERPTPVAEKqyqpLLEVHGLT--YSYDGEKN 313
Cdd:NF040905 229 ---------------TEDRiirgmvgrdLEDR---------------YPERTPKIGEV----VFEVKNWTvyHPLHPERK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 314 ALEDVSFKIGKGEFVSILGKNGSGKstiTKLIMGV--------IdadSGSSYLNGE--DLSELS---------IFERSQK 374
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGR---TELAMSVfgrsygrnI---SGTVFKDGKevDVSTVSdaidaglayVTEDRKG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNP---N------HMISHHMIFDEVafglRNRGVAEQ---EIKEKVENVLELCGlskfrhwpieALSYGQKKRVT 442
Cdd:NF040905 349 YGLNLIDDikrNitlanlGKVSRRGVIDEN----EEIKVAEEyrkKMNIKTPSVFQKVG----------NLSGGNQQKVV 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 443 IASILVLEPELLILDEPTAGQD----YRNYTsmlaFIQKLNRElGITVVIISHDM 493
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGIDvgakYEIYT----IINELAAE-GKGVIVISSEL 464
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-220 |
7.03e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 7.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVT------------------GSL-EI-----NGK 71
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-SGRIArpagarvlflpqrpylplGTLrEAllypaTAE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 72 NISDfsmhdytEQVGTVLQDtdsqfVGLSigediafalenqlvsnidmyplvkstakmvDLADMLDRS---PHDLSGGQK 148
Cdd:COG4178 454 AFSD-------AELREALEA-----VGLG------------------------------HLAERLDEEadwDQVLSLGEQ 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETnkTIVIIEHRleDVLHRDIDRVILMERG 220
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT--TVISVGHR--STLAAFHDRVLELTGD 559
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-511 |
7.29e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaIKGEVTGSLEINGKNISdFSMHDYTEQVGTVLQDTDSQFVG- 98
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTG-----IYTRDAGSILYLGKEVT-FNGPKSSQEAGIGIIHQELNLIPq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 LSIGEDIAFALE--NQLvSNIDMyplvkstAKMVDLADML------DRSPH----DLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PRK10762 94 LTIAENIFLGREfvNRF-GRIDW-------KKMYAEADKLlarlnlRFSSDklvgELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 167 DEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEILASELLETHGIRep 245
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIF--EIcDDVTVFRDGQFIAEREVADLTEDSLIEMMVGR-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 246 lylsalkaakapltsedKLsnlkaldykrfrpavqawfaERPTPVAEKQYQPL-LEVHGLTYSydgeknALEDVSFKIGK 324
Cdd:PRK10762 241 -----------------KL--------------------EDQYPRLDKAPGEVrLKVDNLSGP------GVNDVSFTLRK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 325 GEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS-----------IFERSQKVGVVMQ---NPNHMISHHM 390
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglangivyISEDRKRDGLVLGmsvKENMSLTALR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 391 IFDEVAFGLRNRgvAEQEIkekVENVLELCGL-SKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYT 469
Cdd:PRK10762 358 YFSRAGGSLKHA--DEQQA---VSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKK 432
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 515631642 470 SMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK10762 433 EIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-225 |
7.61e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.01 E-value: 7.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 6 SNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISDFSMHDYT- 82
Cdd:PRK10535 8 KDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCL-----DKPTSGTYRVAGQDVATLDADALAq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 ---EQVGTVLQD-------TDSQFV-------GLSIGEDIAFALEnqLVSNIDmyplvkstakmvdLADMLDRSPHDLSG 145
Cdd:PRK10535 83 lrrEHFGFIFQRyhllshlTAAQNVevpavyaGLERKQRLLRAQE--LLQRLG-------------LEDRVEYQPSQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHrlEDVLHRDIDRVILMERGEIVAD 225
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTH--DPQVAAQAERVIEIRDGEIVRN 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-235 |
1.04e-16 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 79.95 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEINGKNISDFSMHDYT 82
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV-----DIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTdSQFVGlsigeDIAFALENQLVSNID----------MYPLVKSTAKMVDLadMLDRSPHDLSGGQKQRVS 152
Cdd:cd03288 95 SRLSIILQDP-ILFSG-----SIRFNLDPECKCTDDrlwealeiaqLKNMVKSLPGGLDA--VVTEGGENFSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIdqLHKETNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTPDEIL 232
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTIL--DADLVLVLSRGILVECDTPENLL 242
|
...
gi 515631642 233 ASE 235
Cdd:cd03288 243 AQE 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-233 |
1.15e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.74 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKnIS---DFS--MH-DYT--EQV---GTV 88
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE-----PTSGRVEVNGR-VSallELGagFHpELTgrENIylnGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 89 L----QDTDSQFvglsigEDI-AFAlenqlvsnidmyplvkstakmvDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDI 163
Cdd:COG1134 116 LglsrKEIDEKF------DEIvEFA----------------------ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 164 LLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEILA 233
Cdd:COG1134 168 LLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAV--RRLcDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-460 |
1.20e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 82.86 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlIPHAIKGEVtgsleingknisdFSMHDYTeqVGTVLQD---T 92
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEFEGEA-------------RPAPGIK--VGYLPQEpqlD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 93 DSQFVGLSIGE---DIAFALE--NQLVSNI-----DMYPLVKSTAKMVDLADMLD---------------RSPHD----- 142
Cdd:PRK11819 83 PEKTVRENVEEgvaEVKAALDrfNEIYAAYaepdaDFDALAAEQGELQEIIDAADawdldsqleiamdalRCPPWdakvt 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 143 -LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTgkatIEIIDQLHKETNKTIVIIEHrledvlhrdiDRVIL----- 216
Cdd:PRK11819 163 kLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLEQFLHDYPGTVVAVTH----------DRYFLdnvag 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 217 ----MERGEIVadmtPDEILASELLETHGIRepLYLSALKAAKAPLTSEDKL----SNLKALDYK------RFRPAVQAW 282
Cdd:PRK11819 229 wileLDRGRGI----PWEGNYSSWLEQKAKR--LAQEEKQEAARQKALKRELewvrQSPKARQAKskarlaRYEELLSEE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 283 FAERPT------PVAEKQYQPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGss 356
Cdd:PRK11819 303 YQKRNEtneifiPPGPRLGDKVIEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 357 ylngedlsELSIFErSQKVGVVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIkekveNVLELCGLSKFR----HWPIEA 432
Cdd:PRK11819 380 --------TIKIGE-TVKLAYVDQSRDALDPNKTVWEEISGGLDIIKVGNREI-----PSRAYVGRFNFKggdqQKKVGV 445
|
490 500
....*....|....*....|....*...
gi 515631642 433 LSYGQKKRVTIASILVLEPELLILDEPT 460
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-241 |
1.21e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 83.87 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYES-LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgeVTGSLEINGKNIsdfsmhdY 81
Cdd:PLN03232 615 ISIKNGYFSWDSkTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA----ETSSVVIRGSVA-------Y 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDT-------DSQFVGLSIGEDI-AFALENQLvsniDMYPlvkstakMVDLADMLDRSPhDLSGGQKQRVSL 153
Cdd:PLN03232 684 VPQVSWIFNATvrenilfGSDFESERYWRAIdVTALQHDL----DLLP-------GRDLTEIGERGV-NISGGQKQRVSM 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 154 AGILVDDVDILLFDEPLASLDPKTGKatiEIIDQLHKE--TNKTIVIIEHRLEdvLHRDIDRVILMERGEI-----VADM 226
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHVAH---QVFDSCMKDelKGKTRVLVTNQLH--FLPLMDRIILVSEGMIkeegtFAEL 826
|
250
....*....|....*
gi 515631642 227 TPDEILASELLETHG 241
Cdd:PLN03232 827 SKSGSLFKKLMENAG 841
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-220 |
1.35e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.92 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphAIKGEVTGSLEINGKNISDFSMHDY----TEQVGTVLQD-TDSQF 96
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLL--AANGRIGGSATFNGREILNLPEKELnklrAEQISMIFQDpMTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 97 VGLSIGEDIAFALenQLVSNIDMYPLVKSTAKMVDLADM------LDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:PRK09473 112 PYMRVGEQLMEVL--MLHKGMSKAEAFEESVRMLDAVKMpearkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515631642 171 ASLDpKTGKATI-EIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERG 220
Cdd:PRK09473 190 TALD-VTVQAQImTLLNELKREFNTAIIMITHDL-GVVAGICDKVLVMYAG 238
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-218 |
1.89e-16 |
|
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: 78.99 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 27 IEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISdfsmhdYTEQvgTVLQDTDSQFVGLSIGEDI 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLkPDE------GDIEIELDTVS------YKPQ--YIKADYEGTVRDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 106 AFALENQLVSNIdMYPLvkstakmvDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEII 185
Cdd:cd03237 88 DFYTHPYFKTEI-AKPL--------QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 515631642 186 DQLHKETNKTIVIIEHrleDVLHRDI--DRVILME 218
Cdd:cd03237 159 RRFAENNEKTAFVVEH---DIIMIDYlaDRLIVFE 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-265 |
1.93e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.23 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDFSMHDy 81
Cdd:PRK13537 8 IDFRNVEKRYG--DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLThPDA------GSISLCGEPVPSRARHA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQ--DTDSQFvglSIGEDIA-----FALENQLVSniDMYPLVKSTAKMVDLADMLDRsphDLSGGQKQRVSLA 154
Cdd:PRK13537 79 RQRVGVVPQfdNLDPDF---TVRENLLvfgryFGLSAAAAR--ALVPPLLEFAKLENKADAKVG---ELSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEA-ERLCDRLCVIEEGRKIAEGAPHALIES 228
|
250 260 270
....*....|....*....|....*....|....*
gi 515631642 235 EL----LETHGIReplyLSALKAAKAPLTSEDKLS 265
Cdd:PRK13537 229 EIgcdvIEIYGPD----PVALRDELAPLAERTEIS 259
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-274 |
2.05e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.25 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYES-LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTgsleINGKNIsdfsmhdY 81
Cdd:PLN03130 615 ISIKNGYFSWDSkAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV----IRGTVA-------Y 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTdsqfvglsIGEDIAFALENQLV---SNIDMYPLVKSTAKMV--DLADMLDRSPhDLSGGQKQRVSLAGI 156
Cdd:PLN03130 684 VPQVSWIFNAT--------VRDNILFGSPFDPEryeRAIDVTALQHDLDLLPggDLTEIGERGV-NISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 157 LVDDVDILLFDEPLASLDPKTGKATIE--IIDQLHketNKTIVIIEHRLEDVLHrdIDRVILMERGEIVADMTPDEILAS 234
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELR---GKTRVLVTNQLHFLSQ--VDRIILVHEGMIKEEGTYEELSNN 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 515631642 235 -----ELLETHGIREPlYLSALKAAKAPLTSEDKLSNLKALDYKR 274
Cdd:PLN03130 830 gplfqKLMENAGKMEE-YVEENGEEEDDQTSSKPVANGNANNLKK 873
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
20-234 |
2.06e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 79.07 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAikgevtGSLEINGKNIS-------DFSMHDYTE------QV 85
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLeTPDS------GEIRVGGEEIRlkpdrdgELVPADRRQlqrirtRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 86 GTVLQdtdsQF-------------------VGLSIGEDIAFALENqlvsnidmypLVKstakmVDLADMLDRSPHDLSGG 146
Cdd:COG4598 98 GMVFQ----SFnlwshmtvlenvieapvhvLGRPKAEAIERAEAL----------LAK-----VGLADKRDAYPAHLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 147 QKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHrlEDVLHRDI-DRVILMERGEIVAD 225
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTH--EMGFARDVsSHVVFLHQGRIEEQ 235
|
....*....
gi 515631642 226 MTPDEILAS 234
Cdd:COG4598 236 GPPAEVFGN 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
296-524 |
2.22e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKStITKL-IMGVIDAD-----SGSSYLNGEDL--- 363
Cdd:PRK15134 3 QPLLAIENLSVAFrqqQTVRTVVNDVSLQIEAGETLALVGESGSGKS-VTALsILRLLPSPpvvypSGDIRFHGESLlha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 364 SELSIFE-RSQKVGVVMQNPnhMISH---HMIFDEVAFGLR-NRGVAEQEIKEKVENVLELCG-------LSKFRHwpie 431
Cdd:PRK15134 82 SEQTLRGvRGNKIAMIFQEP--MVSLnplHTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGirqaakrLTDYPH---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 432 ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
250
....*....|...
gi 515631642 512 IANAAMTEVFSQP 524
Cdd:PRK15134 236 VEQNRAATLFSAP 248
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
299-492 |
2.33e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 82.15 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKnalEDVSFKIG-------KGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFER 371
Cdd:COG4615 328 LELRGVTYRYPGED---GDEGFTLGpidltirRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 372 SQKVGVVMQNpnhmisHHMiFDEVaFGLRNRGVAEQ--------EIKEKVEnvlelcglskfrhwpIE-------ALSYG 436
Cdd:COG4615 405 RQLFSAVFSD------FHL-FDRL-LGLDGEADPARarellerlELDHKVS---------------VEdgrfsttDLSQG 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 437 QKKRVtiASIL-VLE--PeLLILDEPTAGQD--YRN--YTSMLafiQKLnRELGITVVIISHD 492
Cdd:COG4615 462 QRKRL--ALLVaLLEdrP-ILVFDEWAADQDpeFRRvfYTELL---PEL-KARGKTVIAISHD 517
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-223 |
2.79e-16 |
|
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: 77.69 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 7 NFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKgeVTGSLEINGKNISDFSMHdYTEQVG 86
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS--VEGDIHYNGIPYKEFAEK-YPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 87 TVLQDtDSQFVGLSIGEDIAFALE---NQLVSNIdmyplvkstakmvdladmldrsphdlSGGQKQRVSLAGILVDDVDI 163
Cdd:cd03233 87 YVSEE-DVHFPTLTVRETLDFALRckgNEFVRGI--------------------------SGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 164 LLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDIDRVILMERGEIV 223
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-231 |
2.98e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 78.62 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTE-------QVGTVlqdt 92
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPD-----SGSVLFGGTDLTGLDEHEIARlgigrkfQKPTV---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 93 dsqFVGLSIGE--DIAFALENQLVSNI------DMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:COG4674 97 ---FEELTVFEnlELALKGDRGVFASLfarltaEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLHKEtnKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEI 231
Cdd:COG4674 174 LLDEPVAGMTDAETERTAELLKSLAGK--HSVVVVEHDMEFV--RQIaRKVTVLHQGSVLAEGSLDEV 237
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
10-238 |
3.20e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.06 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 10 FRYESLDkpTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISdFSMHDYTEQ-VGTV 88
Cdd:PRK15112 21 FRRQTVE--AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-----SGELLIDDHPLH-FGDYSYRSQrIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 89 LQDTDSQfvgLSIGEDIAFALENQLVSNIDMYPL-----VKSTAKMVDL-ADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK15112 93 FQDPSTS---LNPRQRISQILDFPLRLNTDLEPEqrekqIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEILASELLE 238
Cdd:PRK15112 170 VIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHIS-DQVLVMHQGEVVERGSTADVLASPLHE 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-237 |
3.71e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.92 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 35 IIGPSGSGKSTLGQCLNGLIpHAIKGEVTgsleINGKNISDFSMHDY--TEQ--VGTVLQDTdSQFVGLSIGEDIAFALE 110
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLT-RPQKGRIV----LNGRVLFDAEKGIClpPEKrrIGYVFQDA-RLFPHYKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 111 NQLVSNIDmyplvkSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHK 190
Cdd:PRK11144 103 KSMVAQFD------KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515631642 191 ETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASELL 237
Cdd:PRK11144 177 EINIPILYVSHSLDEIL-RLADRVVVLEQGKVKAFGPLEEVWASSAM 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
308-493 |
3.96e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.67 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 308 YDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITK-------LIMGVidADSGSSYLNGEDL--SELSIFERSQKVGVV 378
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHGKNLyaPDVDPVEVRRRIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 379 MQNPNHMISHhmIFDEVAFGLRNRGVaEQEIKEKVENVLELCGL-----SKFRHWPIeALSYGQKKRVTIASILVLEPEL 453
Cdd:PRK14243 97 FQKPNPFPKS--IYDNIAYGARINGY-KGDMDELVERSLRQAALwdevkDKLKQSGL-SLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515631642 454 LILDEPTAGQDyrnYTSMLAfIQKLNRELG--ITVVIISHDM 493
Cdd:PRK14243 173 ILMDEPCSALD---PISTLR-IEELMHELKeqYTIIIVTHNM 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
133-496 |
4.37e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 81.44 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 133 ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKtgkATIEIIDQLHKETnKTIVIIEHRLE-------D 205
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH---AVLWLETYLLKWP-KTFIVVSHAREflntvvtD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 206 VLHRDIDRVILMERGEIVADMTPDEIL--------ASELLETHgIREPLYLSALKAAKAPLTSedklSNLKALDYKRFRP 277
Cdd:PLN03073 411 ILHLHGQKLVTYKGDYDTFERTREEQLknqqkafeSNERSRSH-MQAFIDKFRYNAKRASLVQ----SRIKALDRLGHVD 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 278 AV---QAWFAERPTPvAEKQYQPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSG 354
Cdd:PLN03073 486 AVvndPDYKFEFPTP-DDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 355 SSYlngedlselsifeRSQKVGVVMQNPNHMISHHMIFDEVAFGLR-NRGVAEQEIKEKVENVlelcGLS-KFRHWPIEA 432
Cdd:PLN03073 565 TVF-------------RSAKVRMAVFSQHHVDGLDLSSNPLLYMMRcFPGVPEQKLRAHLGSF----GVTgNLALQPMYT 627
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 433 LSYGQKKRVTIASILVLEPELLILDEPTagqDYRNYTSMLAFIQKLNRELGiTVVIISHDMHLV 496
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPS---NHLDLDAVEALIQGLVLFQG-GVLMVSHDEHLI 687
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
297-524 |
5.71e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.08 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGV------IDADSgsSYLNGEDLSELS 367
Cdd:PRK15093 2 PLLDIRNLTIEFktsDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrVTADR--MRFDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 368 IFERSQKVG----VVMQ------NPNHMISHHMIfdEVAFGLRNRGVAEQEIKEKVENVLEL---CGLSK----FRHWPI 430
Cdd:PRK15093 80 PRERRKLVGhnvsMIFQepqsclDPSERVGRQLM--QNIPGWTYKGRWWQRFGWRKRRAIELlhrVGIKDhkdaMRSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 431 EaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:PRK15093 158 E-LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250
....*....|....
gi 515631642 511 LIANAAMTEVFSQP 524
Cdd:PRK15093 237 TVETAPSKELVTTP 250
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
298-461 |
5.85e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.77 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDgEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELsifeRSQKVGV 377
Cdd:PRK13538 1 MLEARNLACERD-ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ----RDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMqnpnhMISHHM-IFDE------VAFGLRNRGVAEQeikEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLE 450
Cdd:PRK13538 76 LL-----YLGHQPgIKTEltalenLRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTR 147
|
170
....*....|..
gi 515631642 451 PELLILDEP-TA 461
Cdd:PRK13538 148 APLWILDEPfTA 159
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-210 |
5.94e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.06 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 12 YESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEINGKNISDFSMHDYTEQVGTVLQd 91
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLI-----SPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 92 TDSQFvGLSIGEDIAFA--LENQLVsniDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEP 169
Cdd:PRK10247 89 TPTLF-GDTVYDNLIFPwqIRNQQP---DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515631642 170 LASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRD 210
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHAD 205
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-270 |
6.13e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.02 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikGEVTG-SLEINGKNISDFSMHDYTEQVGT----VLQDTDSQF 96
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP--GRVMAeKLEFNGQDLQRISEKERRNLVGAevamIFQDPMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 97 -----VGLSIGEdiafALENQLVSN--------IDMYPLVKstakMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDI 163
Cdd:PRK11022 103 npcytVGFQIME----AIKVHQGGNkktrrqraIDLLNQVG----IPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 164 LLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILaselletHGIR 243
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEA-AHKIIVMYAGQVVETGKAHDIF-------RAPR 246
|
250 260
....*....|....*....|....*..
gi 515631642 244 EPlYLSALKAAkAPLTSEDKlSNLKAL 270
Cdd:PRK11022 247 HP-YTQALLRA-LPEFAQDK-ARLASL 270
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
299-524 |
7.65e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.43 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEknALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD----SGSSYLNGEDLSELSIfeRSQK 374
Cdd:PRK10418 5 IELRNIALQAAQP--LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCAL--RGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNPN------HMISHHMIFDEVAFGLRNRGVAEQEIKEKV--ENVLELCGLSKFRhwpieaLSYGQKKRVTIASI 446
Cdd:PRK10418 81 IATIMQNPRsafnplHTMHTHARETCLALGKPADDATLTAALEAVglENAARVLKLYPFE------MSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
307-498 |
9.65e-16 |
|
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: 80.25 E-value: 9.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 307 SYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSifERS--QKVGVVMQNP-- 382
Cdd:COG5265 366 GYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT--QASlrAAIGIVPQDTvl 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 383 -NhmishHMIFDEVAFGlrnRGVAEQeikEKVENVLELCGLSKFrhwpIEA---------------LSYGQKKRVTIASI 446
Cdd:COG5265 444 fN-----DTIAYNIAYG---RPDASE---EEVEAAARAAQIHDF----IESlpdgydtrvgerglkLSGGEKQRVAIART 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRelGITVVIISH--------DMHLVLE 498
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivdaDEILVLE 566
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-227 |
1.01e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.78 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 6 SNFSFRYE--SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISDFSMHDYTE 83
Cdd:PRK11629 9 DNLCKRYQegSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 84 ----QVGTVLQ--DTDSQFVGLsigEDIAFALenqLVSNIDMYPLVKSTAKMVDLADMLDRSPH---DLSGGQKQRVSLA 154
Cdd:PRK11629 84 lrnqKLGFIYQfhHLLPDFTAL---ENVAMPL---LIGKKKPAEINSRALEMLAAVGLEHRANHrpsELSGGERQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEdvLHRDIDRVILMERGEIVADMT 227
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ--LAKRMSRQLEMRDGRLTAELS 228
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
309-504 |
1.26e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 79.93 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 309 DGEKN-ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSG-------------SSYLNGedlsELSIFERSQK 374
Cdd:PRK13545 33 DGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGtvdikgsaaliaiSSGLNG----QLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMqnpnhmishhmifdevafglrnrGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13545 109 KGLMM-----------------------GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515631642 455 ILDEPTAGQDyRNYTSMLafIQKLN--RELGITVVIISHDMHLVLEYTTRSI 504
Cdd:PRK13545 166 VIDEALSVGD-QTFTKKC--LDKMNefKEQGKTIFFISHSLSQVKSFCTKAL 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
284-464 |
2.29e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.23 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 284 AERPTPVAEKQYQPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL 363
Cdd:PRK13657 320 RDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 364 SELSIFERSQKVGVVMQNPnhmishhmifdevafGLRNRGVAEQ-------EIKEKVENVLELCGLSKFrhwpIEA---- 432
Cdd:PRK13657 400 RTVTRASLRRNIAVVFQDA---------------GLFNRSIEDNirvgrpdATDEEMRAAAERAQAHDF----IERkpdg 460
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515631642 433 -----------LSYGQKKRVTIASILVLEPELLILDEPTAGQD 464
Cdd:PRK13657 461 ydtvvgergrqLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
12-221 |
2.62e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.08 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 12 YESLDKpTLKNINLRIE-----KGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTGSLEINGK--NISDfsmhDYTEQ 84
Cdd:PRK13409 343 YPDLTK-KLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVL-KPDEGEVDPELKISYKpqYIKP----DYDGT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 85 VGTVLQdtdsqfvglSIGEDIAfalENQLVSNIdMYPLvkstakmvDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:PRK13409 417 VEDLLR---------SITDDLG---SSYYKSEI-IKPL--------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHrleDVLHRDI--DRVILMErGE 221
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDH---DIYMIDYisDRLMVFE-GE 530
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-241 |
3.58e-15 |
|
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: 79.22 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIPHAIKgeVTGSLEINGKNIsdfsmhdY 81
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMDK--VEGHVHMKGSVA-------Y 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDtdsqfvglSIGEDIAF--ALENQLVSNIdmyplVKSTAKMVDLaDML---DRSP-----HDLSGGQKQRV 151
Cdd:TIGR00957 704 VPQQAWIQND--------SLRENILFgkALNEKYYQQV-----LEACALLPDL-EILpsgDRTEigekgVNLSGGQKQRV 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIE-IIDQLHKETNKTIVIIEHRLEDVLHRDIdrVILMERGEIvADMTPDE 230
Cdd:TIGR00957 770 SLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDV--IIVMSGGKI-SEMGSYQ 846
|
250
....*....|.
gi 515631642 231 ilasELLETHG 241
Cdd:TIGR00957 847 ----ELLQRDG 853
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-223 |
4.40e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleiNGKNIsdfsmhdyt 82
Cdd:COG0488 316 LELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE-PDSGTVK-----LGETV--------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 eQVGTVLQDTDSQFVGLSIGE---DIAFALENQLVSNIdmyplvkstakmvdLADML------DRSPHDLSGGQKQRVSL 153
Cdd:COG0488 379 -KIGYFDQHQEELDPDKTVLDelrDGAPGGTEQEVRGY--------------LGRFLfsgddaFKPVGVLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 154 AGILVDDVDILLFDEPLASLDPktgkATIEIIDQLHKETNKTIVIIEH-R--LEDVlhrdIDRVILMERGEIV 223
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHdRyfLDRV----ATRILEFEDGGVR 508
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
298-491 |
4.77e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDgEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL-SELSIFERS---- 372
Cdd:PRK13540 1 MLDVIELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQlcfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 -QKVGVvmqNPNHMISHHMIFDeVAFGLRNRGVAeqeikekvenvlELCGLSKFRH---WPIEALSYGQKKRVTIASILV 448
Cdd:PRK13540 80 gHRSGI---NPYLTLRENCLYD-IHFSPGAVGIT------------ELCRLFSLEHlidYPCGLLSSGQKRQVALLRLWM 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515631642 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKlNRELGITVVIISH 491
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-251 |
5.61e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 1 MTIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDfSMHD 80
Cdd:PRK13536 40 VAIDLAGVSKSYG--DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-----AGKITVLGVPVPA-RARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVlqdtdSQFVGLsigeDIAFAL-ENQLV-------SNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVS 152
Cdd:PRK13536 112 ARARIGVV-----PQFDNL----DLEFTVrENLLVfgryfgmSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTP---- 228
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEA-ERLCDRLCVLEAGRKIAEGRPhali 260
|
250 260
....*....|....*....|...
gi 515631642 229 DEILASELLETHGiREPLYLSAL 251
Cdd:PRK13536 261 DEHIGCQVIEIYG-GDPHELSSL 282
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
297-520 |
5.79e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.52 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQ-KV 375
Cdd:PRK09700 4 PYISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQN----------PNHMISHHMIFDEVAFGLrnrgVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIAS 445
Cdd:PRK09700 83 GIIYQElsvideltvlENLYIGRHLTKKVCGVNI----IDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 446 ILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-251 |
5.86e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.48 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGL--IPHAIKGEVTgsleINGKNISDFSMH 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSM---LNALfrIVELEKGRIM----IDDCDVAKFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DyTEQVGTVLQDTDSQFVGLSIGEDIAFALENqlvsNIDMYPLVKSTakmvDLADMLDRSPHDL-----------SGGQK 148
Cdd:PLN03232 1307 D-LRRVLSIIPQSPVLFSGTVRFNIDPFSEHN----DADLWEALERA----HIKDVIDRNPFGLdaevseggenfSVGQR 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETnkTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTP 228
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSC--TMLVIAHRLNTII--DCDKILVLSSGQVLEYDSP 1453
|
250 260
....*....|....*....|....*....
gi 515631642 229 DEILASE------LLETHGIREPLYLSAL 251
Cdd:PLN03232 1454 QELLSRDtsaffrMVHSTGPANAQYLSNL 1482
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
310-491 |
8.72e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 8.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD---SGSSYLNGEDLSELSIFERSqkvGVVMQN----P 382
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS---AYVQQDdlfiP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 383 NHMISHHMIFDEVafgLR-NRGVAEQEIKEKVENVLELCGLSKFRHWPI------EALSYGQKKRVTIASILVLEPELLI 455
Cdd:TIGR00955 113 TLTVREHLMFQAH---LRmPRRVTKKEKRERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISH 491
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIH 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-234 |
8.77e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 77.15 E-value: 8.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESLDKP---TLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAikgevtGSLEINGKNISDFS 77
Cdd:COG4615 327 TLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLyRPES------GEILLDGQPVTADN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 78 MHDYTEQVGTVLQD---TDsQFVGLSIGEDIAFAleNQLVSNIDMyplvkstAKMVDLADmlDR-SPHDLSGGQKQRVSL 153
Cdd:COG4615 401 REAYRQLFSAVFSDfhlFD-RLLGLDGEADPARA--RELLERLEL-------DHKVSVED--GRfSTTDLSQGQRKRLAL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 154 AGILVDDVDILLFDEPLASLDPkTGKATI--EIIDQLhKETNKTIVIIEH--RLEDVlhrdIDRVILMERGEIVADMTPD 229
Cdd:COG4615 469 LVALLEDRPILVFDEWAADQDP-EFRRVFytELLPEL-KARGKTVIAISHddRYFDL----ADRVLKMDYGKLVELTGPA 542
|
....*
gi 515631642 230 EILAS 234
Cdd:COG4615 543 ALAAS 547
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-235 |
9.21e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 9.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQVGTVLQDTDSQFVGL 99
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD-----AGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAFALE-NQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTG 178
Cdd:PRK10895 94 SVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 179 KATIEIIDQLhKETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEILASE 235
Cdd:PRK10895 174 IDIKRIIEHL-RDSGLGVLITDHNVRETL--AVcERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
290-511 |
1.01e-14 |
|
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: 73.66 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 290 VAEKQYQPLLEVHGLTYSYDG--EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS 367
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 368 IFERSQKVGVVMQNPnhMISHHMIFDEVAFGLRnrGVAEQEIKEKVENVLELCGLSKFRHWPIEA-------LSYGQKKR 440
Cdd:cd03248 83 HKYLHSKVSLVGQEP--VLFARSLQDNIAYGLQ--SCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631642 441 VTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELgiTVVIISHDMHLVlEYTTRSIVIADSKL 511
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
296-529 |
1.29e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSelsiF---ERS 372
Cdd:PRK10762 2 QALLQLKGIDKAFPGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT----FngpKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 373 QK--VGVVMQNPNhMISHHMIFDEVAFG--LRNR--GVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:PRK10762 77 QEagIGIIHQELN-LIPQLTIAENIFLGreFVNRfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVfSQPSL 526
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL-TEDSL 233
|
...
gi 515631642 527 LER 529
Cdd:PRK10762 234 IEM 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-221 |
1.41e-14 |
|
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: 76.75 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 10 FRYESLDKpTLKNINLRIE-----KGEKIVIIGPSGSGKSTLGQCLNGLI-PHaiKGEVTGSLEINGK--NISdfsmHDY 81
Cdd:COG1245 342 VEYPDLTK-SYGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLkPD--EGEVDEDLKISYKpqYIS----PDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTDSQFVGLSIgediafaLENQLVSnidmyPLvkstakmvDLADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:COG1245 415 DGTVEEFLRSANTDDFGSSY-------YKTEIIK-----PL--------GLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 162 DILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHrleDVLHRDI--DRVILMErGE 221
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH---DIYLIDYisDRLMVFE-GE 532
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
298-517 |
2.11e-14 |
|
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: 75.63 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADS--GSSYLNGEDLSELSIFERSQKV 375
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMISHHMIFDEVAFG----LRNRGVAEQEIKEKVENVLELCGLSKFRH-WPIEALSYGQKKRVTIASILVLE 450
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 451 PELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAM 517
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDM 225
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-223 |
2.12e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.90 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 9 SFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIPHAikgEVT-GSLEINGKNISDFSMHDYTEQVGT 87
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTL---LSLIQRHF---DVSeGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 88 VLQdTDSQFVGlSIGEDIAFALENQLVSNIDmyplvkSTAKMVDLADMLDRSPHD-----------LSGGQKQRVSLAGI 156
Cdd:PRK10789 394 VSQ-TPFLFSD-TVANNIALGRPDATQQEIE------HVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 157 LVDDVDILLFDEPLASLDpktGKATIEIIDQLHK-ETNKTIVIIEHRLEDVLhrDIDRVILMERGEIV 223
Cdd:PRK10789 466 LLLNAEILILDDALSAVD---GRTEHQILHNLRQwGEGRTVIISAHRLSALT--EASEILVMQHGHIA 528
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
299-508 |
2.13e-14 |
|
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: 72.12 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKN----ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGedlselsifersqK 374
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNPNHMisHHMIFDEVAFGlrnrgvaEQEIKEKVENVLELCGLSK-FRHWP-----------IeALSYGQKKRVT 442
Cdd:cd03250 68 IAYVSQEPWIQ--NGTIRENILFG-------KPFDEERYEKVIKACALEPdLEILPdgdlteigekgI-NLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 443 IASILVLEPELLILDEPTAGQDyrNYTSMLAFIQKLNREL--GITVVIISHDMHLvLEYTTRSIVIAD 508
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVD--AHVGRHIFENCILGLLlnNKTRILVTHQLQL-LPHADQIVVLDN 202
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-222 |
2.78e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 71.31 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQ-VGTVLQDTDSQ 95
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA-----SGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 --FVGLSIGEDIAFalenqlvsnidmyplvkstakmvdladmldrsPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:cd03215 88 glVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515631642 174 DPKTgKATI-EIIDQLhKETNKTIVIIEHRLEDVLHrdI-DRVILMERGEI 222
Cdd:cd03215 136 DVGA-KAEIyRLIREL-ADAGKAVLLISSELDELLG--LcDRILVMYEGRI 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
296-521 |
2.83e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKV 375
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMISHHMIFDEVAFGlrNRGVAEQEIKEKVENVLELCG-LSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG--GFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 455 ILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRS-------IVIADS--KLIANAAMTEVF 521
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGyvlenghVVLEDTgdALLANEAVRSAY 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
298-512 |
4.63e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADS--GSSYLNGEdLSELSIFERSQKV 375
Cdd:NF040905 1 ILEMRGITKTFPGVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE-VCRFKDIRDSEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVmqnpnhmISH-------HM-----IF--DEVA-FGLRNRGVAEQEIKEKVENVlelcGLSKFRHWPIEALSYGQKKR 440
Cdd:NF040905 79 GIV-------IIHqelalipYLsiaenIFlgNERAkRGVIDWNETNRRARELLAKV----GLDESPDTLVTDIGVGKQQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 441 VTIASILVLEPELLILDEPTAG---QDYRNytsMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:NF040905 148 VEIAKALSKDVKLLILDEPTAAlneEDSAA---LLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
296-499 |
5.20e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.98 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDgEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMG-----VIdadSGSSYLNGEDLSELSIFE 370
Cdd:CHL00131 5 KPILEIKNLHASVN-ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykIL---EGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 371 RSQKvGVVM--QNPNHMIS-HHMIFDEVAFGLRN--RGVAEQE-------IKEKvenvLELCGLS-KFRHWPI-EALSYG 436
Cdd:CHL00131 81 RAHL-GIFLafQYPIEIPGvSNADFLRLAYNSKRkfQGLPELDplefleiINEK----LKLVGMDpSFLSRNVnEGFSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 437 QKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLvLEY 499
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQRL-LDY 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
299-491 |
5.32e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLT-YSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIdADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:PRK11174 350 IEAEDLEiLSPDG-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnhMISHHMIFDEVAFGlrnrgvAEQEIKEKVENVLELCGLSKFR-------HWPIE----ALSYGQKKRVTIASI 446
Cdd:PRK11174 428 VGQNP--QLPHGTLRDNVLLG------NPDASDEQLQQALENAWVSEFLpllpqglDTPIGdqaaGLSVGQAQRLALARA 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515631642 447 LVLEPELLILDEPTAGQDYRnytSMLAFIQKLNRE-LGITVVIISH 491
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAH---SEQLVMQALNAAsRRQTTLMVTH 542
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-247 |
6.98e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.31 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEvtGSLEINGKNISDFSMHD---YTEQ----VGTVL 89
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGS--GSVLLNGMPIDAKEMRAisaYVQQddlfIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 90 QDTDSQFVG-LSIGEDIAFALENQLVSN-IDMYPLVKStakmvdlADMLDRSPHD---LSGGQKQRVSLAGILVDDVDIL 164
Cdd:TIGR00955 116 VREHLMFQAhLRMPRRVTKKEKRERVDEvLQALGLRKC-------ANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVLHRDIDRVILMERGEIVADMTPDEilASELLETHGIRE 244
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ--AVPFFSDLGHPC 265
|
...
gi 515631642 245 PLY 247
Cdd:TIGR00955 266 PEN 268
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-242 |
7.25e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.74 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDY 81
Cdd:PRK10575 11 TFALRNVSFRVP--GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-----EGEILLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDTdSQFVGLSIGEDIAfalenqlvsnIDMYPL--------------VKSTAKMVDLADMLDRSPHDLSGGQ 147
Cdd:PRK10575 84 ARKVAYLPQQL-PAAEGMTVRELVA----------IGRYPWhgalgrfgaadrekVEEAISLVGLKPLAHRLVDSLSGGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMT 227
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDI-NMAARYCDYLVALRGGEMIAQGT 231
|
250
....*....|....*.
gi 515631642 228 PDEILASELLET-HGI 242
Cdd:PRK10575 232 PAELMRGETLEQiYGI 247
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-220 |
8.01e-14 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 70.82 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqclngLIphAIKGE---VTGSLEINGKNISD--FSMHDYTEQVGTVLQ 90
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSL------LL--AILGEmqtLEGKVHWSNKNESEpsFEATRSRNRYSVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 91 DTDSQFVGLSIGEDIAFAlenqlvsnidmYPLVKSTAKMV----DLADMLDRSPH-----------DLSGGQKQRVSLAG 155
Cdd:cd03290 85 AQKPWLLNATVEENITFG-----------SPFNKQRYKAVtdacSLQPDIDLLPFgdqteigergiNLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 156 ILVDDVDILLFDEPLASLDPKTGKATI-EIIDQLHKETNKTIVIIEHRLEDVLHrdIDRVILMERG 220
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPH--ADWIIAMKDG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-234 |
9.06e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 35 IIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEINGKNISDF-SMHDYTEQVGTVLQDTDSqfVGLSIGEDI-AFALENQ 112
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNP--FPMSIMDNVlAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 113 LVSNIDMYPLVKSTAKMVDL----ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQL 188
Cdd:PRK14271 130 LVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515631642 189 HKETnkTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK14271 210 ADRL--TVIIVTHNLAQAA-RISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
146-512 |
1.02e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 73.77 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKTgkatIEIIDQLHKETNKTIVIIEHrledvlhrdiDRVILMERGEIVAD 225
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISH----------DRHFLNSVCTHMAD 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 226 MTPDEI-----------LASELlethgIREPLyLSALKAAKAPL--------------------TSEDK-LSNLKALDYK 273
Cdd:PRK15064 225 LDYGELrvypgnydeymTAATQ-----ARERL-LADNAKKKAQIaelqsfvsrfsanaskakqaTSRAKqIDKIKLEEVK 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 274 ---RFRPAVQawFAERptpvaEKQYQPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID 350
Cdd:PRK15064 299 pssRQNPFIR--FEQD-----KKLHRNALEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 351 ADSGSSylngeDLSElsiferSQKVGVVMQNPNHMISHHM-IFDEVAfGLRNRGVAEQ--------------EIKEKVEN 415
Cdd:PRK15064 371 PDSGTV-----KWSE------NANIGYYAQDHAYDFENDLtLFDWMS-QWRQEGDDEQavrgtlgrllfsqdDIKKSVKV 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 416 vlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILDEPTagqdyrNYTSMLAfIQKLNRELGI---TVVIISHD 492
Cdd:PRK15064 439 -----------------LSGGEKGRMLFGKLMMQKPNVLVMDEPT------NHMDMES-IESLNMALEKyegTLIFVSHD 494
|
410 420
....*....|....*....|
gi 515631642 493 MHLVLEYTTRSIVIADSKLI 512
Cdd:PRK15064 495 REFVSSLATRIIEITPDGVV 514
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
314-511 |
1.43e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 74.28 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLsELSIFERSQKVGVVMQNpNHMISHHMIFD 393
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQH-NILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 394 EVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLA 473
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*...
gi 515631642 474 FIQKLNRelGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:TIGR01257 1103 LLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-220 |
1.49e-13 |
|
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: 74.18 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 5 FSNFSFryesLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHaiKGEVTGSLEINgknisdfsmhdYTE 83
Cdd:TIGR01271 431 FSNFSL----YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPS--EGKIKHSGRIS-----------FSP 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 84 QVGTVLQDT--DSQFVGLSIGEDIAFALEN--QLVSNIDMYPLVKSTakmvdladMLDRSPHDLSGGQKQRVSLAGILVD 159
Cdd:TIGR01271 494 QTSWIMPGTikDNIIFGLSYDEYRYTSVIKacQLEEDIALFPEKDKT--------VLGEGGITLSGGQRARISLARAVYK 565
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 160 DVDILLFDEPLASLDPKTGKATIE-IIDQLHkeTNKTIVIIEHRLEDVlhRDIDRVILMERG 220
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKEIFEsCLCKLM--SNKTRILVTSKLEHL--KKADKILLLHEG 623
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-235 |
1.95e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.62 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGL--IPHAIKGEVTgsleINGKNISDFSMHD 80
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSM---LNALfrIVELERGRIL----IDGCDISKFGLMD 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQdTDSQFVGlsigeDIAFALE--NQLvSNIDMYplvkSTAKMVDLADMLDRSPHDL-----------SGGQ 147
Cdd:PLN03130 1311 LRKVLGIIPQ-APVLFSG-----TVRFNLDpfNEH-NDADLW----ESLERAHLKDVIRRNSLGLdaevseagenfSVGQ 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKatieIIDQLHKETNK--TIVIIEHRLEDVLhrDIDRVILMERGEIVAD 225
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVDVRTDA----LIQKTIREEFKscTMLIIAHRLNTII--DCDRILVLDAGRVVEF 1453
|
250
....*....|
gi 515631642 226 MTPDEILASE 235
Cdd:PLN03130 1454 DTPENLLSNE 1463
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-225 |
2.12e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.48 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHA-----IKGEVTGSLEINGKNISDFSMHDYTEQVGTVLq 90
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDsgtvtVRGRVSSLLGLGGGFNPELTGRENIYLNGRLL- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 91 dtdsqfvGLSIGED-------IAFAlenqlvsnidmyplvkstakmvDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDI 163
Cdd:cd03220 113 -------GLSRKEIdekideiIEFS----------------------ELGDFIDLPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 164 LLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVAD 225
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSI--KRLcDRALVLEKGKIRFD 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
3-221 |
2.42e-13 |
|
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: 70.66 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFryesLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQClngliphaikgeVTGSLEINGKNISDFSMHDYT 82
Cdd:cd03291 40 LFFSNLCL----VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLML------------ILGELEPSEGKIKHSGRISFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTdsqfvglsIGEDIAFAL---ENQLVSNIDMYPLVKSTAKMVDLAD-MLDRSPHDLSGGQKQRVSLAGILV 158
Cdd:cd03291 104 SQFSWIMPGT--------IKENIIFGVsydEYRYKSVVKACQLEEDITKFPEKDNtVLGEGGITLSGGQRARISLARAVY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 159 DDVDILLFDEPLASLDPKTGKatiEIIDQ--LHKETNKTIVIIEHRLEDVlhRDIDRVILMERGE 221
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEK---EIFEScvCKLMANKTRILVTSKMEHL--KKADKILILHEGS 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
311-491 |
2.58e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.60 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADS--GSSYLNGEDLSELSIfersQKVGVVMQN----PNH 384
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL----KRTGFVTQDdilyPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 385 MISHHMIFdeVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWP-----IEALSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:PLN03211 156 TVRETLVF--CSLLRLPKSLTKQEKILVAESVISELGLTKCENTIignsfIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190
....*....|....*....|....*....|....*.
gi 515631642 460 TAGQD----YRNYTSMLAFIQKlnrelGITVVIISH 491
Cdd:PLN03211 234 TSGLDataaYRLVLTLGSLAQK-----GKTIVTSMH 264
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
304-487 |
2.69e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) 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: 213199 [Multi-domain] Cd Length: 192 Bit Score: 68.81 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 304 LTYSYD---GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLI-----MGVIdadSGSSYLNGEDLSElsIFERSqkV 375
Cdd:cd03232 9 LNYTVPvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPLDK--NFQRS--T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHmishhmifdevafglrnrgvaeqEIKEKVENVLELCGLskfrhwpIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:cd03232 82 GYVEQQDVH-----------------------SPNLTVREALRFSAL-------LRGLSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190
....*....|....*....|....*....|..
gi 515631642 456 LDEPTAGQDYRNYTSMLAFIQKLNRElGITVV 487
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLADS-GQAIL 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
296-520 |
2.69e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGssylngedlsELSIFERSQKV 375
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAG----------SILIDGQEMRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPNHMIShhMIFDE--------VA-----------FGLRNRGVAEQEIKEKVENVlelcGLSKFRHWPIEALSYG 436
Cdd:PRK11288 71 ASTTAALAAGVA--IIYQElhlvpemtVAenlylgqlphkGGIVNRRLLNYEAREQLEHL----GVDIDPDTPLKYLSIG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 437 QKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIAN-A 515
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVATfD 223
|
....*
gi 515631642 516 AMTEV 520
Cdd:PRK11288 224 DMAQV 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
330-526 |
2.93e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 330 ILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--SELSIF---ERsQKVGVVMQNpnHMISHHMifdEVAFGLRnRGV 404
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKGIClppEK-RRIGYVFQD--ARLFPHY---KVRGNLR-YGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 405 AEQEiKEKVENVLELCG----LSKFrhwPIeALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNR 480
Cdd:PRK11144 102 AKSM-VAQFDKIVALLGieplLDRY---PG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515631642 481 ELGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSL 526
Cdd:PRK11144 177 EINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAM 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-235 |
3.07e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.52 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDkpTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEVTgsleINGKNISDFSMHDYT 82
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIV----FDGKDITDWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTDSQFVGLSIGEDIA----FALENQLVSNI----DMYPlvkstakmvDLADMLDRSPHDLSGGQKQRVSLA 154
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAmggfFAERDQFQERIkwvyELFP---------RLHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQAL-KLADRGYVLENGHVVLEDTGDALLAN 227
|
.
gi 515631642 235 E 235
Cdd:PRK11614 228 E 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-246 |
3.57e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.75 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESL-DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCL----------NGLIPHAIKGEVT-------- 63
Cdd:PTZ00265 1166 IEIMDVNFRYISRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhHIVFKNEHTNDMTneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 64 -------------------------------GSLEINGKNISDFSMHDYTEQVGTVLQDtdSQFVGLSIGEDIAFALENQ 112
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQE--PMLFNMSIYENIKFGKEDA 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 113 LVSNidmyplVKSTAKMVDLADMLDRSPH-----------DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKAT 181
Cdd:PTZ00265 1324 TRED------VKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 182 IEIIDQLHKETNKTIVIIEHRLEDVLHRDidrvilmergEIVADMTPDEilASELLETHGIREPL 246
Cdd:PTZ00265 1398 EKTIVDIKDKADKTIITIAHRIASIKRSD----------KIVVFNNPDR--TGSFVQAHGTHEEL 1450
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-233 |
4.75e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.12 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 8 FSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVtgslEINGKNISDFSMhDYTEQVGT 87
Cdd:COG4586 28 FRREYR--EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIL-VPTSGEV----RVLGYVPFKRRK-EFARRIGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 88 V------------LQDTdsqfvglsigediaFAL--------ENQLVSNIDMYplvkstAKMVDLADMLDRSPHDLSGGQ 147
Cdd:COG4586 100 VfgqrsqlwwdlpAIDS--------------FRLlkaiyripDAEYKKRLDEL------VELLDLGELLDTPVRQLSLGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADM 226
Cdd:COG4586 160 RMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDI--EALcDRVIVIDHGRIIYDG 237
|
....*..
gi 515631642 227 TPDEILA 233
Cdd:COG4586 238 SLEELKE 244
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-511 |
4.95e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 71.74 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVT--GSLEINGKNIS----DF 76
Cdd:PRK10636 2 IVFSSLQIRRGV--RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEI-SADGGSYTfpGNWQLAWVNQEtpalPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 77 SMHDYT-------EQVGTVLQDTDSQFVGLSIgediafALENQLVSNIDMYPLVKSTAKMVD----LADMLDRSPHDLSG 145
Cdd:PRK10636 79 PALEYVidgdreyRQLEAQLHDANERNDGHAI------ATIHGKLDAIDAWTIRSRAASLLHglgfSNEQLERPVSDFSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKtgkATIEIIDQLhKETNKTIVIIEHRlEDVLHRDIDRVILMER---GEI 222
Cdd:PRK10636 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWL-KSYQGTLILISHD-RDFLDPIVDKIIHIEQqslFEY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 223 VADMTPDEIL-ASELLEthgiREPLYLSalkaakapltSEDKLSNLKALdYKRFRP----AVQAW----FAERPTPVA-- 291
Cdd:PRK10636 228 TGNYSSFEVQrATRLAQ----QQAMYES----------QQERVAHLQSY-IDRFRAkatkAKQAQsrikMLERMELIApa 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 292 -------------EKQYQPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYL 358
Cdd:PRK10636 293 hvdnpfhfsfrapESLPNPLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 359 ngedlselsifERSQKVGVVMQnpnhmisHHMIF---DEVAFGLRNRgVAEQEIKEKVENVLELCGLSKFR-HWPIEALS 434
Cdd:PRK10636 372 -----------AKGIKLGYFAQ-------HQLEFlraDESPLQHLAR-LAPQELEQKLRDYLGGFGFQGDKvTEETRRFS 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 435 YGQKKRVTIASILVLEPELLILDEPTAGQDyrnytsmLAFIQKLNREL----GiTVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:PRK10636 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLD-------LDMRQALTEALidfeG-ALVVVSHDRHLLRSTTDDLYLVHDGK 504
|
.
gi 515631642 511 L 511
Cdd:PRK10636 505 V 505
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
299-522 |
5.55e-13 |
|
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: 71.37 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID--ADSGSSYLNGEDLSELSIFERSQKVG 376
Cdd:TIGR03269 1 IEVKNLTKKFDG-KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHVALCEKCGYVERPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 ---------------------------------VVMQNPNHMISHHMIFDEVafgLRNRGVAEQEIKEKVENVLELCGLS 423
Cdd:TIGR03269 80 epcpvcggtlepeevdfwnlsdklrrrirkriaIMLQRTFALYGDDTVLDNV---LEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 424 KFRHWPIEA---LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYT 500
Cdd:TIGR03269 157 QLSHRITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|..
gi 515631642 501 TRSIVIADSKLIANAAMTEVFS 522
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
314-511 |
8.07e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 68.69 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEdLSELSIFE--RSQKVGVvmqnpnhmishhmi 391
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIAISAglSGQLTGI-------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 392 fDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSM 471
Cdd:PRK13546 104 -ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515631642 472 LAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK13546 183 LDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-241 |
8.48e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.51 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlipHAIKGEVTGSLEINGKNISD-----------FSMHDYTEQ 84
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---HPAYKILEGDILFKGESILDlepeerahlgiFLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 85 VGTVlqdTDSQFVGLSIGEDIAFALENQLvSNIDMYPLVKSTAKMVDL-ADMLDRSPHD-LSGGQKQRVSLAGILVDDVD 162
Cdd:CHL00131 96 IPGV---SNADFLRLAYNSKRKFQGLPEL-DPLEFLEIINEKLKLVGMdPSFLSRNVNEgFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEH--RLEDVLHRDIdrVILMERGEIVadMTPDEILASElLETH 240
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHyqRLLDYIKPDY--VHVMQNGKII--KTGDAELAKE-LEKK 245
|
.
gi 515631642 241 G 241
Cdd:CHL00131 246 G 246
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-234 |
8.81e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.98 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikGEVTgsleINGKNISDfsmhdyteqvgtvlqdTDS 94
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPDS--GEVL----WDGEPLDP----------------EDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 QFVG-----------LSIGEDIAF--ALENqlvsnidmypLVKSTAKM--------VDLADMLDRSPHDLSGGQKQRVSL 153
Cdd:COG4152 71 RRIGylpeerglypkMKVGEQLVYlaRLKG----------LSKAEAKRradewlerLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 154 AGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEILA 233
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELV-EELCDRIVIINKGRKVLSGSVDEIRR 218
|
.
gi 515631642 234 S 234
Cdd:COG4152 219 Q 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-231 |
1.17e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 17 KPTLKNINLRIEKGEkIV-IIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQ-VGTVLQDTDS 94
Cdd:COG1129 265 GGVVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPAD-----SGEIRLDGKPVRIRSPRDAIRAgIAYVPEDRKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 Q--FVGLSIGEDIAFALENQLVSNIdmyplVKSTAKMVDLA-DMLDR------SPHD----LSGGQKQRVSLAGILVDDV 161
Cdd:COG1129 339 EglVLDLSIRENITLASLDRLSRGG-----LLDRRRERALAeEYIKRlriktpSPEQpvgnLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 162 DILLFDEPLASLDPKTgKATI-EIIDQLHKEtNKTIVIIEHRLEDVLHrdI-DRVILMERGEIVADMTPDEI 231
Cdd:COG1129 414 KVLILDEPTRGIDVGA-KAEIyRLIRELAAE-GKAVIVISSELPELLG--LsDRILVMREGRIVGELDREEA 481
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-222 |
1.19e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 68.34 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVTGSLEINGKNISDFSMHDYT 82
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL------NTEGDIQIDGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 EQVGTVLQDTdsqfvglsigediaFALENQLVSNIDMYPLVKS-----TAKMVDLADMLDRSPHD-----------LSGG 146
Cdd:cd03289 77 KAFGVIPQKV--------------FIFSGTFRKNLDPYGKWSDeeiwkVAEEVGLKSVIEQFPGQldfvlvdggcvLSHG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 147 QKQRVSLAGILVDDVDILLFDEPLASLDPktgkATIEIIDQLHKE--TNKTIVIIEHRLEDVLhrDIDRVILMERGEI 222
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDP----ITYQVIRKTLKQafADCTVILSEHRIEAML--ECQRFLVIEENKV 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
298-502 |
2.02e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.43 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGEKN-ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSElSIFERSQKVG 376
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQnpnhmishHMIFDEVAFG-------LRNRGVAEQEIkEKVEN-VLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:TIGR01257 2016 YCPQ--------FDAIDDLLTGrehlylyARLRGVPAEEI-EKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515631642 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRElGITVVIISHDMHLVLEYTTR 502
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTR 2139
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
252-478 |
2.59e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 252 KAAKAPLTSEDKLSNLKALDYKRFRPAVQAWFAERPTPVAEKQY-QPLLEVHGLTYS--YDGEKNA-LEDVSFKIGKGEF 327
Cdd:TIGR00956 712 RAKKAGETSASNKNDIEAGEVLGSTDLTDESDDVNDEKDMEKESgEDIFHWRNLTYEvkIKKEKRViLNNVDGWVKPGTL 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 328 VSILGKNGSGKSTI-----TKLIMGVIDadSGSSYLNGEDLSelSIFERSqkVGVVMQNPNHmISHHMIFDEVAFGLRNR 402
Cdd:TIGR00956 792 TALMGASGAGKTTLlnvlaERVTTGVIT--GGDRLVNGRPLD--SSFQRS--IGYVQQQDLH-LPTSTVRESLRFSAYLR 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 403 GVAEQEIKEK---VENVLELCGLSKFRH----WPIEALSYGQKKRVTIASILVLEPELLI-LDEPTAGQDYRNYTSMLAF 474
Cdd:TIGR00956 865 QPKSVSKSEKmeyVEEVIKLLEMESYADavvgVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKL 944
|
....
gi 515631642 475 IQKL 478
Cdd:TIGR00956 945 MRKL 948
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
297-464 |
2.75e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.41 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 297 PLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELsifERSQKVG 376
Cdd:PRK13543 10 PLLAAHALAFSRNEEP-VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 vvmqnpnhMISHHMIFDEVAFGLRN----RGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPE 452
Cdd:PRK13543 86 --------YLGHLPGLKADLSTLENlhflCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAP 157
|
170
....*....|..
gi 515631642 453 LLILDEPTAGQD 464
Cdd:PRK13543 158 LWLLDEPYANLD 169
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-201 |
3.06e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEVtgslEINGKNISDFSMHDYTE----QVGTVLQD---- 91
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGL-DDGSSGEV----SLVGQPLHQMDEEARAKlrakHVGFVFQSfmli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 92 ------TDSQFVGLSIGEDiafalENQLVSNidmyplVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK10584 101 ptlnalENVELPALLRGES-----SRQSRNG------AKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEH 201
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-263 |
3.25e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNgLIPHAIKGEvtgsLEINGKnisDFSMHDYTEQ------VGTVLQDTd 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETPTGGE----LYYQGQ---DLLKADPEAQkllrqkIQIVFQNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 94 sqFVGLSIGEDIAFALENQLVSNIDmypLVKSTAKMVDLADM---------LDRSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:PRK11308 102 --YGSLNPRKKVGQILEEPLLINTS---LSAAERREKALAMMakvglrpehYDRYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 165 LFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIVADMTPDEILASEllethgiR 243
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEH--IaDEVMVMYLGRCVEKGTKEQIFNNP-------R 247
|
250 260
....*....|....*....|
gi 515631642 244 EPlYLSALKAAKAPLTSEDK 263
Cdd:PRK11308 248 HP-YTQALLSATPRLNPDDR 266
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
302-492 |
3.35e-12 |
|
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: 68.81 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 302 HGLTYSYDGEKNALEDVSF------KIGkgefvsILGKNGSGKSTITKlIMGVIDADSgssylNGEDLSELSIfersqKV 375
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLsffpgaKIG------VLGLNGAGKSTLLR-IMAGVDKDF-----NGEARPQPGI-----KV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNP----------NHMISHHMI------FDEV--AFGL----RNRGVAEQEikeKVENVLELCGLSKFRH------ 427
Cdd:TIGR03719 71 GYLPQEPqldptktvreNVEEGVAEIkdaldrFNEIsaKYAEpdadFDKLAAEQA---ELQEIIDAADAWDLDSqleiam 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 428 ---------WPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNytsmLAFIQKLNRELGITVVIISHD 492
Cdd:TIGR03719 148 dalrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
319-523 |
3.78e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.50 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 319 SFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSiFERSQKVgvVMQ----NPNHMISHhmifDE 394
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS-FEQLQKL--VSDewqrNNTDMLSP----GE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 395 VAFGLRNRGVAEQEIK--EKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSML 472
Cdd:PRK10938 96 DDTGRTTAEIIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515631642 473 AFIQKLNRElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQ 523
Cdd:PRK10938 176 ELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-228 |
3.96e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.66 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 12 YESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNIsDFSMHDYTEQVGTVLQD 91
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP-----PTSGTVLVGGKDI-ETNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 92 tDSQFVGLSIGEDIAFALE----NQLVSNIDMYPLVKSTAkmvdLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:TIGR01257 1012 -NILFHHLTVAEHILFYAQlkgrSWEEAQLEMEAMLEDTG----LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 168 EPLASLDPKTGKATIEIIdqLHKETNKTIVIIEHRLEDVlhrDI--DRVILMERGEIVADMTP 228
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEA---DLlgDRIAIISQGRLYCSGTP 1144
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-229 |
4.44e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAIKGEVTGSLEINgknisdfsmhdYTEQ---VGTVLQDTDSQ 95
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVIKRNGKLRIG-----------YVPQklyLDTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGediafalenqlVSNIDMYPLVKStakmVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:PRK09544 89 FLRLRPG-----------TKKEDILPALKR----VQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515631642 176 KTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRdIDRVILMERgEIVADMTPD 229
Cdd:PRK09544 154 NGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAK-TDEVLCLNH-HICCSGTPE 205
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
272-491 |
4.56e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 272 YKRFRpavqAWFAERPtpVAEKQYQPLLEVHGL------TYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKL 344
Cdd:PRK10789 287 YSRIR----AMLAEAP--VVKDGSEPVPEGRGEldvnirQFTYPQtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 345 IMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPnhmishhMIF-DEVA--FGLRNRGVAEQEIKEKV------EN 415
Cdd:PRK10789 361 IQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP-------FLFsDTVAnnIALGRPDATQQEIEHVArlasvhDD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 416 VLELCglskfRHWPIEA------LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRelGITVVII 489
Cdd:PRK10789 434 ILRLP-----QGYDTEVgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIIS 506
|
..
gi 515631642 490 SH 491
Cdd:PRK10789 507 AH 508
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-176 |
6.14e-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: 64.69 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVtgslEINGKNISDFSMHdYTEQVgTVLQDTDSQFV 97
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPD-SGEV----RWNGTPLAEQRDE-PHENI-LYLGHLPGLKP 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 98 GLSIGEDIAFAleNQLVSNIDMYPLvKSTAKmVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPK 176
Cdd:TIGR01189 87 ELSALENLHFW--AAIHGGAQRTIE-DALAA-VGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-207 |
7.52e-12 |
|
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: 68.40 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 7 NFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVTGSLEINGKNISDFSMHDYTEQVG 86
Cdd:TIGR01271 1222 GLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL------STEGEIQIDGVSWNSVTLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 87 TVLQDTdsqfvglsigediaFALENQLVSNIDMYPL-----VKSTAKMVDLADMLDRSPHDL-----------SGGQKQR 150
Cdd:TIGR01271 1296 VIPQKV--------------FIFSGTFRKNLDPYEQwsdeeIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQL 1361
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 151 VSLAGILVDDVDILLFDEPLASLDPktgkATIEIIDQLHKET--NKTIVIIEHRLEDVL 207
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDP----VTLQIIRKTLKQSfsNCTVILSEHRVEALL 1416
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-505 |
1.10e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAikgevtGSLEINGKNISDFSMHDYTEQ-VGTVLQDTdsQFV 97
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDA------GSILIDGQEMRFASTTAALAAgVAIIYQEL--HLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 98 -GLSIGEDIafaLENQLVSN---IDMYPLVKSTAKMvdLADM-LDRSPH----DLSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:PRK11288 92 pEMTVAENL---YLGQLPHKggiVNRRLLNYEAREQ--LEHLgVDIDPDtplkYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 169 PLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLhRDIDRVILMERGEIVA---DM--TPDEILASELLEthgiR 243
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIF-ALCDAITVFKDGRYVAtfdDMaqVDRDQLVQAMVG----R 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 244 EplylsalkaakapltsedkLSNLkaldykrfrpavqawFAERPTPVAEkqyqPLLEVHGLtysyDGEKNAlEDVSFKIG 323
Cdd:PRK11288 241 E-------------------IGDI---------------YGYRPRPLGE----VRLRLDGL----KGPGLR-EPISFSVR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 324 KGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNG--------------------EDLSELSIFErsqkVGVVMQNPN 383
Cdd:PRK11288 278 AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidirsprdairagimlcpEDRKAEGIIP----VHSVADNIN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 384 hmIS---HHMIFDEVAFGLRNRGVAEQEIKE---KVENvlelcglskfRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:PRK11288 354 --ISarrHHLRAGCLINNRWEAENADRFIRSlniKTPS----------REQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 515631642 458 EPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIV 505
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVV 468
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-206 |
2.53e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESL-DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEIN-GKNISDFSMHD 80
Cdd:PTZ00265 383 IQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY-----DPTEGDIIINdSHNLKDINLKW 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQVGTVLQDtdSQFVGLSIGEDIAF---------ALENQLVSN-------------------IDMYPLVKSTA----- 127
Cdd:PTZ00265 458 WRSKIGVVSQD--PLLFSNSIKNNIKYslyslkdleALSNYYNEDgndsqenknkrnscrakcaGDLNDMSNTTDsneli 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 128 ------KMVDLADMLDRSP----HD-------------------LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTG 178
Cdd:PTZ00265 536 emrknyQTIKDSEVVDVSKkvliHDfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260
....*....|....*....|....*...
gi 515631642 179 KATIEIIDQLHKETNKTIVIIEHRLEDV 206
Cdd:PTZ00265 616 YLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-223 |
4.96e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.58 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 11 RYESLDKP------TLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaIKGEVTGSLEINGKNISDFSMHD---Y 81
Cdd:PRK10908 3 RFEHVSKAylggrqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-----IERPSAGKIWFSGHDITRLKNREvpfL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQDtDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK10908 78 RRQIGMIFQD-HHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 162 DILLFDEPLASLDpktgKATIEIIDQLHKETNK---TIVIIEHRLEDVLHRDIdRVILMERGEIV 223
Cdd:PRK10908 157 AVLLADEPTGNLD----DALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSY-RMLTLSDGHLH 216
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-224 |
5.21e-11 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 62.66 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTL--------GQ--CLNGLIPHA--------------IKGeVTGSLEINGKNISd 75
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaeGQrrYVESLSAYArqflgqmdkpdvdsIEG-LSPAIAIDQKTTS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 76 fsmHDYTEQVGTVLQDTDsqFVGLsigediafalenqLVSNIdmyPLVKSTAKMVDLAD---MLDRSPHDLSGGQKQRVS 152
Cdd:cd03270 89 ---RNPRSTVGTVTEIYD--YLRL-------------LFARV---GIRERLGFLVDVGLgylTLSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 153 LAGILVDDVD--ILLFDEPLASLDPKTGKATIEIIDQLHKETNkTIVIIEHRLEDVLHrdIDRVILM------ERGEIVA 224
Cdd:cd03270 148 LATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRA--ADHVIDIgpgagvHGGEIVA 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-175 |
5.75e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVtgslEINGKNIS--DFSMH-DYTEQVGTVLQDt 92
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLL-HVESGQI----QIDGKTATrgDRSRFmAYLGHLPGLKAD- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 93 dsqfvgLSIGEDIAF--ALENQLVSNIDmyplvKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:PRK13543 97 ------LSTLENLHFlcGLHGRRAKQMP-----GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....*
gi 515631642 171 ASLDP 175
Cdd:PRK13543 166 ANLDL 170
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-243 |
1.25e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTL-----GQCLNGLIPHAIKgeVTGSLEINGKNISDFSMHDYTEQVGTVLQDTDS 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLlkalaGDLTGGGAPRGAR--VTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 QFvglsigediAFALEnQLVSnIDMYPLVKSTAKM-----------VDLAD---MLDRSPHDLSGGQKQRVSLAGILVD- 159
Cdd:PRK13547 95 AF---------AFSAR-EIVL-LGRYPHARRAGALthrdgeiawqaLALAGataLVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 160 --------DVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEI 231
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDP-NLAARHADRIAMLADGAIVAHGAPADV 242
|
250
....*....|...
gi 515631642 232 LASELLE-THGIR 243
Cdd:PRK13547 243 LTPAHIArCYGFA 255
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-201 |
2.08e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.58 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVtgsleingknisdfsmhdyteqvgtVLQDTDSQFVGL 99
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL-AGRV-------------------------LLNGGPLDFQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAF-----ALENQL--VSNIDMYPLVKSTAKM------VDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:cd03231 70 SIARGLLYlghapGIKTTLsvLENLRFWHADHSDEQVeealarVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....*
gi 515631642 167 DEPLASLDpKTGKATIEIIDQLHKETNKTIVIIEH 201
Cdd:cd03231 150 DEPTTALD-KAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
315-489 |
2.71e-10 |
|
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: 59.97 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD---SGSSYLNGEDLSELSIFERSQKVGVVmQNPNHMishhmi 391
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVS-EEDVHF------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 392 fdevafglrnrgvAEQEIKEKVENVLELCGLSKFRhwpieALSYGQKKRVTIASILVLEPELLILDEPTAGQDyrnytSM 471
Cdd:cd03233 96 -------------PTLTVRETLDFALRCKGNEFVR-----GISGGERKRVSIAEALVSRASVLCWDNSTRGLD-----SS 152
|
170 180
....*....|....*....|...
gi 515631642 472 LAF-----IQKLNRELGITVVII 489
Cdd:cd03233 153 TALeilkcIRTMADVLKTTTFVS 175
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-203 |
2.75e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 61.23 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 30 GEKIVIIGPSGSGKSTLGQCLNG-LIPHAIKGEVTGSLEINGKNISDFSMHDYTEQV--GTVLQDTDSQFVGL------- 99
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPNLGKFDDPPDWDEILDEFRGSELQNYFTKLleGDVKVIVKPQYVDLipkavkg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEdiafalenqLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGK 179
Cdd:cd03236 106 KVGE---------LLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|....
gi 515631642 180 ATIEIIDQLHKETNkTIVIIEHRL 203
Cdd:cd03236 177 NAARLIRELAEDDN-YVLVVEHDL 199
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-220 |
3.35e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) 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: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.56 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIPHAIKGEVTGSLEINGKNISDfsmhDYTEQVGTVLQdTDSQ 95
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTL---LDVLAGRKTAGVITGEILINGRPLDK----NFQRSTGYVEQ-QDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGEDIAFalenqlvsnidmyplvksTAKMvdladmldrspHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:cd03232 91 SPNLTVREALRF------------------SALL-----------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515631642 176 KTGKATIEIIDQLhKETNKTIVIIEHRLEDVLHRDIDRVILMERG 220
Cdd:cd03232 142 QAAYNIVRFLKKL-ADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-244 |
3.77e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.87 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 11 RYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTGSLEINgknisdfsmhdYTEQVGTVLQ 90
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF-EISEGRVWAERSIA-----------YVPQQAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 91 DTdsqfvglsIGEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLD----RSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PTZ00243 735 AT--------VRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLEteigEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 167 DEPLASLDPKTGKATIE--IIDQLHketNKTIVIIEHRLEDVLHrdIDRVILMERGEIV-----ADM--TP-DEILASEL 236
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEecFLGALA---GKTRVLATHQVHVVPR--ADYVVALGDGRVEfsgssADFmrTSlYATLAAEL 881
|
....*...
gi 515631642 237 LETHGIRE 244
Cdd:PTZ00243 882 KENKDSKE 889
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
20-208 |
4.55e-10 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 59.72 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEINGKNISDFSMHDyteqVGtVLQDTDSQFVGL 99
Cdd:TIGR03740 16 VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGIL-----RPTSGEIIFDGHPWTRKDLHK----IG-SLIESPPLYENL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SigediafALENQLVSNIdMYPLVKSTA----KMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:TIGR03740 86 T-------ARENLKVHTT-LLGLPDSRIdevlNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDP 157
|
170 180 190
....*....|....*....|....*....|...
gi 515631642 176 KTGKATIEIIdQLHKETNKTIVIIEHRLEDVLH 208
Cdd:TIGR03740 158 IGIQELRELI-RSFPEQGITVILSSHILSEVQQ 189
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
315-506 |
5.32e-10 |
|
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: 62.66 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPNhMISHHMIFDE 394
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPV-LFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 395 VAFGlrnrgvaeQEIKEKVENVLELCGLSKF-RHWPI----------EALSYGQKKRVTIASILVLEPELLILDEPTAGQ 463
Cdd:TIGR00957 1381 DPFS--------QYSDEEVWWALELAHLKTFvSALPDkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515631642 464 DYRNYTSMLAFIQKLNRElgITVVIISHDMHLVLEYtTRSIVI 506
Cdd:TIGR00957 1453 DLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDY-TRVIVL 1492
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-223 |
9.14e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.33 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKgEVTGSLEINGKNISDFSMHDYTeqVGTVLQDTDSQ 95
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVR-QTAGRVLLDGKPVAPCALRGRK--IATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGL-SIGediAFALENQLV----SNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:PRK10418 92 FNPLhTMH---THARETCLAlgkpADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515631642 171 ASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLeDVLHRDIDRVILMERGEIV 223
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDM-GVVARLADDVAVMSHGRIV 220
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-496 |
9.18e-10 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 61.57 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 136 LDRSPHDLSGGQKQRVSLA--------GILVddvdILlfDEPLASLDPKTGKATIEIIDQLHKETNkTIVIIEHRLEDVL 207
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLAtqigsgltGVLY----VL--DEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHDEDTIR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 208 HrdIDRVILM------ERGEIVADMTPDEILASELLEThgirePLYLSALKAAKAPltsedklsnlkaldykrfrpavqa 281
Cdd:TIGR00630 555 A--ADYVIDIgpgageHGGEVVASGTPEEILANPDSLT-----GQYLSGRKKIEVP------------------------ 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 282 wfAERpTPVAEKQyqplLEVHGltysydGEKNALEDVSFKIGKGEFVSILGKNGSGKSTitkLIMGVIdADSGSSYLNG- 360
Cdd:TIGR00630 604 --AER-RPGNGKF----LTLKG------ARENNLKNITVSIPLGLFTCITGVSGSGKST---LINDTL-YPALANRLNGa 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 361 --EDLSELSI--FERSQKVGVVMQNP-----------------------------------------------------N 383
Cdd:TIGR00630 667 ktVPGRYTSIegLEHLDKVIHIDQSPigrtprsnpatytgvfdeirelfaetpeakvrgytpgrfsfnvkggrceacqgD 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 384 HMISHHMIFD-------EVAFGLR-NRGVAEQEIKEK-VENVLE----------------------LC--GLSKFR-HWP 429
Cdd:TIGR00630 747 GVIKIEMHFLpdvyvpcEVCKGKRyNRETLEVKYKGKnIADVLDmtveeayeffeavpsisrklqtLCdvGLGYIRlGQP 826
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 430 IEALSYGQKKRVTIASIL---VLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLV 496
Cdd:TIGR00630 827 ATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVI 895
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-174 |
1.44e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 7 NFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTGSLEINgknisdfsmhdyteqVG 86
Cdd:PRK15064 324 NLTKGFD--NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPD-SGTVKWSENAN---------------IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 87 TVLQDTDSQFvglsiGEDIA-FALENQLVSNIDMYPLVKST-AKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:PRK15064 386 YYAQDHAYDF-----ENDLTlFDWMSQWRQEGDDEQAVRGTlGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170
....*....|
gi 515631642 165 LFDEPLASLD 174
Cdd:PRK15064 461 VMDEPTNHMD 470
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
299-530 |
1.51e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.08 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNA-LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADsGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAvLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQ-------------NPNHMISHHMIF---DEVafGLRNrgVAEQeIKEKVENVLELCGLskfrhwpieALSYGQKKRV 441
Cdd:TIGR01271 1297 IPQkvfifsgtfrknlDPYEQWSDEEIWkvaEEV--GLKS--VIEQ-FPDKLDFVLVDGGY---------VLSNGHKQLM 1362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 442 TIASILVLEPELLILDEPTAGQDYRNYtsmlafiQKLNREL-----GITVVIISHDMHLVLEyTTRSIVIADSKLIANAA 516
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTL-------QIIRKTLkqsfsNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDS 1434
|
250
....*....|....
gi 515631642 517 MTEVFSQPSLLERA 530
Cdd:TIGR01271 1435 IQKLLNETSLFKQA 1448
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
298-505 |
1.61e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSylngedlselsIFERSQKVGV 377
Cdd:PRK11147 3 LISIHGAWLSF-SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-----------IYEQDLIVAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPN-------------------------HMISHHMIFDEVAFGLrNRGVAEQEIKE---------KVENVLELCGLS 423
Cdd:PRK11147 71 LQQDPPrnvegtvydfvaegieeqaeylkryHDISHLVETDPSEKNL-NELAKLQEQLDhhnlwqlenRINEVLAQLGLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 424 KfrHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIqklnRELGITVVIISHDMHLVLEYTTRs 503
Cdd:PRK11147 150 P--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHDRSFIRNMATR- 222
|
..
gi 515631642 504 IV 505
Cdd:PRK11147 223 IV 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-202 |
1.67e-09 |
|
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: 56.78 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFrYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEIngknisdfsmhdyt 82
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-----SGRIGM-------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 83 eqvgtvLQDTDSQFVG----LSIGediafALENQLVsnidmYPLvkstaKMVdladmldrsphdLSGGQKQRVSLAGILV 158
Cdd:cd03223 61 ------PEGEDLLFLPqrpyLPLG-----TLREQLI-----YPW-----DDV------------LSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515631642 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHketnKTIVIIEHR 202
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGHR 147
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-209 |
2.00e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVT------GSleinGKNISDF---------SMH- 79
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTlfgrrrGS----GETIWDIkkhigyvssSLHl 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 DYteQVGTVLQDTD-SQFVGlSIGEDIAFALENQLVSN--IDMYPLVKSTAKmvdladmldrSP-HDLSGGQKQRVSLAG 155
Cdd:PRK10938 348 DY--RVSTSVRNVIlSGFFD-SIGIYQAVSDRQQKLAQqwLDILGIDKRTAD----------APfHSLSWGQQRLALIVR 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLED----VLHR 209
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDapacITHR 472
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
299-530 |
2.27e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 58.71 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADsGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQ-------------NPNHMISHHMIF---DEVafGLRNrgVAEQeIKEKVENVLELCGLskfrhwpieALSYGQKKRV 441
Cdd:cd03289 82 IPQkvfifsgtfrknlDPYGKWSDEEIWkvaEEV--GLKS--VIEQ-FPGQLDFVLVDGGC---------VLSHGHKQLM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 442 TIASILVLEPELLILDEPTAGQDYRNYtsmlafiQKLNREL-----GITVVIISHDMHLVLEyTTRSIVIADSKLIANAA 516
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITY-------QVIRKTLkqafaDCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDS 219
|
250
....*....|....
gi 515631642 517 MTEVFSQPSLLERA 530
Cdd:cd03289 220 IQKLLNEKSHFKQA 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-239 |
2.90e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 14 SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQ-VGTVlqdT 92
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA-----GGEIRLNGKDISPRSPLDAVKKgMAYI---T 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 93 DSQ-----FVGLSIGEDIAFA--LENQ-------LVSNIDMYPLVKSTAKMVDL-ADMLDRSPHDLSGGQKQRVSLAGIL 157
Cdd:PRK09700 345 ESRrdngfFPNFSIAQNMAISrsLKDGgykgamgLFHEVDEQRTAENQRELLALkCHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 158 VDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVA------DMTPDEI 231
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITV-CDRIAVFCEGRLTQiltnrdDMSEEEI 502
|
....*...
gi 515631642 232 LASELLET 239
Cdd:PRK09700 503 MAWALPQE 510
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-231 |
3.03e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 17 KPTLKNINLRIEKGEkIV-IIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQ-VGTVLQdtDS 94
Cdd:COG3845 271 VPALKDVSLEVRAGE-ILgIAGVAGNGQSELAEALAGLRPPA-----SGSIRLDGEDITGLSPRERRRLgVAYIPE--DR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 95 QFVGLSIGEDIAfalENQLVSNIDMYPLVK----STAKMVDLADML----D---RSPHD----LSGGQKQRVSLAGILVD 159
Cdd:COG3845 343 LGRGLVPDMSVA---ENLILGRYRRPPFSRggflDRKAIRAFAEELieefDvrtPGPDTparsLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 160 DVDILLFDEPLASLDPktgKATIEIIDQL--HKETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEI 231
Cdd:COG3845 420 DPKLLIAAQPTRGLDV---GAIEFIHQRLleLRDAGAAVLLISEDLDEIL--ALsDRIAVMYEGRIVGEVPAAEA 489
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-232 |
8.64e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.47 E-value: 8.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAikgevtGSLEINGKNISDFSMHDYTEQVGTVLQDTDSQFV--- 97
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDA------GEVHYRMRDGQLRDLYALSEAERRRLLRTEWGFVhqh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 98 ---GL----SIGEDIAfalENQLVSNIDMYPLVKSTA----KMVDL-ADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK11701 98 prdGLrmqvSAGGNIG---ERLMAVGARHYGDIRATAgdwlERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 166 FDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEdVLHRDIDRVILMERGEIVADMTPDEIL 232
Cdd:PRK11701 175 MDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLA-VARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-238 |
9.79e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTgsleINGknisdfsmhdytEQVGTVLQDTDSQFVGL 99
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV-RLASGKIS----ILG------------QPTRQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 SIGEDIAFALenqLVSNIDM-----------------YPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK15056 86 SEEVDWSFPV---LVEDVVMmgryghmgwlrrakkrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 163 ILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDEILASELLE 238
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSV--TEFCDYTVMVKGTVLASGPTETTFTAENLE 235
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-218 |
9.92e-09 |
|
ATP-binding cassette domain 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 more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.89 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 27 IEKGEKIVIIGPSGSGKSTLGQCLngliphaikgevTGSLEINGKNISdfsmhdyteqvgtvlqdtdsqfvglsigedia 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKIL------------AGQLIPNGDNDE-------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 107 falenqlvsnidmYPLVKSTAKmvdladmldrsPH--DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEI 184
Cdd:cd03222 58 -------------WDGITPVYK-----------PQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|....*.
gi 515631642 185 IDQLHKETNKTIVIIEHrleDVLHRDI--DRVILME 218
Cdd:cd03222 114 IRRLSEEGKKTALVVEH---DLAVLDYlsDRIHVFE 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
287-513 |
1.08e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 287 PTPVAEKQYQP-LLEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLS 364
Cdd:PTZ00243 1296 PTSAAPHPVQAgSLVFEGVQMRYrEGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 365 ELSIFERSQKVGVVMQNPnhmishhMIFD----------------EV-----AFGLRNRGVAEQE-IKEKvenVLElcGL 422
Cdd:PTZ00243 1376 AYGLRELRRQFSMIPQDP-------VLFDgtvrqnvdpfleassaEVwaaleLVGLRERVASESEgIDSR---VLE--GG 1443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 423 SKFrhwpiealSYGQKKRVTIASILVLEPELLIL-DEPTAGQDYR-----NYTSMLAFIqklnrelGITVVIISHDMHLV 496
Cdd:PTZ00243 1444 SNY--------SVGQRQLMCMARALLKKGSGFILmDEATANIDPAldrqiQATVMSAFS-------AYTVITIAHRLHTV 1508
|
250
....*....|....*..
gi 515631642 497 LEYTtrSIVIADSKLIA 513
Cdd:PTZ00243 1509 AQYD--KIIVMDHGAVA 1523
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-234 |
1.37e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVT--GSlEINGKNIS----------DFSMhdYTEQvgTVL 89
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP-ASEGEAWlfGQ-PVDAGDIAtrrrvgymsqAFSL--YGEL--TVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 90 QDTD--SQFVGLSiGEDIAfalenqlvsnidmyPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:NF033858 358 QNLElhARLFHLP-AAEIA--------------ARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631642 168 EPLASLDPKTGKATIEIIDQLHKETNKTIVIIEH------RledvlhrdIDRVILMERGEIVADMTPDEILAS 234
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSREDGVTIFISTHfmneaeR--------CDRISLMHAGRVLASDTPAALVAA 487
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
300-464 |
1.42e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 300 EVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSE-------------- 365
Cdd:NF033858 3 RLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADarhrravcpriaym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 366 -----------LSIFErsqkvgvvmqnpNhmishhmifdeVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALS 434
Cdd:NF033858 82 pqglgknlyptLSVFE------------N-----------LDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLS 138
|
170 180 190
....*....|....*....|....*....|
gi 515631642 435 YGQKKRVTIASILVLEPELLILDEPTAGQD 464
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-220 |
2.02e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIPHAIKGEVTGSLEINGKNISDFSMhdytEQVGTVLQDtDSQ 95
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTL---LNALAGRIQGNNFTGTILANNRKPTKQIL----KRTGFVTQD-DIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 96 FVGLSIGEDIAFA----LENQLvSNIDMYPLVKSTAKMVDLAD-----MLDRSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PLN03211 152 YPHLTVRETLVFCsllrLPKSL-TKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515631642 167 DEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHRDIDRVILMERG 220
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-252 |
2.37e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqclngLIPHAIKGEVT-GSLEINGKNISDFSMHD 80
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTL------LLTFMRMVEVCgGEIRVNGREIGAYGLRE 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 81 YTEQV-----------GTVLQDTDSqFVGLSIGEDIAfALEnqLVSnidMYPLVKSTAKMVDlADMLDrSPHDLSGGQKQ 149
Cdd:PTZ00243 1382 LRRQFsmipqdpvlfdGTVRQNVDP-FLEASSAEVWA-ALE--LVG---LRERVASESEGID-SRVLE-GGSNYSVGQRQ 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 150 RVSLA-GILVDDVDILLFDEPLASLDP---KTGKATIeiidqLHKETNKTIVIIEHRLEDVLHrdIDRVILMERGeIVAD 225
Cdd:PTZ00243 1453 LMCMArALLKKGSGFILMDEATANIDPaldRQIQATV-----MSAFSAYTVITIAHRLHTVAQ--YDKIIVMDHG-AVAE 1524
|
250 260
....*....|....*....|....*...
gi 515631642 226 M-TPDEILASELLETHGIREPLYLSALK 252
Cdd:PTZ00243 1525 MgSPRELVMNRQSIFHSMVEALGRSEAK 1552
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
315-523 |
2.44e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPNhMISHHMIFDE 394
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPV-LFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 395 VAFGLRN-----RGVAEQEIKEKVENvlELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRnyt 469
Cdd:PLN03232 1331 DPFSEHNdadlwEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR--- 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515631642 470 sMLAFIQKLNRE--LGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQ 523
Cdd:PLN03232 1406 -TDSLIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
302-492 |
2.72e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 302 HGLTYSYDGEKNALEDV--SF----KIGkgefvsILGKNGSGKSTITKlIMGVIDADSgssylNGEdlselSIFERSQKV 375
Cdd:PRK11819 10 NRVSKVVPPKKQILKDIslSFfpgaKIG------VLGLNGAGKSTLLR-IMAGVDKEF-----EGE-----ARPAPGIKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNP----------NHM---------------ISHHM-----IFDEVAfglrnrgvAEQeikEKVENVLELCGLSKF 425
Cdd:PRK11819 73 GYLPQEPqldpektvreNVEegvaevkaaldrfneIYAAYaepdaDFDALA--------AEQ---GELQEIIDAADAWDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 426 RH---------------WPIEALSYGQKKRVTIASILVLEPELLILDEPTagqdyrNY---TSMLAFIQKLNRELGiTVV 487
Cdd:PRK11819 142 DSqleiamdalrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT------NHldaESVAWLEQFLHDYPG-TVV 214
|
....*
gi 515631642 488 IISHD 492
Cdd:PRK11819 215 AVTHD 219
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-202 |
2.99e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 7 NFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHaikgevTGSLEINGKNIsDFSMHDYTEQV 85
Cdd:PRK13540 6 ELDFDYH--DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPE------KGEILFERQSI-KKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 86 GTVLQDTDSQfVGLSIGEDIAFALENQlVSNIDMYPLVKstakMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK13540 77 CFVGHRSGIN-PYLTLRENCLYDIHFS-PGAVGITELCR----LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 515631642 166 FDEPLASLDPKTGKATIEIIdQLHKETNKTIVIIEHR 202
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKI-QEHRAKGGAVLLTSHQ 186
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
299-523 |
3.19e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 54.91 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGE-KNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03288 20 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnhmishhMIFD-EVAFGLR-NRGVAEQEIKEKVE-----NVLELC--GLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:cd03288 100 ILQDP-------ILFSgSIRFNLDpECKCTDDRLWEALEiaqlkNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 449 LEPELLILDEPTAGQDYR-----NYTSMLAFIQKlnrelgiTVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQ 523
Cdd:cd03288 173 RKSSILIMDEATASIDMAtenilQKVVMTAFADR-------TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
298-464 |
3.26e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 298 LLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID--ADSGSSYLNGEDLSELSIFERSQKv 375
Cdd:PRK09580 1 MLSIKDLHVSVED-KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRAGE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVM--QNPNHM--ISHHMIFDEVAFGLRN-RGVAEQE-------IKEKVEnVLELCGLSKFRHWPIeALSYGQKKRVTI 443
Cdd:PRK09580 79 GIFMafQYPVEIpgVSNQFFLQTALNAVRSyRGQEPLDrfdfqdlMEEKIA-LLKMPEDLLTRSVNV-GFSGGEKKRNDI 156
|
170 180
....*....|....*....|.
gi 515631642 444 ASILVLEPELLILDEPTAGQD 464
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLD 177
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
16-238 |
3.26e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGevtGSLEINGKNISDFSMHDYT-EQVGTVLQ---- 90
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTG---GTVEFKGKDLLELSPEDRAgEGIFMAFQypve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 91 --DTDSQFVGLSIGEDIAFALENQLVSNIDMYPLVKSTAKMVDL-ADMLDRSPH-DLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PRK09580 90 ipGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515631642 167 DEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEH--RLEDVLHRDIdrVILMERGEIVAdmTPDEILASELLE 238
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHyqRILDYIKPDY--VHVLYQGRIVK--SGDFTLVKQLEE 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
303-513 |
3.66e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 303 GLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFER-SQKVGVVMQN 381
Cdd:PRK10982 3 NISKSFPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAlENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 382 PNhMISHHMIFDEVAFG---LRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:PRK10982 82 LN-LVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 459 PTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-238 |
5.42e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 14 SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaIKGEVTGSLEINGKNISDFSMHDYTEQvGTVLQDTD 93
Cdd:PRK10982 258 SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG-----IREKSAGTITLHGKKINNHNANEAINH-GFALVTEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 94 SQFVGLSIGEDIAFaleNQLVSNIDMYP----LVKSTAKMVDLADMLD----RSPH------DLSGGQKQRVSLAGILVD 159
Cdd:PRK10982 332 RRSTGIYAYLDIGF---NSLISNIRNYKnkvgLLDNSRMKSDTQWVIDsmrvKTPGhrtqigSLSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 160 DVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILASELLE 238
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGI-TDRILVMSNGLVAGIVDTKTTTQNEILR 485
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
131-234 |
5.98e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.81 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 131 DLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEdVLHRD 210
Cdd:PRK15093 147 DHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQ-MLSQW 225
|
90 100
....*....|....*....|....
gi 515631642 211 IDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK15093 226 ADKINVLYCGQTVETAPSKELVTT 249
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
306-505 |
7.10e-08 |
|
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: 53.57 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 306 YSYDGEKNALEDVSFKIGKGEF-----VSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLS----ELSIFERSQKVG 376
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 VVMQNPNHMISHHMIFDEVAFGLRNRGVAEQEIKEkvenvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLIL 456
Cdd:cd03237 81 LLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPE---------------------LSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515631642 457 DEPTAGQDYRNYTSMLAFIQKLNRELGITVVIISHDMHLVLEYTTRSIV 505
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
315-466 |
7.30e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTItkliMGVIDADSGSSYLNGEdlSELSIFERSQKV-----GVVMQN----PNHM 385
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTL----MDVLAGRKTGGYIEGD--IRISGFPKKQETfarisGYCEQNdihsPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 386 ISHHMIFDevAFGLRNRGVAEQEIKEKVENVLELCGLSKFRH----WP-IEALSYGQKKRVTIASILVLEPELLILDEPT 460
Cdd:PLN03140 970 VRESLIYS--AFLRLPKEVSKEEKMMFVDEVMELVELDNLKDaivgLPgVTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
....*.
gi 515631642 461 AGQDYR 466
Cdd:PLN03140 1048 SGLDAR 1053
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
315-491 |
9.35e-08 |
|
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: 55.14 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLngedlselsifERSQKVGVVMQNP---NHMISHHMI 391
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK-----------PAKGKLFYVPQRPymtLGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 392 FDEVAFGLRNRGVAEQEIKEKVENV------LELCGLSKFRHWpIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDy 465
Cdd:TIGR00954 537 YPDSSEDMKRRGLSDKDLEQILDNVqlthilEREGGWSAVQDW-MDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS- 614
|
170 180
....*....|....*....|....*.
gi 515631642 466 rnyTSMLAFIQKLNRELGITVVIISH 491
Cdd:TIGR00954 615 ---VDVEGYMYRLCREFGITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-183 |
1.18e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 3 IAFSNFSFRYESldKPTL-KNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPhaIKGEVTGSLEIngkNISDFSMH- 79
Cdd:PLN03073 509 ISFSDASFGYPG--GPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQP--SSGTVFRSAKV---RMAVFSQHh 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 80 -DYTEQVGTVLQDTDSQFVGlsigediafALENQLVSNIDMYPLVKSTAkmvdLADMldrspHDLSGGQKQRVSLAGILV 158
Cdd:PLN03073 582 vDGLDLSSNPLLYMMRCFPG---------VPEQKLRAHLGSFGVTGNLA----LQPM-----YTLSGGQKSRVAFAKITF 643
|
170 180
....*....|....*....|....*
gi 515631642 159 DDVDILLFDEPLASLDPKTGKATIE 183
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDAVEALIQ 668
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
299-493 |
1.33e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNA--LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLN-GEDLSELSIFERSQKV 375
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 376 GVVMQNPnhMISHHMIFDEVAFGL-------------RNRGVAEQEIKEKVENVLELC--------------GLSKFR-- 426
Cdd:PTZ00265 463 GVVSQDP--LLFSNSIKNNIKYSLyslkdlealsnyyNEDGNDSQENKNKRNSCRAKCagdlndmsnttdsnELIEMRkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 427 ------------------HWPIEA---------------LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLA 473
Cdd:PTZ00265 541 yqtikdsevvdvskkvliHDFVSAlpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260
....*....|....*....|
gi 515631642 474 FIQKLNRELGITVVIISHDM 493
Cdd:PTZ00265 621 TINNLKGNENRITIIIAHRL 640
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-223 |
1.46e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTGSLEINGKNISDFSMHdY 81
Cdd:TIGR00956 59 TRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNT-DGFHIGVEGVITYDGITPEEIKKH-Y 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 82 TEQVGTVLQdTDSQFVGLSIGEDIAFALENQLVSN-IDMYPLVKSTAKMVDLA----------------DMLdrspHDLS 144
Cdd:TIGR00956 137 RGDVVYNAE-TDVHFPHLTVGETLDFAARCKTPQNrPDGVSREEYAKHIADVYmatyglshtrntkvgnDFV----RGVS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDPKTgkaTIEIIDQLH---KETNKTIVIIEHRLEDVLHRDIDRVILMERGE 221
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSAT---ALEFIRALKtsaNILDTTPLVAIYQCSQDAYELFDKVIVLYEGY 288
|
..
gi 515631642 222 IV 223
Cdd:TIGR00956 289 QI 290
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
310-494 |
2.93e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGS-SYLNGEDLSELS----IFERSQKVGVVMQ---- 380
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNvSLDPNERLGKLRqdqfAFEEFTVLDTVIMghte 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 381 -------------NPNhmishhMIFDEvafGLRnrgVAEQEIK-----------EKVENVLELcGLSKFRHW-PIEALSY 435
Cdd:PRK15064 92 lwevkqerdriyaLPE------MSEED---GMK---VADLEVKfaemdgytaeaRAGELLLGV-GIPEEQHYgLMSEVAP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515631642 436 GQKKRVTIASILVLEPELLILDEPTAGQDYrNYTSMLAfiQKLNrELGITVVIISHDMH 494
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDI-NTIRWLE--DVLN-ERNSTMIIISHDRH 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
315-464 |
3.00e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMG-----VIDADSGSSYlNGEDLSELsifeRSQKVGVVM---QNPNHmI 386
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgfHIGVEGVITY-DGITPEEI----KKHYRGDVVynaETDVH-F 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 387 SHHMIFDEVAF-------GLRNRGVAEQEIKEKVENV-LELCGLSKFRHWP-----IEALSYGQKKRVTIASILVLEPEL 453
Cdd:TIGR00956 151 PHLTVGETLDFaarcktpQNRPDGVSREEYAKHIADVyMATYGLSHTRNTKvgndfVRGVSGGERKRVSIAEASLGGAKI 230
|
170
....*....|.
gi 515631642 454 LILDEPTAGQD 464
Cdd:TIGR00956 231 QCWDNATRGLD 241
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-183 |
3.50e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISdfsmhdytEQVGTVLQDTdsQFVG--- 98
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPD-----AGEVLWQGEPIR--------RQRDEYHQDL--LYLGhqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 -----LSIGEDIAFALenQLVSNIDMYPLVKSTAKmVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:PRK13538 84 gikteLTALENLRFYQ--RLHGPGDDEALWEALAQ-VGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170
....*....|
gi 515631642 174 DpKTGKATIE 183
Cdd:PRK13538 161 D-KQGVARLE 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
299-491 |
4.19e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNA--LEDVSFKIGKGEFVSILGKNGSGKSTITKLIM------------------------------ 346
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 347 -----GVIDADSGSSYLNGEDLSELSIFERSQKV-------------------GVVMQNPnhMISHHMIFDEVAFGlrnr 402
Cdd:PTZ00265 1246 eeqnvGMKNVNEFSLTKEGGSGEDSTVFKNSGKIlldgvdicdynlkdlrnlfSIVSQEP--MLFNMSIYENIKFG---- 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 403 gvAEQEIKEKVENVLELCGLSKFrhwpIEAL---------------SYGQKKRVTIASILVLEPELLILDEPTAGQDYRN 467
Cdd:PTZ00265 1320 --KEDATREDVKRACKFAAIDEF----IESLpnkydtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
250 260
....*....|....*....|....
gi 515631642 468 YTSMLAFIQKLNRELGITVVIISH 491
Cdd:PTZ00265 1394 EKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-238 |
5.35e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTgsleINGKNISDFSMHDYTEQvGTVLQDTDSQFVG--- 98
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIF----IDGKPVKIRNPQQAIAQ-GIAMVPEDRKRDGivp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 99 -LSIGEDIAFALENQLV--SNIDmyplvkSTAKMVDLADMLDR------SPH----DLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK13549 355 vMGVGKNITLAALDRFTggSRID------DAAELKTILESIQRlkvktaSPElaiaRLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 166 FDEPLASLDpkTG-KATI-EIIDQLHKEtNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEILASELLE 238
Cdd:PRK13549 429 LDEPTRGID--VGaKYEIyKLINQLVQQ-GVAIIVISSELPEVLGLS-DRVLVMHEGKLKGDLINHNLTQEQVME 499
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
315-491 |
6.02e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPNhMISHHMIFDE 394
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPV-LFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 395 VAFGLRNrgvaEQEIKEKVE----------NVLelcGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQD 464
Cdd:PLN03130 1334 DPFNEHN----DADLWESLErahlkdvirrNSL---GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180
....*....|....*....|....*....
gi 515631642 465 YRNYtsmlAFIQKLNRE--LGITVVIISH 491
Cdd:PLN03130 1407 VRTD----ALIQKTIREefKSCTMLIIAH 1431
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-496 |
6.58e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.52 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 136 LDRSPHDLSGGQKQRVSLAGILVDDVD--ILLFDEPLASLDPKTGKATIEIIDQLHKETNkTIVIIEHrlEDVLHRDIDR 213
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEH--DEQMISLADR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 214 VILMER------GEIVADMTPDEILASEllethgireplylSALKAAKapltsedkLSNLKALDYKRFRPAVQAWfaerp 287
Cdd:PRK00635 547 IIDIGPgagifgGEVLFNGSPREFLAKS-------------DSLTAKY--------LRQELTIPIPEKRTNSLGT----- 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 288 tpvaekqyqpllevhgLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKS-----TITKLIMGVIDADSGSS-YLNGE 361
Cdd:PRK00635 601 ----------------LTLSK-ATKHNLKDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFIEQGFCSNlSIQWG 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 362 DLSEL-------------SI-------FE----------RSQKVGV------------------------VMQN------ 381
Cdd:PRK00635 664 AISRLvhitrdlpgrsqrSIpltyikaFDdlrelfaeqpRSKRLGLtkshfsfntplgacaecqglgsitTTDNrtsipc 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 382 ---------PNHMISHHM------IFDEVAFGLRNRGVAEQEIKEKVEnvlELCGLSkFRHWPI----EALSYGQKKRVT 442
Cdd:PRK00635 744 psclgkrflPQVLEVRYKgkniadILEMTAYEAEKFFLDEPSIHEKIH---ALCSLG-LDYLPLgrplSSLSGGEIQRLK 819
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515631642 443 IASIL---VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNrELGITVVIISHDMHLV 496
Cdd:PRK00635 820 LAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLT-HQGHTVVIIEHNMHVV 875
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-239 |
3.17e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 10 FRYESLDKPTLKN-INLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISDFSMHDYTEQvGT 87
Cdd:PRK11288 258 LRLDGLKGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATrRTA------GQVYLDGKPIDIRSPRDAIRA-GI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 88 VLQDTDSQFVGL----SIGEDIafalenqlvsNIDMYPLvKSTAKMV-------DLAD-----MLDRSPH------DLSG 145
Cdd:PRK11288 331 MLCPEDRKAEGIipvhSVADNI----------NISARRH-HLRAGCLinnrweaENADrfirsLNIKTPSreqlimNLSG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 146 GQKQRVSLAGILVDDVDILLFDEPLASLDpkTGkATIEIIDQLHK--ETNKTIVIIEHRLEDVLHRDiDRVILMERGEIV 223
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGID--VG-AKHEIYNVIYElaAQGVAVLFVSSDLPEVLGVA-DRIVVMREGRIA 475
|
250 260
....*....|....*....|.
gi 515631642 224 -----ADMTPDEILASELLET 239
Cdd:PRK11288 476 gelarEQATERQALSLALPRT 496
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-206 |
4.10e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 2 TIAFSNFSFRYESLDKP------------------TLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHaikgev 62
Cdd:PRK13545 4 KVKFEHVTKKYKMYNKPfdklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPN------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 63 TGSLEINGKnisdfsmhdyteqvgtvlqdtdSQFVGLSIGediafaLENQL--VSNID----MYPLVKS-----TAKMVD 131
Cdd:PRK13545 78 KGTVDIKGS----------------------AALIAISSG------LNGQLtgIENIElkglMMGLTKEkikeiIPEIIE 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 132 LADM---LDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhKETNKTIVIIEHRLEDV 206
Cdd:PRK13545 130 FADIgkfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQV 206
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
15-219 |
4.11e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.60 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 15 LDKPTLKNI-----NLRIEKGEKI-VIIGPSGSGKSTLGQCL--------------NGLIPHAI-KGEVTGSLEINGKNI 73
Cdd:cd03240 1 IDKLSIRNIrsfheRSEIEFFSPLtLIVGQNGAGKTTIIEALkyaltgelppnskgGAHDPKLIrEGEVRAQVKLAFENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 74 SDfsmHDYTeqvgtVLQDtdsqfvgLSIGEDIAFalenqlVSNIDMYPLvkstakmvdLADMLDRsphdLSGGQKQ---- 149
Cdd:cd03240 81 NG---KKYT-----ITRS-------LAILENVIF------CHQGESNWP---------LLDMRGR----CSGGEKVlasl 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631642 150 --RVSLAGILVDDVDILLFDEPLASLDP-KTGKATIEIIDQLHKETNKTIVIIEH--RLEDVlhrdIDRVILMER 219
Cdd:cd03240 127 iiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHdeELVDA----ADHIYRVEK 197
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-204 |
5.19e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLgqCLNGLIPHAIKgevtgsleingKNISDFSMHDYTEQVgtvlqdtdsqFVGl 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKA-----------RLISFLPKFSRNKLI----------FID- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 sigediafalenQLVSNIDMyplvkstakmvDLADM-LDRSPHDLSGGQKQRVSLAGILVDDVD--ILLFDEPLASLDPK 176
Cdd:cd03238 67 ------------QLQFLIDV-----------GLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180
....*....|....*....|....*...
gi 515631642 177 TGKATIEIIDQLHKETNkTIVIIEHRLE 204
Cdd:cd03238 124 DINQLLEVIKGLIDLGN-TVILIEHNLD 150
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-46 |
5.30e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 49.64 E-value: 5.30e-06
10 20
....*....|....*....|....*..
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
299-491 |
9.45e-06 |
|
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: 45.99 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGS-SYLNGEDLselsIFersqkvgv 377
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRiGMPEGEDL----LF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 378 VMQNPnHMIShhmifdevafG-LRnrgvaEQeikekvenvleLCglskfRHWPiEALSYGQKKRVTIASILVLEPELLIL 456
Cdd:cd03223 69 LPQRP-YLPL----------GtLR-----EQ-----------LI-----YPWD-DVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*
gi 515631642 457 DEPTAGQDyrnyTSMLAFIQKLNRELGITVVIISH 491
Cdd:cd03223 116 DEATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
315-459 |
9.82e-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: 48.75 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSsylngedlselsiFERSQKVGVVMQNPnhMISHHMIFDE 394
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK-------------IKHSGRISFSPQTS--WIMPGTIKDN 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 395 VAFGL-----RNRGVA-----EQEIK---EKVENVLELCGLSkfrhwpieaLSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:TIGR01271 507 IIFGLsydeyRYTSVIkacqlEEDIAlfpEKDKTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSP 575
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-221 |
1.02e-05 |
|
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: 45.83 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 29 KGEKIVIIGPSGSGKSTLGQCLNGLIphaiKGEVTGSLEINGKNISDfsmhdyteqvgtvlqdtdsqfvglsigediafa 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAREL----GPPGGGVIYIDGEDILE--------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 109 lenqlvsnidmyplvksTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIID-- 186
Cdd:smart00382 44 -----------------EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515631642 187 ---QLHKETNKTIVIIEHRLEDVLHRDI----DRVILMERGE 221
Cdd:smart00382 107 lllLLKSEKNLTVILTTNDEKDLGPALLrrrfDRRIVLLLIL 148
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
315-459 |
1.11e-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: 47.54 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEdlselsiFERSQKVGVVMQNpnhmishhMIFDE 394
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------ISFSSQFSWIMPG--------TIKEN 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 395 VAFGL-----RNRGVA-----EQEIK---EKVENVLELCGLSkfrhwpieaLSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:cd03291 118 IIFGVsydeyRYKSVVkacqlEEDITkfpEKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSP 186
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-245 |
1.32e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.30 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKgeVTGSLEINGKNISDF---------SMHDYTEQVGTVLQ 90
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLK--VSGEITYNGYRLNEFvprktsayiSQNDVHVGVMTVKE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 91 DTDsqFVGLSIGEDIAFALENQLVS-----------NIDMYplVKSTA--------------KMVDL---ADML--DRSP 140
Cdd:PLN03140 259 TLD--FSARCQGVGTRYDLLSELARrekdagifpeaEVDLF--MKATAmegvksslitdytlKILGLdicKDTIvgDEMI 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 141 HDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIVIIEHRLEDVLHRDIDRVILMERG 220
Cdd:PLN03140 335 RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILLSEG 414
|
250 260
....*....|....*....|....*
gi 515631642 221 EIVADMTPDEILasELLETHGIREP 245
Cdd:PLN03140 415 QIVYQGPRDHIL--EFFESCGFKCP 437
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-204 |
1.63e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.43 E-value: 1.63e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 141 HDLSGGQKQRVSLAGIL----VDDVDILLFDEPLASLDPKTGKATIEIIDQLHKETNKTIViIEHRLE 204
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPE 142
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
299-494 |
1.77e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.17 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK---- 374
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 375 VGVVMQNP---NHMISHHMIFDEVAFGLRNRGVAEQEIKEKVENVLELCGLSKFRHWPIEaLSYGQKKRVTIASILVLEP 451
Cdd:cd03290 81 VAYAAQKPwllNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515631642 452 ELLILDEPTAGQD-YRNYTSMLAFIQKLNRELGITVVIISHDMH 494
Cdd:cd03290 160 NIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
312-496 |
3.54e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.68 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 312 KNALEDVSFKIGKGEFVSILGKNGSGKST-ITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQ---------N 381
Cdd:cd03271 8 ENNLKNIDVDIPLGVLTCVTGVSGSGKSSlINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQspigrtprsN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 382 PNHMIShhmIFD-------EVAFGLR-NRGVAEQEIKEK-VENVLELC---GLSKFRHWP-----IEA------------ 432
Cdd:cd03271 88 PATYTG---VFDeirelfcEVCKGKRyNRETLEVRYKGKsIADVLDMTveeALEFFENIPkiarkLQTlcdvglgyiklg 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515631642 433 -----LSYGQKKRVTIASILVLE---PELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHDMHLV 496
Cdd:cd03271 165 qpattLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVI 235
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
308-492 |
4.09e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 308 YDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMgvidADSGSSYLNgedlSELSIFERsqkvgvvmqNPNHMIS 387
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLI----SFLPKFSR---------NKLIFID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 388 hhmifdevafglrnrgvaeqEIKEKVENVLELCGLSKfrhwPIEALSYGQKKRVTIASILVLEPE--LLILDEPTAGQDY 465
Cdd:cd03238 67 --------------------QLQFLIDVGLGYLTLGQ----KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180
....*....|....*....|....*..
gi 515631642 466 RNYTSMLAFIQKLnRELGITVVIISHD 492
Cdd:cd03238 123 QDINQLLEVIKGL-IDLGNTVILIEHN 148
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-46 |
4.77e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.22 E-value: 4.77e-05
10 20
....*....|....*....|....*..
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-349 |
4.88e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.17 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 136 LDRSPHDLSGGQKQRVSLAG-I---LVDDVDILlfDEPLASLDPK-TGKatieIIDQLHKETNK--TIVIIEHRlEDVLh 208
Cdd:COG0178 479 LDRSAGTLSGGEAQRIRLATqIgsgLVGVLYVL--DEPSIGLHQRdNDR----LIETLKRLRDLgnTVIVVEHD-EDTI- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 209 RDIDRVILM-----ER-GEIVADMTPDEILASEllethgirEPL---YLSALKAAKAPLtsedklsnlkaldyKRfRPAV 279
Cdd:COG0178 551 RAADYIIDIgpgagEHgGEVVAQGTPEEILKNP--------DSLtgqYLSGRKRIPVPK--------------KR-RKGN 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 280 QAWfaerptpvaekqyqplLEVHGLTysydgeKNALEDVSFKIGKGEFVSILGKNGSGKSTitkLIMGVI 349
Cdd:COG0178 608 GKF----------------LTIKGAR------ENNLKNVDVEIPLGVLTCVTGVSGSGKST---LVNDIL 652
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-230 |
5.47e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 13 ESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISDFSMHDYTEQvGTVLQDT 92
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT-----SGYVTLDGHEVVTRSPQDGLAN-GIVYISE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 93 DSQ----FVGLSIGEDIAF-AL--------------ENQLVSN-IDMYPLvkSTAKMvdladmlDRSPHDLSGGQKQRVS 152
Cdd:PRK10762 335 DRKrdglVLGMSVKENMSLtALryfsraggslkhadEQQAVSDfIRLFNI--KTPSM-------EQAIGLLSGGNQQKVA 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631642 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDE 230
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMS-DRILVMHEGRISGEFTREQ 481
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
315-492 |
1.64e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 315 LEDVSFKIGKGEFVSILGKNGSGKSTitkLIMGVIDADSGSSYLNGedlseLSIFERsQKVGVvMQNPN----------- 383
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSS---LAFDTIYAEGQRRYVES-----LSAYAR-QFLGQ-MDKPDvdsieglspai 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 384 ----HMISHH----------------MIFDEVafGLRNRgvaeqeIKEKVENVLELCGLSKfrhwPIEALSYGQKKRVTI 443
Cdd:cd03270 81 aidqKTTSRNprstvgtvteiydylrLLFARV--GIRER------LGFLVDVGLGYLTLSR----SAPTLSGGEAQRIRL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515631642 444 ASIL--VLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHD 492
Cdd:cd03270 149 ATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD 198
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
400-520 |
1.64e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 400 RNRGVAEQEIKEKVENVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLN 479
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 515631642 480 RElGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:NF000106 192 RD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
132-231 |
1.68e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 132 LADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHKEtNKTIVIIEHRLEDVlHRDI 211
Cdd:NF000106 134 LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEA-EQLA 211
|
90 100
....*....|....*....|
gi 515631642 212 DRVILMERGEIVADMTPDEI 231
Cdd:NF000106 212 HELTVIDRGRVIADGKVDEL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-46 |
2.29e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 2.29e-04
10 20
....*....|....*....|....*..
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-231 |
2.45e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 136 LDRSPHDLSGGQKQRVSLAGILVDDVD---ILLFDEPLASLDPKTGKATIEIIDQLHKETNkTIVIIEHRLeDVLhRDID 212
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNL-DVI-KTAD 899
|
90 100
....*....|....*....|....*
gi 515631642 213 RVILM-----ER-GEIVADMTPDEI 231
Cdd:TIGR00630 900 YIIDLgpeggDGgGTVVASGTPEEV 924
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-206 |
2.95e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGknisDFSmhdyteqVGTVLQDTDSQFVGL 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS-----PTVGKVDRNG----EVS-------VIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 100 sigEDIAFALENQLVSNIDMYPLVKSTAKMVDLADMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGK 179
Cdd:PRK13546 104 ---ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180
....*....|....*....|....*..
gi 515631642 180 ATIEIIDQLhKETNKTIVIIEHRLEDV 206
Cdd:PRK13546 181 KCLDKIYEF-KEQNKTIFFVSHNLGQV 206
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-230 |
3.29e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlipHAIKGEVTGSLEINGKNISDFSMHD-------Y-TEqvgt 87
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG---RSYGRNISGTVFKDGKEVDVSTVSDaidaglaYvTE---- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 88 vlqdtDSQFVGLSIGEDIAFalenqlvsNIDMYPLVK-STAKMVDL-----------ADMLDRSPH------DLSGGQKQ 149
Cdd:NF040905 345 -----DRKGYGLNLIDDIKR--------NITLANLGKvSRRGVIDEneeikvaeeyrKKMNIKTPSvfqkvgNLSGGNQQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 150 RVSLAGILVDDVDILLFDEPLASLDpkTG-KATI-EIIDQLHKEtNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMT 227
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGID--VGaKYEIyTIINELAAE-GKGVIVISSELPELLGM-CDRIYVMNEGRITGELP 487
|
...
gi 515631642 228 PDE 230
Cdd:NF040905 488 REE 490
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
20-228 |
6.14e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTL----------------------------GQCLNGLI----------PHAIKGE 61
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlypalarrlhlkkeqpgnhdriegLEHIDKVIvidqspigrtPRSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 62 VTG---------------------SLEI--NGKNISDfsmhdyteqvgtVLQdtdsqfvgLSIGEDIAFaLENQlvsnid 118
Cdd:cd03271 91 YTGvfdeirelfcevckgkrynreTLEVryKGKSIAD------------VLD--------MTVEEALEF-FENI------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 119 myPLVKstAKMVDLADM------LDRSPHDLSGGQKQRVSLAGILVDDVD---ILLFDEPLASLDPKTGKATIEIIDQLH 189
Cdd:cd03271 144 --PKIA--RKLQTLCDVglgyikLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLV 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 515631642 190 KETNkTIVIIEHRLeDVLhRDIDRVILM-----ER-GEIVADMTP 228
Cdd:cd03271 220 DKGN-TVVVIEHNL-DVI-KCADWIIDLgpeggDGgGQVVASGTP 261
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
35-220 |
6.96e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 35 IIGPSGSGKSTLGQCLNGlipHAIKGEVTGSLEING--KNISDFS-MHDYTEQvgtvlqdTDSQFVGLSIGEDIAFALEN 111
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGfpKKQETFArISGYCEQ-------NDIHSPQVTVRESLIYSAFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 112 QL---VSNIDMYPLVKSTAKMVDLADMLDR-----SPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIE 183
Cdd:PLN03140 981 RLpkeVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR 1060
|
170 180 190
....*....|....*....|....*....|....*..
gi 515631642 184 IIDQLhKETNKTIVIIEHRLEDVLHRDIDRVILMERG 220
Cdd:PLN03140 1061 TVRNT-VDTGRTVVCTIHQPSIDIFEAFDELLLMKRG 1096
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-46 |
1.09e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 1.09e-03
10 20
....*....|....*....|....*..
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTL 650
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
322-506 |
1.16e-03 |
|
ATP-binding cassette domain 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 more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.25 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 322 IGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGedlseLSIFERSQKVgvvmqnpnhmishhmifdevafglrn 401
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-----ITPVYKPQYI-------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 402 rgvaeqeikekvenvlelcglskfrhwpieALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRE 481
Cdd:cd03222 71 ------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*
gi 515631642 482 LGITVVIISHDMhLVLEYTTRSIVI 506
Cdd:cd03222 121 GKKTALVVEHDL-AVLDYLSDRIHV 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
310-561 |
1.24e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITK-LIMGVIDADSGSSYL-------NGEDLSEL-----SIFERSQkvg 376
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRyMAMHAIDGIPKNCQIlhveqevVGDDTTALqcvlnTDIERTQ--- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 377 vVMQNPNHMISHHMIFDEVAF-----GLRNRGVAEQEIKEKVENV---LE--------------LCGLS---KFRHWPIE 431
Cdd:PLN03073 265 -LLEEEAQLVAQQRELEFETEtgkgkGANKDGVDKDAVSQRLEEIykrLElidaytaearaasiLAGLSftpEMQVKATK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 432 ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRelgiTVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 515631642 512 IANAAMTEVFsqpsllERanlctTSIYELATMMKIDDTN----AFMQYFIDYER 561
Cdd:PLN03073 420 VTYKGDYDTF------ER-----TREEQLKNQQKAFESNersrSHMQAFIDKFR 462
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
324-498 |
1.49e-03 |
|
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: 39.28 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 324 KGEFVSILGKNGSGKSTITKLIMGVIDADSGSS-YLNGEDLSELSIFERSQKVGVVMQnpnhmishhmifdevafglrnr 402
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 403 gvaeqeikekvenvlelcglskfrhwpiEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNY-----TSMLAFIQK 477
Cdd:smart00382 59 ----------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLLLL 110
|
170 180
....*....|....*....|.
gi 515631642 478 LNRELGITVVIISHDMHLVLE 498
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGP 131
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-46 |
2.01e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 2.01e-03
10 20
....*....|....*....|....*..
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-46 |
2.23e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 2.23e-03
10 20
....*....|....*....|....*..
gi 515631642 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTL 651
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
316-492 |
2.29e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 316 EDVSFkiGKGEFVSILGKNGSGKSTITKLImgvidadsgssylngedlselsifersqKVGVVMQNPNhmishhmifdev 395
Cdd:cd03227 14 NDVTF--GEGSLTIITGPNGSGKSTILDAI----------------------------GLALGGAQSA------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 396 afGLRNRGVAEQEIKEKVEnvLELCGLSKfrhwpieALSYGQKKRVTIASILVLEPE----LLILDEPTAGQDYRNyTSM 471
Cdd:cd03227 52 --TRRRSGVKAGCIVAAVS--AELIFTRL-------QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRD-GQA 119
|
170 180
....*....|....*....|.
gi 515631642 472 LAFIQKLNRELGITVVIISHD 492
Cdd:cd03227 120 LAEAILEHLVKGAQVIVITHL 140
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
35-137 |
3.36e-03 |
|
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling.
Pssm-ID: 410900 [Multi-domain] Cd Length: 172 Bit Score: 38.74 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 35 IIGPSGSGKSTLG-Q-CLNGLIPHAIKGEVTGSLEIN---GKNISDFSMHDYTEQVGTVL-------QDTDsqfVGLSIG 102
Cdd:cd19492 6 ICGVPGVGKTQLCmQlAVNVQIPKCFGGLAGEAIYIDtegSFNIHYFRVHDYVELLALINslpkfleDHPK---VKLIVV 82
|
90 100 110
....*....|....*....|....*....|....*.
gi 515631642 103 EDIAFALENQLVSNIDMYPLVKSTA-KMVDLADMLD 137
Cdd:cd19492 83 DSIAFPFRHDFDDLAQRTRLLNGLAqLLHSLARQHN 118
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-188 |
3.89e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 33 IVIIGPSGSGKSTL---------------GQCLNGLIPH-AIKGEVTGSLEINGKN---------ISDFSMHDYTEqvgt 87
Cdd:COG0419 26 NLIVGPNGAGKSTIleairyalygkarsrSKLRSDLINVgSEEASVELEFEHGGKRyrierrqgeFAEFLEAKPSE---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 88 vLQDTDSQFVGLSIGEDI---AFALENQLVSNIDMYPLVKsTAKMVDLADMLD-RSPHDLSGGQKQRVSLAgilvdDVDI 163
Cdd:COG0419 102 -RKEALKRLLGLEIYEELkerLKELEEALESALEELAELQ-KLKQEILAQLSGlDPIETLSGGERLRLALA-----DLLS 174
|
170 180
....*....|....*....|....*
gi 515631642 164 LLFDepLASLDPKTGKATIEIIDQL 188
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEEL 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-46 |
4.46e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 4.46e-03
10 20 30
....*....|....*....|....*....|....*
gi 515631642 12 YESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:PRK11147 327 YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTL 361
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
355-492 |
6.92e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 355 SSYLNGE---DLSELSIFErsqkvgvvmqnpnhmiSHHMiFDEVAFGLRNRGVAEQ---EIKEKVE---NV-LELCGLSK 424
Cdd:TIGR00630 422 AVTVGGKsiaDVSELSIRE----------------AHEF-FNQLTLTPEEKKIAEEvlkEIRERLGfliDVgLDYLSLSR 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 425 frhwPIEALSYGQKKRVTIASIL--VLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRELGITVVIISHD 492
Cdd:TIGR00630 485 ----AAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD 549
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
143-235 |
7.57e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 143 LSGGQKQRVSLAGILVdDVD----ILLFDEP------------LASLDpktgkatiEIIDQLHketnkTIVIIEHRLeDV 206
Cdd:COG0178 827 LSGGEAQRVKLASELS-KRStgktLYILDEPttglhfhdirklLEVLH--------RLVDKGN-----TVVVIEHNL-DV 891
|
90 100 110
....*....|....*....|....*....|....*...
gi 515631642 207 lhrdI---DRVILM-----ER-GEIVADMTPDEILASE 235
Cdd:COG0178 892 ----IktaDWIIDLgpeggDGgGEIVAEGTPEEVAKVK 925
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
330-496 |
8.80e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.97 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 330 ILGKNGSGKSTITKLI-MGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPN---HMISHHM-IFDEVAFglrnrgV 404
Cdd:cd03240 27 IVGQNGAGKTTIIEALkYALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANgkkYTITRSLaILENVIF------C 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631642 405 AEQEIKekvenvlelcglskfrhWPIE----ALSYGQKK------RVTIASILVLEPELLILDEPTAGQDYRN-YTSMLA 473
Cdd:cd03240 101 HQGESN-----------------WPLLdmrgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAE 163
|
170 180
....*....|....*....|...
gi 515631642 474 FIQKLNRELGITVVIISHDMHLV 496
Cdd:cd03240 164 IIEERKSQKNFQLIVITHDEELV 186
|
|
| |
