|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-532 |
6.54e-171 |
|
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: 494.04 E-value: 6.54e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MT--IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaiKGEVTGSLEINGKNISEFSM 78
Cdd:COG1123 1 MTplLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPH--GGRISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 79 HDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILV 158
Cdd:COG1123 79 ALRGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILASklld 238
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEI-ADRVVVMDDGRIVEDGPPEEILAA---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 239 thgirePLYLSAlkaakAPltcedklsnlkaldykrfRPAVQAWFADRPAPAAEkqyqPLLEVHGLTYSYD----GEKNA 314
Cdd:COG1123 234 ------PQALAA-----VP------------------RLGAARGRAAPAAAAAE----PLLEVRNLSKRYPvrgkGGVRA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS---IFERSQKVGVVMQNPNHMISHHM- 390
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYSSLNPRMt 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 391 IFDEIAFGLRNRNIA-EELITEKVEHVLELCGLS-KFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNY 468
Cdd:COG1123 361 VGDIIAEPLRLHGLLsRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQ 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 469 TSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP-SLLERANL 532
Cdd:COG1123 441 AQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPqHPYTRALL 505
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
299-529 |
9.57e-90 |
|
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: 275.75 E-value: 9.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:COG1122 81 FQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 459 PTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLER 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 |
2.56e-89 |
|
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: 273.96 E-value: 2.56e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 300 EVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 459 PTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSK 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 |
2.20e-87 |
|
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: 268.95 E-value: 2.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 5 FSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEINGKNISEFSMHDYTEQ 84
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL-----GPTSGEVLVDGKDLTKLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 85 VGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:cd03225 77 VGLVFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 165 LFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLhRDIDRVILMERGE 221
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLL-ELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-233 |
2.72e-82 |
|
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: 256.49 E-value: 2.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikgeVTGSLEINGKNISEFSMHDYT 82
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP-----TSGEVLVDGKDITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:COG1122 75 RKVGLVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILA 233
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVA-ELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-235 |
1.29e-72 |
|
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: 232.71 E-value: 1.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKN-ISEFSMHDY 81
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLL-PTSGKVT----VDGLDtLDEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:TIGR04520 76 RKKVGMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTPDEILASK 235
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV--LADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
299-545 |
1.26e-66 |
|
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: 217.30 E-value: 1.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGED-LSELSIFERSQKVG 376
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLIL 456
Cdd:TIGR04520 81 MVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 457 DEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCTTS 536
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVELLKEIGLDVPF 239
|
....*....
gi 1382220129 537 IYELATMMK 545
Cdd:TIGR04520 240 ITELAKALK 248
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-234 |
2.99e-61 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 203.71 E-value: 2.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYT 82
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-----AGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK13635 81 RQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdiDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQA--DRVIVMNKGEILEEGTPEEIFKS 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-235 |
5.91e-61 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 202.53 E-value: 5.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEFSMHDY 81
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQS------GEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK13632 82 RKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTPDEILASK 235
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI--LADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-245 |
4.03e-60 |
|
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: 200.37 E-value: 4.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYE---SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PhaikgeVTGSLEINGKNIS---E 75
Cdd:TIGR04521 1 IKLKNVSYIYQpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLkP------TSGTVTIDGRDITakkK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 76 FSMHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDL-ADMLERSPHDLSGGQKQRVSLA 154
Cdd:TIGR04521 75 KKLKDLRKKVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILA- 233
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEY-ADRVIVMHKGKIVLDGTPREVFSd 233
|
250
....*....|..
gi 1382220129 234 SKLLDTHGIREP 245
Cdd:TIGR04521 234 VDELEKIGLDVP 245
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
299-545 |
1.89e-59 |
|
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: 198.83 E-value: 1.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS-- 372
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 -QKVGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVL 449
Cdd:TIGR04521 81 rKKVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeyLERSPFE-LSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 450 EPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLER 529
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDELEK 239
|
250
....*....|....*.
gi 1382220129 530 ANLCTTSIYELATMMK 545
Cdd:TIGR04521 240 IGLDVPEITELARKLK 255
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
298-530 |
2.37e-55 |
|
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: 187.17 E-value: 2.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:COG1120 1 MLEAENLSVGYGG-RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhmishhmifdEIAFGLRnrniAEELI------------------TEKVEHVLELCGLSKFRHWPIEALSYGQKK 439
Cdd:COG1120 80 VPQEP-----------PAPFGLT----VRELValgryphlglfgrpsaedREAVEEALERTGLEHLADRPVDELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
250
....*....|.
gi 1382220129 520 VFSqPSLLERA 530
Cdd:COG1120 225 VLT-PELLEEV 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
296-545 |
5.93e-55 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 187.14 E-value: 5.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK 374
Cdd:PRK13635 3 EEIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13635 83 VGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCT 534
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQEIGLDV 241
|
250
....*....|.
gi 1382220129 535 TSIYELATMMK 545
Cdd:PRK13635 242 PFSVKLKELLK 252
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
298-564 |
1.58e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 185.67 E-value: 1.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--SELSIFERSQKV 375
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 456 LDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCTT 535
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLRLP 239
|
250 260 270
....*....|....*....|....*....|
gi 1382220129 536 SIYELATMM-KIDDTNAFMQYFIDYERSSL 564
Cdd:PRK13639 240 RVAHLIEILnKEDNLPIKMGYTIGEARRNI 269
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
296-521 |
3.02e-54 |
|
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: 183.64 E-value: 3.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS--- 372
Cdd:COG1127 3 EPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 QKVGVVMQNP---NHMishhMIFDEIAFGLR-NRNIAEELITEKVEHVLELCGLSKFRH-WPIEaLSYGQKKRVTIASIL 447
Cdd:COG1127 82 RRIGMLFQGGalfDSL----TVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADkMPSE-LSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 448 VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVF 521
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
296-524 |
3.42e-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: 184.09 E-value: 3.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKv 375
Cdd:COG0411 2 DPLLEVRGLTKRFGGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVM--QNP----------NHMISHHM----IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKK 439
Cdd:COG0411 80 GIARtfQNPrlfpeltvleNVLVAAHArlgrGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
....*
gi 1382220129 520 VFSQP 524
Cdd:COG0411 240 VRADP 244
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
298-552 |
1.72e-53 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 183.13 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE--DLSELSIFERSQKV 375
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK13636 85 GMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 456 LDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCTT 535
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNLRLP 244
|
250
....*....|....*..
gi 1382220129 536 SIYELATMMKIDDTNAF 552
Cdd:PRK13636 245 RIGHLMEILKEKDGFVF 261
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
299-521 |
1.38e-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: 179.23 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQ---KV 375
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNpNHMISHHMIFDEIAFGLR-NRNIAEELITEKVEHVLELCGLSKFRH-WPIEaLSYGQKKRVTIASILVLEPEL 453
Cdd:cd03261 80 GMLFQS-GALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDlYPAE-LSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVF 521
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-235 |
9.54e-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: 9.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYT 82
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT-----SGRILIDGIDLRQIDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDtDSQFVGlSIGEDIAFALEnqlmsNIDMYPLVKStAKMVDLADMLERSPH-----------DLSGGQKQRV 151
Cdd:COG2274 549 RQIGVVLQD-VFLFSG-TIRENITLGDP-----DATDEEIIEA-ARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDEI 231
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI--RLADRIIVLDKGRIVEDGTHEEL 696
|
....
gi 1382220129 232 LASK 235
Cdd:COG2274 697 LARK 700
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
299-524 |
8.39e-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: 174.55 E-value: 8.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKvGVV 378
Cdd:cd03219 1 LEVRGLTKRFGGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARL-GIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 M--QNP----------NHMISHHMIFDEIAFGLRNRNiAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:cd03219 79 RtfQIPrlfpeltvleNVMVAAQARTGSGLLLARARR-EEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-245 |
9.63e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 175.56 E-value: 9.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEFS-MHD 80
Cdd:PRK13644 2 IRLENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQK------GKVLVSGIDTGDFSkLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDD 160
Cdd:PRK13644 75 IRKLVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 161 VDILLFDEPLASLDPKTGKATIEIIDQLHnETNKTIVIIEHRLEDvLHrDIDRVILMERGEIVADMTPDEILASKLLDTH 240
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEE-LH-DADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
....*
gi 1382220129 241 GIREP 245
Cdd:PRK13644 232 GLTPP 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
299-545 |
1.38e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 175.62 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSE--LSIFERS 372
Cdd:PRK13637 3 IKIENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 QKVGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLS--KFR-HWPIEaLSYGQKKRVTIASILVL 449
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKdKSPFE-LSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 450 EPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLER 529
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLES 241
|
250
....*....|....*.
gi 1382220129 530 ANLCTTSIYELATMMK 545
Cdd:PRK13637 242 IGLAVPQVTYLVRKLR 257
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
296-549 |
3.61e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 174.02 E-value: 3.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK 374
Cdd:PRK13632 5 SVMIKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13632 85 IGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCT 534
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEILEKAKIDS 243
|
250
....*....|....*.
gi 1382220129 535 TSIYELATMMK-IDDT 549
Cdd:PRK13632 244 PFIYKLSKKLKgIDPT 259
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
296-528 |
3.76e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.97 E-value: 3.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSelsifERSQKV 375
Cdd:COG1121 4 MPAIELENLTVSYGG-RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQnpNHMISHHM---IFDEIAFGLRNRNIAEELIT----EKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:COG1121 78 GYVPQ--RAEVDWDFpitVRDVVLMGRYGRRGLFRRPSradrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADsKLIANAAMTEVFSQPSLLE 528
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEEVLTPENLSR 233
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
308-495 |
8.86e-50 |
|
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: 170.30 E-value: 8.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 308 YDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE--DLSELSIFERSQKVGVVMQNPNHM 385
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRKGLLERRQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 386 ISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDY 465
Cdd:TIGR01166 81 LFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 1382220129 466 RNYTSMLAFIQKLnRDLGITVVIISHDMHL 495
Cdd:TIGR01166 161 AGREQMLAILRRL-RAEGMTVVISTHDVDL 189
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
300-513 |
9.05e-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: 169.54 E-value: 9.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 300 EVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVM 379
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 380 QnpnhmishhmifdeiafglrnrniaeelitekvehVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:cd03214 80 Q-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 460 TAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-523 |
3.19e-49 |
|
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: 178.07 E-value: 3.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL----------IPHAIKGEVTGSLEINGK-------------- 71
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriIYHVALCEKCGYVERPSKvgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 72 ------NISEFSMHDYTEQVGTVLQDTDSQFvglsiGEDIAfaLENQLMSNIDM-YPLVKSTAKMVDLADMLE---RSPH 141
Cdd:TIGR03269 92 eevdfwNLSDKLRRRIRKRIAIMLQRTFALY-----GDDTV--LDNVLEALEEIgYEGKEAVGRAVDLIEMVQlshRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 142 ---DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEdVLHRDIDRVILME 218
Cdd:TIGR03269 165 iarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE-VIEDLSDKAIWLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 219 RGEIVADMTPDEILAsKLLDThgireplyLSALKAAKAPLTCED--KLSNLKaldykrfrpavqawfadrpapaaeKQYq 296
Cdd:TIGR03269 244 NGEIKEEGTPDEVVA-VFMEG--------VSEVEKECEVEVGEPiiKVRNVS------------------------KRY- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 pllevhgltYSYD-GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLN-GE---DLSELSIFER 371
Cdd:TIGR03269 290 ---------ISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvDMTKPGPDGR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 372 ---SQKVGVVMQNPNhMISHHMIFDEI--AFGLrnrNIAEELITEKVEHVLELCGLSKFRHWPI-----EALSYGQKKRV 441
Cdd:TIGR03269 361 graKRYIGILHQEYD-LYPHRTVLDNLteAIGL---ELPDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 442 TIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVF 521
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
..
gi 1382220129 522 SQ 523
Cdd:TIGR03269 517 EE 518
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
300-513 |
3.88e-49 |
|
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: 169.25 E-value: 3.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 300 EVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSElsifeRSQKVGVVM 379
Cdd:cd03235 1 EVEDLTVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 380 QNPNhmISHHM---IFDEIAFGLRNRNIAEELIT----EKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPE 452
Cdd:cd03235 75 QRRS--IDRDFpisVRDVVLMGLYGHKGLFRRLSkadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 453 LLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIaDSKLIA 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 |
5.63e-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: 168.85 E-value: 5.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR--NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPNHMisHHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03259 78 FQDYALF--PHLtVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-247 |
3.92e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 168.83 E-value: 3.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAIKgevTGSLEINGKNISEFSMHDY 81
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNP---NSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK13640 83 REKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHrdIDRVILMERGEIVADMTPDEILA-SKLLDTH 240
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM--ADQVLVLDDGKLLAQGSPVEIFSkVEMLKEI 240
|
....*..
gi 1382220129 241 GIREPLY 247
Cdd:PRK13640 241 GLDIPFV 247
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
296-524 |
4.18e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 171.05 E-value: 4.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKV 375
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR--NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQN----PnhmishHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLE 450
Cdd:COG3842 80 GMVFQDyalfP------HLtVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 451 PELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERP 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
16-224 |
5.14e-48 |
|
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: 166.16 E-value: 5.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDytEQVGTVLQDtDSQ 95
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-----SGEILIDGRDVTGVPPER--RNIGMVFQD-YAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:cd03259 84 FPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1382220129 176 KTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVA 224
Cdd:cd03259 164 KLREELREELKELQRELGITTIYVTHDQEEAL-ALADRIAVMNEGRIVQ 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-231 |
6.08e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 168.69 E-value: 6.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRY---ESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHaikgevTGSLEINGKNISE- 75
Cdd:PRK13637 1 MSIKIENLTHIYmegTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPT------SGKIIIDGVDITDk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 76 -FSMHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMV--DLADMLERSPHDLSGGQKQRVS 152
Cdd:PRK13637 75 kVKLSDIRKKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEI 231
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVA-KLADRIIVMNKGKCELQGTPREV 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
299-520 |
6.10e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.78 E-value: 6.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsQKVGVV 378
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPNhmishhmiFDE-------IAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:COG1131 79 PQEPA--------LYPdltvrenLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
298-532 |
7.18e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 167.99 E-value: 7.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDG--EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKV 375
Cdd:PRK13650 4 IIEVKNLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 456 LDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVlEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANL 532
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDLLQLGL 239
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-235 |
2.06e-47 |
|
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: 165.54 E-value: 2.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVtgslEINGKNISEFSMHDYT 82
Cdd:COG1127 6 IEVRNLTKSFG--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR-PDSGEI----LVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 E---QVGTVLQDT---DSqfvgLSIGEDIAFAL-ENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAG 155
Cdd:COG1127 79 ElrrRIGMLFQGGalfDS----LTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEILAS 234
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSA--FAIaDRVAVLADGKIIAEGTPEELLAS 232
|
.
gi 1382220129 235 K 235
Cdd:COG1127 233 D 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
296-516 |
4.06e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.45 E-value: 4.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS 372
Cdd:COG1136 2 SPLLELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 ----QKVGVVMQNPNhMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:COG1136 82 rlrrRHIGFVFQFFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLvLEYTTRSIVIADSKLIANAA 516
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
299-511 |
5.31e-47 |
|
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: 163.81 E-value: 5.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKN---ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS----IFER 371
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 372 SQKVGVVMQNPNhMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:cd03255 81 RRHIGFVFQSFN-LLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVlEYTTRSIVIADSKL 511
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
295-545 |
5.69e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 165.65 E-value: 5.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 295 YQPLLEVHGLTYSY-----DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS-I 368
Cdd:PRK13633 1 MNEMIKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 369 FERSQKVGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQPSLLE 528
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMK 239
|
250
....*....|....*..
gi 1382220129 529 RANLCTTSIYELATMMK 545
Cdd:PRK13633 240 KIGLDVPQVTELAYELK 256
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
298-555 |
5.88e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 165.75 E-value: 5.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:PRK13652 83 VFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCTTSI 537
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLPSL 242
|
250
....*....|....*...
gi 1382220129 538 YELATMMKIDDTNAFMQY 555
Cdd:PRK13652 243 PKLIRSLQAQGIAIDMAY 260
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
299-512 |
6.88e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 163.68 E-value: 6.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSifeRSQ----- 373
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK---RREipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 374 -KVGVVMQNpNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPE 452
Cdd:COG2884 79 rRIGVVFQD-FRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 453 LLILDEPTAGQDYRNYTSMLAFIQKLNRdLGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-524 |
7.07e-47 |
|
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: 171.79 E-value: 7.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 9 SFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIkGEVTGSLEINGKNISEFSMHDYTE----Q 84
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPA-AHPSGSILFDGQDLLGLSERELRRirgnR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 85 VGTVLQD---------TdsqfvglsIGEDIAFALE-NQLMSNidmyplVKSTAKMVDL---------ADMLERSPHDLSG 145
Cdd:COG4172 94 IAMIFQEpmtslnplhT--------IGKQIAEVLRlHRGLSG------AAARARALELlervgipdpERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPkTGKATI-EIIDQLHNETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIV 223
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDV-TVQAQIlDLLKDLQRELGMALLLITHDLGVV--RRFaDRVAVMRQGEIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 224 ADMTPDEILASKlldthgiREPlYLSALKAAkapltcedklsnlkaldykrfRPAVQAwfadRPAPAAEKqyqPLLEVHG 303
Cdd:COG4172 237 EQGPTAELFAAP-------QHP-YTRKLLAA---------------------EPRGDP----RPVPPDAP---PLLEARD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 304 LTYSYD----------GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAdSGSSYLNGEDLSELSifeRSQ 373
Cdd:COG4172 281 LKVWFPikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLS---RRA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 374 ------KVGVVMQNPNHMISHHM-IFDEIAFGLR--NRNIAEELITEKVEHVLELCGLSK-FRH-WPIEaLSYGQKKRVT 442
Cdd:COG4172 357 lrplrrRMQVVFQDPFGSLSPRMtVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPaARHrYPHE-FSGGQRQRIA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 443 IASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFS 522
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFD 515
|
..
gi 1382220129 523 QP 524
Cdd:COG4172 516 AP 517
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
310-525 |
1.34e-46 |
|
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: 163.14 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE---RSQKVGVVMQNPNhMI 386
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkARRRIGMIFQHFN-LL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 387 SHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYR 466
Cdd:cd03258 95 SSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 467 NYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:cd03258 175 TTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-221 |
3.70e-46 |
|
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: 159.86 E-value: 3.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikgeVTGSLEINGKNISEFSMHDYT 82
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP-----TSGEILIDGVDLRDLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTdsQFVGLSIGEdiafalenqlmsNIdmyplvkstakmvdladmlersphdLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03228 76 KNIAYVPQDP--FLFSGTIRE------------NI-------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNetNKTIVIIEHRLEDVlhRDIDRVILMERGE 221
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI--RDADRIIVLDDGR 171
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
299-532 |
5.95e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 162.60 E-value: 5.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:PRK13647 85 FQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 459 PTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAmTEVFSQPSLLERANL 532
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KSLLTDEDIVEQAGL 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-235 |
5.97e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 170.35 E-value: 5.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISEFSMHD 80
Cdd:COG1132 339 EIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY------DPTsGRILIDGVDIRDLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQDTdSQFVGlSIGEDIAFALEnqlmsNIDMyPLVKSTAKMVDLADMLERSPH-----------DLSGGQKQ 149
Cdd:COG1132 412 LRRQIGVVPQDT-FLFSG-TIRENIRYGRP-----DATD-EEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 150 RVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHneTNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPD 229
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTI--RNADRILVLDDGRIVEQGTHE 559
|
....*.
gi 1382220129 230 EILASK 235
Cdd:COG1132 560 ELLARG 565
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-270 |
1.32e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 162.50 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYES---LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVT-GSLEI-NGKNisE 75
Cdd:PRK13634 1 MDITFQKVEHRYQYktpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL-QPTSGTVTiGERVItAGKK--N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 76 FSMHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDL-ADMLERSPHDLSGGQKQRVSLA 154
Cdd:PRK13634 78 KKLKPLRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILA- 233
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAA-RYADQIVVMHKGTVFLQGTPREIFAd 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1382220129 234 SKLLDTHGIREP---LYLSALKAA------KAPLTCEDKLSNLKAL 270
Cdd:PRK13634 237 PDELEAIGLDLPetvKFKRALEEKfgisfpKPCLTLEELAHEVVQL 282
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
299-545 |
1.59e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 161.89 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVI---DADSGSSYLNGEDLSELSIFERSQK 374
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13640 86 VGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVlEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCT 534
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDI 244
|
250
....*....|.
gi 1382220129 535 TSIYELATMMK 545
Cdd:PRK13640 245 PFVYKLKNKLK 255
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-235 |
1.62e-45 |
|
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: 168.78 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDY 81
Cdd:COG4988 336 SIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDtdSQFVGLSIGEDIAFALEN----QLMSnidmyplvksTAKMVDLADMLERSPHD-----------LSGG 146
Cdd:COG4988 410 RRQIAWVPQN--PYLFAGTIRENLRLGRPDasdeELEA----------ALEAAGLDEFVAALPDGldtplgeggrgLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 147 QKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADM 226
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL--AQADRILVLDDGRIVEQG 553
|
....*....
gi 1382220129 227 TPDEILASK 235
Cdd:COG4988 554 THEELLAKN 562
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
298-520 |
2.17e-45 |
|
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: 160.02 E-value: 2.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVGV 377
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNpNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:COG4555 79 LPDE-RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG4555 158 EPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
298-512 |
2.22e-45 |
|
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: 159.59 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS---IFER 371
Cdd:cd03257 1 LLEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 372 SQKVGVVMQNPNHMISHHM-IFDEIAFGLR--NRNIAEELITEKVEHVLELCGLSK--FRHWPIEaLSYGQKKRVTIASI 446
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMtIGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLPEevLNRYPHE-LSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
299-492 |
4.73e-45 |
|
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: 158.94 E-value: 4.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR--PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNpnHMISHHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03300 78 FQN--YALFPHLtVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHD 492
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHD 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-237 |
1.11e-44 |
|
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: 158.67 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYT 82
Cdd:COG1120 2 LEAENLSVGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-----SGEVLLDGRDLASLSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTDSQFvGLSIGEDIA---------FALENQlmsniDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSL 153
Cdd:COG1120 75 RRIAYVPQEPPAPF-GLTVRELVAlgryphlglFGRPSA-----EDREAVEEALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 154 AGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIiehrledVLHrDI-------DRVILMERGEIVADM 226
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVM-------VLH-DLnlaaryaDRLVLLKDGRIVAQG 220
|
250
....*....|.
gi 1382220129 227 TPDEILASKLL 237
Cdd:COG1120 221 PPEEVLTPELL 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
299-494 |
1.26e-44 |
|
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: 157.25 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSelsifERSQKV 375
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNhMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKF-RHWPIEaLSYGQKKRVTIASILVLEPELL 454
Cdd:cd03293 76 GYVFQQDA-LLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFeNAYPHQ-LSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMH 494
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDID 193
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-234 |
1.72e-44 |
|
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: 157.66 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVtgslEINGKNISEFSMHDYT 82
Cdd:cd03261 1 IELRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR-PDSGEV----LIDGEDISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 E---QVGTVLQDTdSQFVGLSIGEDIAFAL-ENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILV 158
Cdd:cd03261 74 RlrrRMGMLFQSG-ALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTA-FAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-222 |
5.93e-44 |
|
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: 155.34 E-value: 5.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgeVT-GSLEINGKNISEFSMH 79
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR------PTsGEVRVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DYT----EQVGTVLQdtdsQF---VGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVS 152
Cdd:cd03255 75 ELAafrrRHIGFVFQ----SFnllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHrlEDVLHRDIDRVILMERGEI 222
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTH--DPELAEYADRIIELRDGKI 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-512 |
7.17e-44 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 163.31 E-value: 7.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 5 FSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTGSleiNGKNISEFSMHDYTEQ 84
Cdd:COG0488 1 LENLSKSFG--GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGEL-EPDSGEVSIP---KGLRIGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 85 VGTVLQDTDSQFVGL-SIGEDIAFALENQLMSNIDMYPLVKSTAKMVDL-------------------ADMLERSPHDLS 144
Cdd:COG0488 75 DLTVLDTVLDGDAELrALEAELEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsglgfpEEDLDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDpktgkatIEII----DQLHNETNkTIVIIEH-R--LEDVlhrdIDRVILM 217
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIewleEFLKNYPG-TVLVVSHdRyfLDRV----ATRILEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 218 ERGEIvadmTP------------DEILA-------------SKLLDThgIREPLYlSALKAAKApltcEDKLSNLKALDY 272
Cdd:COG0488 223 DRGKL----TLypgnysayleqrAERLEqeaaayakqqkkiAKEEEF--IRRFRA-KARKAKQA----QSRIKALEKLER 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 273 KRFRPAvqawfaDRPA----PAAEKQYQPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGV 348
Cdd:COG0488 292 EEPPRR------DKTVeirfPPPERLGKKVLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 349 IDADSGSSYLnGEDLselsifersqKVGVVMQNPNHMISHHMIFDEIafglrnRNIAEELITEKVEHVLELCGLSKFRHW 428
Cdd:COG0488 365 LEPDSGTVKL-GETV----------KIGYFDQHQEELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSGDDAF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 429 -PIEALSYGQKKRVTIASILVLEPELLILDEPTagqdyrNY--TSML-AFIQKLNRDLGiTVVIISHDMHLVLEYTTRSI 504
Cdd:COG0488 428 kPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT------NHldIETLeALEEALDDFPG-TVLLVSHDRYFLDRVATRIL 500
|
....*...
gi 1382220129 505 VIADSKLI 512
Cdd:COG0488 501 EFEDGGVR 508
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-231 |
7.39e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 156.37 E-value: 7.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFS---MH 79
Cdd:COG3638 3 LELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGEILVDGQDVTALRgraLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DYTEQVGTVLQdtdsQF--VG-LSigediafALENQLMSNIDMYPLVKSTAKM---------------VDLADMLERSPH 141
Cdd:COG3638 77 RLRRRIGMIFQ----QFnlVPrLS-------VLTNVLAGRLGRTSTWRSLLGLfppedreralealerVGLADKAYQRAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 142 DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERGE 221
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQV-DLARRYADRIIGLRDGR 224
|
250
....*....|
gi 1382220129 222 IVADMTPDEI 231
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-524 |
9.63e-44 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 164.64 E-value: 9.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 7 NFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEV-TGSLEINGKNisefsmhdytEQV 85
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQA-GGLVqCDKMLLRRRS----------RQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 86 GTVLQDTDSQFVGLSiGEDIAFALENQLMSNIDMYPLVKSTA-------------------KMVDLA------DMLERSP 140
Cdd:PRK10261 88 IELSEQSAAQMRHVR-GADMAMIFQEPMTSLNPVFTVGEQIAesirlhqgasreeamveakRMLDQVripeaqTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 141 HDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERG 220
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDM-GVVAEIADRVLVMYQG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 221 EIVADMTPDEILasklldtHGIREPlYLSALKAAkAPltcedKLSNLKALDYKRFRPAVQAWFADRPAPAAEKQY----Q 296
Cdd:PRK10261 246 EAVETGSVEQIF-------HAPQHP-YTRALLAA-VP-----QLGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTvvdgE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSY----------DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSEL 366
Cdd:PRK10261 312 PILQVRNLVTRFplrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 367 SIFERS---QKVGVVMQNPNHMIS-HHMIFDEIAFGLRNRNIAE-ELITEKVEHVLELCGLSKFRHW--PIEaLSYGQKK 439
Cdd:PRK10261 392 SPGKLQalrRDIQFIFQDPYASLDpRQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAWryPHE-FSGGQRQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
|
....*
gi 1382220129 520 VFSQP 524
Cdd:PRK10261 551 VFENP 555
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-231 |
1.55e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 158.34 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEFSMHDy 81
Cdd:COG3842 6 LELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFEtPDS------GRILLDGRDVTGLPPEK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 tEQVGTVLQDtDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:COG3842 77 -RNVGMVFQD-YALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhrdiDRVILMERGEIVADMTPDEI 231
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALal-aDRIAVMNDGRIEQVGTPEEI 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
296-492 |
1.93e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 155.63 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELsiferS 372
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 QKVGVVMQNPNHMisHHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFR-HWPIEaLSYGQKKRVTIASILVLE 450
Cdd:COG1116 80 PDRGVVFQEPALL--PWLtVLDNVALGLELRGVPKAERRERARELLELVGLAGFEdAYPHQ-LSGGMRQRVAIARALAND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1382220129 451 PELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHD 492
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-233 |
2.04e-43 |
|
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: 163.01 E-value: 2.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEFSMHD 80
Cdd:COG4987 333 SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLdPQS------GSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQDT---DSqfvglSIGEDIAFALEN----QLMSnidmyplvksTAKMVDLADMLERSPHDL---------- 143
Cdd:COG4987 407 LRRRIAVVPQRPhlfDT-----TLRENLRLARPDatdeELWA----------ALERVGLGDWLAALPDGLdtwlgeggrr 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 144 -SGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKAtieIIDQLHNET-NKTIVIIEHRLEDVlhRDIDRVILMERGE 221
Cdd:COG4987 472 lSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQA---LLADLLEALaGRTVLLITHRLAGL--ERMDRILVLEDGR 546
|
250
....*....|..
gi 1382220129 222 IVADMTPDEILA 233
Cdd:COG4987 547 IVEQGTHEELLA 558
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-231 |
6.49e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 154.52 E-value: 6.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlIPHAIKGEVT-GSLEINGKNISEFSMHdy 81
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IEKVKSGEIFyNNQAITDDNFEKLRKH-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 teqVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK13648 85 ---IGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdiDRVILMERGEIVADMTPDEI 231
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA--DHVIVMNKGTVYKEGTPTEI 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-222 |
8.51e-43 |
|
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: 8.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYT 82
Cdd:COG4619 1 LELEGLSFRVG--GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPLSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDtdSQFVGLSIGEDIAFALenQLMSNIDMYPLVKSTAKMVDL-ADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:COG4619 74 RQVAYVPQE--PALWGGTVRDNLPFPF--QLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHrLEDVLHRDIDRVILMERGEI 222
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSH-DPEQIERVADRVLTLEAGRL 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
299-511 |
1.15e-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: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:COG4619 1 LELEGLSFRVGG-KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNP---NHMISHHMIFdeiAFGLRNRNIAEEliteKVEHVLELCGLSK-FRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:COG4619 80 PQEPalwGGTVRDNLPF---PFQLRERKFDRE----RALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
298-544 |
1.82e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 153.24 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE--DLSELSIFERSQKV 375
Cdd:PRK13638 1 MLATSDLWFRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK13638 80 ATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 456 LDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLCTT 535
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQP 238
|
....*....
gi 1382220129 536 SIYELATMM 544
Cdd:PRK13638 239 WLVKLHTQL 247
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
298-525 |
2.30e-42 |
|
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: 152.26 E-value: 2.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYD---GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK 374
Cdd:COG1124 1 MLEVRNLSVSYGqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMQNPnhMIS---HHMIFDEIAFGLRNRNIAEelITEKVEHVLELCGLSK-FRHWPIEALSYGQKKRVTIASILVLE 450
Cdd:COG1124 81 VQMVFQDP--YASlhpRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 451 PELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-233 |
2.81e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 152.96 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRY-ESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaiKGEvTGSLEINGKNISEFSMHDY 81
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL----EAE-SGQIIIDGDLLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK13650 80 RHKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdiDRVILMERGEIVADMTPDEILA 233
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALS--DRVLVMKNGQVESTSTPRELFS 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-270 |
4.04e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 152.58 E-value: 4.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlIPHAIKGEVTgsleINGKNISEFSMHDYT 82
Cdd:PRK13647 5 IEVEDLHFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG-IYLPQRGRVK----VMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK13647 79 SKVGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 163 ILLFDEPLASLDPKtGKATI-EIIDQLHNEtNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILASKLLDTHG 241
Cdd:PRK13647 159 VIVLDEPMAYLDPR-GQETLmEILDRLHNQ-GKTVIVATHDV-DLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAG 235
|
250 260 270
....*....|....*....|....*....|....*
gi 1382220129 242 IREPL------YLSALKAAKAPLTCEDKLSNLKAL 270
Cdd:PRK13647 236 LRLPLvaqifeDLPELGQSKLPLTVKEAVQIIRKL 270
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-236 |
7.25e-42 |
|
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: 150.80 E-value: 7.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNI---SEFSMH 79
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-----PTSGSVLIDGTDInklKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DYTEQVGTVLQDTdsQFVG-LSigediafALENQLMSNIDMYPLVKSTAKM---------------VDLADMLERSPHDL 143
Cdd:cd03256 75 QLRRQIGMIFQQF--NLIErLS-------VLENVLSGRLGRRSTWRSLFGLfpkeekqralaalerVGLLDKAYQRADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 144 SGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEdvLHRDI-DRVILMERGEI 222
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVD--LAREYaDRIVGLKDGRI 223
|
250
....*....|....
gi 1382220129 223 VADMTPDEILASKL 236
Cdd:cd03256 224 VFDGPPAELTDEVL 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
7-231 |
7.59e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 151.78 E-value: 7.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 7 NFSFRYESLD----KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAIKGEVTGSLEINGKNIsefsmHDY 81
Cdd:PRK13633 9 NVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlIPSEGKVYVDGLDTSDEENL-----WDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK13633 84 RNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTPDEI 231
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV--EADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
300-512 |
9.06e-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: 149.33 E-value: 9.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 300 EVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELsifERSQKVGVVM 379
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 380 QNPNHMISHHMIFDEIAFGlrNRNIAEELitEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:cd03226 78 QDVDYQLFTDSVREELLLG--LKELDAGN--EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 460 TAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
299-510 |
1.54e-41 |
|
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: 147.72 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIF--ERSQKVG 376
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQNPNhMISHHMIFDEIAFGlrnrniaeelitekvehvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLIL 456
Cdd:cd03229 80 MVFQDFA-LFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 457 DEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-225 |
1.67e-41 |
|
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: 147.58 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 6 SNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISEFSMHDYTEQV 85
Cdd:cd03214 3 ENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK-PSSGEIL----LDGKDLASLSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 86 GTVLQdtdsqfvglsigediafALEnqlmsnidmyplvkstakMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:cd03214 76 AYVPQ-----------------ALE------------------LLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 166 FDEPLASLDPKTGKATIEIIDQLHNETNKTIVIiehrledVLHrDI-------DRVILMERGEIVAD 225
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVM-------VLH-DLnlaaryaDRVILLKDGRIVAQ 179
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-234 |
2.11e-41 |
|
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: 149.37 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTgsleINGKNISEFSMHDYT 82
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPT-SGEIF----IDGEDIREQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDtdsqfVGL----SIGEDIAF--ALENQLMSNIDMYplVKSTAKMVDL--ADMLERSPHDLSGGQKQRVSLA 154
Cdd:cd03295 75 RKIGYVIQQ-----IGLfphmTVEENIALvpKLLKWPKEKIRER--ADELLALVGLdpAEFADRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAF-RLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-223 |
2.13e-41 |
|
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: 148.81 E-value: 2.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 9 SFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFS---MHDYTEQV 85
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-----PTSGSIIFDGKDLLKLSrrlRKIRRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 86 GTVLQDTDSQF-VGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDL---ADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:cd03257 85 QMVFQDPMSSLnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEdvLHRDI-DRVILMERGEIV 223
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLG--VVAKIaDRVAVMYAGKIV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-231 |
2.82e-41 |
|
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: 148.48 E-value: 2.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEINGKNISEFSMHDYT 82
Cdd:cd03260 1 IELRDLNVYYG--DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 --EQVGTVLQDTdSQFVGlSIGEDIAFALENQLMSNID-MYPLVKSTAKMVDLADMLERSPH--DLSGGQKQRVSLAGIL 157
Cdd:cd03260 79 lrRRVGMVFQKP-NPFPG-SIYDNVAYGLRLHGIKLKEeLDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 158 VDDVDILLFDEPLASLDPkTGKATIE-IIDQLHNETnkTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEI 231
Cdd:cd03260 157 ANEPEVLLLDEPTSALDP-ISTAKIEeLIAELKKEY--TIVIVTHNMQQAA-RVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-233 |
3.90e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 148.36 E-value: 3.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLdkptLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDyt 82
Cdd:COG3840 2 LRLDDLTYRYGDF----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLP-----PDSGRILWNGQDLTALPPAE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTDsQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:COG3840 71 RPVSMLFQENN-LFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIVADMTPDEILA 233
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAAR--IaDRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-233 |
6.34e-41 |
|
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: 147.73 E-value: 6.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAikgevtGSLEINGKNI---SEFSMHDYTEQVGTVLQdtd 93
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTS------GSVLVDGTDLtllSGKELRKARRRIGMIFQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 94 sQFVGLS---IGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:cd03258 90 -HFNLLSsrtVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 171 ASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEILA 233
Cdd:cd03258 169 SALDPETTQSILALLRDINRELGLTIVLITHEMEVV--KRIcDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-525 |
8.93e-41 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 154.86 E-value: 8.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 10 FRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEINGKnisefsmhdyteqvgTVL 89
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGE---------------SLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 90 QDTDSQFVGLSiGEDIAF-------------ALENQLMSNIDMYPLVKSTAKMVDLADMLERS------------PHDLS 144
Cdd:PRK15134 80 HASEQTLRGVR-GNKIAMifqepmvslnplhTLEKQLYEVLSLHRGMRREAARGEILNCLDRVgirqaakrltdyPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVA 224
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNL-SIVRKLADRVAVMQNGRCVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 225 DMTPDEILAS-------KLLDThgirEPlylsalkaakapltcedklsnlkaldykrfrpavqawfADRPAPAAEkQYQP 297
Cdd:PRK15134 238 QNRAATLFSApthpytqKLLNS----EP--------------------------------------SGDPVPLPE-PASP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYD----------GEKNALEDVSFKIGKGEFVSILGKNGSGKSTiTKLIMGVIDADSGSSYLNGEDLSELS 367
Cdd:PRK15134 275 LLDVEQLQVAFPirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKST-TGLALLRLINSQGEIWFDGQPLHNLN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 368 ifeRSQ------KVGVVMQNPNHMISHHM-IFDEIAFGLR--NRNIAEELITEKVEHVLELCGLS-KFRH-WPIEaLSYG 436
Cdd:PRK15134 354 ---RRQllpvrhRIQVVFQDPNSSLNPRLnVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDpETRHrYPAE-FSGG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 437 QKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAA 516
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
....*....
gi 1382220129 517 MTEVFSQPS 525
Cdd:PRK15134 510 CERVFAAPQ 518
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-237 |
9.07e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.93 E-value: 9.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikgeVTGSLEINGKNISEFSmhdyt 82
Cdd:COG1121 7 IELENLTVSYG--GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-----TSGTVRLFGKPPRRAR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQ--DTDSQF-------VGL----SIG----------EDIAFALEnqlmsnidmyplvkstakMVDLADMLERS 139
Cdd:COG1121 75 RRIGYVPQraEVDWDFpitvrdvVLMgrygRRGlfrrpsradrEAVDEALE------------------RVGLEDLADRP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 140 PHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHRdIDRVILMER 219
Cdd:COG1121 137 IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREY-FDRVLLLNR 214
|
250
....*....|....*...
gi 1382220129 220 GeIVADMTPDEILASKLL 237
Cdd:COG1121 215 G-LVAHGPPEEVLTPENL 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
299-525 |
1.19e-40 |
|
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: 147.10 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLtySYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:cd03299 1 LKVENL--SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR--DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNpnHMISHHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03299 77 PQN--YALFPHMtVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-231 |
1.43e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 150.22 E-value: 1.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISE----- 75
Cdd:COG3839 3 SLELENVSKSYG--GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLE------DPTsGEILIGGRDVTDlppkd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 76 --FSMhdyteqvgtVLQdtdsQFV---GLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQR 150
Cdd:COG3839 75 rnIAM---------VFQ----SYAlypHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhrdiDRVILMERGEIVADMTPDE 230
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMtl-aDRIAVMNDGRIQQVGTPEE 220
|
.
gi 1382220129 231 I 231
Cdd:COG3839 221 L 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
299-525 |
1.50e-40 |
|
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: 147.10 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQnpNHMISHHM-IFDEIAFGLRNRNIA----EELITEKVEHVLELCGLSKF-RHWPIEaLSYGQKKRVTIASILVLEPE 452
Cdd:cd03296 80 FQ--HYALFRHMtVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLaDRYPAQ-LSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 453 LLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-229 |
1.90e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 147.54 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSmhd 80
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT-----SGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 ytEQVGTVLQDtDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDD 160
Cdd:COG1116 80 --PDRGVVFQE-PALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 161 VDILLFDEPLASLDPKTgKATI-EIIDQLHNETNKTIVIIEHrledvlhrDI-------DRVILMER--GEIVADMTPD 229
Cdd:COG1116 157 PEVLLMDEPFGALDALT-RERLqDELLRLWQETGKTVLFVTH--------DVdeavflaDRVVVLSArpGRIVEEIDVD 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
2.27e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 148.70 E-value: 2.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYESlDKPT----LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHaikgevTGSLEINGKNISE 75
Cdd:PRK13651 1 MQIKVKNIVKIFNK-KLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALlLPD------TGTIEWIFKDEKN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 76 FSMHDYTE------------------------QVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVD 131
Cdd:PRK13651 74 KKKTKEKEkvleklviqktrfkkikkikeirrRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 132 L-ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHnETNKTIVIIEHRLEDVLHRd 210
Cdd:PRK13651 154 LdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEW- 231
|
250 260
....*....|....*....|...
gi 1382220129 211 IDRVILMERGEIVADMTPDEILA 233
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDILS 254
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-229 |
3.23e-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: 145.31 E-value: 3.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSmhd 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT-----SGEVLVDGEPVTGPG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 ytEQVGTVLQDtDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDD 160
Cdd:cd03293 73 --PDRGYVFQQ-DALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 161 VDILLFDEPLASLDPKTgKATI--EIIDQLHnETNKTIVIIEHRLEDVLHRDiDRVILMER--GEIVADMTPD 229
Cdd:cd03293 150 PDVLLLDEPFSALDALT-REQLqeELLDIWR-ETGKTVLLVTHDIDEAVFLA-DRVVVLSArpGRIVAEVEVD 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
297-560 |
3.26e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 147.21 E-value: 3.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYDGEKN-ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKV 375
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNP-NHMISHHMIFDeIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13648 86 GIVFQNPdNQFVGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQPSLLERANLct 534
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGL-- 241
|
250 260
....*....|....*....|....*.
gi 1382220129 535 tsiyELATMMKIDDTNAFMQYFIDYE 560
Cdd:PRK13648 242 ----DLPFPIKINQMLGHQTSFLTYE 263
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-225 |
3.53e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.57 E-value: 3.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgeVT-GSLEINGKNISEFSMH 79
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDR------PTsGEVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DYT----EQVGTVLQdtDSQFV-GLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLA 154
Cdd:COG1136 79 ELArlrrRHIGFVFQ--FFNLLpELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHrlEDVLHRDIDRVILMERGEIVAD 225
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH--DPELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-235 |
9.17e-40 |
|
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: 144.68 E-value: 9.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTgsleINGKNISEFSMHDYT 82
Cdd:cd03254 3 IEFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-KGQIL----IDGIDIRDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTdsqfvglsigediaFALENQLMSNIDMYPL------VKSTAKMVDLADMLERSP-----------HDLSG 145
Cdd:cd03254 77 SMIGVVLQDT--------------FLFSGTIMENIRLGRPnatdeeVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVAD 225
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTI--KNADKILVLDDGKIIEE 218
|
250
....*....|
gi 1382220129 226 MTPDEILASK 235
Cdd:cd03254 219 GTHDELLAKK 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-519 |
1.24e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 150.94 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQ-VGTVLQDTdSQFVG 98
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD-----SGEILLDGEPVRFRSPRDAQAAgIAIIHQEL-NLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 LSIGEDIAFALENQLMSNIDMYPLVKSTAKMvdLADM-LERSPH----DLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:COG1129 94 LSVAENIFLGREPRRGGLIDWRAMRRRAREL--LARLgLDIDPDtpvgDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 174 DPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVlhRDI-DRVILMERGEIV-----ADMTPDEIlASKLLDthgiREply 247
Cdd:COG1129 172 TEREVERLFRIIRRLKAQ-GVAIIYISHRLDEV--FEIaDRVTVLRDGRLVgtgpvAELTEDEL-VRLMVG----RE--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 248 lsalkaakapltcedkLSNLkaldykrfrpavqawFADRPAPAAEkqyqPLLEVHGLTysydgEKNALEDVSFKIGKGEF 327
Cdd:COG1129 241 ----------------LEDL---------------FPKRAAAPGE----VVLEVEGLS-----VGGVVRDVSFSVRAGEI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 328 VSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE-------------RSQkvGVVmqnPNHMISHHMI--- 391
Cdd:COG1129 281 LGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayvpedrKGE--GLV---LDLSIRENITlas 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 392 FDEIA-FGLRNRN----IAEELITE---KVEHVLElcglskfrhwPIEALSYG--QKkrVTIASILVLEPELLILDEPTA 461
Cdd:COG1129 356 LDRLSrGGLLDRRreraLAEEYIKRlriKTPSPEQ----------PVGNLSGGnqQK--VVLAKWLATDPKVLILDEPTR 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 462 GQD-------YRnytsmlaFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIA---NAAMTE 519
Cdd:COG1129 424 GIDvgakaeiYR-------LIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGeldREEATE 483
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-234 |
1.69e-39 |
|
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: 144.56 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 9 SFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQVGTV 88
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW-----SGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 89 LQDTDSQF-----VGLSIGEdiafALENQLMSNIDMYplVKSTAKMVDL-ADMLERSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:COG1124 85 FQDPYASLhprhtVDRILAE----PLRIHGLPDREER--IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILAS 234
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHL-CDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
299-511 |
1.70e-39 |
|
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: 143.16 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGVV 378
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNpnHMISHHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03301 78 FQN--YALYPHMtVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-224 |
1.82e-39 |
|
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: 143.06 E-value: 1.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 5 FSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSmhdytEQ 84
Cdd:cd03235 2 VEDLTVSYG--GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT-----SGSIRVFGKPLEKER-----KR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 85 VGTVLQ----DTDS-----QFVGLSIGEDIAFAlenQLMSNIDmYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAG 155
Cdd:cd03235 70 IGYVPQrrsiDRDFpisvrDVVLMGLYGHKGLF---RRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHnETNKTIVIIEHRLEDVLHRdIDRVILMERgEIVA 224
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEY-FDRVLLLNR-TVVA 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-234 |
2.06e-39 |
|
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: 144.71 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISEFSMHDYTE----QVGTVLQDTdS 94
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI------EPTsGKVLIDGQDIAAMSRKELRElrrkKISMVFQSF-A 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 QFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLD 174
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 175 PKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEAL-RLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
300-510 |
2.19e-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: 141.23 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 300 EVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVM 379
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 380 QnpnhmishhmifdeiafglrnrniaeelitekvehvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 460 TAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-235 |
2.23e-39 |
|
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: 143.53 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNgLIPHAIkgEVT-GSLEINGKNISEFSMHDY 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTL---VN-LIPRFY--DVDsGRILIDGHDVRDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTdSQFVGlSIGEDIAFALENQLMSNidmyplVKSTAKMVDLADMLERSPH-----------DLSGGQKQR 150
Cdd:cd03251 75 RRQIGLVSQDV-FLFND-TVAENIAYGRPGATREE------VEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhnETNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDE 230
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLSTI--ENADRIVVLEDGKIVERGTHEE 222
|
....*
gi 1382220129 231 ILASK 235
Cdd:cd03251 223 LLAQG 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
299-511 |
4.64e-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: 140.61 E-value: 4.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVGVV 378
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPnhmishhMIFDEIafglrnrniaeeliteKVEHVLElcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILDE 458
Cdd:cd03230 79 PEEP-------SLYENL----------------TVRENLK--------------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 459 PTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-223 |
1.81e-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: 140.08 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 7 NFSFRYESLDKpTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEfsmHDYTEQVG 86
Cdd:cd03226 4 NISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPIKA---KERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 87 TVLQDTDSQFVGLSIGEDIAFALENqlmsnIDMYPLVKSTA-KMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:cd03226 75 YVMQDVDYQLFTDSVREELLLGLKE-----LDAGNEQAETVlKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 166 FDEPLASLDPKTGKATIEIIDQLHNETnKTIVIIEHRLEdVLHRDIDRVILMERGEIV 223
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQG-KAVIVITHDYE-FLAKVCDRVLLLANGAIV 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
299-524 |
1.88e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.06 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSifERS--- 372
Cdd:COG1135 2 IELENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALS--ERElra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 --QKVGVVMQNPNhMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRH-WPIEaLSYGQKKRVTIASILVL 449
Cdd:COG1135 80 arRKIGMIFQHFN-LLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADaYPSQ-LSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 450 EPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVleyttRSI-----VIADSKLIANAAMTEVFSQP 524
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVV-----RRIcdrvaVLENGRIVEQGPVLDVFANP 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
16-234 |
2.06e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 141.28 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNI--SEFSMHDYTEQVGTVLQDtd 93
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPD-----SGTITVDGEDLtdSKKDINKLRRKVGMVFQQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 94 sqfvglsigediaFALENQL--MSNIdMYPLV------KSTAK--------MVDLADMLERSPHDLSGGQKQRVSLAGIL 157
Cdd:COG1126 86 -------------FNLFPHLtvLENV-TLAPIkvkkmsKAEAEeramelleRVGLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 158 VDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIiehrledVLH-----RDI-DRVILMERGEIVADMTPDEI 231
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVV-------VTHemgfaREVaDRVVFMDGGRIVEEGPPEEF 223
|
...
gi 1382220129 232 LAS 234
Cdd:COG1126 224 FEN 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-223 |
2.16e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.06 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEkIV-IIGPSGSGKSTLGQCLNGLiphaikgEV--TGSLEINGKNISEFS 77
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGE-IFgIIGYSGAGKSTLIRCINLL-------ERptSGSVLVDGVDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 78 MHDYTE---QVGTVLQdtdsQFVGLS---IGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRV 151
Cdd:COG1135 74 ERELRAarrKIGMIFQ----HFNLLSsrtVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIV 223
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVV--RRIcDRVAVLENGRIV 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-236 |
2.52e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.97 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEFSmHDY 81
Cdd:COG1131 1 IEVRGLTKRYG--DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTS------GEVRVLGEDVARDP-AEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDtDSQFVGLSIGEDIAFALenqlmsniDMYPLVKSTAK--------MVDLADMLERSPHDLSGGQKQRVSL 153
Cdd:COG1131 72 RRRIGYVPQE-PALYPDLTVRENLRFFA--------RLYGLPRKEAReridelleLFGLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 154 AGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEILA 233
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEA-ERLCDRVAIIDKGRIVADGTPDELKA 220
|
...
gi 1382220129 234 SKL 236
Cdd:COG1131 221 RLL 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
299-513 |
2.78e-38 |
|
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: 149.98 E-value: 2.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:COG2274 474 IELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhMISHHMIFDEIAFGLRNRNIaeelitEKVEHVLELCGLSKFrhwpIEA---------------LSYGQKKRVT 442
Cdd:COG2274 554 VLQDV--FLFSGTIRENITLGDPDATD------EEIIEAARLAGLHDF----IEAlpmgydtvvgeggsnLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 443 IASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRdlGITVVIISHDMHLVlEYTTRSIVIADSKLIA 513
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVE 689
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
299-492 |
2.85e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.06 E-value: 2.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:COG3839 4 LELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR--NIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQN----PnhmishHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPEL 453
Cdd:COG3839 81 FQSyalyP------HMtVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHD 492
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
299-524 |
3.10e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 143.75 E-value: 3.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL-SELSIFERsqKVGV 377
Cdd:COG1118 3 IEVRNISKRFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER--RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQN----PnhmishHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKF-RHWPIEaLSYGQKKRVTIASILVLEP 451
Cdd:COG1118 80 VFQHyalfP------HMtVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLaDRYPSQ-LSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 452 ELLILDEPTAGQDyrnytsmlAFIQK--------LNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQ 523
Cdd:COG1118 153 EVLLLDEPFGALD--------AKVRKelrrwlrrLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
.
gi 1382220129 524 P 524
Cdd:COG1118 225 P 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
299-512 |
4.02e-38 |
|
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: 140.40 E-value: 4.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE-RSQ--KV 375
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlRQLrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNhMISHHMIFDEIAFG----------LRNRNIAEEliTEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIAS 445
Cdd:cd03256 81 GMIFQQFN-LIERLSVLENVLSGrlgrrstwrsLFGLFPKEE--KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 446 ILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-231 |
4.03e-38 |
|
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: 140.06 E-value: 4.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISEFSMHDy 81
Cdd:cd03300 1 IELENVSKFYG--GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE------TPTsGEILLDGKDITNLPPHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 tEQVGTVLQDTdSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:cd03300 72 -RPVNTVFQNY-ALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEI 231
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMS-DRIAVMNKGKIQQIGTPEEI 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-225 |
4.58e-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: 139.65 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAikgevtGSLEINGKNISEFSMHDY 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTS------GSVLLDGTDIRQLDPADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTdSQFVGlSIGEDIAFAlenqlMSNIDMYPLVKStAKMVDLADMLERSPH-----------DLSGGQKQR 150
Cdd:cd03245 77 RRNIGYVPQDV-TLFYG-TLRDNITLG-----APLADDERILRA-AELAGVTDFVNKHPNgldlqigergrGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtnKTIVIIEHRLedVLHRDIDRVILMERGEIVAD 225
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRP--SLLDLVDRIIVMDSGRIVAD 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
299-513 |
1.66e-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: 138.11 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKN-ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03245 3 IEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhmishHMIF----DEIAFGLRNRNiaeeliTEKVEHVLELCGLSKF--RH-----WPI----EALSYGQKKRVT 442
Cdd:cd03245 83 VPQDV------TLFYgtlrDNITLGAPLAD------DERILRAAELAGVTDFvnKHpngldLQIgergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 443 IASILVLEPELLILDEPTAGQDYRnytSMLAFIQKLNRDL-GITVVIISHDMHLvLEYTTRSIVIADSKLIA 513
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMN---SEERLKERLRQLLgDKTLIIITHRPSL-LDLVDRIIVMDSGRIVA 218
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-201 |
2.04e-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: 136.78 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHaikgevTGSLEINGKNI--SEFSMHDYTEQVGTVLQDTDSQF 96
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLrPQ------SGAVLIDGEPLdySRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 VGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPK 176
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....*
gi 1382220129 177 TGKATIEIIDQLhNETNKTIVIIEH 201
Cdd:TIGR01166 162 GREQMLAILRRL-RAEGMTVVISTH 185
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
297-520 |
2.39e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 138.71 E-value: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-V 375
Cdd:COG4674 9 PILYVEDLTVSFDGFK-ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLgI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNhMISHHMIFD--EIAFG--------LRNRNIAEEliTEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIAS 445
Cdd:COG4674 88 GRKFQKPT-VFEELTVFEnlELALKgdrgvfasLFARLTAEE--RDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGM 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 446 ILVLEPELLILDEPTAG--QDYRNYTSMLafIQKLNRDLgiTVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG4674 165 LLAQDPKLLLLDEPVAGmtDAETERTAEL--LKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEV 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-232 |
2.90e-37 |
|
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: 137.85 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDytEQVGTVLQDTdSQFVGL 99
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK-----PDSGKILLNGKDITNLPPEK--RDISYVPQNY-ALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGK 179
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 180 ATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEIL 232
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWALA-DKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
298-522 |
5.31e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 138.69 E-value: 5.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEK--NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKV 375
Cdd:PRK13642 4 ILEVENLVFKYEKESdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 456 LDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFS 522
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
296-531 |
9.27e-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: 137.14 E-value: 9.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSS-YLNGEDLSELSIFERSQK 374
Cdd:COG1119 1 DPLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVV---MQN--PNHMISHHMI----FDEIafGLRNRniAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIAS 445
Cdd:COG1119 80 IGLVspaLQLrfPRDETVLDVVlsgfFDSI--GLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 446 ILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIA---------NAA 516
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAagpkeevltSEN 235
|
250
....*....|....*
gi 1382220129 517 MTEVFSQPSLLERAN 531
Cdd:COG1119 236 LSEAFGLPVEVERRD 250
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-222 |
9.55e-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: 134.27 E-value: 9.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDYT 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR-----PTSGRVRLDGADISQWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDtDSQFVGlSIGEDIafalenqlmsnidmyplvkstakmvdladmlersphdLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03246 76 DHVGYLPQD-DELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEdvLHRDIDRVILMERGEI 222
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPE--TLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-231 |
9.64e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 137.95 E-value: 9.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYES---LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPhaikgeVTGSLEINGKNISEF 76
Cdd:PRK13649 1 MGINLQNVSYTYQAgtpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVP------TQGSVRVDDTLITST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 77 S----MHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLA-DMLERSPHDLSGGQKQRV 151
Cdd:PRK13649 75 SknkdIKQIRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHnETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEI 231
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANY-ADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-240 |
1.60e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 137.60 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYES---LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFS 77
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLK-----PTTGTVTVDDITITHKT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 78 MHDYTEQ----VGTVLQDTDSQFVGLSIGEDIAFALENQLMsNIDMyplVKSTAK--MVDLA---DMLERSPHDLSGGQK 148
Cdd:PRK13646 76 KDKYIRPvrkrIGMVFQFPESQLFEDTVEREIIFGPKNFKM-NLDE---VKNYAHrlLMDLGfsrDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTP 228
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVA-RYADEVIVMKEGSIVSQTSP 230
|
250
....*....|....
gi 1382220129 229 DEILA--SKLLDTH 240
Cdd:PRK13646 231 KELFKdkKKLADWH 244
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
315-461 |
1.73e-36 |
|
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: 132.77 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPNHmISHHMIFDE 394
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQL-FPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 395 IAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEA----LSYGQKKRVTIASILVLEPELLILDEPTA 461
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-231 |
2.35e-36 |
|
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: 135.54 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYESLdkPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEVTgsleINGKNISEFSMHD 80
Cdd:cd03296 1 MSIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-ERPDSGTIL----FGGEDATDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 ytEQVGTVLQDTdSQFVGLSIGEDIAFALE----NQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGI 156
Cdd:cd03296 74 --RNVGFVFQHY-ALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEI 231
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEV-ADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-234 |
2.47e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 136.76 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 7 NFSFRYE-SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDYTEQV 85
Cdd:PRK13642 9 NLVFKYEkESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-----EFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 86 GTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 166 FDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdiDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASS--DRILVMKAGEIIKEAAPSELFAT 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
283-513 |
2.52e-36 |
|
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: 142.59 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 283 FADRPAPAAEKQYQPL-------LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGS 355
Cdd:COG4988 314 LLDAPEPAAPAGTAPLpaagppsIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 356 SYLNGEDLSELSIFERSQKVGVVMQNPnhmishhMIF-----DEIAFGLRNRNIAEelitekVEHVLELCGLSKFrhwpI 430
Cdd:COG4988 394 ILINGVDLSDLDPASWRRQIAWVPQNP-------YLFagtirENLRLGRPDASDEE------LEAALEAAGLDEF----V 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 431 EA---------------LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHDMHL 495
Cdd:COG4988 457 AAlpdgldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLAL 534
|
250
....*....|....*...
gi 1382220129 496 VLEYtTRSIVIADSKLIA 513
Cdd:COG4988 535 LAQA-DRILVLDDGRIVE 551
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
288-532 |
2.57e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 139.31 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 288 APAAEKQYQPLLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS 367
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDG-KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 368 IFERsqKVGVVMQnpNHMISHHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:PRK09452 83 AENR--HVNTVFQ--SYALFPHMtVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPsl 526
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP-- 236
|
....*.
gi 1382220129 527 lerANL 532
Cdd:PRK09452 237 ---KNL 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
299-496 |
3.60e-36 |
|
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: 132.89 E-value: 3.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKN-ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhmishhMIFdeiafglrNRNIAEELitekvehvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03228 81 VPQDP-------FLF--------SGTIRENI------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLNRdlGITVVIISHDMHLV 496
Cdd:cd03228 122 EATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI 158
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
298-524 |
5.49e-36 |
|
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: 136.72 E-value: 5.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKN---ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDA---DSGSSYLNGEDLSELSIFE- 370
Cdd:COG0444 1 LLEVRNLKVYFPTRRGvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 371 ---RSQKVGVVMQNPnhMIS---HHMIFDEIAFGLRNRNIA-EELITEKVEHVLELCGLSK----FRHWPIEaLSYGQKK 439
Cdd:COG0444 81 rkiRGREIQMIFQDP--MTSlnpVMTVGDQIAEPLRIHGGLsKAEARERAIELLERVGLPDperrLDRYPHE-LSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 440 RVTIASILVLEPELLILDEPTAGQDyrnyTSM----LAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIV--------IA 507
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALD----VTIqaqiLNLLKDLQRELGLAILFITHDLGVVAEIADRVAVmyagriveEG 233
|
250
....*....|....*..
gi 1382220129 508 DSKlianaamtEVFSQP 524
Cdd:COG0444 234 PVE--------ELFENP 242
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
16-222 |
6.97e-36 |
|
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: 133.42 E-value: 6.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNI--SEFSMHDYTEQVGTVLQDTD 93
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD-----SGTIIIDGLKLtdDKKNINELRQKVGMVFQQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 94 sQFVGLSIGEDIAFALEN-QLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLAS 172
Cdd:cd03262 87 -LFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 173 LDPKTGKATIEIIDQLhNETNKTIVIIEHRLEdvLHRDI-DRVILMERGEI 222
Cdd:cd03262 166 LDPELVGEVLDVMKDL-AEEGMTMVVVTHEMG--FAREVaDRVIFMDDGRI 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
299-511 |
7.15e-36 |
|
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: 133.30 E-value: 7.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSEL---SIFERSQKV 375
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNpNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLS-KFRHWPIEaLSYGQKKRVTIASILVLEPELL 454
Cdd:cd03292 81 GVVFQD-FRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLShKHRALPAE-LSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLNrDLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-225 |
7.54e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 133.64 E-value: 7.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISEFSMHD-- 80
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER-PTSGQVL----VNGQDLSRLKRREip 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 -YTEQVGTVLQD----TDsqfvgLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAG 155
Cdd:COG2884 76 yLRRRIGVVFQDfrllPD-----RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 156 ILVDDVDILLFDEPLASLDPKTgkaTIEIIDQLH--NETNKTIVIIEHRLEDVLHRDIdRVILMERGEIVAD 225
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPET---SWEIMELLEeiNRRGTTVLIATHDLELVDRMPK-RVLELEDGRLVRD 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-221 |
7.72e-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: 131.21 E-value: 7.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 5 FSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQ 84
Cdd:cd00267 2 IENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 85 VGTVLQdtdsqfvglsigediafalenqlmsnidmyplvkstakmvdladmlersphdLSGGQKQRVSLAGILVDDVDIL 164
Cdd:cd00267 75 IGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 165 LFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLhRDIDRVILMERGE 221
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAE-LAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-221 |
9.44e-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: 131.93 E-value: 9.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYT 82
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-----SGSILIDGEDLTDLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQ--VGTVLQDTdSQFVGLSIGEDIAFALenqlmsnidmyplvkstakmvdladmlersphdlSGGQKQRVSLAGILVDD 160
Cdd:cd03229 74 LRrrIGMVFQDF-ALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 161 VDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGE 221
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAA-RLADRVVVLRDGK 178
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-268 |
1.26e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 134.96 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYE---SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNI---- 73
Cdd:PRK13641 1 MSIKFENVDYIYSpgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS-----SGTITIAGYHItpet 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 74 SEFSMHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLA-DMLERSPHDLSGGQKQRVS 152
Cdd:PRK13641 76 GNKNLKKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQlHNETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEIL 232
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD-YQKAGHTVILVTHNMDDVAEY-ADDVLVLEHGKLIKHASPKEIF 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1382220129 233 A-SKLLDTHGIREP--------LYLSALKAAKAPLTCEDKLSNLK 268
Cdd:PRK13641 234 SdKEWLKKHYLDEPatsrfaskLEKGGFKFSEMPLTIDELVDGIK 278
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-258 |
1.26e-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: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHdYT 82
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD-----SGSILIDGEDVRKEPRE-AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTDSqFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:COG4555 74 RQIGVLPDERGL-YDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHrDIDRVILMERGEIVADMTPDEILASKLLDThgi 242
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEA-LCDRVVILHKGKVVAQGSLDELREEIGEEN--- 227
|
250
....*....|....*.
gi 1382220129 243 REPLYLSALKAAKAPL 258
Cdd:COG4555 228 LEDAFVALIGSEEGEA 243
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-231 |
1.93e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 136.62 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEVTgsleINGKNISEFSMHDyt 82
Cdd:PRK09452 15 VELRGISKSFD--GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-ETPDSGRIM----LDGQDITHVPAEN-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTdSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK09452 86 RHVNTVFQSY-ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEI 231
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMS-DRIVVMRDGRIEQDGTPREI 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-231 |
2.25e-35 |
|
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: 132.81 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEINGKNISEFSMHDYT 82
Cdd:TIGR02315 2 LEVENLSKVYPN-GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLV-----EPSSGSILLEGTDITKLRGKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 E---QVGTVLQDTdsQFVGLSigediaFALENQLMSNIDMYPLVKSTAKM---------------VDLADMLERSPHDLS 144
Cdd:TIGR02315 76 KlrrRIGMIFQHY--NLIERL------TVLENVLHGRLGYKPTWRSLLGRfseedkeralsalerVGLADKAYQRADQLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVA 224
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQV-DLAKKYADRIVGLKAGEIVF 226
|
....*..
gi 1382220129 225 DMTPDEI 231
Cdd:TIGR02315 227 DGAPSEL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-235 |
2.79e-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: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISEFSMHDY 81
Cdd:cd03253 1 IEFENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFY------DVSsGSILIDGQDIREVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDT----DsqfvglSIGEDIAFALENqlMSNIDMYplvkSTAKMVDLADMLERSPHD-----------LSGG 146
Cdd:cd03253 74 RRAIGVVPQDTvlfnD------TIGYNIRYGRPD--ATDEEVI----EAAKAAQIHDKIMRFPDGydtivgerglkLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 147 QKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhnETNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADM 226
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIV--NADKIIVLKDGRIVERG 217
|
....*....
gi 1382220129 227 TPDEILASK 235
Cdd:cd03253 218 THEELLAKG 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
311-514 |
3.11e-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: 132.46 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVGVVMQNPNHMISHHM 390
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK-KFLRRIGVVFGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 391 IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTS 470
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1382220129 471 MLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIAN 514
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
311-528 |
4.23e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.61 E-value: 4.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYL---------NGEDLSELSifersQKVGVVMQN 381
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkKNKKLKPLR-----KKVGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 382 PNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:PRK13634 94 PEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEelLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 460 TAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLE 528
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELE 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
300-524 |
4.83e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 134.93 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 300 EVHGLTYSYDG---EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS----IFERs 372
Cdd:PRK11153 3 ELKNISKVFPQggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelRKAR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 QKVGVVMQNPNhMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRH-WPIEaLSYGQKKRVTIASILVLEP 451
Cdd:PRK11153 82 RQIGMIFQHFN-LLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADrYPAQ-LSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
298-545 |
5.13e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 132.80 E-value: 5.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VG 376
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLIL 456
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 457 DEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHlVLEYTTRSIVIADSKLIANAAMTEVFSQPSlLERANLCTTS 536
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVS-LQTLGLTPPS 237
|
....*....
gi 1382220129 537 IYELATMMK 545
Cdd:PRK13644 238 LIELAENLK 246
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
276-513 |
7.43e-35 |
|
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: 138.36 E-value: 7.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 276 RPAVQawFADRPAPAAEkqyQPLLEVHGLTYSYDGE-KNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSG 354
Cdd:COG4987 316 PPAVT--EPAEPAPAPG---GPSLELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 355 SSYLNGEDLSELSIFERSQKVGVVMQNPnHmishhmIFDEiafGLRNrNI---AEELITEKVEHVLELCGLSKF-RHWPI 430
Cdd:COG4987 391 SITLGGVDLRDLDEDDLRRRIAVVPQRP-H------LFDT---TLRE-NLrlaRPDATDEELWAALERVGLGDWlAALPD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 431 ----------EALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHDMHLvLEYT 500
Cdd:COG4987 460 gldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAG-LERM 536
|
250
....*....|...
gi 1382220129 501 TRSIVIADSKLIA 513
Cdd:COG4987 537 DRILVLEDGRIVE 549
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
299-513 |
1.30e-34 |
|
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: 129.93 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSElSIFERSQKVGV 377
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQnpnhmisHHMIFDE------IAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:cd03263 80 CPQ-------FDALFDEltvrehLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-234 |
1.50e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 133.73 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNI-SEFSM 78
Cdd:COG1118 1 MSIEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLEtPDS------GRIVLNGRDLfTNLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 79 HDytEQVGTVLQDTDsQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILV 158
Cdd:COG1118 73 RE--RRVGFVFQHYA-LFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 159 DDVDILLFDEPLASLDPKTgKATIEI-IDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKV-RKELRRwLRRLHDELGGTTVFVTHDQEEAL-ELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-231 |
1.67e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 131.46 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 7 NFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDYTEQVG 86
Cdd:PRK13652 8 DLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK-----PTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 87 TVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PRK13652 82 LVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 167 DEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEI 231
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQL-DLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
299-515 |
1.79e-34 |
|
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: 129.26 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSifERSQKVGVV 378
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNP---NHMIS-HHMIFDEIAFGLRNRNIAEelitekvehVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:cd03268 78 IEAPgfyPNLTArENLRLLARLLGIRKKRIDE---------VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANA 515
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-245 |
1.97e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 131.35 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 7 NFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNI--SEFSMHDYTEQ 84
Cdd:PRK13639 6 DLKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILK-----PTSGEVLIKGEPIkyDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 85 VGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:PRK13639 80 VGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 165 LFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILA-SKLLDTHGIR 243
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDV-DLVPVYADKVYVMSDGKIIKEGTPKEVFSdIETIRKANLR 237
|
..
gi 1382220129 244 EP 245
Cdd:PRK13639 238 LP 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
285-525 |
2.07e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 133.81 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 285 DRPAPAAEKQYQPLLEVHGLTYSYDGEkNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLS 364
Cdd:PRK11607 6 PRPQAKTRKALTPLLEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 365 ELSIFERSqkvgVVMQNPNHMISHHMIFDE-IAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTI 443
Cdd:PRK11607 85 HVPPYQRP----INMMFQSYALFPHMTVEQnIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 444 ASILVLEPELLILDEPTAGQDYRNYTSM-LAFIQKLNRdLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFS 522
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
...
gi 1382220129 523 QPS 525
Cdd:PRK11607 240 HPT 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-251 |
2.35e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 131.67 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYES---LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEI--NGKNISEfs 77
Cdd:PRK13645 7 IILDNVSYTYAKktpFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 78 MHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLA-DMLERSPHDLSGGQKQRVSLAGI 156
Cdd:PRK13645 85 VKRLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASKL 236
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVL-RIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
250
....*....|....*
gi 1382220129 237 LDTHGIREPLYLSAL 251
Cdd:PRK13645 244 LLTKIEIDPPKLYQL 258
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
299-512 |
3.00e-34 |
|
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: 129.22 E-value: 3.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDA-----DSGSSYLNGEDLSELSIF--ER 371
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 372 SQKVGVVMQNPNhMIshHM-IFDEIAFGLRNRNIAE-ELITEKVEHVLELCGLSKF--RHWPIEALSYGQKKRVTIASIL 447
Cdd:cd03260 80 RRRVGMVFQKPN-PF--PGsIYDNVAYGLRLHGIKLkEELDERVEEALRKAALWDEvkDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 448 VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlgITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
299-524 |
4.24e-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: 129.20 E-value: 4.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VGV 377
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPNhmishhmIF------DEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:cd03218 80 LPQEAS-------IFrkltveENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 452 ELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-234 |
1.54e-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: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISEFSMHDYT 82
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV-PENGRVL----VDGHDLALADPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQdtDSQFVGLSIGEDIAFALENQLMSNIDmyplvkSTAKMVDLADMLERSPH-----------DLSGGQKQRV 151
Cdd:cd03252 76 RQVGVVLQ--ENVLFNRSIRDNIALADPGMSMERVI------EAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 152 SLAGILVDDVDILLFDEPLASLDPKTGKAtieIIDQLHN-ETNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDE 230
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHA---IMRNMHDiCAGRTVIIIAHRLSTV--KNADRIIVMEKGRIVEQGSHDE 222
|
....
gi 1382220129 231 ILAS 234
Cdd:cd03252 223 LLAE 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-237 |
2.27e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 127.01 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLdkPTlkNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNisefsmHDYT 82
Cdd:PRK10771 2 LKLTDITWLYHHL--PM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA-----SGSLTLNGQD------HTTT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 ----EQVGTVLQDtDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILV 158
Cdd:PRK10771 67 ppsrRPVSMLFQE-NNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEIL-----A 233
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDA-ARIAPRSLVVADGRIAWDGPTDELLsgkasA 224
|
....
gi 1382220129 234 SKLL 237
Cdd:PRK10771 225 SALL 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-233 |
2.87e-33 |
|
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: 134.99 E-value: 2.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISEFSMHDYT 82
Cdd:TIGR03375 464 IEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQ-PTEGSVL----LDGVDIRQIDPADLR 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTdSQFVGlSIGEDIAF---ALENQLMSNIdmyplvkstAKMVDLADMLERSPH-----------DLSGGQK 148
Cdd:TIGR03375 539 RNIGYVPQDP-RLFYG-TLRDNIALgapYADDEEILRA---------AELAGVTEFVRRHPDgldmqigergrSLSGGQR 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKatiEIIDQLHNET-NKTIVIIEHRLEdvLHRDIDRVILMERGEIVADMT 227
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSEE---RFKDRLKRWLaGKTLVLVTHRTS--LLDLVDRIIVMDNGRIVADGP 682
|
....*.
gi 1382220129 228 PDEILA 233
Cdd:TIGR03375 683 KDQVLE 688
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
296-519 |
3.61e-33 |
|
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: 126.39 E-value: 3.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSifE-- 370
Cdd:COG4181 6 APIIELRGLTKTVgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD--Eda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 371 ----RSQKVGVVMQNpNHMISHH------MIFDEIAfGLRN-RNIAEELitekvehvLELCGLSK-FRHWPIEaLSYGQK 438
Cdd:COG4181 84 rarlRARHVGFVFQS-FQLLPTLtalenvMLPLELA-GRRDaRARARAL--------LERVGLGHrLDHYPAQ-LSGGEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 439 KRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLvLEYTTRSIVIADSKLIANAAMT 518
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL-AARCDRVLRLRAGRLVEDTAAT 231
|
.
gi 1382220129 519 E 519
Cdd:COG4181 232 A 232
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-234 |
4.27e-33 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 130.61 E-value: 4.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISEFSMHDYTE----QVGTVLQdtds 94
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLI------EPTaGEVLIDGEDITKLSKKELRElrrkKMSMVFQ---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 QFvGL----SIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:COG4175 113 HF-ALlphrTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAF 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 171 ASLDPktgkatieII-----DQ---LHNETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIVADMTPDEILAS 234
Cdd:COG4175 192 SALDP--------LIrremqDElleLQAKLKKTIVFITHDLDEALR--LgDRIAIMKDGRIVQIGTPEEILTN 254
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-217 |
4.44e-33 |
|
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: 132.80 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESLDkPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDY 81
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDtdSQFVGLSIGEDIAFALENQLMSnidmypLVKSTAKMVDLADMLE-----------RSPHDLSGGQKQR 150
Cdd:TIGR02857 395 RDQIAWVPQH--PFLFAGTIAENIRLARPDASDA------EIREALERAGLDEFVAalpqgldtpigEGGAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNetNKTIVIIEHRLEDVlhRDIDRVILM 217
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA--ALADRIVVL 529
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
304-541 |
6.12e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 127.17 E-value: 6.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 304 LTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS----IFERSQKV 375
Cdd:PRK13649 8 VSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVLEPEL 453
Cdd:PRK13649 88 GLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKNPFE-LSGGQMRRVAIAGILAMEPKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANLC 533
Cdd:PRK13649 167 LVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLEEKQLG 245
|
....*...
gi 1382220129 534 TTSIYELA 541
Cdd:PRK13649 246 VPKITKFA 253
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-228 |
7.08e-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: 7.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDYT 82
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE-----LSSGSILIDGVDISKIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDtdsqfvglsigediAFALENQLMSNID------------------MYPLVKSTAKMVDLadMLERSPHDLS 144
Cdd:cd03244 78 SRISIIPQD--------------PVLFSGTIRSNLDpfgeysdeelwqalervgLKEFVESLPGGLDT--VVEEGGENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDPktgkATIEIIDQL--HNETNKTIVIIEHRLEDVLhrDIDRVILMERGEI 222
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDP----ETDALIQKTirEAFKDCTVLTIAHRLDTII--DSDRILVLDKGRV 215
|
....*.
gi 1382220129 223 VADMTP 228
Cdd:cd03244 216 VEFDSP 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
299-506 |
8.54e-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: 125.24 E-value: 8.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VGV 377
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPNhmISHHM-IFDEIAFGLRNRNIAEelITEKVEHVLELC-GLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:cd03224 80 VPEGRR--IFPELtVEENLLLGAYARRRAK--RKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 456 LDEPTAG------QDyrnytsMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVI 506
Cdd:cd03224 156 LDEPSEGlapkivEE------IFEAIREL-RDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
311-532 |
8.78e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 127.25 E-value: 8.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL----SELSIFERSQKVGVVMQNPNHMI 386
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 387 SHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVLEPELLILDEPTAGQD 464
Cdd:PRK13641 99 FENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdlISKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 465 YRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANL 532
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYL 244
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
299-532 |
1.43e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 127.12 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGS---SYLNGEDLSELSIFE- 370
Cdd:PRK13651 3 IKVKNIVKIFNKklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 371 ----------RSQK----------VGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGL--SKFRHW 428
Cdd:PRK13651 83 vleklviqktRFKKikkikeirrrVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdeSYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 429 PIEaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIAD 508
Cdd:PRK13651 163 PFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250 260
....*....|....*....|....
gi 1382220129 509 SKLIANAAMTEVFSQPSLLERANL 532
Cdd:PRK13651 241 GKIIKDGDTYDILSDNKFLIENNM 264
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-225 |
1.72e-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: 124.14 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKptlkNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHaikgevTGSLEINGKNISEFSMHDy 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQ------SGRVLINGVDVTAAPPAD- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 tEQVGTVLQDtDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:cd03298 70 -RPVSMLFQE-NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVAD 225
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLA-QRVVFLDNGRIAAQ 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-237 |
2.40e-32 |
|
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: 124.81 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHA------IKGEVTGSLEING--KNIS 74
Cdd:COG1119 4 LELRNVTVRRG--GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTygndvrLFGERRGGEDVWElrKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 75 EFS--MHDYTEQVGTVLQDTDSQFVGlSIG-------EDIAFALEnqLMsnidmyplvkstaKMVDLADMLERSPHDLSG 145
Cdd:COG1119 82 LVSpaLQLRFPRDETVLDVVLSGFFD-SIGlyreptdEQRERARE--LL-------------ELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVAD 225
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIP-PGITHVLLLKDGRVVAA 224
|
250
....*....|..
gi 1382220129 226 MTPDEILASKLL 237
Cdd:COG1119 225 GPKEEVLTSENL 236
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-222 |
3.15e-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: 123.43 E-value: 3.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 24 NLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISefSMHDYTEQVGTVLQDtDSQFVGLSIGE 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPA-----SGSIKVNDQSHT--GLAPYQRPVSMLFQE-NNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 104 DIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIE 183
Cdd:TIGR01277 90 NIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1382220129 184 IIDQLHNETNKTIVIIEHRLEDvLHRDIDRVILMERGEI 222
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSD-ARAIASQIAVVSQGKI 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-513 |
3.83e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.76 E-value: 3.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVtgslEINGKNISEFSMHDYTEQ-VGTVLQ-----DTd 93
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLY-QPDSGEI----LIDGKPVRIRSPRDAIALgIGMVHQhfmlvPN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 94 sqfvgLSIGEDIAFALENQLMSNIDMyplvKSTAKMV-DLADM------LERSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:COG3845 95 -----LTVAENIVLGLEPTKGGRLDR----KAARARIrELSERygldvdPDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 167 DEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEilasklldthgirep 245
Cdd:COG3845 166 DEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREV--MAIaDRVTVLRRGKVVGTVDTAE--------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 246 lylsalkaakaplTCEDKLSNL---KALDYKRFRPavqawfadrPAPAAEkqyqPLLEVHGLTYSYDGEKNALEDVSFKI 322
Cdd:COG3845 228 -------------TSEEELAELmvgREVLLRVEKA---------PAEPGE----VVLEVENLSVRDDRGVPALKDVSLEV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 323 GKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VGVVMQNPNHM-------ISHHMIFDE 394
Cdd:COG3845 282 RAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRglvpdmsVAENLILGR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 395 IA------FGLRNRNIAEELITEKVEhvlelcglsKFR------HWPIEALSYG--QKkrVTIASILVLEPELLILDEPT 460
Cdd:COG3845 362 YRrppfsrGGFLDRKAIRAFAEELIE---------EFDvrtpgpDTPARSLSGGnqQK--VILARELSRDPKLLIAAQPT 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 461 AGQDYRNytsmLAFI-QKLN--RDLGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:COG3845 431 RGLDVGA----IEFIhQRLLelRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
297-530 |
4.34e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 124.11 E-value: 4.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVG 376
Cdd:PRK13548 1 AMLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQnpnhmiSHHMIFD----EI-AFGL---RNRNIAEELItekVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:PRK13548 80 VLPQ------HSSLSFPftveEVvAMGRaphGLSRAEDDAL---VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 449 ------LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFs 522
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL- 229
|
....*...
gi 1382220129 523 QPSLLERA 530
Cdd:PRK13548 230 TPETLRRV 237
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-225 |
4.74e-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: 121.65 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTgsleINGKNISEfsmhdyt 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL-KPQQGEIT----LDGVPVSD------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 eqvgtvLQDTDSQFVGLsigediafalenqlmsnIDMYPLVKSTAKMVDLAdmlERsphdLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03247 69 ------LEKALSSLISV-----------------LNQRPYLFDTTLRNNLG---RR----FSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEII-DQLHnetNKTIVIIEHRLEDVLHrdIDRVILMERGEIVAD 225
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIfEVLK---DKTLIWITHHLTGIEH--MDKILFLENGKIIMQ 177
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-215 |
6.14e-32 |
|
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: 122.34 E-value: 6.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNglIPHAIKGEVTGSLEINGKNI----SEFSMHDYTEQVGTVLQD 91
Cdd:TIGR03608 10 DKVILDDLNLTIEKGKMYAIIGESGSGKSTL---LN--IIGLLEKFDSGQVYLNGQETpplnSKKASKFRREKLGYLFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 92 ---TDSQfvglSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:TIGR03608 85 falIENE----TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1382220129 169 PLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEdvLHRDIDRVI 215
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPE--VAKQADRVI 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
284-491 |
8.42e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.51 E-value: 8.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 284 ADRPAPAAEKQYQPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL 363
Cdd:COG1132 325 PDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 364 SELSIFERSQKVGVVMQNPnhmishhMIFDE-----IAFGlrNRNIAEelitEKVEHVLELCGLSKFrhwpIEA------ 432
Cdd:COG1132 405 RDLTLESLRRQIGVVPQDT-------FLFSGtirenIRYG--RPDATD----EEVEEAAKAAQAHEF----IEAlpdgyd 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 433 ---------LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRdlGITVVIISH 491
Cdd:COG1132 468 tvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH 533
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
299-524 |
9.42e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 122.56 E-value: 9.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGE-KNAledvSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGV 377
Cdd:COG3840 2 LRLDDLTYRYGDFpLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER--PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNpNHMISHHMIFDEIAFGLR---NRNIAEElitEKVEHVLELCGLSKF--RHwPiEALSYGQKKRVTIASILVLEPE 452
Cdd:COG3840 76 LFQE-NNLFPHLTVAQNIGLGLRpglKLTAEQR---AQVEQALERVGLAGLldRL-P-GQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 453 LLILDEPTAGQD--YRNytSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:COG3840 150 ILLLDEPFSALDpaLRQ--EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-240 |
9.95e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 124.96 E-value: 9.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTGSLEINGKNISEFSMHDYTEQ------------VGT 87
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK-YGTIQVGDIYIGDKKNNHELITNPYSkkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 88 VLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDL-ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PRK13631 121 VFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 167 DEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEILASKLLDTH 240
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVA-DEVIVMDKGKILKTGTPYEIFTDQHIINS 272
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-231 |
1.02e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 125.58 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEfsMHDYTEQVGTVLQDTdSQFVGL 99
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT-----SGHIRFHGTDVSR--LHARDRKVGFVFQHY-ALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAFAL------ENQLMSNIDMYplVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:PRK10851 90 TVFDNIAFGLtvlprrERPNAAAIKAK--VTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 174 DPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEI 231
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEV-ADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
299-519 |
1.07e-31 |
|
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: 122.09 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsQKVGVV 378
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR-RRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPnhmishhmIFDEIAFGLRN-------RNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEP 451
Cdd:cd03265 79 FQDL--------SVDDELTGWENlyiharlYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-235 |
1.17e-31 |
|
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: 122.55 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVtgslEINGKNISEFSMHDYTEQ-VGTVLQDTdSQFVG 98
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR-PTSGSV----LFDGEDITGLPPHEIARLgIGRTFQIP-RLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 LSIGEDIAFALENQLMSNIDMYPLVKS----------TAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:cd03219 90 LTVLENVMVAAQARTGSGLLLARARREereareraeeLLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 169 PLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEILASK 235
Cdd:cd03219 170 PAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVV--MSLaDRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-223 |
1.21e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 122.43 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYESLdkPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPhaikgeVTGSLEING------KNI 73
Cdd:COG4161 1 MSIQLKNINCFYGSH--QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLeTP------DSGQLNIAGhqfdfsQKP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 74 SEFSMHDYTEQVGTVLQdtdsQF---VGLSIgediafaLENQLMSNIDMYPLVKSTA--------KMVDLADMLERSPHD 142
Cdd:COG4161 73 SEKAIRLLRQKVGMVFQ----QYnlwPHLTV-------MENLIEAPCKVLGLSKEQArekamkllARLRLTDKADRFPLH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 143 LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEdVLHRDIDRVILMERGEI 222
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVE-FARKVASQVVYMEKGRI 219
|
.
gi 1382220129 223 V 223
Cdd:COG4161 220 I 220
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-223 |
1.99e-31 |
|
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: 121.28 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRY--ESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNI---SEF 76
Cdd:TIGR02982 1 VISIRNLNHYYghGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGL-----RSVQEGSLKVLGQELhgaSKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 77 SMHDYTEQVGTVLQdTDSQFVGLSIGEDIAFALE-NQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAG 155
Cdd:TIGR02982 76 QLVQLRRRIGYIFQ-AHNLLGFLTARQNVQMALElQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEH--RLEDVlhrdIDRVILMERGEIV 223
Cdd:TIGR02982 155 ALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHdnRILDV----ADRILQMEDGKLL 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
299-514 |
2.49e-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: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE-RSQKVGV 377
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQnpnhmishhmifdeiafglrnrniaeelitekvehvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIAN 514
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-232 |
2.63e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLipHAIKGE--VTGSLEINGKNISEfsmHD 80
Cdd:PRK09493 2 IEFKNVSKHFG--PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL--EEITSGdlIVDGLKVNDPKVDE---RL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQdtdsQFV---GLSIGEDIAFA-LENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGI 156
Cdd:PRK09493 75 IRQEAGMVFQ----QFYlfpHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEdvLHRDI-DRVILMERGEIVADMTPDEIL 232
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIG--FAEKVaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-245 |
4.08e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 122.53 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKP----TLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEV-TGSLEINGKNiSEFS 77
Cdd:PRK13643 2 IKFEKVNYTYQP-NSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL-QPTEGKVtVGDIVVSSTS-KQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 78 MHDYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLA-DMLERSPHDLSGGQKQRVSLAGI 156
Cdd:PRK13643 79 IKPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHnETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILAS-K 235
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADY-ADYVYLLEKGHIISCGTPSDVFQEvD 236
|
250
....*....|
gi 1382220129 236 LLDTHGIREP 245
Cdd:PRK13643 237 FLKAHELGVP 246
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
16-223 |
4.31e-31 |
|
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: 120.05 E-value: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISEFSMHDytEQVGTVLQDTdS 94
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE------EPTsGRIYIGGRDVTDLPPKD--RDIAMVFQNY-A 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 QFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLD 174
Cdd:cd03301 83 LYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1382220129 175 PKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERGEIV 223
Cdd:cd03301 163 AKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMA-DRIAVMNDGQIQ 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
314-493 |
4.43e-31 |
|
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: 121.60 E-value: 4.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE----RSQKVGVVMQNPNHMiSHH 389
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelRRKKISMVFQSFALL-PHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 390 MIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYT 469
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180
....*....|....*....|....
gi 1382220129 470 SMLAFIQKLNRDLGITVVIISHDM 493
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHDL 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
298-524 |
4.84e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 121.80 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSyDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS---IFERSQK 374
Cdd:PRK11831 7 LVDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMQNpNHMISHHMIFDEIAFGLR-NRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPEL 453
Cdd:PRK11831 86 MSMLFQS-GALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-235 |
5.42e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.88 E-value: 5.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNI--SEFSMHDYTEQVGTVLQDTDSQFV 97
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK-----PSSGRILFDGKPIdySRKGLMKLRESVGMVFQDPDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 98 GLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKT 177
Cdd:PRK13636 97 SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 178 GKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILASK 235
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDI-DIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-245 |
5.81e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 121.65 E-value: 5.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHaiKGEVTGsleiNGK--NISEFSMH 79
Cdd:PRK13638 2 LATSDLWFRYQ--DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ--KGAVLW----QGKplDYSKRGLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVD 159
Cdd:PRK13638 74 ALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 160 DVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKtIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILA-SKLLD 238
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDI-DLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAME 231
|
....*..
gi 1382220129 239 THGIREP 245
Cdd:PRK13638 232 QAGLTQP 238
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-222 |
8.36e-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: 117.88 E-value: 8.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISEfSMHDYT 82
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-PDSGEIK----VLGKDIKK-EPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDtDSQFVGLSIGEdiafalenqlmsNIDmyplvkstakmvdladmlersphdLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03230 73 RRIGYLPEE-PSLYENLTVRE------------NLK------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHRdIDRVILMERGEI 222
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERL-CDRVAILNNGRI 173
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-233 |
8.41e-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: 127.38 E-value: 8.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPhaikgeVTGSLEINGKNISEFSMHDY 81
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFeTP------ESGSVFYDGQDLAGLDVQAV 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDtdSQFVGLSIGEDIAFAleNQLmsNIDmypLVKSTAKMVDLADMLERSP---H--------DLSGGQKQR 150
Cdd:TIGR03797 526 RRQLGVVLQN--GRLMSGSIFENIAGG--APL--TLD---EAWEAARMAGLAEDIRAMPmgmHtvisegggTLSGGQRQR 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhnetNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPDE 230
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTI--RNADRIYVLDAGRVVQQGTYDE 670
|
...
gi 1382220129 231 ILA 233
Cdd:TIGR03797 671 LMA 673
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
296-496 |
1.42e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 121.76 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKN----------ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSE 365
Cdd:COG4608 5 EPLLEVRDLKKHFPVRGGlfgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 366 LS---IFERSQKVGVVMQNP----NhmiSHHMIFDEIAFGLRNRNIA-EELITEKVEHVLELCGLSK--FRHWPIEaLSY 435
Cdd:COG4608 85 LSgreLRPLRRRMQMVFQDPyaslN---PRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLRPehADRYPHE-FSG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 436 GQKKRVTIASILVLEPELLILDEPTAGQDYrnytSMLAfiQKLN------RDLGITVVIISHDMHLV 496
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDV----SIQA--QVLNlledlqDELGLTYLFISHDLSVV 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-235 |
1.49e-30 |
|
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: 119.57 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESL-DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQclngLI-----PhaikgeVTGSLEINGKNISEF 76
Cdd:cd03249 1 IEFKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVS----LLerfydP------TSGEILLDGVDIRDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 77 SMHDYTEQVGTVLQDtdSQFVGLSIGEDIAFALENQLMSnidmypLVKSTAKMVDLADMLERSPH-----------DLSG 145
Cdd:cd03249 71 NLRWLRSQIGLVSQE--PVLFDGTIAENIRYGKPDATDE------EVEEAAKKANIHDFIMSLPDgydtlvgergsQLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHneTNKTIVIIEHRLEDVlhRDIDRVILMERGEIVAD 225
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTI--RNADLIAVLQNGQVVEQ 218
|
250
....*....|
gi 1382220129 226 MTPDEILASK 235
Cdd:cd03249 219 GTHDELMAQK 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
304-545 |
2.13e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 120.50 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 304 LTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSS----YLNGEDLSELSIFERSQK- 374
Cdd:PRK13645 12 VSYTYAKktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIKEVKRLRKe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILVLEPE 452
Cdd:PRK13645 92 IGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdyVKRSPFE-LSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 453 LLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERANL 532
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEI 250
|
250
....*....|...
gi 1382220129 533 CTTSIYELATMMK 545
Cdd:PRK13645 251 DPPKLYQLMYKLK 263
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-229 |
3.53e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 119.20 E-value: 3.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYESL--DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSm 78
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS-----SGEITLDGVPVTGPG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 79 hdyTEQvGTVLQDtDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILV 158
Cdd:COG4525 76 ---ADR-GVVFQK-DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMER--GEIVADMTPD 229
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLA-TRLVVMSPgpGRIVERLELD 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-223 |
3.54e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 118.99 E-value: 3.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG---LIPHAikgEVTGSLEINGKNISEFSMh 79
Cdd:COG1117 12 IEVRNLNVYYG--DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGA---RVEGEILLDGEDIYDPDV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DYTE---QVGTVLQdtdsQ---FVgLSIGEDIAFALE-NQLMSNIDMYPLVKSTAKMVDL----ADMLERSPHDLSGGQK 148
Cdd:COG1117 86 DVVElrrRVGMVFQ----KpnpFP-KSIYDNVAYGLRlHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETnkTIVIIEHRLEDVLhRDIDRVILMERGEIV 223
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAA-RVSDYTAFFYLGELV 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
299-525 |
6.41e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.57 E-value: 6.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsqKVGVV 378
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR--KVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNpnHMISHHM-IFDEIAFGL-----RNR-NIAEelITEKVEHVLELCGLSKF-RHWPIEaLSYGQKKRVTIASILVLE 450
Cdd:PRK10851 80 FQH--YALFRHMtVFDNIAFGLtvlprRERpNAAA--IKAKVTQLLEMVQLAHLaDRYPAQ-LSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 451 PELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-235 |
7.29e-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: 124.16 E-value: 7.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISEFSMHD 80
Cdd:COG5265 357 EVRFENVSFGYDP-ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY------DVTsGRILIDGQDIRDVTQAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQDT----DsqfvglSIGEDIAF----ALENQlmsnidmyplVKSTAKMVDLADMLERSPH----------- 141
Cdd:COG5265 430 LRAAIGIVPQDTvlfnD------TIAYNIAYgrpdASEEE----------VEAAARAAQIHDFIESLPDgydtrvgergl 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 142 DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKAtieIIDQLHNET-NKTIVIIEHRLEDVlhRDIDRVILMERG 220
Cdd:COG5265 494 KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA---IQAALREVArGRTTLVIAHRLSTI--VDADEILVLEAG 568
|
250
....*....|....*
gi 1382220129 221 EIVADMTPDEILASK 235
Cdd:COG5265 569 RIVERGTHAELLAQG 583
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
299-513 |
7.58e-30 |
|
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: 116.61 E-value: 7.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSelsiFERSQKVGVV 378
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQN----PNHMISHHMIFdeiaFG-LRNRNIAEelITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPEL 453
Cdd:cd03269 76 PEErglyPKMKVIDQLVY----LAqLKGLKKEE--ARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
299-512 |
8.26e-30 |
|
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: 116.52 E-value: 8.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVsILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsQKVGVV 378
Cdd:cd03264 1 LQLENLTKRYGK-KRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPNhMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:cd03264 78 PQEFG-VYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 459 PTAGQDYRNYTSMLAFIQKLNRDlgiTVVIIS-HDMHLVLEYTTRSIVIADSKLI 512
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGED---RIVILStHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-519 |
1.06e-29 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 122.59 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQ-VGTVLQDTdSQFVG 98
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT-----KGTITINNINYNKLDHKLAAQLgIGIIYQEL-SVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 LSIGED--IAFALENQLMS-NIDMYPLVKSTAKMVDLADMLERSPH----DLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:PRK09700 95 LTVLENlyIGRHLTKKVCGvNIIDWREMRVRAAMMLLRVGLKVDLDekvaNLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 172 SLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLhRDIDRVILMERGE-----IVADMTPDEILasKLLDThgiREpl 246
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIR-RICDRYTVMKDGSsvcsgMVSDVSNDDIV--RLMVG---RE-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 247 ylsalkaakapltcedklsnlkaldykrfrpaVQAWFADRPAPAAEKQYQPLLEVHGLTySYDGEKnaLEDVSFKIGKGE 326
Cdd:PRK09700 246 --------------------------------LQNRFNAMKENVSNLAHETVFEVRNVT-SRDRKK--VRDISFSVCRGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 327 FVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VGVVMQN-------PNHMISHHM-IFDEI-- 395
Cdd:PRK09700 291 ILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYITESrrdngffPNFSIAQNMaISRSLkd 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 396 -----AFGLRNRNiAEELITEKVEHVLELCGLSKFRHwpIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTS 470
Cdd:PRK09700 371 ggykgAMGLFHEV-DEQRTAENQRELLALKCHSVNQN--ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAE 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 471 MLAFIQKLNrDLGITVVIISHDMHLVLEYTTRSIVIADSK----LIANAAMTE 519
Cdd:PRK09700 448 IYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRltqiLTNRDDMSE 499
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
296-524 |
1.11e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.40 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSiferSQKV 375
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLL-AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP----GHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 ---GVV--MQN----------PNHMISHHM---------IFDEIAFglrNRNIAEELitEKVEHVLELCGLSKFRHWPIE 431
Cdd:PRK11300 78 armGVVrtFQHvrlfremtviENLLVAQHQqlktglfsgLLKTPAF---RRAESEAL--DRAATWLERVGLLEHANRQAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 432 ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
250
....*....|...
gi 1382220129 512 IANAAMTEVFSQP 524
Cdd:PRK11300 233 LANGTPEEIRNNP 245
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-171 |
1.12e-29 |
|
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: 113.90 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTgsleINGKNISEFSMHDYTEQVGTVLQDtDSQFVGL 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL-SPTEGTIL----LDGQDLTDDERKSLRKEIGYVFQD-PQLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 100 SIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLER----SPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-221 |
1.40e-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: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYES---LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIphaikGEVT---GSLEINGKnISef 76
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSL---LSALL-----GELEklsGSVSVPGS-IA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 77 smhdYTEQVGTVLQDTdsqfvglsIGEDIAFALEnqlmSNIDMYPLV-KSTAKMVDLADMlersPH-D----------LS 144
Cdd:cd03250 70 ----YVSQEPWIQNGT--------IRENILFGKP----FDEERYEKViKACALEPDLEIL----PDgDlteigekginLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIE--IIDQLHNetNKTIVIIEHRLEDVLHrdIDRVILMERGE 221
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPH--ADQIVVLDNGR 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
296-524 |
1.40e-29 |
|
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: 122.49 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKStITKL-IMGVIDAD----SGSSYLNGEDLSELS 367
Cdd:COG4172 4 MPLLSVEDLSVAFgqgGGTVEAVKGVSFDIAAGETLALVGESGSGKS-VTALsILRLLPDPaahpSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 368 IFE----RSQKVGVVMQNPnhMIS---HHMIFDEIAFGLR-NRNIAEELITEKVEHVLELCGL----SKFRHWPIEaLSY 435
Cdd:COG4172 83 ERElrriRGNRIAMIFQEP--MTSlnpLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIpdpeRRLDAYPHQ-LSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 436 GQKKRVTIASILVLEPELLILDEPT-------AGQdyrnytsMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIAD 508
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTtaldvtvQAQ-------ILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQ 232
|
250
....*....|....*.
gi 1382220129 509 SKLIANAAMTEVFSQP 524
Cdd:COG4172 233 GEIVEQGPTAELFAAP 248
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-223 |
1.59e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.14 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaikgE--VTGSLEINGKNISEFSM 78
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL-------ErpTSGRVLVDGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 79 HDYTE---QVGTVLQdtdsQFVGLS---IGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVS 152
Cdd:PRK11153 75 KELRKarrQIGMIFQ----HFNLLSsrtVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIV 223
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEM-DVVKRICDRVAVIDAGRLV 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
297-529 |
1.81e-29 |
|
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: 116.23 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-V 375
Cdd:COG0410 2 PMLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNpnhmishHMIF------DEIAFGLRNRNIAEElITEKVEHVLELcglskF------RHWPIEALSYGQKKRVTI 443
Cdd:COG0410 81 GYVPEG-------RRIFpsltveENLLLGAYARRDRAE-VRADLERVYEL-----FprlkerRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 444 ASILVLEPELLILDEPTAG------QDyrnytsMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAM 517
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGlaplivEE------IFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
250
....*....|..
gi 1382220129 518 TEVFSQPSLLER 529
Cdd:COG0410 221 AELLADPEVREA 232
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-235 |
1.82e-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: 123.31 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHaikgevTGSLEINGKNISEFSMHDY 81
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLyTPQ------HGQVLVDGVDLAIADPAWL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDtdSQFVGLSIGEDIAFALENQLMSNidmyplVKSTAKMVDLADMLERSPH-----------DLSGGQKQR 150
Cdd:TIGR01846 530 RRQMGVVLQE--NVLFSRSIRDNIALCNPGAPFEH------VIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPKTGKAtieIIDQLHNET-NKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPD 229
Cdd:TIGR01846 602 IAIARALVGNPRILIFDEATSALDYESEAL---IMRNMREICrGRTVIIIAHRLSTV--RACDRIIVLEKGQIAESGRHE 676
|
....*.
gi 1382220129 230 EILASK 235
Cdd:TIGR01846 677 ELLALQ 682
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-237 |
2.40e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 116.37 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAikGEVTgsleINGKNISEFSMHDYTEQVGTVLQDTDSQ 95
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSS--GEVR----LNGRPLAAWSPWELARRRAVLPQHSSLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FvGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILV---DDVD----ILLFDE 168
Cdd:COG4559 88 F-PFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwEPVDggprWLFLDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 169 PLASLDPKTGKATIEIIDQLHNEtnKTIVIIehrledVLHrDI-------DRVILMERGEIVADMTPDEILASKLL 237
Cdd:COG4559 167 PTSALDLAHQHAVLRLARQLARR--GGGVVA------VLH-DLnlaaqyaDRILLLHQGRLVAQGTPEEVLTDELL 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
299-520 |
2.68e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 117.52 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIF-------ER 371
Cdd:COG4152 2 LELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpeER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 372 ----SQKVGvvmqnpnhmisHHMIFdeiaFG-LRNRNIAEelITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:COG4152 81 glypKMKVG-----------EQLVY----LArLKGLSKAE--AKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
298-532 |
3.74e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 116.76 E-value: 3.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEK----NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS----IF 369
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 370 ERSQKVGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSK--FRHWPIEaLSYGQKKRVTIASIL 447
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADefWEKSPFE-LSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 448 VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLL 527
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFL 238
|
....*
gi 1382220129 528 ERANL 532
Cdd:PRK13643 239 KAHEL 243
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-234 |
3.76e-29 |
|
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: 121.39 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISEFSMHDYT 82
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP-PTAGSVR----LDGADLSQWDREELG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDtdsqfVGL---SIGEDIAfalenqLMSNIDMYpLVKSTAKMVDLADMLERSPH--D---------LSGGQK 148
Cdd:COG4618 406 RHIGYLPQD-----VELfdgTIAENIA------RFGDADPE-KVVAAAKLAGVHEMILRLPDgyDtrigeggarLSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHR---LEDVlhrdiDRVILMERGEIVAD 225
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRpslLAAV-----DKLLVLRDGRVQAF 547
|
....*....
gi 1382220129 226 MTPDEILAS 234
Cdd:COG4618 548 GPRDEVLAR 556
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
298-522 |
4.32e-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: 116.06 E-value: 4.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSY--------DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELsif 369
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 370 ERSQK------VGVVMQNPNHMISHHMIFDE-IAFGLRN-RNIAEELITEKVEHVLELCGL--SKFRHWPIEaLSYGQKK 439
Cdd:TIGR02769 79 DRKQRrafrrdVQLVFQDSPSAVNPRMTVRQiIGEPLRHlTSLDESEQKARIAELLDMVGLrsEDADKLPRQ-LSGGQLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQ 237
|
...
gi 1382220129 520 VFS 522
Cdd:TIGR02769 238 LLS 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
297-492 |
4.38e-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: 114.11 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQkvg 376
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 vvMqnpnHMISHH-MIFDE------IAF--GLRNRNIAEELITEkvehVLELCGLSKFRHWPIEALSYGQKKRVTIASIL 447
Cdd:COG4133 77 --L----AYLGHAdGLKPEltvrenLRFwaALYGLRADREAIDE----ALEAVGLAGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1382220129 448 VLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHD 492
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQ 190
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-233 |
4.39e-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: 117.59 E-value: 4.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 35 IIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEFSMHdyTEQVGTVLQDTdSQFVGLSIGEDIAFALENQL 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEqPDS------GSIMLDGEDVTNVPPH--LRHINMVFQSY-ALFPHMTVEENVAFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 114 MSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETN 193
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1382220129 194 KTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEILA 233
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMS-DRIAIMRKGKIAQIGTPEEIYE 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-223 |
6.91e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 114.73 E-value: 6.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHaikgevTGSLEING------KNI 73
Cdd:PRK11124 1 MSIQLNGINCFYGA--HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLeMPR------SGTLNIAGnhfdfsKTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 74 SEFSMHDYTEQVGTVLQdtdsQF---VGLSIgediafaLENQLMSNIDMYPLVKSTAKM--------VDLADMLERSPHD 142
Cdd:PRK11124 73 SDKAIRELRRNVGMVFQ----QYnlwPHLTV-------QQNLIEAPCRVLGLSKDQALAraekllerLRLKPYADRFPLH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 143 LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEdVLHRDIDRVILMERGEI 222
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVE-VARKTASRVVYMENGHI 219
|
.
gi 1382220129 223 V 223
Cdd:PRK11124 220 V 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
299-493 |
7.65e-29 |
|
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: 114.71 E-value: 7.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPNhMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGL--SKFRH-WPIEaLSYGQKKRVTIASILVLEPELLI 455
Cdd:cd03295 81 IQQIG-LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADrYPHE-LSGGQQQRVGVARALAADPPLLL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1382220129 456 LDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDM 493
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDI 196
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
299-508 |
8.89e-29 |
|
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: 113.78 E-value: 8.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--SELSIFERSQKVG 376
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQNPNhMISHHMIFDEIAFGLRN-RNIAEELITEKVEHVLELCGLSKFRH-WPIEaLSYGQKKRVTIASILVLEPELL 454
Cdd:cd03262 80 MVFQQFN-LFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADaYPAQ-LSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIAD 508
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
278-499 |
1.10e-28 |
|
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: 119.70 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 278 AVQAWFADRPAPAAEKQ-----YQPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD 352
Cdd:TIGR02857 296 ALFAVLDAAPRPLAGKApvtaaPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 353 SGSSYLNGEDLSELSIFERSQKVGVVMQNPnhmishHMIFDEIAFGLR-NRNIAEElitEKVEHVLELCGLSKF------ 425
Cdd:TIGR02857 376 EGSIAVNGVPLADADADSWRDQIAWVPQHP------FLFAGTIAENIRlARPDASD---AEIREALERAGLDEFvaalpq 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 426 -RHWPI----EALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRdlGITVVIISHDMHLVLEY 499
Cdd:TIGR02857 447 gLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA 523
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
317-513 |
1.74e-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: 112.77 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 317 DVSFKIgKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--SELSIFERSQ--KVGVVMQNpNHMISHHMIF 392
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKINLPPQqrKIGLVFQQ-YALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 393 DEIAFGLRNRNIAEELIteKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSML 472
Cdd:cd03297 94 ENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1382220129 473 AFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-233 |
2.41e-28 |
|
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: 113.60 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTE-------QVGTVlqdt 92
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT-----SGRILFDGRDITGLPPHRIARlgiartfQNPRL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 93 dsqFVGLSIGEDIAFALENQLMSNIDMYPL---------------VKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGIL 157
Cdd:COG0411 91 ---FPELTVLENVLVAAHARLGRGLLAALLrlprarreerearerAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 158 VDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMTPDEILA 233
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDM-DLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
2.79e-28 |
|
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: 118.62 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISEFSMHDY 81
Cdd:TIGR02868 334 TLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-PLQGEVT----LDGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDtdSQFVGLSIGEDIAFALENqlMSNIDMYPLVKStakmVDLADMLERSPHDL-----------SGGQKQR 150
Cdd:TIGR02868 408 RRRVSVCAQD--AHLFDTTVRENLRLARPD--ATDEELWAALER----VGLADWLRALPDGLdtvlgeggarlSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEiiDQLHNETNKTIVIIEHRL 203
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLE--DLLAALSGRTVVLITHHL 530
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
296-520 |
3.10e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.20 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFErSQKV 375
Cdd:COG1129 2 EPLLEMRGISKSFGGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVM--QNPNhmishhmIFDE------IAFG---LRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIA 444
Cdd:COG1129 80 GIAIihQELN-------LVPNlsvaenIFLGrepRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 445 SILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-237 |
3.11e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 113.25 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISEFSMHDYT 82
Cdd:COG4604 2 IEIKNVSKRYG--GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLP-PDSGEVL----VDGLDVATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTDSQfVGLSIGEDIAFAlenqlmsnidMYP-----LVKSTAKMVD-------LADMLERSPHDLSGGQKQR 150
Cdd:COG4604 75 KRLAILRQENHIN-SRLTVRELVAFG----------RFPyskgrLTAEDREIIDeaiayldLEDLADRYLDELSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIiehrledVLHrDI-------DRVILMERGEIV 223
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVI-------VLH-DInfascyaDHIVAMKDGRVV 215
|
250
....*....|....
gi 1382220129 224 ADMTPDEILASKLL 237
Cdd:COG4604 216 AQGTPEEIITPEVL 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
304-548 |
3.61e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 113.54 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 304 LTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQN-- 381
Cdd:PRK10253 13 LTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNat 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 382 -PNHMISHHMIfdeiafgLRNRNIAEELIT-------EKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPEL 453
Cdd:PRK10253 92 tPGDITVQELV-------ARGRYPHQPLFTrwrkedeEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSqPSLLERanlc 533
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT-AELIER---- 239
|
250
....*....|....*
gi 1382220129 534 ttsIYELATMMkIDD 548
Cdd:PRK10253 240 ---IYGLRCMI-IDD 250
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-234 |
3.71e-28 |
|
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: 115.58 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFsNFSFRYESLdkpTLkNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGknisefsmhd 80
Cdd:COG4148 1 MMLEV-DFRLRRGGF---TL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD-----SGRIRLGG---------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 yteqvgTVLQDTDS-QFV-------G-----------LSIGEDIAFALENQLMSNidMYPLVKSTAKMVDLADMLERSPH 141
Cdd:COG4148 61 ------EVLQDSARgIFLpphrrriGyvfqearlfphLSVRGNLLYGRKRAPRAE--RRISFDEVVELLGIGHLLDRRPA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 142 DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTgKATI-EIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERG 220
Cdd:COG4148 133 TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR-KAEIlPYLERLRDELDIPILYVSHSLDEVA-RLADHVVLLEQG 210
|
250
....*....|....
gi 1382220129 221 EIVADMTPDEILAS 234
Cdd:COG4148 211 RVVASGPLAEVLSR 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
311-512 |
3.98e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 114.80 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDlselsIFERSQK----VGVVMQNPNHMI 386
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKRRKEfarrIGVVFGQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 387 SHHMIFDeiAFGLrNR---NIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQ 463
Cdd:COG4586 109 WDLPAID--SFRL-LKaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1382220129 464 DYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-221 |
4.02e-28 |
|
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: 111.96 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAikgevtGSLEINGKNISEFSMHD- 80
Cdd:TIGR02673 2 IEFHNVSKAYPG-GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGaLTPSR------GQVRIAGEDVNRLRGRQl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 --YTEQVGTVLQDtdSQFVG-LSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGIL 157
Cdd:TIGR02673 75 plLRRRIGVVFQD--FRLLPdRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 158 VDDVDILLFDEPLASLDPKTGKATIEIIDQLHnETNKTIVIIEHRLEdVLHRDIDRVILMERGE 221
Cdd:TIGR02673 153 VNSPPLLLADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLS-LVDRVAHRVIILDDGR 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-222 |
5.27e-28 |
|
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: 111.35 E-value: 5.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLnglipHAIKGEVTGSLEINGKNISEF---SMH 79
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLI-----YKEELPTSGTIRVNGQDVSDLrgrAIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DYTEQVGTVLQDTdSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVD 159
Cdd:cd03292 75 YLRRKIGVVFQDF-RLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 160 DVDILLFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRlEDVLHRDIDRVILMERGEI 222
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHA-KELVDTTRHRVIALERGKL 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
299-531 |
8.45e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.43 E-value: 8.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGVV 378
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD--ICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNpnHMISHHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:PRK11432 84 FQS--YALFPHMsLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLERAN 531
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMAS 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
296-544 |
8.50e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.05 E-value: 8.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDlselsifersqkv 375
Cdd:COG3845 3 PPALELRGITKRFGGVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 gVVMQNPNH-------MISHH-MIFDE------IAFGLRNRNIAEELITEKVEHVLELCGLSKFR---HWPIEALSYGQK 438
Cdd:COG3845 69 -VRIRSPRDaialgigMVHQHfMLVPNltvaenIVLGLEPTKGGRLDRKAARARIRELSERYGLDvdpDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 439 KRVTIASILVLEPELLILDEPTAG---QDYRnytSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANA 515
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVltpQEAD---ELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTV 223
|
250 260
....*....|....*....|....*....
gi 1382220129 516 AMTEvfsqpslleranlctTSIYELATMM 544
Cdd:COG3845 224 DTAE---------------TSEEELAELM 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
298-513 |
8.79e-28 |
|
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: 110.92 E-value: 8.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKN---ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSElSIFERSQK 374
Cdd:cd03266 1 MITADALTKRFRDVKKtvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMQNpnhmishhmifdeiaFGLRNRNIAEELI--------------TEKVEHVLELCGLSKFRHWPIEALSYGQKKR 440
Cdd:cd03266 80 LGFVSDS---------------TGLYDRLTARENLeyfaglyglkgdelTARLEELADRLGMEELLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 441 VTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-530 |
1.23e-27 |
|
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: 116.46 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikGEVTGSLEINGKNISEFSMHDyTEQVGTVLQDTDSQFV-G 98
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPH---GTWDGEIYWSGSPLKASNIRD-TERAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 LSIGEDI----AFALENQLMSNIDMYPLVKSTAKMVDLADM-LERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:TIGR02633 93 LSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 174 DPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVlHRDIDRVILMERGEIVA-----DMTPDEILASKLLdthgiREplyL 248
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAH-GVACVYISHKLNEV-KAVCDTICVIRDGQHVAtkdmsTMSEDDIITMMVG-----RE---I 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 249 SALKAAKaPLTCEDKLSNLKALdykrfrpavQAWFADRPapaaekqyqpllevhgltysydgEKNALEDVSFKIGKGEFV 328
Cdd:TIGR02633 243 TSLYPHE-PHEIGDVILEARNL---------TCWDVINP-----------------------HRKRVDDVSFSLRRGEIL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 329 SILGKNGSGKSTITKLIMGVID-ADSGSSYLNGEDLSELS-----------IFERSQKVGVVmqnPNHMISHHM---IFD 393
Cdd:TIGR02633 290 GVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpaqairagiamVPEDRKRHGIV---PILGVGKNItlsVLK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 394 EIAFGLRNRNIAEELITEKVEHVLELCGLSKFrhWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQD----YRNYT 469
Cdd:TIGR02633 367 SFCFKMRIDAAAELQIIGSAIQRLKVKTASPF--LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDvgakYEIYK 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 470 SMLAFIQKlnrdlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVfSQPSLLERA 530
Cdd:TIGR02633 445 LINQLAQE-----GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL-TQEQVLAAA 499
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-233 |
1.32e-27 |
|
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: 117.12 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQclngLIPHAIKGEvTGSLEINGKNISEFSMHDYT 82
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVN----LIPRFYEPD-SGQILLDGHDLADYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDtdsqfVGL---SIGEDIAFAlenqLMSNIDMYPlVKSTAKMVDLADMLERSPH-----------DLSGGQK 148
Cdd:TIGR02203 406 RQVALVSQD-----VVLfndTIANNIAYG----RTEQADRAE-IERALAAAYAQDFVDKLPLgldtpigengvLLSGGQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNetNKTIVIIEHRLEDVLHrdIDRVILMERGEIVADMTP 228
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK--ADRIVVMDDGRIVERGTH 551
|
....*
gi 1382220129 229 DEILA 233
Cdd:TIGR02203 552 NELLA 556
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
296-495 |
1.82e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 110.68 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEK---NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE-- 370
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 371 --RSQKVGVVMQNpNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSK-FRHWPIEaLSYGQKKRVTIASIL 447
Cdd:PRK11629 83 elRNQKLGFIYQF-HHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHrANHRPSE-LSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1382220129 448 VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHL 495
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
298-537 |
3.56e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.87 E-value: 3.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKN----ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSS-----YLNGEDLSELSI 368
Cdd:PRK13631 21 ILRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 369 FERSQK-----------VGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGL--SKFRHWPIEaLSY 435
Cdd:PRK13631 101 TNPYSKkiknfkelrrrVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLddSYLERSPFG-LSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 436 GQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIqKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANA 515
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
250 260
....*....|....*....|..
gi 1382220129 516 AMTEVFSQPSLLEranlcTTSI 537
Cdd:PRK13631 259 TPYEIFTDQHIIN-----STSI 275
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
311-512 |
3.76e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.56 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPnhMI--SH 388
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDP--MMgtAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 389 HMIFDE---IA------FGLRNRNIAE--ELITEKVEHvLELcGLSKFRHWPIEALSYGQKKRVT--IASIlvLEPELLI 455
Cdd:COG1101 96 SMTIEEnlaLAyrrgkrRGLRRGLTKKrrELFRELLAT-LGL-GLENRLDTKVGLLSGGQRQALSllMATL--TKPKLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 456 LDEPTAGQDYRnyTSmlAFIQKLNRDL----GITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:COG1101 172 LDEHTAALDPK--TA--ALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
298-522 |
3.97e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 109.98 E-value: 3.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQK-VG 376
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQNPNhMISHHMIFDEIAFGLRNR-NIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:PRK10895 82 YLPQEAS-IFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 456 LDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFS 522
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-493 |
5.64e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 115.99 E-value: 5.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLgqcLnGLIP--HAIKgevTGSLEINGKNISEfsmHDYTEQV-----------G 86
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSL---L-SLIAgaRKIQ---QGRVEVLGGDMAD---ARHRRAVcpriaympqglG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 87 TVLQDTdsqfvgLSIGEDIAF--------ALENQlmSNIDMypLVKSTakmvDLADMLERSPHDLSGGQKQRVSLAGILV 158
Cdd:NF033858 87 KNLYPT------LSVFENLDFfgrlfgqdAAERR--RRIDE--LLRAT----GLAPFADRPAGKLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVII--------EHrledvlhrdIDRVILMERGEIVADMTPDE 230
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVataymeeaER---------FDWLVAMDAGRVLATGTPAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 231 ILASKLLDThgireplylsaLKAAKAPLTCEDKLSNLKALDykrfRPAVQAWFADRPApaaekqyqplLEVHGLTYSYdG 310
Cdd:NF033858 224 LLARTGADT-----------LEAAFIALLPEEKRRGHQPVV----IPPRPADDDDEPA----------IEARGLTMRF-G 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE--DLSELSIfeRsQKVG------------ 376
Cdd:NF033858 278 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIAT--R-RRVGymsqafslygel 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQNpnhMISHHMIFDeiafglrnrnIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLIL 456
Cdd:NF033858 355 TVRQN---LELHARLFH----------LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1382220129 457 DEPTAGQD--YRNytsmlAFIQ---KLNRDLGITVVIISHDM 493
Cdd:NF033858 422 DEPTSGVDpvARD-----MFWRlliELSREDGVTIFISTHFM 458
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
297-532 |
5.68e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.16 E-value: 5.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSY--------DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSi 368
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 369 feRSQK------VGVVMQ------NPNHMISHhmIFDEIAFGLRNRNIAEELitEKVEHVLELCGL--SKFRHWPiEALS 434
Cdd:PRK10419 81 --RAQRkafrrdIQMVFQdsisavNPRKTVRE--IIREPLRHLLSLDKAERL--ARASEMLRAVDLddSVLDKRP-PQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 435 YGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIAN 514
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
250 260
....*....|....*....|..
gi 1382220129 515 AAMTEV--FSQPS--LLERANL 532
Cdd:PRK10419 234 QPVGDKltFSSPAgrVLQNAVL 255
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-292 |
7.00e-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: 111.74 E-value: 7.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 23 INLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEFSMHDYT----EQVGTVLQDTdSQFV 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDE------GEIVLNGRTLFDSRKGIFLppekRRIGYVFQEA-RLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 98 GLSIGEDIAFALENQLMSNIDMYPlvKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKT 177
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 178 GKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASKLLDTHGIREPLYLsaLKAAKAP 257
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVL-RLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSL--IEGVVAE 243
|
250 260 270
....*....|....*....|....*....|....*
gi 1382220129 258 LTCEDKLSNLKAldykrfrPAVQAWFADRPAPAAE 292
Cdd:TIGR02142 244 HDQHYGLTALRL-------GGGHLWVPENLGPTGA 271
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
304-512 |
1.05e-26 |
|
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: 108.08 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 304 LTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPn 383
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 384 hMISHHMIFDEIAFGlrnRNIAEElitEKVEHVLELCGLSKF-RHWPI----------EALSYGQKKRVTIASILVLEPE 452
Cdd:cd03254 87 -FLFSGTIMENIRLG---RPNATD---EEVIEAAKEAGAHDFiMKLPNgydtvlgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 453 LLILDEPTAGQDYRNYTSMLAFIQKLNRdlGITVVIISHdmHL-VLEYTTRSIVIADSKLI 512
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH--RLsTIKNADKILVLDDGKII 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
297-526 |
1.08e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.24 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVG 376
Cdd:PRK09536 2 PMIDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQNPNhmishhmifdeIAFGLRNRNIAE--------------ELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVT 442
Cdd:PRK09536 81 SVPQDTS-----------LSFEFDVRQVVEmgrtphrsrfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 443 IASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFS 522
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
....
gi 1382220129 523 QPSL 526
Cdd:PRK09536 229 ADTL 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
299-491 |
1.14e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 108.62 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID--ADSGSSYLNGEDLSELSIFERSQK-V 375
Cdd:COG0396 1 LEIKNLHVSVEG-KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERARAgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPnhmishhmifDEIAfGLRNRN--------IAEELIT-----EKVEHVLELCGLSK-FRHWPI-EALSYGQKKR 440
Cdd:COG0396 80 FLAFQYP----------VEIP-GVSVSNflrtalnaRRGEELSareflKLLKEKMKELGLDEdFLDRYVnEGFSGGEKKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 441 VTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISH 491
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITH 198
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
298-493 |
1.31e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 108.63 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERsqkvGV 377
Cdd:PRK11248 1 MLQISHLYADYGG-KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ER----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNpNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:PRK11248 75 VFQN-EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDM 493
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
309-513 |
1.77e-26 |
|
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: 107.62 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 309 DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSI---FERSQkvgVVMQNpnhm 385
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgggFNPEL---TGREN---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 386 ishhmifdeIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDY 465
Cdd:cd03220 105 ---------IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1382220129 466 RNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03220 176 AFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-511 |
2.48e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 112.45 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSmHDYTEQVGTVLQDTDSQ-F 96
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD-----SGTLEIGGNPCARLT-PAKAHQLGIYLVPQEPLlF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 VGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLaDMLERSphdLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPK 176
Cdd:PRK15439 99 PNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDL-DSSAGS---LEVADRQIVEILRGLMRDSRILILDEPTASLTPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 177 TGKATIEIIDQLHNEtNKTIVIIEHRLEDVlhRDI-DRVILMERGEIV-----ADMTPDEILasklldthgireplylsa 250
Cdd:PRK15439 175 ETERLFSRIRELLAQ-GVGIVFISHKLPEI--RQLaDRISVMRDGTIAlsgktADLSTDDII------------------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 251 lkAAKAPLTCEDKLSNLKALdykrfrpavqaWFADRPAPAAEKQYQPLLEVHGLTysydGEknALEDVSFKIGKGEFVSI 330
Cdd:PRK15439 234 --QAITPAAREKSLSASQKL-----------WLELPGNRRQQAAGAPVLTVEDLT----GE--GFRNISLEVRAGEILGL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 331 LGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFER-----------SQKVGVVMQNPNHMISHHMIFDEIAFGL 399
Cdd:PRK15439 295 AGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarglvylpedRQSSGLYLDAPLAWNVCALTHNRRGFWI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 400 RNRniAEELITEKVEHVLELcglsKFRH--WPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDyrnyTSMLAFIQK 477
Cdd:PRK15439 375 KPA--RENAVLERYRRALNI----KFNHaeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD----VSARNDIYQ 444
|
490 500 510
....*....|....*....|....*....|....*..
gi 1382220129 478 LNRDL---GITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK15439 445 LIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-235 |
2.48e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 113.19 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISEFSMHDY 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY------DIDeGEILLDGHDLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVlqdtdSQFVGL---SIGEDIAFALENQLmSNIDmyplVKSTAKMVDLADMLERSPHD-----------LSGGQ 147
Cdd:PRK11176 416 RNQVALV-----SQNVHLfndTIANNIAYARTEQY-SREQ----IEEAARMAYAMDFINKMDNGldtvigengvlLSGGQ 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhnETNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMT 227
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTI--EKADEILVVEDGEIVERGT 561
|
....*...
gi 1382220129 228 PDEILASK 235
Cdd:PRK11176 562 HAELLAQN 569
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-223 |
2.59e-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: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSF----RYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAIKGEVTgsleINGKNISE 75
Cdd:cd03213 2 VTLSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVSGEVL----INGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 76 FSmhdYTEQVGTVLQDtDSQFVGLSIGEDIAFAlenqlmsnidmyplvkstAKMvdladmleRSphdLSGGQKQRVSLAG 155
Cdd:cd03213 78 RS---FRKIIGYVPQD-DILHPTLTVRETLMFA------------------AKL--------RG---LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNeTNKTIVIIEHRLEDVLHRDIDRVILMERGEIV 223
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSSEIFELFDKLLLLSQGRVI 191
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
269-492 |
3.86e-26 |
|
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: 112.07 E-value: 3.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 269 ALDYKRFRPAVQAwfadrPAPAAEKQYQPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGV 348
Cdd:TIGR02868 310 VLDAAGPVAEGSA-----PAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 349 IDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPnHMIsHHMIFDEIAFGlrnrniAEELITEKVEHVLELCGLSKfrhW 428
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDA-HLF-DTTVRENLRLA------RPDATDEELWAALERVGLAD---W 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 429 PIE--------------ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIqkLNRDLGITVVIISHD 492
Cdd:TIGR02868 454 LRAlpdgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
314-524 |
5.31e-26 |
|
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: 106.30 E-value: 5.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD----SGSSYLNGEDLSELSIfeRSQKVGVVMQNPN------ 383
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSI--RGRHIATIMQNPRtafnpl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 384 HMISHHMIfDEIAFGLRNRNIAEELITEKVEHVlelcGLSK----FRHWPIEaLSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:TIGR02770 79 FTMGNHAI-ETLRSLGKLSKQARALILEALEAV----GLPDpeevLKKYPFQ-LSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 460 TAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
299-511 |
5.53e-26 |
|
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: 104.61 E-value: 5.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNA-LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNpnhmishhmifDEIAFGLRNRNIaeelitekvehvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03246 81 LPQD-----------DELFSGSIAENI----------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLvLEYTTRSIVIADSKL 511
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPET-LASADRILVLEDGRV 173
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-201 |
5.82e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 109.35 E-value: 5.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 21 KNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaikGEVT-GSLEINGKNISEFSMHDytEQVGTVLQdTDSQFVGL 99
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL------EDITsGDLFIGEKRMNDVPPAE--RGVGMVFQ-SYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTG- 178
Cdd:PRK11000 91 SVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRv 170
|
170 180
....*....|....*....|...
gi 1382220129 179 KATIEiIDQLHNETNKTIVIIEH 201
Cdd:PRK11000 171 QMRIE-ISRLHKRLGRTMIYVTH 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-223 |
7.74e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 111.86 E-value: 7.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikgevTGSLEINGKNISEFSMHDYTEQVGTVLQdtDSQ 95
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY------QGSLKINGIELRELDPESWRKHLSWVGQ--NPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVGLSIGEDIAFAleNQLMSNIDMYPLVKSTakmvDLADMLERSPHDL-----------SGGQKQRVSLAGILVDDVDIL 164
Cdd:PRK11174 434 LPHGTLRDNVLLG--NPDASDEQLQQALENA----WVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 165 LFDEPLASLDPKTGKATIEIIDQLHNetNKTIVIIEHRLEDVlhRDIDRVILMERGEIV 223
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDL--AQWDQIWVMQDGQIV 562
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
307-511 |
1.24e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 104.96 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 307 SYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS----IFERSQkVGVVMQNp 382
Cdd:PRK10908 10 AYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrevPFLRRQ-IGMIFQD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 383 NHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCG-LSKFRHWPIEaLSYGQKKRVTIASILVLEPELLILDEPTA 461
Cdd:PRK10908 88 HHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGlLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1382220129 462 GQDYRNYTSMLAFIQKLNRdLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
296-493 |
1.37e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 105.78 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGS-SYLNGE----DLSELSIFE 370
Cdd:PRK11701 4 QPLLSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvHYRMRDgqlrDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 371 RSQKV----GVVMQNPnhmishhmifdeiAFGLRNR-----NIAEELITEKVEHVLELcgLSKFRHW--PIE-------- 431
Cdd:PRK11701 83 RRRLLrtewGFVHQHP-------------RDGLRMQvsaggNIGERLMAVGARHYGDI--RATAGDWleRVEidaaridd 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 432 ---ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDM 493
Cdd:PRK11701 148 lptTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDL 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
317-526 |
1.58e-25 |
|
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: 107.89 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 317 DVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSE------LSIFERsqKVGVVMQNPNhMISHHM 390
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKR--RIGYVFQEAR-LFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 391 IFDEIAFGLRNRNIAEELITEkvEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTS 470
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 471 MLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSL 526
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
308-513 |
1.59e-25 |
|
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: 104.50 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 308 YDGEKNALEDVSFKigKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGVVMQNpNHMIS 387
Cdd:cd03298 9 SYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQE-NNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 388 HHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRN 467
Cdd:cd03298 84 HLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1382220129 468 YTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
299-498 |
1.65e-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: 105.01 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhMISHHMIFDEIAFGLRNrniAEElitEKVEHVLELCGLSKF-------RHWPIE----ALSYGQKKRVTIASI 446
Cdd:cd03251 81 VSQDV--FLFNDTVAENIAYGRPG---ATR---EEVEEAARAANAHEFimelpegYDTVIGergvKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 447 LVLEPELLILDEPTAGQDyrNYTSML--AFIQKLNRDLgiTVVIISH--------DMHLVLE 498
Cdd:cd03251 153 LLKDPPILILDEATSALD--TESERLvqAALERLMKNR--TTFVIAHrlstienaDRIVVLE 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
304-540 |
1.81e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.40 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 304 LTYSYDG----EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNgedlsELSIFERS------- 372
Cdd:PRK13646 8 VSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-----DITITHKTkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 --QKVGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSK--FRHWPIEaLSYGQKKRVTIASILV 448
Cdd:PRK13646 83 vrKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdvMSQSPFQ-MSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLLE 528
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLA 241
|
250
....*....|..
gi 1382220129 529 RANLCTTSIYEL 540
Cdd:PRK13646 242 DWHIGLPEIVQL 253
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-239 |
2.16e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.10 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPhaikgeVTGSLEINGKNISEFSMH 79
Cdd:PRK11231 1 MTLRTENLTVGYG--TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARlLTP------QSGTVFLGDKPISMLSSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DYTEQVGTVLQdtdsQFV---GLSIGEDIAFALENQL-----MSNIDmYPLVKSTAKMVDLADMLERSPHDLSGGQKQRV 151
Cdd:PRK11231 73 QLARRLALLPQ----HHLtpeGITVRELVAYGRSPWLslwgrLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEI 231
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQA-SRYCDHLVVLANGHVMAQGTPEEV 225
|
....*...
gi 1382220129 232 LASKLLDT 239
Cdd:PRK11231 226 MTPGLLRT 233
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-223 |
2.36e-25 |
|
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: 106.68 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaiKGEVTGSLEINGKNISEFSMHDYTE----QVGTVLQDTDSQF- 96
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPP--PGITSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDPMTSLn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 -VgLSIGEDIAFALE-NQLMSNIDMYPLVKSTAKMVDL---ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:COG0444 101 pV-MTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 172 SLDpktgkATI--EIID---QLHNETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIV 223
Cdd:COG0444 180 ALD-----VTIqaQILNllkDLQRELGLAILFITHDLGVVAE--IaDRVAVMYAGRIV 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-223 |
2.81e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.83 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNgLIPHAIKGEVT-GSLEING-KNISEFS--MHDYTEQVGTVLQDtdsq 95
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCIN-LLEQPEAGTIRvGDITIDTaRSLSQQKglIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 fvglsigediaFAL--ENQLMSNIDMYPL-VKSTAK------------MVDLADMLERSPHDLSGGQKQRVSLAGILVDD 160
Cdd:PRK11264 94 -----------FNLfpHRTVLENIIEGPViVKGEPKeeatararellaKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 161 VDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHrlEDVLHRDI-DRVILMERGEIV 223
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTH--EMSFARDVaDRAIFMDQGRIV 223
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-235 |
2.92e-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: 110.60 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYeSLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDYT 82
Cdd:TIGR01193 474 IVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ-----ARSGEILLNGFSLKDIDRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTdSQFVGlSIgediafaLENQLMSN-----IDMyplVKSTAKMVDLADMLERSPH-----------DLSGG 146
Cdd:TIGR01193 548 QFINYLPQEP-YIFSG-SI-------LENLLLGAkenvsQDE---IWAACEIAEIKDDIENMPLgyqtelseegsSISGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 147 QKQRVSLAGILVDDVDILLFDEPLASLDPKTGKatiEIIDQLHNETNKTIVIIEHRLEdvLHRDIDRVILMERGEIVADM 226
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEK---KIVNNLLNLQDKTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQG 690
|
....*....
gi 1382220129 227 TPDEILASK 235
Cdd:TIGR01193 691 SHDELLDRN 699
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
307-520 |
3.12e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.39 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 307 SYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEdLSelSIFErsqkVGVVMqnpnhmi 386
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VS--ALLE----LGAGF------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 387 shHMIF---DEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQ 463
Cdd:COG1134 100 --HPELtgrENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 464 DyrnytsmLAFIQKLN------RDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:COG1134 178 D-------AAFQKKCLarirelRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-237 |
3.18e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHD 80
Cdd:PRK13548 1 AMLEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-----SGEVRLNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQDTDSQFvGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILV-- 158
Cdd:PRK13548 74 LARRRAVLPQHSSLSF-PFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 159 ----DDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIiehrledVLHrDI-------DRVILMERGEIVADMT 227
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIV-------VLH-DLnlaaryaDRIVLLHQGRLVADGT 224
|
250
....*....|
gi 1382220129 228 PDEILASKLL 237
Cdd:PRK13548 225 PAEVLTPETL 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-233 |
4.45e-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: 103.28 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVtgslEINGKNISEFSMHDYTEQ-VGTVLQDTDSqF 96
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-PRSGSI----RFDGRDITGLPPHERARAgIGYVPEGRRI-F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 VGLSIGEDIAFALENQLMSNI--------DMYPlvkstakmvDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:cd03224 88 PELTVEENLLLGAYARRRAKRkarlervyELFP---------RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 169 PLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILA 233
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEI-ADRAYVLERGRVVLEGTAAELLA 221
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
300-493 |
6.28e-25 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 105.17 E-value: 6.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 300 EVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVM 379
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 380 QN----PnhmishHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGL--SKFRH-WPIEaLSYGQKKRVTIASILVLEP 451
Cdd:COG1125 83 QQiglfP------HMtVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDrYPHE-LSGGQQQRVGVARALAADP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 452 ELLILDEP---------TAGQDyrnytsmlaFIQKLNRDLGITVVIISHDM 493
Cdd:COG1125 156 PILLMDEPfgaldpitrEQLQD---------ELLRLQRELGKTIVFVTHDI 197
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-235 |
6.42e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 108.76 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQclngLIPHA---IKGEVTgsleINGKNISEFSMH 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ----LLTRAwdpQQGEIL----LNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DYTEQVGTVlqdtdSQFVGL---SIGEDIAFALEN----QLmsnIDMypLVKstakmVDLADMLE-RSPHD--------- 142
Cdd:PRK11160 411 ALRQAISVV-----SQRVHLfsaTLRDNLLLAAPNasdeAL---IEV--LQQ-----VGLEKLLEdDKGLNawlgeggrq 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 143 LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKatiEIIDQLHNE-TNKTIVIIEHRLEDVLHrdIDRVILMERGE 221
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETER---QILELLAEHaQNKTVLMITHRLTGLEQ--FDRICVMDNGQ 550
|
250
....*....|....
gi 1382220129 222 IVADMTPDEILASK 235
Cdd:PRK11160 551 IIEQGTHQELLAQQ 564
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-233 |
7.46e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.01 E-value: 7.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNgliphAIKGEV---TGSLEINGKNISEFSMHDYTEQVGTVLQD-- 91
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTL---LN-----AIAGSLppdSGSILIDGKDVTKLPEYKRAKYIGRVFQDpm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 92 --TDSqfvGLSIGEDIAFALEN---------QLMSNIDMYplvKSTAKMVDLAdmLERSPHD----LSGGQKQRVSLAGI 156
Cdd:COG1101 91 mgTAP---SMTIEENLALAYRRgkrrglrrgLTKKRRELF---RELLATLGLG--LENRLDTkvglLSGGQRQALSLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVAD--------MTP 228
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYG-NRLIMMHEGRIILDvsgeekkkLTV 241
|
....*
gi 1382220129 229 DEILA 233
Cdd:COG1101 242 EDLLE 246
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
299-513 |
9.40e-25 |
|
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: 101.24 E-value: 9.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVGV 377
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPNhmishhmIFDEIafgLRNrNIAEElitekvehvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03247 80 LNQRPY-------LFDTT---LRN-NLGRR-------------------------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 458 EPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHdmHLV-LEYTTRSIVIADSKLIA 513
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDK--TLIWITH--HLTgIEHMDKILFLENGKIIM 176
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-233 |
9.75e-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: 108.20 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDY 81
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP-----PTSGSVRLDGADLKQWDRETF 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTDsQFVGlSIGEDIAfalenQLMSNIDMYPLVKStAKMVDLADMLERSP--HD---------LSGGQKQR 150
Cdd:TIGR01842 391 GKHIGYLPQDVE-LFPG-TVAENIA-----RFGENADPEKIIEA-AKLAGVHELILRLPdgYDtvigpggatLSGGQRQR 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEdvLHRDIDRVILMERGEIVADMTPDE 230
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPS--LLGCVDKILVLQDGRIARFGERDE 539
|
...
gi 1382220129 231 ILA 233
Cdd:TIGR01842 540 VLA 542
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-231 |
1.13e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.57 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISEFSMHDytEQVGTVLQdTDSQFVGLSI 101
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL-----EKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQ-SYALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 102 GEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKAT 181
Cdd:PRK11432 96 GENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1382220129 182 IEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEI 231
Cdd:PRK11432 176 REKIRELQQQFNITSLYVTHDQSEAFAVS-DTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
299-491 |
1.29e-24 |
|
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: 101.45 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSyDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID--ADSGSSYLNGEDLSELSIFERSQK-V 375
Cdd:cd03217 1 LEIKDLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPN--HMIShhmifdeIAFGLRNRNiaeelitekvehvlelcglskfrhwpiEALSYGQKKRVTIASILVLEPEL 453
Cdd:cd03217 80 FLAFQYPPeiPGVK-------NADFLRYVN---------------------------EGFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISH 491
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITH 162
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-219 |
1.40e-24 |
|
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: 101.40 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEfSMHD 80
Cdd:COG4133 1 MMLEAENLSCRRG--ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS-----AGEVLWNGEPIRD-ARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQDtDSQFVGLSIGEDIAF--ALENQLMSNIDmyplVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILV 158
Cdd:COG4133 73 YRRRLAYLGHA-DGLKPELTVRENLRFwaALYGLRADREA----IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 159 DDVDILLFDEPLASLDpktgKATIEIIDQL---HNETNKTIVIIEHRLEDVLHrdiDRVILMER 219
Cdd:COG4133 148 SPAPLWLLDEPFTALD----AAGVALLAELiaaHLARGGAVLLTTHQPLELAA---ARVLDLGD 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-175 |
1.79e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.40 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKgeVTGSLEINGKNISEFSMHDytEQVGTVLQDtDSQ 95
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFS--ASGEVLLNGRRLTALPAEQ--RRIGILFQD-DLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVGLSIGEDIAFALENQLMSNiDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:COG4136 88 FPHLSVGENLAFALPPTIGRA-QRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-228 |
2.11e-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: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYT 82
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE-----EGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTdSQFVGlsigediafalenQLMSNIDmyPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03369 82 SSLTIIPQDP-TLFSG-------------TIRSNLD--PFDEYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHneTNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTP 228
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEF--TNSTILTIAHRLRTII--DYDKILVMDAGEVKEYDHP 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-231 |
2.25e-24 |
|
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: 101.43 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 11 RYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNISEfSMHDYTEQVGTVLQ 90
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR-PTSGTAY----INGYSIRT-DRKAARQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 91 DtDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:cd03263 83 F-DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 171 ASLDPKTGKATIEIIDQLhnETNKTIVIIEHRLEDVlhrDI--DRVILMERGEIVADMTPDEI 231
Cdd:cd03263 162 SGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEA---EAlcDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
317-492 |
3.65e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.34 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 317 DVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGVVMQnpNHMISHHM-IFDEI 395
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VGMVFQ--SYALYPHLsVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 396 AFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFI 475
Cdd:PRK11000 97 SFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEI 176
|
170
....*....|....*..
gi 1382220129 476 QKLNRDLGITVVIISHD 492
Cdd:PRK11000 177 SRLHKRLGRTMIYVTHD 193
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
315-530 |
4.19e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 101.46 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAdSGSSYLNGEDLSELSIFERSQKVGVVMQN--PNHMIShhmIF 392
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQqsPPFAMP---VF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 393 DEIAFGLRnRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILV-------LEPELLILDEPTAGQDY 465
Cdd:COG4138 88 QYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 466 RNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFsQPSLLERA 530
Cdd:COG4138 167 AQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPENLSEV 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-229 |
4.79e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 101.31 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 6 SNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISefsmhDYTEQV 85
Cdd:PRK11248 5 SHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-----HGSITLDGKPVE-----GPGAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 86 GTVLQDtDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK11248 73 GVVFQN-EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 166 FDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDIDRVILMER-GEIVADMTPD 229
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGpGRVVERLPLN 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-496 |
5.02e-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: 106.02 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 28 EKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAikGEVTGSLEINgKNISEFSmhdyteqvGTVLQDtdsQFVGLSIGEdIA 106
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGeLKPNL--GDYDEEPSWD-EVLKRFR--------GTELQD---YFKKLANGE-IK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 107 FALENQ---------------LMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:COG1245 162 VAHKPQyvdlipkvfkgtvreLLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 172 SLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLedvlhrdidrvilmergeIVADMTPDEI-----------LASKLLDTH 240
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEE-GKYVLVVEHDL------------------AILDYLADYVhilygepgvygVVSKPKSVR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 241 -GIREPL--YLSAlkaakapltcedklSNLkaldykRFRP-AVQawFaDRPAPAAEKQYQPLLEVHGLTYSYDGEKnaLE 316
Cdd:COG1245 303 vGINQYLdgYLPE--------------ENV------RIRDePIE--F-EVHAPRREKEEETLVEYPDLTKSYGGFS--LE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 317 DVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYlngedlSELSIFERSQKV-----GVVMQNpnhmishhmi 391
Cdd:COG1245 358 VEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD------EDLKISYKPQYIspdydGTVEEF---------- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 392 fdeiafgLRNRNiAEELITEKVEH-VLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTS 470
Cdd:COG1245 422 -------LRSAN-TDDFGSSYYKTeIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
490 500
....*....|....*....|....*.
gi 1382220129 471 MLAFIQKLNRDLGITVVIISHDMHLV 496
Cdd:COG1245 494 VAKAIRRFAENRGKTAMVVDHDIYLI 519
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
276-523 |
5.45e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 106.06 E-value: 5.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 276 RPAVQawFADRPAPAAEkqyQPLLEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSG 354
Cdd:PRK11160 321 KPEVT--FPTTSTAAAD---QVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 355 SSYLNGEDLSELSifERS--QKVGVVMQNPnHMISHhmifdeiafGLR-NRNIAEELIT-EKVEHVLELCGLSK------ 424
Cdd:PRK11160 396 EILLNGQPIADYS--EAAlrQAISVVSQRV-HLFSA---------TLRdNLLLAAPNASdEALIEVLQQVGLEKlleddk 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 425 -FRHWPIE---ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHDMHLvLEYT 500
Cdd:PRK11160 464 gLNAWLGEggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTG-LEQF 540
|
250 260
....*....|....*....|...
gi 1382220129 501 TRSIVIADSKLIANAAMTEVFSQ 523
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-230 |
6.72e-24 |
|
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: 100.20 E-value: 6.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaikgEV--TGSLEINGKNISEFSmhdytE---------QVGTV 88
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-------DRptSGTVRLAGQDLFALD-----EdararlrarHVGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 89 LQDtdSQFVG-LSigediafALENQLMsnidmyPL-------VKSTAK----MVDLADMLERSPHDLSGGQKQRVSLAGI 156
Cdd:COG4181 96 FQS--FQLLPtLT-------ALENVML------PLelagrrdARARARalleRVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEdvLHRDIDRVILMERGEIVADMTPDE 230
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA--LAARCDRVLRLRAGRLVEDTAATA 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-514 |
7.27e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 105.01 E-value: 7.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikGEVTGSLEINGKNISEFSMHDyTEQVGTVLQDTDSQFV-G 98
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPH---GTYEGEIIFEGEELQASNIRD-TERAGIAIIHQELALVkE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 LSIGEDIaFaLENQLMSNIDM-YPLVKSTAKMVdLADM-LERSPH----DLSGGQKQRVSLAGILVDDVDILLFDEPLAS 172
Cdd:PRK13549 97 LSVLENI-F-LGNEITPGGIMdYDAMYLRAQKL-LAQLkLDINPAtpvgNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 173 LDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVlhRDI-DRVILMERGEIV-----ADMTPDEILASKLldthGiREpl 246
Cdd:PRK13549 174 LTESETAVLLDIIRDLKAH-GIACIYISHKLNEV--KAIsDTICVIRDGRHIgtrpaAGMTEDDIITMMV----G-RE-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 247 ylsalkaakapltcedkLSNLkaldykrfrpavqawFADRPAPAAEKqyqpLLEVHGLTySYDGE---KNALEDVSFKIG 323
Cdd:PRK13549 244 -----------------LTAL---------------YPREPHTIGEV----ILEVRNLT-AWDPVnphIKRVDDVSFSLR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 324 KGEFVSILGKNGSGKSTITKLIMGVID-ADSGSSYLNGEDLSelsifersqkvgvvMQNPNHMISHHM------------ 390
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVK--------------IRNPQQAIAQGIamvpedrkrdgi 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 391 -------------IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRhwPIEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:PRK13549 353 vpvmgvgknitlaALDRFTGGSRIDDAAELKTILESIQRLKVKTASPEL--AIARLSGGNQQKAVLAKCLLLNPKILILD 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 458 EPTAGQD----YRNYTSMLAFIQKlnrdlGITVVIISHDMHLVLEYTTRSIVIADSKLIAN 514
Cdd:PRK13549 431 EPTRGIDvgakYEIYKLINQLVQQ-----GVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-237 |
8.89e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 100.30 E-value: 8.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevtGSLEINGKNISEFSMHDYTEQVGTVLQDTDSQFVgL 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ------GEILLNGRPLSDWSAAELARHRAYLSQQQSPPFA-M 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAFALENQLMSnidmyPLVKSTAKMV----DLADMLERSPHDLSGGQKQRVSLAGIL--VDDVD-----ILLFDE 168
Cdd:COG4138 85 PVFQYLALHQPAGASS-----EAVEQLLAQLaealGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWPTInpegqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 169 PLASLDPKTGKATIEIIDQLHnETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASKLL 237
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTL-RHADRVWLLKQGKLVASGETAEVMTPENL 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
306-524 |
1.11e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 306 YSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDA-DS-----GSSYLNGEDLSELSIFERSQKVGVVM 379
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSkikvdGKVLYFGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 380 QNPNHMiSHHMIFDEIAFGLRNRNIAEEL-ITEKVEHVLELCGLSKFRH----WPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK14246 97 QQPNPF-PHLSIYDNIAYPLKSHGIKEKReIKKIVEECLRKVGLWKEVYdrlnSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLNRDlgITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
299-496 |
1.19e-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: 99.87 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQnpNHMISHHMIFDEIAFGlrnrniAEELITEKVEHVLELCGLSKF-RHWPI----------EALSYGQKKRVTIASI 446
Cdd:cd03252 81 VLQ--ENVLFNRSIRDNIALA------DPGMSMERVIEAAKLAGAHDFiSELPEgydtivgeqgAGLSGGQRQRIAIARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 447 LVLEPELLILDEPTAGQDYRnytSMLAFIQKLNRDL-GITVVIISHDMHLV 496
Cdd:cd03252 153 LIHNPRILIFDEATSALDYE---SEHAIMRNMHDICaGRTVIIIAHRLSTV 200
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-217 |
1.40e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.07 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 11 RYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIkgevtgsleingknisefsmhdyteqvGTVLQ 90
Cdd:NF040873 1 GYGG--RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS---------------------------GTVRR 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 91 DTdsqfvglsiGEDIAFALenQLMSNIDMYPL-VKSTAKM--------------------------VDLADMLERSPHDL 143
Cdd:NF040873 52 AG---------GARVAYVP--QRSEVPDSLPLtVRDLVAMgrwarrglwrrltrddraavddalerVGLADLAGRQLGEL 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 144 SGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHnETNKTIVIIEHRLEDVlhRDIDRVILM 217
Cdd:NF040873 121 SGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEH-ARGATVVVVTHDLELV--RRADPCVLL 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-234 |
1.42e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 100.04 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISEFSMHDyteqvGTVLQDTDSQFVGL 99
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSIVVNGQTINLVRDKD-----GQLKVADKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAF----------ALENQLMSNIDMYPLVKSTA-----KMVDLADMLERS----PHDLSGGQKQRVSLAGILVDD 160
Cdd:PRK10619 91 RTRLTMVFqhfnlwshmtVLENVMEAPIQVLGLSKQEAreravKYLAKVGIDERAqgkyPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 161 VDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVS-SHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-235 |
1.57e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.19 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESL-DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPhaikgeVTGSLEINGKNISEFSMHD 80
Cdd:TIGR00958 479 IEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQP------TGGQVLLDGVPLVQYDHHY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQdtDSQFVGLSIGEDIAFALENQLMSNIdmyplvKSTAKMVDLADMLERSPHD-----------LSGGQKQ 149
Cdd:TIGR00958 553 LHRQVALVGQ--EPVLFSGSVRENIAYGLTDTPDEEI------MAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQ 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 150 RVSLAGILVDDVDILLFDEPLASLDPKTGKAtieiIDQLHNETNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMTPD 229
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAECEQL----LQESRSRASRTVLLIAHRLSTV--ERADQILVLKKGSVVEMGTHK 698
|
....*.
gi 1382220129 230 EILASK 235
Cdd:TIGR00958 699 QLMEDQ 704
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-492 |
1.72e-23 |
|
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: 104.25 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlIPHAIKGEVTGSLEIN------------GKNISEFSMhdytE 83
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDFNGEARPQPGIKvgylpqepqldpTKTVRENVE----E 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 84 QVGTVLQDTDsQFVGLSIgediAFALENQlmsniDMYPLVKSTAKMVDL----------------ADMLERSPHD----- 142
Cdd:TIGR03719 92 GVAEIKDALD-RFNEISA----KYAEPDA-----DFDKLAAEQAELQEIidaadawdldsqleiaMDALRCPPWDadvtk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 143 LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTgkatIEIIDQLHNETNKTIVIIEHrledvlhrdiDRVILmergei 222
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTH----------DRYFL------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 223 vaDMTPDEILAsklLDT-HGIR-EPLYLSALKAAKAPLTCEDK----------------LSNLKALDYK------RFRPA 278
Cdd:TIGR03719 222 --DNVAGWILE---LDRgRGIPwEGNYSSWLEQKQKRLEQEEKeesarqktlkrelewvRQSPKGRQAKskarlaRYEEL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 279 VQAWFADRPA------PAAEKQYQPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD 352
Cdd:TIGR03719 297 LSQEFQKRNEtaeiyiPPGPRLGDKVIEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 353 SGSsylngedlseLSIFErSQKVGVVMQNPNHMISHHMIFDEIAFGLrnrniaEELITEKVE-HVLELCGLSKFR----H 427
Cdd:TIGR03719 376 SGT----------IEIGE-TVKLAYVDQSRDALDPNKTVWEEISGGL------DIIKLGKREiPSRAYVGRFNFKgsdqQ 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 428 WPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRnytSMLAFIQKLnRDLGITVVIISHD 492
Cdd:TIGR03719 439 KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE---TLRALEEAL-LNFAGCAVVISHD 499
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
299-492 |
2.61e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.94 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD---SGSSYLNGEDLSELSIFERsqKV 375
Cdd:COG4136 2 LSLENLTITLGG-RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR--RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPnHMISHHMIFDEIAFGLRNRnIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:COG4136 79 GILFQDD-LLFPHLSVGENLAFALPPT-IGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1382220129 456 LDEPTAG--QDYRNYTSMLAFIQKlnRDLGITVVIISHD 492
Cdd:COG4136 157 LDEPFSKldAALRAQFREFVFEQI--RQRGIPALLVTHD 193
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
297-516 |
2.74e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 100.65 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERsQKVG 376
Cdd:PRK13537 6 APIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-QRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQ----NPNHMISHHMIFDEIAFGLRNRNIAEeliteKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPE 452
Cdd:PRK13537 84 VVPQfdnlDPDFTVRENLLVFGRYFGLSAAAARA-----LVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 453 LLILDEPTAGQD-------YRNYTSMLAfiqklnrdLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAA 516
Cdd:PRK13537 159 VLVLDEPTTGLDpqarhlmWERLRSLLA--------RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
317-527 |
2.86e-23 |
|
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: 101.33 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 317 DVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--SELSIFERSQK--VGVVMQNPnHMISHHMIF 392
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPHRrrIGYVFQEA-RLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 393 DEIAFGLRNRNIAEELIteKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSML 472
Cdd:COG4148 96 GNLLYGRKRAPRAERRI--SFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 473 AFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSLL 527
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-225 |
3.36e-23 |
|
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: 97.75 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEK--------------GEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGK--NISEFSMHDYTEQ 84
Cdd:cd03297 1 MLCVDIEKrlpdftlkidfdlnEEVTGIFGASGAGKSTLLRCIAGLEkPDG------GTIVLNGTvlFDSRKKINLPPQQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 85 --VGTVLQDTdSQFVGLSIGEDIAFALenQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03297 75 rkIGLVFQQY-ALFPHLNVRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDvLHRDIDRVILMERGEIVAD 225
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSE-AEYLADRIVVMEDGRLQYI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
298-524 |
3.49e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS--QKV 375
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNhMISHHMIFDEIAFG-LRNRNIAEELITEKVEHVLELCGLS-KFRHWPIEaLSYGQKKRVTIASILVLEPEL 453
Cdd:PRK09493 80 GMVFQQFY-LFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAeRAHHYPSE-LSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
299-529 |
3.90e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQnpnhmisHHMIFDEI------AFG------LRNRNIAEEliTEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:PRK11231 82 PQ-------HHLTPEGItvrelvAYGrspwlsLWGRLSAED--NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNrDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFsQPSL 526
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM-TPGL 230
|
...
gi 1382220129 527 LER 529
Cdd:PRK11231 231 LRT 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
17-231 |
4.03e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.45 E-value: 4.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISEfsMHDYTEQVGTVLQdTDSQF 96
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDGVDLSH--VPPYQRPINMMFQ-SYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 VGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPK 176
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 177 -TGKATIEIIDQLHnETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEI 231
Cdd:PRK11607 184 lRDRMQLEVVDILE-RVGVTCVMVTHDQEEAMTM-AGRIAIMNRGKFVQIGEPEEI 237
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
20-240 |
4.29e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 98.76 E-value: 4.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKnisEFSMHDY---TEQVGTVLQDTDSQF 96
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIE-----PTSGEILINGH---KLEYGDYkyrCKHIRMIFQDPNTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 -VGLSIGEdiafALENQLMSNIDMYP-----LVKSTAKMVDL-ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEP 169
Cdd:COG4167 101 nPRLNIGQ----ILEEPLRLNTDLTAeereeRIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 170 LASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIVADMTPDEILAS-------KLLDTH 240
Cdd:COG4167 177 LAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKH--IsDKVLVMHQGEVVEYGKTAEVFANpqhevtkRLIESH 253
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
285-512 |
4.46e-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: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 285 DRPAPAAEKQYQPL----LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNG 360
Cdd:PRK10790 323 DGPRQQYGNDDRPLqsgrIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 361 EDLSELSIFERSQKVGVVMQNPnhMISHHMIFDEIAFGlrnRNIAEelitEKVEHVLELCGLSKF-RHWP--IEA----- 432
Cdd:PRK10790 403 RPLSSLSHSVLRQGVAMVQQDP--VVLADTFLANVTLG---RDISE----EQVWQALETVQLAELaRSLPdgLYTplgeq 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 433 ---LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSM---LAFIQKLNrdlgiTVVIISHDMhlvleyttRSIVI 506
Cdd:PRK10790 474 gnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIqqaLAAVREHT-----TLVVIAHRL--------STIVE 540
|
....*.
gi 1382220129 507 ADSKLI 512
Cdd:PRK10790 541 ADTILV 546
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-235 |
5.57e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 102.87 E-value: 5.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVtgslEINGKNISEFSMHDY 81
Cdd:PRK10790 340 RIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT-EGEI----RLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQD----TDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKStakMVD-LADMLERSPHDLSGGQKQRVSLAGI 156
Cdd:PRK10790 414 RQGVAMVQQDpvvlADTFLANVTLGRDISEEQVWQALETVQLAELARS---LPDgLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 157 LVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETnkTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTPDEILASK 235
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIV--EADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-522 |
5.94e-23 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 102.96 E-value: 5.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 27 IEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAIKGEVTGSLEingKNISEFSmhdyteqvGTVLQDtdsQFVGLSIGEdI 105
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGeLIPNLGDYEEEPSWD---EVLKRFR--------GTELQN---YFKKLYNGE-I 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 106 AFALENQLmsnIDMYP---------LVKST---------AKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:PRK13409 161 KVVHKPQY---VDLIPkvfkgkvreLLKKVdergkldevVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 168 EPLASLDPKTGKATIEIIDQLHNetNKTIVIIEHRLedvlhrdidrvilmergeIVADMTPDEI-----------LASKL 236
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL------------------AVLDYLADNVhiaygepgaygVVSKP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 237 LDTH-GIREPL--YLSAlkaakapltcedklSNLkaldykRFRP-AVQawFADRPaPAAEKQYQPLLEVHGLTYSYDGEK 312
Cdd:PRK13409 298 KGVRvGINEYLkgYLPE--------------ENM------RIRPePIE--FEERP-PRDESERETLVEYPDLTKKLGDFS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 313 naLEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSgssylnGEDLSELSIFERSQ--------KVGVVMQNPNH 384
Cdd:PRK13409 355 --LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDE------GEVDPELKISYKPQyikpdydgTVEDLLRSITD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 385 MISHHMIFDEIAFGLRnrniaeelitekVEHVLELcglskfrhwPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQD 464
Cdd:PRK13409 427 DLGSSYYKSEIIKPLQ------------LERLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 465 YRNYTSMLAFIQKLNRDLGITVVIISHDmhlvleyttrsIVIADskLIANAAMteVFS 522
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEREATALVVDHD-----------IYMID--YISDRLM--VFE 528
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-234 |
6.64e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.73 E-value: 6.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLipHAIKGEVTGSLEINGKNISEFSMHDY 81
Cdd:PRK13657 334 AVEFDDVSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLL--QRVFDPQSGRILIDGTDIRTVTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTdsqfvGL---SIGEDIAFALENQlmSNIDMYplvkSTAKMVDLADMLERSPH-----------DLSGGQ 147
Cdd:PRK13657 408 RRNIAVVFQDA-----GLfnrSIEDNIRVGRPDA--TDEEMR----AAAERAQAHDFIERKPDgydtvvgergrQLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhnETNKTIVIIEHRLEDVlhRDIDRVILMERGEIVADMT 227
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTV--RNADRILVFDNGRVVESGS 552
|
....*..
gi 1382220129 228 PDEILAS 234
Cdd:PRK13657 553 FDELVAR 559
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
304-496 |
8.40e-23 |
|
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: 97.30 E-value: 8.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 304 LTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPn 383
Cdd:cd03253 6 VTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 384 hMISHHMIFDEIAFGlrNRNIAEELITE--KVEHVlelcglskfrHWPIEA---------------LSYGQKKRVTIASI 446
Cdd:cd03253 85 -VLFNDTIGYNIRYG--RPDATDEEVIEaaKAAQI----------HDKIMRfpdgydtivgerglkLSGGEKQRVAIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRdlGITVVIISHDMHLV 496
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI 199
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
299-492 |
1.11e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.53 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGVV 378
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD--IAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQN----PnhmishHM-IFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPEL 453
Cdd:PRK11650 82 FQNyalyP------HMsVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHD 492
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
300-491 |
1.15e-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: 96.84 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 300 EVHGLTYSYDGEKN--ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03249 2 EFKNVSFRYPSRPDvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhMISHHMIFDEIAFGLRNRniaeelITEKVEHVLELCGLSKFrhwpIEA---------------LSYGQKKRVT 442
Cdd:cd03249 82 VSQEP--VLFDGTIAENIRYGKPDA------TDEEVEEAAKKANIHDF----IMSlpdgydtlvgergsqLSGGQKQRIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1382220129 443 IASILVLEPELLILDEPTAGQDYRnytSMLAFIQKLNR-DLGITVVIISH 491
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAE---SEKLVQEALDRaMKGRTTIVIAH 196
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-236 |
1.26e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.06 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlIPhaiKGEVT-GSLEINGKNISEFSMHD-----------YTE 83
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HP---KYEVTsGSILLDGEDILELSPDEraragiflafqYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 84 QVGTVlqdTDSQFVGLSIGediafALENQLMSNIDMYPLVKSTAKMVDLA-DMLERSPHD-LSGGQKQRVSLAGILVDDV 161
Cdd:COG0396 88 EIPGV---SVSNFLRTALN-----ARRGEELSAREFLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEH--RLEDVLHrdIDRVILMERGEIVAdmTPDEILASKL 236
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHyqRILDYIK--PDFVHVLVDGRIVK--SGGKELALEL 231
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
16-261 |
2.34e-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: 97.46 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAIKGEVTGsleingknisefsmHDYTEQVGTVLQDTDS 94
Cdd:TIGR01188 5 DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLrPTSGTARVAG--------------YDVVREPRKVRRSIGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 QFVGLSIGEDIAfALENQLMSNiDMYPLVKSTA--------KMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:TIGR01188 71 VPQYASVDEDLT-GRENLEMMG-RLYGLPKDEAeeraeellELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 167 DEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEiLASKLLDTHGIREPL 246
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEA-DKLCDRIAIIDHGRIIAEGTPEE-LKRRLGKDTLESRPR 225
|
250
....*....|....*
gi 1382220129 247 YLSALKAAKAPLTCE 261
Cdd:TIGR01188 226 DIQSLKVEVSMLIAE 240
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
293-492 |
2.36e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.55 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 293 KQYQPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS 372
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 QKVGVVMQNPnhMISHHMIFDEIAFGLRNRNIAEE---LITEKVEHVLELCGLSKfrhwPIEALSYGQKKRVTIASILVL 449
Cdd:PRK10247 81 QQVSYCAQTP--TLFGDTVYDNLIFPWQIRNQQPDpaiFLDDLERFALPDTILTK----NIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1382220129 450 EPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHD 492
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
299-493 |
3.42e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.98 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqKVGVV 378
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA-RIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQ----NPNHMISHHMIFDEIAFGLRNRNIaEELITEkvehVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13536 120 PQfdnlDLEFTVRENLLVFGRYFGMSTREI-EAVIPS----LLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1382220129 455 ILDEPTAGQD-------YRNYTSMLAfiqklnrdLGITVVIISHDM 493
Cdd:PRK13536 195 ILDEPTTGLDpharhliWERLRSLLA--------RGKTILLTTHFM 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
315-493 |
5.89e-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: 94.84 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSqkvgVVMQNPNhMISHHMIFDE 394
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRM----VVFQNYS-LLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 395 IAFGLR--NRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSML 472
Cdd:TIGR01184 75 IALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180
....*....|....*....|.
gi 1382220129 473 AFIQKLNRDLGITVVIISHDM 493
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDV 175
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
299-524 |
9.12e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.59 E-value: 9.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID-----ADSGSSYLNGEDLSELSIFERSQ 373
Cdd:PRK14247 4 IEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 374 KVGVVMQNPNHmISHHMIFDEIAFGLR-NR--NIAEELiTEKVEHVLElcglsKFRHW---------PIEALSYGQKKRV 441
Cdd:PRK14247 83 RVQMVFQIPNP-IPNLSIFENVALGLKlNRlvKSKKEL-QERVRWALE-----KAQLWdevkdrldaPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 442 TIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHdmhlvleYTTRSIVIAD-------SKLIAN 514
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTH-------FPQQAARISDyvaflykGQIVEW 226
|
250
....*....|
gi 1382220129 515 AAMTEVFSQP 524
Cdd:PRK14247 227 GPTREVFTNP 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
298-511 |
1.29e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.88 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKNALedvSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSqkVGV 377
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP--VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNpNHMISHHMIFDEIAFGLR---NRNIAEElitEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK10771 76 LFQE-NNLFSHLTVAQNIGLGLNpglKLNAAQR---EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 455 ILDEPTAGQD--YRNytSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK10771 152 LLDEPFSALDpaLRQ--EMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-234 |
1.32e-21 |
|
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: 93.89 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQ-VGTVLQDTDSqFVG 98
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR-----SGSIRFDGEDITGLPPHRIARLgIGYVPEGRRI-FPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 LSIgediafaLENQLMSnidMYPLVKSTAKMVDLADMLERSPH----------DLSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:COG0410 93 LTV-------EENLLLG---AYARRDRAEVRADLERVYELFPRlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 169 PLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEILAS 234
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFAL--EIaDRAYVLERGRIVLEGTAAELLAD 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
287-511 |
1.41e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.36 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 287 PAPAAEKQYQPLLeVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGvIDADSGSSYLNGE-DLSE 365
Cdd:PRK11247 2 MNTARLNQGTPLL-LNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTaPLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 366 LSIFERsqkvgvVMQNPNHMISHHMIFDEIAFGLRN--RNIAEElitekvehVLELCGLS-KFRHWPiEALSYGQKKRVT 442
Cdd:PRK11247 79 AREDTR------LMFQDARLLPWKKVIDNVGLGLKGqwRDAALQ--------ALAAVGLAdRANEWP-AALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 443 IASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-232 |
1.84e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDYTE----QVGTVLQdTDSQ 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQ-SFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 176 KTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEIL 232
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-492 |
1.97e-21 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 98.10 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI----------------------PHAIKGEV----TGSLEIN 69
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVllddgriiyeqdlivarlqqdpPRNVEGTVydfvAEGIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 70 GKNISEFsmHDYTEQVGTvlQDTDSQFVGLSigediafalenQLMSNIDMYPLVKSTAKMVDLADMLERSPH----DLSG 145
Cdd:PRK11147 95 AEYLKRY--HDISHLVET--DPSEKNLNELA-----------KLQEQLDHHNLWQLENRINEVLAQLGLDPDaalsSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 146 GQKQRVSLAGILVDDVDILLFDEPLASLDpktgKATIEIIDQLHNETNKTIVIIEHRlEDVLHRDIDRVILMERGEIVAd 225
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHD-RSFIRNMATRIVDLDRGKLVS- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 226 mTP---DEILASKlldthgiREPLYLSALKAA-----------------KAPLT-CEDKLSNLKALDYKRF-RPAVQAwF 283
Cdd:PRK11147 234 -YPgnyDQYLLEK-------EEALRVEELQNAefdrklaqeevwirqgiKARRTrNEGRVRALKALRRERSeRREVMG-T 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 284 ADRPAPAAEKQYQPLLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLnGEDL 363
Cdd:PRK11147 305 AKMQVEEASRSGKIVFEMENVNYQIDG-KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 364 sELSIF---------ERSqkvgvVMQNpnhmishhmifdeIAFGLRnrniaEELITEKVEHVLELcgLSKF------RHW 428
Cdd:PRK11147 383 -EVAYFdqhraeldpEKT-----VMDN-------------LAEGKQ-----EVMVNGRPRHVLGY--LQDFlfhpkrAMT 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 429 PIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDyrnyTSMLAFIQKLNRDLGITVVIISHD 492
Cdd:PRK11147 437 PVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-243 |
2.31e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFryESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHD 80
Cdd:PRK09536 2 PMIDVSDLSV--EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-----AGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQDTDsqfvglsigedIAFALENQLMSNIDMYP--------------LVKSTAKMVDLADMLERSPHDLSGG 146
Cdd:PRK09536 75 ASRRVASVPQDTS-----------LSFEFDVRQVVEMGRTPhrsrfdtwtetdraAVERAMERTGVAQFADRPVTSLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 147 QKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADM 226
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDL-DLAARYCDELVLLADGRVRAAG 221
|
250
....*....|....*...
gi 1382220129 227 TPDEIL-ASKLLDTHGIR 243
Cdd:PRK09536 222 PPADVLtADTLRAAFDAR 239
|
|
| DUF3744 |
pfam12558 |
ATP-binding cassette cobalt transporter; This domain family is found in bacteria, and is ... |
234-305 |
2.34e-21 |
|
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: 87.98 E-value: 2.34e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 234 SKLLDTHGIREPLYLSALKAAKAPLTCEDKLSNLKALDYKRFRPAVQAWFADRPAPAAEKQYQPLLEVHGLT 305
Cdd:pfam12558 1 SDLLEQNGIREPLYLTALKYAGCDLTKEDHLSNLETLNLSEDKEKLKSWFEKQEEPKKEPEKEPLLEVKNLS 72
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-206 |
2.60e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.56 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLipHAIKGEV--TGSLEINGKNISE--FSM 78
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM--NELESEVrvEGRVEFFNQNIYErrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 79 HDYTEQVGTVLQDTDsqFVGLSIGEDIAFALenQLMS---NIDMYPLVKSTAKMVDLADMLERSPH----DLSGGQKQRV 151
Cdd:PRK14258 84 NRLRRQVSMVHPKPN--LFPMSVYDNVAYGV--KIVGwrpKLEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDV 206
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQV 214
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-491 |
2.96e-21 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 97.01 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTGSLeingKNISEFSMhdy 81
Cdd:PRK10938 3 SLQISQGTFRLS--DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELP-LLSGERQSQF----SHITRLSF--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 tEQVGTVLQD------TDsqfvGLSIGED-----IAFALENQLMSNidmyPLVKSTAKMVDLADMLERSPHDLSGGQKQR 150
Cdd:PRK10938 73 -EQLQKLVSDewqrnnTD----MLSPGEDdtgrtTAEIIQDEVKDP----ARCEQLAQQFGITALLDRRFKYLSTGETRK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVlhrdidrvilmergeivadmtPDE 230
Cdd:PRK10938 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEI---------------------PDF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 231 I-----LASKLLDTHGIREPLYLSALKAAkapLTCEDKLSNLkALdykrfrPAVQAWFADRPAPAAekqyQPLLEVHGLT 305
Cdd:PRK10938 202 VqfagvLADCTLAETGEREEILQQALVAQ---LAHSEQLEGV-QL------PEPDEPSARHALPAN----EPRIVLNNGV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 306 YSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGvidaDSGSSYLNgeDL--------SELSIFERSQKVGV 377
Cdd:PRK10938 268 VSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQGYSN--DLtlfgrrrgSGETIWDIKKHIGY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VmQNPNHM------------ISHHmiFDEI----AFGLRNRNIAEELitekvehvLELCGLSK-FRHWPIEALSYGQKKR 440
Cdd:PRK10938 341 V-SSSLHLdyrvstsvrnviLSGF--FDSIgiyqAVSDRQQKLAQQW--------LDILGIDKrTADAPFHSLSWGQQRL 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 441 VTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISH 491
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-223 |
3.49e-21 |
|
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: 92.33 E-value: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaiKGEVTGSLEINGKnisEFSMHDYTEQVGTVLQDtDSQFVGL 99
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG--GGTTSGQILFNGQ---PRKPDQFQKCVAYVRQD-DILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAFALENQLMsnidmYPLVKSTAKMVDlADMLERSPHD----------LSGGQKQRVSLAGILVDDVDILLFDEP 169
Cdd:cd03234 97 TVRETLTYTAILRLP-----RKSSDAIRKKRV-EDVLLRDLALtriggnlvkgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 170 LASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVLHRDIDRVILMERGEIV 223
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQL-ARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-234 |
3.96e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.19 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIP-HAIKGEVTGSLEINGKNISEFSMHDYTEQVGTVLQDTDS 94
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 qFVGLSIGEDIAFALENQ-LMSNIDMYPLVKSTAKMVDL----ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEP 169
Cdd:PRK14246 102 -FPHLSIYDNIAYPLKSHgIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 170 LASLDPKTGKATIEIIDQLHNETnkTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVA-RVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
307-498 |
4.10e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 307 SYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGED----LSELSIFERSQKVGVVmqnp 382
Cdd:NF040873 1 GYGG-RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayVPQRSEVPDSLPLTVR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 383 nhmishhmifDEIAFG-------LRNRNIAEELItekVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:NF040873 76 ----------DLVAMGrwarrglWRRLTRDDRAA---VDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1382220129 456 LDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLE 498
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-225 |
6.26e-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: 89.80 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikgeVTGSLEINGKNISefsmhdyteqvgtVLQDTDSQFVGL 99
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKP-----DSGEILVDGKEVS-------------FASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SigediafalenqlmsnidmyplvkstakMVdladmlerspHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGK 179
Cdd:cd03216 78 A----------------------------MV----------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1382220129 180 ATIEIIDQLHNEtNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVAD 225
Cdd:cd03216 120 RLFKVIRRLRAQ-GVAVIFISHRLDEV--FEIaDRVTVLRDGRVVGT 163
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
299-491 |
6.47e-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: 90.69 E-value: 6.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYD-----GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID--ADSGSSYLNGEDLSELSIfer 371
Cdd:cd03213 4 LSFRNLTVTVKsspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 372 SQKVGVVMQnpnhmishhmifDEIAFGlrnrniaeEL-ITEKVEHVLELCGLSKfrhwpiealsyGQKKRVTIASILVLE 450
Cdd:cd03213 81 RKIIGYVPQ------------DDILHP--------TLtVRETLMFAAKLRGLSG-----------GERKRVSIALELVSN 129
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1382220129 451 PELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISH 491
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-225 |
6.65e-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: 91.10 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESldKPTLKNINLRIEKGeKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEfSMHDYT 82
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP-----PSSGTIRIDGQDVLK-QPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQD--TDSQFVGLSIGEDIAFALEnqlMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDD 160
Cdd:cd03264 72 RRIGYLPQEfgVYPNFTVREFLDYIAWLKG---IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 161 VDILLFDEPLASLDPKTGKATIEIIDQLhnETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVAD 225
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVE--SLcNQVAVLNKGKLVFE 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
299-512 |
7.12e-21 |
|
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: 91.40 E-value: 7.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhmishHMIFDEIAFGLRNRNIAEElitEKVEHVLELCGLSKFrhwpIEA---------------LSYGQKKRVT 442
Cdd:cd03244 83 IPQDP------VLFSGTIRSNLDPFGEYSD---EELWQALERVGLKEF----VESlpggldtvveeggenLSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 443 IASILVLEPELLILDEPTAGQDYRnyTSMLafIQKLNRDL--GITVVIISHDMHLVLEYtTRSIVIADSKLI 512
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPE--TDAL--IQKTIREAfkDCTVLTIAHRLDTIIDS-DRILVLDKGRVV 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
299-464 |
9.88e-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: 90.11 E-value: 9.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSyDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVgvv 378
Cdd:TIGR01189 1 LAARNLACS-RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 mqnpnHMISHhmifdeiAFGLRNRNIAEELIT----------EKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:TIGR01189 76 -----LYLGH-------LPGLKPELSALENLHfwaaihggaqRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWL 143
|
170
....*....|....*.
gi 1382220129 449 LEPELLILDEPTAGQD 464
Cdd:TIGR01189 144 SRRPLWILDEPTTALD 159
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-231 |
1.05e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.75 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaikGEVT-GSLEINGKNISEFSMHDytEQVGTVLQDtdsqf 96
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL------ERITsGEIWIGGRVVNELEPAD--RDIAMVFQN----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 VGL----SIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLAS 172
Cdd:PRK11650 85 YALyphmSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 173 LDPKTGKAT-IEiIDQLHNETNKTIVIIEH-RLEDV-LhrdIDRVILMERGEIVADMTPDEI 231
Cdd:PRK11650 165 LDAKLRVQMrLE-IQRLHRRLKTTSLYVTHdQVEAMtL---ADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
314-525 |
1.10e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 94.33 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFE----RSQKVGVVMQNpNHMISHH 389
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQS-FALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 390 MIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYT 469
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 470 SMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
296-494 |
1.15e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 91.64 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKST-------ITKLIMGV-IdadSGSSYLNGEDlsels 367
Cdd:COG1117 9 EPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTllrclnrMNDLIPGArV---EGEILLDGED----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 368 IFERS-------QKVGVVMQNPN--HMiShhmIFDEIAFGLRNRNIA-EELITEKVEHVLELCGLskfrhW--------- 428
Cdd:COG1117 80 IYDPDvdvvelrRRVGMVFQKPNpfPK-S---IYDNVAYGLRLHGIKsKSELDEIVEESLRKAAL-----Wdevkdrlkk 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 429 PIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNyTSML-AFIQKLNRDLgiTVVIISHDMH 494
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIS-TAKIeELILELKKDY--TIVIVTHNMQ 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-222 |
1.15e-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: 90.99 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESL-DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTgsleINGKNISEFSMHDY 81
Cdd:cd03248 12 VKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-GGQVL----LDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDtdSQFVGLSIGEDIAFALENQLMsniDMYPLVKSTAKMVDLADMLERSPHD--------LSGGQKQRVSL 153
Cdd:cd03248 87 HSKVSLVGQE--PVLFARSLQDNIAYGLQSCSF---ECVKEAAQKAHAHSFISELASGYDTevgekgsqLSGGQKQRVAI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 154 AGILVDDVDILLFDEPLASLDPKTGkatiEIIDQLHNE--TNKTIVIIEHRLEDVLHrdIDRVILMERGEI 222
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESE----QQVQQALYDwpERRTVLVIAHRLSTVER--ADQILVLDGGRI 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-227 |
1.34e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.77 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQC---LNGLIPHAikgEVTGSLEINGKNI--SEFSMHDYTEQVGTVLQDTDS 94
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGF---RVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 qfVGLSIGEDIAF-ALENQLMSNIDmyPLVKSTAKMVDL----ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEP 169
Cdd:PRK14243 103 --FPKSIYDNIAYgARINGYKGDMD--ELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 170 LASLDPKTGKATIEIIDQLHNETnkTIVIIEHRledvlhrdidrvilMERGEIVADMT 227
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQY--TIIIVTHN--------------MQQAARVSDMT 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-201 |
1.38e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.44 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEINGKNISEFSMH--DYTEQVGTVLQdTDSQFV 97
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQ-YPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 98 GLSIGEDIAFALE-NQLMSNIDMYP-----LVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:PRK14267 99 HLTIYDNVAIGVKlNGLVKSKKELDervewALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190
....*....|....*....|....*....|
gi 1382220129 172 SLDPKTGKATIEIIDQLHNETnkTIVIIEH 201
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-220 |
1.44e-20 |
|
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: 90.60 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFS---MhdyteqvgTVLQDTdSQF 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPT-----SGGVILEGKQITEPGpdrM--------VVFQNY-SLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 VGLSIGEDIAFALENQL--MSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLD 174
Cdd:TIGR01184 67 PWLTVRENIALAVDRVLpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1382220129 175 PKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERG 220
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLS-DRVVMLTNG 191
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-232 |
2.08e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.76 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 27 IEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaiKGEVTgsleINGKNISEFSMHDYTEQVGTVLQDTDS-------QFVGL 99
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQ----FAGQPLEAWSAAELARHRAYLSQQQTPpfampvfQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAFALENQLMSNIdmyplvkstAKMVDLADMLERSPHDLSGGQKQRVSLAGILVD-------DVDILLFDEPLAS 172
Cdd:PRK03695 93 HQPDKTRTEAVASALNEV---------AEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 173 LDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEIL 232
Cdd:PRK03695 164 LDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRH-ADRVWLLKQGKLLASGRRDEVL 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
310-500 |
2.20e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.56 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSylngEDLSELSIFERSQKVGVVMQNPnHMISHH 389
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKLRIGYVPQKLYLDTTLP-LTVNRF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 390 MIFDEiafGLRNRNIAEELITEKVEHVLElcglskfrhWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYT 469
Cdd:PRK09544 90 LRLRP---GTKKEDILPALKRVQAGHLID---------APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|.
gi 1382220129 470 SMLAFIQKLNRDLGITVVIISHDMHLVLEYT 500
Cdd:PRK09544 158 ALYDLIDQLRRELDCAVLMVSHDLHLVMAKT 188
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-225 |
3.42e-20 |
|
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: 89.70 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 10 FRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTGSLEINGKNISEFsmhdyTEQVGTVL 89
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL-QPTSGEVRVAGLVPWKRRKKF-----LRRIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 90 QDTDSQFVGLSIGEDIAFalenqlmsNIDMYPLVKSTAK--------MVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:cd03267 101 GQKTQLWWDLPVIDSFYL--------LAAIYDLPPARFKkrldelseLLDLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVAD 225
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDI-EALARRVLVIDKGRLLYD 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
299-510 |
3.82e-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: 86.73 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSsylngedlselsifersqkvgvV 378
Cdd:cd03221 1 IELENLSKTYGG-KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI----------------------V 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPNHMISHhmifdeiafglrnrniaeelitekvehvlelcglskfrhwpIEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:cd03221 58 TWGSTVKIGY-----------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 459 PTAGQDYRNYTSMLAFIQKLNRdlgiTVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-231 |
4.86e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.66 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEFSMHDYTEQvGTV--LQDTdSQFVG 98
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTG------GTILLRGQHIEGLPGHQIARM-GVVrtFQHV-RLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 LSIGEDIAFALENQLMSNIdMYPLVKSTA----------------KMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVD 162
Cdd:PRK11300 95 MTVIENLLVAQHQQLKTGL-FSGLLKTPAfrraesealdraatwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEI 231
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVM--GIsDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
296-506 |
6.95e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 90.92 E-value: 6.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKN------------ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL 363
Cdd:PRK15079 6 KVLLEVADLKVHFDIKDGkqwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 364 SELSIFERSQK---VGVVMQNPNHMISHHMIFDEIafglrnrnIAEELIT-----------EKVEHVLELCGL--SKFRH 427
Cdd:PRK15079 86 LGMKDDEWRAVrsdIQMIFQDPLASLNPRMTIGEI--------IAEPLRTyhpklsrqevkDRVKAMMLKVGLlpNLINR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 428 WPIEaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVI 506
Cdd:PRK15079 158 YPHE-FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
299-524 |
8.75e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.92 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE--DLS----ELSIFERS 372
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSktpsDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 QKVGVVMQNPN---HMIshhMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRH-WPIEaLSYGQKKRVTIASILV 448
Cdd:PRK11124 82 RNVGMVFQQYNlwpHLT---VQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADrFPLH-LSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAmTEVFSQP 524
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQP 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-223 |
8.98e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 8.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEINGKNISEFSMHDYTEQVGTVLQdTDSQFVGL 99
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQ-IPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAFALE-NQLM-SNIDMYPLVKSTAKMVDL----ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:PRK14247 98 SIFENVALGLKlNRLVkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 174 DPK-TGKatieiIDQLHNETNK--TIVIIEHRLEDVLhRDIDRVILMERGEIV 223
Cdd:PRK14247 178 DPEnTAK-----IESLFLELKKdmTIVLVTHFPQQAA-RISDYVAFLYKGQIV 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
310-524 |
9.13e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.26 E-value: 9.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLS-------ELSIFERSQ------KVG 376
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADKNQlrllrtRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQNPNhMISHHMIFDEIAFG-LRNRNIAEELITEKVEHVLELCGLSKFRH--WPIEaLSYGQKKRVTIASILVLEPEL 453
Cdd:PRK10619 96 MVFQHFN-LWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQgkYPVH-LSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
296-530 |
9.29e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.56 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSE------LSIF 369
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalqknlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 370 ERSQKVG----------VVMQNPNHMishhmifdeiafGLRNRNIAEEliTEKVEHVLELCGLSKFRHWPIEALSYGQKK 439
Cdd:PRK15056 84 PQSEEVDwsfpvlvedvVMMGRYGHM------------GWLRRAKKRD--RQIVTAALARVDMVEFRHRQIGELSGGQKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAamTE 519
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGP--TE 226
|
250
....*....|.
gi 1382220129 520 VFSQPSLLERA 530
Cdd:PRK15056 227 TTFTAENLELA 237
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
310-526 |
1.04e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.84 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAdSGSSYLNGEDLSELSIFERSQKVGVVMQNPN------ 383
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTppfamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 384 --HMISHHMifdeiAFGLRNRNIAEELitekvEHVLELCGLSKFRHWPIEALSYGQKKRVTIASIL-----VLEPE--LL 454
Cdd:PRK03695 86 vfQYLTLHQ-----PDKTRTEAVASAL-----NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLNRdLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSL 526
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
297-524 |
1.06e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 90.35 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYD---GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID------ADSGSsyLNGEDLSELS 367
Cdd:COG4170 2 PLLDIRNLTIEIDtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtADRFR--WNGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 368 IFERSQKVGvvmqnpnHMIShhMIFDEIAFGLR-NRNIAEELI----------------TEKVEHVLELcgLSK------ 424
Cdd:COG4170 80 PRERRKIIG-------REIA--MIFQEPSSCLDpSAKIGDQLIeaipswtfkgkwwqrfKWRKKRAIEL--LHRvgikdh 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 425 ---FRHWPIEaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTT 501
Cdd:COG4170 149 kdiMNSYPHE-LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWAD 227
|
250 260
....*....|....*....|...
gi 1382220129 502 RSIVIADSKLIANAAMTEVFSQP 524
Cdd:COG4170 228 TITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
242-494 |
1.06e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 92.73 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 242 IREPLyLSALKAAKAPLTCE---DKLSNLKALDYKrfrpavqawfADRPAPAAEKQYQPLlEVHGLTYSYDGEKNALEDV 318
Cdd:PRK10522 275 LRTPL-LSAVGALPTLLSAQvafNKLNKLALAPYK----------AEFPRPQAFPDWQTL-ELRNVTFAYQDNGFSVGPI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 319 SFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMqnpnhmiSHHMIFDEIaFG 398
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVF-------TDFHLFDQL-LG 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 399 LRNRNIAEELITEKVEHvLELCGLSKFRHWPIE--ALSYGQKKRVTIASILVLEPELLILDEPTAGQD--YRNYtsmlaF 474
Cdd:PRK10522 415 PEGKPANPALVEKWLER-LKMAHKLELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDphFRRE-----F 488
|
250 260
....*....|....*....|...
gi 1382220129 475 IQKL---NRDLGITVVIISHDMH 494
Cdd:PRK10522 489 YQVLlplLQEMGKTIFAISHDDH 511
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-249 |
1.08e-19 |
|
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: 87.97 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaIKGevtGSLEINGKNISEFSMHDYTEQ-VGTVLQDTDSqFVG 98
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLP--VKS---GSIRLDGEDITKLPPHERARAgIAYVPQGREI-FPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 LSIGEDIAFALENQLMSN-------IDMYPLVKstakmvdlaDMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:TIGR03410 90 LTVEENLLTGLAALPRRSrkipdeiYELFPVLK---------EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 172 SLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEilasklLDTHGIREplYLS 249
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELA-DRYYVMERGRVVASGAGDE------LDEDKVRR--YLA 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
16-223 |
1.43e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 88.29 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLN---GLIPHAIkgeVTGSLEINGKNI--SEFSMHDYTEQVGTVLQ 90
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPEVT---ITGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 91 DTDSqfVGLSIGEDIAFALE-NQLMSNIDMYPLVKSTAKMVDLADMLERSPHD----LSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK14239 94 QPNP--FPMSIYENVVYGLRlKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 166 FDEPLASLDP-KTGKatieIIDQLHNETNK-TIVIIEHRLEDVlHRDIDRVILMERGEIV 223
Cdd:PRK14239 172 LDEPTSALDPiSAGK----IEETLLGLKDDyTMLLVTRSMQQA-SRISDRTGFFLDGDLI 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-231 |
1.61e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.67 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTE--QVGTVLQDTD 93
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-----HGEILFDGENIPAMSRSRLYTvrKRMSMLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 94 SQFVGLSIGEDIAFALE--NQLMSnidmyPLVKSTAKM----VDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:PRK11831 94 ALFTDMNVFDNVAYPLRehTQLPA-----PLLHSTVMMkleaVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 168 EPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEI 231
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVL-SIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-223 |
2.93e-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: 86.04 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 11 RYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlipHAiKGEVT-GSLEINGKNISEFSMHDYTeQVGtvl 89
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---HP-KYEVTeGEILFKGEDITDLPPEERA-RLG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 90 qdtdsqfVGLSIGEDIAFAlenqlmsnidmyplvkstakMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEP 169
Cdd:cd03217 79 -------IFLAFQYPPEIP--------------------GVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 170 LASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHRDIDRVILMERGEIV 223
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIKPDRVHVLYDGRIV 184
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
297-514 |
3.44e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.32 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKlIMGVID-ADSGSSYLNGEDLSELSIFE-- 370
Cdd:PRK10535 3 ALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDkPTSGTYRVAGQDVATLDADAla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 371 --RSQKVGVVMQNpNHMISHHMIFDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:PRK10535 82 qlRREHFGFIFQR-YHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 449 LEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHlVLEYTTRSIVIADSKLIAN 514
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRN 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
299-464 |
3.62e-19 |
|
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: 86.01 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSElsifersqkVGVV 378
Cdd:cd03231 1 LEADELTCERDGRA-LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF---------QRDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPNHMISHhmifdeiAFGLRNRNIAEELI--------TEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLE 450
Cdd:cd03231 71 IARGLLYLGH-------APGIKTTLSVLENLrfwhadhsDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSG 143
|
170
....*....|....
gi 1382220129 451 PELLILDEPTAGQD 464
Cdd:cd03231 144 RPLWILDEPTTALD 157
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
314-528 |
3.81e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.54 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 314 ALEDVSFKI-GK------------GEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQ 380
Cdd:PRK10575 13 ALRNVSFRVpGRtllhplsltfpaGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 381 N-PNhmiSHHMIFDEIA-------------FGLRNRniaeelitEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:PRK10575 93 QlPA---AEGMTVRELVaigrypwhgalgrFGAADR--------EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFsQPSL 526
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM-RGET 240
|
..
gi 1382220129 527 LE 528
Cdd:PRK10575 241 LE 242
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
299-498 |
3.99e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.85 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:PRK11176 342 IEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhmishHMIFDEIAfglrnRNIA----EELITEKVEHVLELCGLSKFrhwpIE---------------ALSYGQK 438
Cdd:PRK11176 422 VSQNV------HLFNDTIA-----NNIAyartEQYSREQIEEAARMAYAMDF----INkmdngldtvigengvLLSGGQR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 439 KRVTIASILVLEPELLILDEPTAGQDY---RNYTSMLAFIQKlNRdlgiTVVIISH--------DMHLVLE 498
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTeseRAIQAALDELQK-NR----TSLVIAHrlstiekaDEILVVE 552
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-233 |
4.00e-19 |
|
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: 90.63 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLK---NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVtgSLEINGKNIsefsmh 79
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT-SGEV--NVRVGDEWV------ 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DYTEQvGTVLQDTDSQFVGL-----------SIGEDIAFALENQLMSNIDMYPLVkSTAKMVDLAD-----MLERSPHDL 143
Cdd:TIGR03269 351 DMTKP-GPDGRGRAKRYIGIlhqeydlyphrTVLDNLTEAIGLELPDELARMKAV-ITLKMVGFDEekaeeILDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 144 SGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhrDI-DRVILMERGEI 222
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVL--DVcDRAALMRDGKI 506
|
250
....*....|.
gi 1382220129 223 VADMTPDEILA 233
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-231 |
4.69e-19 |
|
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: 85.88 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMhDYTEQVGTVLQDtdsqfvgl 99
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK-----PTSGRATVAGHDVVREPR-EVRRRIGIVFQD-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAFALENQLM-SNIDMYP------LVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLAS 172
Cdd:cd03265 82 LSVDDELTGWENLYIhARLYGVPgaerreRIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 173 LDPKTGKATIEIIDQLHNETNKTIVIIEHRLE--DVLhrdIDRVILMERGEIVADMTPDEI 231
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEeaEQL---CDRVAIIDHGRIIAEGTPEEL 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
287-525 |
5.31e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 88.24 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 287 PAPAAEKQYQPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD---SGSSYLNG 360
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFstpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 361 EDLSELSIFE----RSQKVGVVMQNPNHMISHHMifdeiafglrnrNIAEELItekveHVLELC-GLSK----------- 424
Cdd:PRK09473 81 REILNLPEKElnklRAEQISMIFQDPMTSLNPYM------------RVGEQLM-----EVLMLHkGMSKaeafeesvrml 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 425 -----------FRHWPIEaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDM 493
Cdd:PRK09473 144 davkmpearkrMKMYPHE-FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
250 260 270
....*....|....*....|....*....|..
gi 1382220129 494 HLVLEYTTRSIVIADSKLIANAAMTEVFSQPS 525
Cdd:PRK09473 223 GVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
11-225 |
6.29e-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: 85.50 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 11 RYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEfSMHDYTEQVGt 87
Cdd:cd03266 10 RFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDA------GFATVDGFDVVK-EPAEARRRLG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 88 VLQDTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 168 EPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVlHRDIDRVILMERGEIVAD 225
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEV-ERLCDRVVVLHRGRVVYE 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
16-224 |
7.44e-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: 85.02 E-value: 7.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDY-----------TEQ 84
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL-----PDSGEVLFDGKPLDIAARNRIgylpeerglypKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 85 VGTVLQDTdSQFVGLSIgEDIAfalenqlmSNIDMYplvkstAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:cd03269 87 VIDQLVYL-AQLKGLKK-EEAR--------RRIDEW------LERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 165 LFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVA 224
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELV-EELCDRVLLLNKGRAVL 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
309-474 |
7.64e-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: 85.79 E-value: 7.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 309 DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD---SGSSYLNGEdlsELSIFERSQKVGVVMQNpNHM 385
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQ---PRKPDQFQKCVAYVRQD-DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 386 ISHHMIFDEIAFG--LRNRNIAEELITEKVEHVLEL--CGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTA 461
Cdd:cd03234 93 LPGLTVRETLTYTaiLRLPRKSSDAIRKKRVEDVLLrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170
....*....|...
gi 1382220129 462 GQDyrnytSMLAF 474
Cdd:cd03234 173 GLD-----SFTAL 180
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-235 |
7.81e-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: 90.78 E-value: 7.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRY-ESLDKpTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNgLIPHAIKGEVTgsleINGKNISEFSMHDY 81
Cdd:TIGR00957 1285 VEFRNYCLRYrEDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF-RINESAEGEII----IDGLNIAKIGLHDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQD----TDSQFVGLS-----IGEDIAFALEnqlMSNIDMYplVKSTAKMVDLAdmLERSPHDLSGGQKQRVS 152
Cdd:TIGR00957 1359 RFKITIIPQDpvlfSGSLRMNLDpfsqySDEEVWWALE---LAHLKTF--VSALPDKLDHE--CAEGGENLSVGQRQLVC 1431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 153 LAGILVDDVDILLFDEPLASLDPKTgkatieiiDQLHNETNK------TIVIIEHRLEDVLhrDIDRVILMERGEIVADM 226
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLET--------DNLIQSTIRtqfedcTVLTIAHRLNTIM--DYTRVIVLDKGEVAEFG 1501
|
....*....
gi 1382220129 227 TPDEILASK 235
Cdd:TIGR00957 1502 APSNLLQQR 1510
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-207 |
8.07e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.40 E-value: 8.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 6 SNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaiKGEVTGSLEINGKNISefsmhdyteQV 85
Cdd:COG2401 32 EAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---GTPVAGCVDVPDNQFG---------RE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 86 GTVLQDtdsqfvgLSIGEDIAFALEnqlmsnidmyplVKSTAKMVDLADMLeRSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:COG2401 100 ASLIDA-------IGRKGDFKDAVE------------LLNAVGLSDAVLWL-RRFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1382220129 166 FDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRlEDVL 207
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHH-YDVI 200
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
298-524 |
1.29e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.10 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEK---NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID------ADSGSsyLNGEDLSELSI 368
Cdd:PRK11022 3 LLNVDKLSVHFGDESapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvmAEKLE--FNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 369 FERSQKVG--VVM--QNPnhMISHHMIFdEIAFglrnrNIAEELIT----------EKVEHVLELCGL----SKFRHWPi 430
Cdd:PRK11022 81 KERRNLVGaeVAMifQDP--MTSLNPCY-TVGF-----QIMEAIKVhqggnkktrrQRAIDLLNQVGIpdpaSRLDVYP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 431 EALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSK 510
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
250
....*....|....
gi 1382220129 511 LIANAAMTEVFSQP 524
Cdd:PRK11022 232 VVETGKAHDIFRAP 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
297-519 |
2.23e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIfERSQKVG 376
Cdd:PRK15439 10 PLLCARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 V--VMQNPnHMISHHMIFDEIAFGLRNRNIAEelitEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK15439 88 IylVPQEP-LLFPNLSVKENILFGLPKRQASM----QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
16-229 |
2.26e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.11 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEV-TGSLeingknisefSMHDYTEQVGTVLQDT-- 92
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-ETPSAGELlAGTA----------PLAEAREDTRLMFQDArl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 93 -------DSqfVGLSIGEDIAFALENQLMSnidmyplvkstakmVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK11247 93 lpwkkviDN--VGLGLKGQWRDAALQALAA--------------VGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 166 FDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPD 229
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAM-ADRVLLIEEGKIGLDLTVD 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-201 |
2.40e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNIsEFSMHDyteqvgtvlqdTDSQ 95
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPA-----AGTIKLDGGDI-DDPDVA-----------EACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVG--------LSIGEDIAF--ALENQLMSNIDmyplvkSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK13539 77 YLGhrnamkpaLTVAENLEFwaAFLGGEELDIA------AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1382220129 166 FDEPLASLDPKTGKATIEIIdQLHNETNKTIVIIEH 201
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELI-RAHLAQGGIVIAATH 185
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-237 |
2.57e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.12 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEVTgsleINGKNISEFS---MHDYTEQVGTVLQDTDSQF 96
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGNVS----WRGEPLAKLNraqRKAFRRDIQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 -----VGLSIGEDIAFALEnqlMSNIDMYPLVKSTAKMVDLAD-MLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:PRK10419 103 nprktVREIIREPLRHLLS---LDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 171 ASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEIL-----ASKLL 237
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLV-ERFCQRVMVMDNGQIVETQPVGDKLtfsspAGRVL 250
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
299-512 |
3.00e-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: 83.23 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGE-KNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03369 7 IEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhmishhMIFDEIafgLR-NRNIAEELITEKVEHVLELCGLSkfrhwpiEALSYGQKKRVTIASILVLEPELLIL 456
Cdd:cd03369 87 IPQDP-------TLFSGT---IRsNLDPFDEYSDEEIYGALRVSEGG-------LNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 457 DEPTAGQDYrnytSMLAFIQKLNRDL--GITVVIISHDMHLVLEYtTRSIVIADSKLI 512
Cdd:cd03369 150 DEATASIDY----ATDALIQKTIREEftNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-220 |
3.40e-18 |
|
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: 83.64 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaikgevtgsleingknisefsmhDYTEQVGTVLQDTDSQFV 97
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG---------------------------NYLPDSGSILVRHDGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 98 glsigeDIAFALENQLM--------------------SNID--MYPLV-----KSTAKmVDLADMLER----------SP 140
Cdd:COG4778 78 ------DLAQASPREILalrrrtigyvsqflrviprvSALDvvAEPLLergvdREEAR-ARARELLARlnlperlwdlPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 141 HDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhnetnK----TIVIIEHRlEDVLHRDIDRVIL 216
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-----KargtAIIGIFHD-EEVREAVADRVVD 224
|
....
gi 1382220129 217 MERG 220
Cdd:COG4778 225 VTPF 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
297-464 |
3.49e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTySYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVG 376
Cdd:PRK13539 1 MMLEGEDLA-CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 vvmqNPNHMISHHMIFDEIAFGLRNRNIAEELITEkvehVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLIL 456
Cdd:PRK13539 80 ----HRNAMKPALTVAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
....*...
gi 1382220129 457 DEPTAGQD 464
Cdd:PRK13539 152 DEPTAALD 159
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
290-524 |
3.63e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.99 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 290 AAEKQYQPLLEVHGLTYSYDGEK---NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE----- 361
Cdd:PRK10261 4 SDELDARDVLAVENLNIAFMQEQqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 362 -----DLSELSIFE----RSQKVGVVMQNPnhMISHHMIF---DEIAFGLR-NRNIAEELITEKVEHVLELCG------- 421
Cdd:PRK10261 84 srqviELSEQSAAQmrhvRGADMAMIFQEP--MTSLNPVFtvgEQIAESIRlHQGASREEAMVEAKRMLDQVRipeaqti 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 422 LSKFRHwpieALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTT 501
Cdd:PRK10261 162 LSRYPH----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIAD 237
|
250 260
....*....|....*....|...
gi 1382220129 502 RSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK10261 238 RVLVMYQGEAVETGSVEQIFHAP 260
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
16-226 |
3.87e-18 |
|
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: 83.04 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTgsleINGKNISEfsMHDYTEQVGTVLqDTDSQ 95
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI-KPDSGEIT----FDGKSYQK--NIEALRRIGALI-EAPGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVGLSIGEDI-AFALENQLMSNIdmyplVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLD 174
Cdd:cd03268 84 YPNLTARENLrLLARLLGIRKKR-----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 175 PKTGKATIEIIdQLHNETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADM 226
Cdd:cd03268 159 PDGIKELRELI-LSLRDQGITVLISSHLLSEI-QKVADRIGIINKGKLIEEG 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-236 |
4.32e-18 |
|
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: 83.36 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVtgslEINGKNISEFSMHdYTEQVG-TVLQDTDSQ 95
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK-PDSGKI----LLDGQDITKLPMH-KRARLGiGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:cd03218 87 FRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 176 KTGKATIEIIDQLhNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASKL 236
Cdd:cd03218 167 IAVQDIQKIIKIL-KDRGIGVLITDHNVRETL-SITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
296-519 |
5.06e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.29 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADS--GSSYLNGEDLSELSIFErSQ 373
Cdd:PRK13549 3 EYLLEMKNITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRD-TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 374 KVGVVMQNPNHMISHHM-----IF--DEI-AFGLRNRNiaeeLITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIAS 445
Cdd:PRK13549 81 RAGIAIIHQELALVKELsvlenIFlgNEItPGGIMDYD----AMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 446 ILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAG 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
284-498 |
5.25e-18 |
|
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: 87.57 E-value: 5.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 284 ADRPAPAAEKQYQPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL 363
Cdd:COG5265 343 ADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 364 SELSifERS--QKVGVVMQNP---NhmishHMIFDEIAFGlrnRNIAEElitEKVEHVLELCGLSKFrhwpIEA------ 432
Cdd:COG5265 423 RDVT--QASlrAAIGIVPQDTvlfN-----DTIAYNIAYG---RPDASE---EEVEAAARAAQIHDF----IESlpdgyd 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 433 ---------LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRdlGITVVIISH--------DMHL 495
Cdd:COG5265 486 trvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivdaDEIL 563
|
...
gi 1382220129 496 VLE 498
Cdd:COG5265 564 VLE 566
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
299-524 |
5.27e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 83.65 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLI------------MGVIDADSGSSYLNGEDLsel 366
Cdd:PRK11264 4 IEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 367 sIFERSQKVGVVMQNPNhMISHHMIFDEIAFG-LRNRNIAEELITEKVEHVLELCGLS-KFRHWPiEALSYGQKKRVTIA 444
Cdd:PRK11264 80 -IRQLRQHVGFVFQNFN-LFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAgKETSYP-RRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 445 SILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-225 |
5.74e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.91 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 11 RYESLDKP-----TLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaiKGEVT--GSLEINGKNISEF-----SM 78
Cdd:PRK09984 6 RVEKLAKTfnqhqALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI----TGDKSagSHIELLGRTVQREgrlarDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 79 HDYTEQVGTVLQdtdsQFV---GLSIgediafaLENQLMSNIDMYPLVKSTAKM---------------VDLADMLERSP 140
Cdd:PRK09984 82 RKSRANTGYIFQ----QFNlvnRLSV-------LENVLIGALGSTPFWRTCFSWftreqkqralqaltrVGMVHFAHQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 141 HDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERG 220
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAL-RYCERIVALRQG 229
|
....*
gi 1382220129 221 EIVAD 225
Cdd:PRK09984 230 HVFYD 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-223 |
5.88e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 85.17 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVT-GSLEINGKNISEFS---MHDYTEQVGTVLQDTdsqFV 97
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLE------EPTsGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 98 GL----SIGEDIAFALENQ-LMSNIDMYPLVKSTAKMVDL-ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLA 171
Cdd:COG4608 107 SLnprmTVGDIIAEPLRIHgLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 172 SLDpktgkATIE--II---DQLHNETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIV 223
Cdd:COG4608 187 ALD-----VSIQaqVLnllEDLQDELGLTYLFISHDLSVVRH--IsDRVAVMYLGKIV 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
296-496 |
6.56e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 85.02 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEK---------NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--- 363
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 364 SELSIFERSQKVGVVMQNPnhmishhmifdeiaFGLRN-----RNIAEE--LI---------TEKVEHVLELCGLsKFRH 427
Cdd:PRK11308 83 DPEAQKLLRQKIQIVFQNP--------------YGSLNprkkvGQILEEplLIntslsaaerREKALAMMAKVGL-RPEH 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 428 ---WPiEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLV 496
Cdd:PRK11308 148 ydrYP-HMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVV 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-243 |
7.02e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.88 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 21 KNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNISEFSMHDYTEQVGTVLQDTDSQfvgls 100
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT-----PAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 101 igEDIAFalenQLMSNIDMYP--------------LVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PRK10253 94 --GDITV----QELVARGRYPhqplftrwrkedeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 167 DEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILASKLLD-THGIR 243
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAC-RYASHLIALREGKIVAQGAPKEIVTAELIErIYGLR 244
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
315-496 |
8.45e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.08 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPNHMisHHMIFDE 394
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLF--SGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 395 IAFGLRNRNIAEELITEKVEHVLE-LCGLSKFRHWPI----EALSYGQKKRVTIASILVLEPELLILDEPTAGQDYR-NY 468
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDfIMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEcEQ 654
|
170 180
....*....|....*....|....*...
gi 1382220129 469 TsmlafIQKLNRDLGITVVIISHDMHLV 496
Cdd:TIGR00958 655 L-----LQESRSRASRTVLLIAHRLSTV 677
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-231 |
1.04e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.37 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 19 TLK---NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleINGKNI---SEFSMHDYTEQVGTVLQDT 92
Cdd:PRK15079 33 TLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK-ATDGEVA----WLGKDLlgmKDDEWRAVRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 93 -DSQFVGLSIGEDIAFALENQL--MSNIDMYPLVKSTAKMVDL-ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDE 168
Cdd:PRK15079 108 lASLNPRMTIGEIIAEPLRTYHpkLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 169 PLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEI 231
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHIS-DRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-235 |
1.46e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESlDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPhaikgeVTGSLEINGKNISEFSMHD 80
Cdd:PRK10522 322 TLELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQP------QSGEILLDGKPVTAEQPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQDtdsqfvglsigediaFALENQLMSNIDMYP---LVKSTAKMVDLADMLERSPH-----DLSGGQKQRVS 152
Cdd:PRK10522 395 YRKLFSAVFTD---------------FHLFDQLLGPEGKPAnpaLVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHrlEDVLHRDIDRVILMERGEIvADMTPDEI- 231
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH--DDHYFIHADRLLEMRNGQL-SELTGEERd 536
|
....
gi 1382220129 232 LASK 235
Cdd:PRK10522 537 AASR 540
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
296-508 |
1.65e-17 |
|
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: 81.71 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSY-----DGEK-NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGE----DLSE 365
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 366 LSIFE----RSQKVGVVMQnpnhmishhmiF----------DEIAFGLRNRNIAEELITEKVEHVLELCGLSKfRHWPIE 431
Cdd:COG4778 82 ASPREilalRRRTIGYVSQ-----------FlrviprvsalDVVAEPLLERGVDREEARARARELLARLNLPE-RLWDLP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 432 AL--SYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIAD 508
Cdd:COG4778 150 PAtfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
296-524 |
2.14e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.13 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLI--MGVIDAD---SGSSYLNGEDL--SELSI 368
Cdd:PRK14239 3 EPILQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 369 FERSQKVGVVMQNPNHMisHHMIFDEIAFGLRNRNIAE-ELITEKVEHVLElcGLS-----KFR-HWPIEALSYGQKKRV 441
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPF--PMSIYENVVYGLRLKGIKDkQVLDEAVEKSLK--GASiwdevKDRlHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 442 TIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVF 521
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
...
gi 1382220129 522 SQP 524
Cdd:PRK14239 236 MNP 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
297-496 |
2.16e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS---- 372
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRvnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 ---QKVGVVMQNPNhmISHHMIFDEIAFGLR----NRNIAEELITEKVEHVLELCGLSKFR-HWPIEALSYGQKKRVTIA 444
Cdd:PRK14258 85 rlrRQVSMVHPKPN--LFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDADLWDEIKHKiHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 445 SILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLV 496
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQV 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
297-530 |
2.47e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIF------E 370
Cdd:PRK14271 20 PAMAAVNLTLGFAG-KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFnyrdvlE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 371 RSQKVGVVMQNPNHMISHhmIFDEIAFGLRN---------RNIAEELITEK--VEHVLELCGLSKFRhwpieaLSYGQKK 439
Cdd:PRK14271 99 FRRRVGMLFQRPNPFPMS--IMDNVLAGVRAhklvprkefRGVAQARLTEVglWDAVKDRLSDSPFR------LSGGQQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 440 RVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTE 519
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
250
....*....|.
gi 1382220129 520 VFSQPSLLERA 530
Cdd:PRK14271 249 LFSSPKHAETA 259
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
298-524 |
2.65e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.14 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGL--TYSYDG------EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIF 369
Cdd:PRK15112 4 LLEVRNLskTFRYRTgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 370 ERSQKVGVVMQ------NPNHMISHhmIFDeiaFGLR-NRNIAEELITEKVEHVLELCGL--SKFRHWPiEALSYGQKKR 440
Cdd:PRK15112 84 YRSQRIRMIFQdpstslNPRQRISQ--ILD---FPLRlNTDLEPEQREKQIIETLRQVGLlpDHASYYP-HMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 441 VTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
....
gi 1382220129 521 FSQP 524
Cdd:PRK15112 238 LASP 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-201 |
2.86e-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: 78.64 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleingknisefsmHDYT 82
Cdd:cd03221 1 IELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE-PDEGIVT---------------WGST 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQdtdsqfvglsigediafalenqlmsnidmyplvkstakmvdladmlersphdLSGGQKQRVSLAGILVDDVD 162
Cdd:cd03221 63 VKIGYFEQ----------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*....
gi 1382220129 163 ILLFDEPLASLDPKtgkaTIEIIDQLHNETNKTIVIIEH 201
Cdd:cd03221 91 LLLLDEPTNHLDLE----SIEALEEALKEYPGTVILVSH 125
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
298-491 |
3.03e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.77 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSyDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSylngedlselsifersqkVGV 377
Cdd:COG2401 30 VLEAFGVELR-VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAG------------------CVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhmishhmifdeiaFGlRNRNIAEEL-----ITEKVEhVLELCGLS-------KFRHwpieaLSYGQKKRVTIAS 445
Cdd:COG2401 91 VPDNQ--------------FG-REASLIDAIgrkgdFKDAVE-LLNAVGLSdavlwlrRFKE-----LSTGQKFRFRLAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1382220129 446 ILVLEPELLILDEPTAGQDYRnyTSM-LAF-IQKLNRDLGITVVIISH 491
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQ--TAKrVARnLQKLARRAGITLVVATH 195
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-220 |
3.06e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.85 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphAIKGEVTGSLEINGKNISEFSMHDY----TEQVGTVLQD-TDSQF 96
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLL--AANGRIGGSATFNGREILNLPEKELnklrAEQISMIFQDpMTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 VGLSIGEdiafalenQLMSNIDMYP-LVKSTA-----KMVDLADMLERS------PHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:PRK09473 112 PYMRVGE--------QLMEVLMLHKgMSKAEAfeesvRMLDAVKMPEARkrmkmyPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 165 LFDEPLASLDpKTGKATI-EIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERG 220
Cdd:PRK09473 184 IADEPTTALD-VTVQAQImTLLNELKREFNTAIIMITHDL-GVVAGICDKVLVMYAG 238
|
|
| 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 1382220129 298 LLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD--------SGSSYLNGEDLSELSIF 369
Cdd:PRK13547 1 MLTADHLHVARRH-RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 370 ERSQKVGVVMQ--NPNHMIShhmiFDEI-------------AFGLRNRNIAEelitekveHVLELCGLSKFRHWPIEALS 434
Cdd:PRK13547 80 RLARLRAVLPQaaQPAFAFS----AREIvllgrypharragALTHRDGEIAW--------QALALAGATALVGRDVTTLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 435 YGQKKRVTIASIL---------VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIV 505
Cdd:PRK13547 148 GGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAM 227
|
250 260
....*....|....*....|....
gi 1382220129 506 IADSKLIANAAMTEVFsQPSLLER 529
Cdd:PRK13547 228 LADGAIVAHGAPADVL-TPAHIAR 250
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-237 |
5.19e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 85.17 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYES-LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTgsleINGKNIsefsmhdY 81
Cdd:PLN03130 615 ISIKNGYFSWDSkAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV----IRGTVA-------Y 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTdsqfvglsIGEDIAFALE---NQLMSNIDMYPLVKSTAKMV--DLADMLERSPhDLSGGQKQRVSLAGI 156
Cdd:PLN03130 684 VPQVSWIFNAT--------VRDNILFGSPfdpERYERAIDVTALQHDLDLLPggDLTEIGERGV-NISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 157 LVDDVDILLFDEPLASLDPKTGKATIE--IIDQLHnetNKTIVIIEHRLEDVLHrdIDRVILMERGEIVADMTPDEILAS 234
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELR---GKTRVLVTNQLHFLSQ--VDRIILVHEGMIKEEGTYEELSNN 829
|
...
gi 1382220129 235 KLL 237
Cdd:PLN03130 830 GPL 832
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
297-511 |
5.23e-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: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYsydgeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFER-SQKV 375
Cdd:cd03215 3 PVLEVRGLSV-----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPnhmiSHHMIFDEiafglrnRNIAEELItekvehvlelcgLSKFrhwpieaLSYGQKKRVTIASILVLEPELLI 455
Cdd:cd03215 78 AYVPEDR----KREGLVLD-------LSVAENIA------------LSSL-------LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 456 LDEPTAGQDYRNytsmLAFIQKLNRDL---GITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:cd03215 128 LDEPTRGVDVGA----KAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
284-464 |
6.06e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.24 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 284 ADRPAPAAEKQYQPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL 363
Cdd:PRK13657 320 RDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 364 SELSIFERSQKVGVVMQNPnhmishhmifdeiafGLRNRNIAEEL-------ITEKVEHVLELCGLSKFrhwpIEA---- 432
Cdd:PRK13657 400 RTVTRASLRRNIAVVFQDA---------------GLFNRSIEDNIrvgrpdaTDEEMRAAAERAQAHDF----IERkpdg 460
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1382220129 433 -----------LSYGQKKRVTIASILVLEPELLILDEPTAGQD 464
Cdd:PRK13657 461 ydtvvgergrqLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-225 |
7.68e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.01 E-value: 7.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 6 SNFSFRYESLDKPT--LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISEFSMHDYT- 82
Cdd:PRK10535 8 KDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCL-----DKPTSGTYRVAGQDVATLDADALAq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 ---EQVGTVLQD-------TDSQFV-------GLSIGEDIAFALEnqLMSNIDmyplvkstakmvdLADMLERSPHDLSG 145
Cdd:PRK10535 83 lrrEHFGFIFQRyhllshlTAAQNVevpavyaGLERKQRLLRAQE--LLQRLG-------------LEDRVEYQPSQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHrlEDVLHRDIDRVILMERGEIVAD 225
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTH--DPQVAAQAERVIEIRDGEIVRN 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
298-495 |
8.82e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.82 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSY-DGEK--NALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERS-- 372
Cdd:PRK10584 6 IVEVHHLKKSVgQGEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAkl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 --QKVGVVMQNpnhmishHMIFDEIAfGLRN-------RNIAEELITEKVEHVLELCGLSK-FRHWPIEaLSYGQKKRVT 442
Cdd:PRK10584 86 raKHVGFVFQS-------FMLIPTLN-ALENvelpallRGESSRQSRNGAKALLEQLGLGKrLDHLPAQ-LSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 443 IASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHL 495
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-235 |
9.52e-17 |
|
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: 80.34 E-value: 9.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEINGKNISEFSMHDYT 82
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV-----DIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTdSQFVGlsigeDIAFALENQLMSNID----------MYPLVKSTAKMVDLadMLERSPHDLSGGQKQRVS 152
Cdd:cd03288 95 SRLSIILQDP-ILFSG-----SIRFNLDPECKCTDDrlwealeiaqLKNMVKSLPGGLDA--VVTEGGENFSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIdqLHNETNKTIVIIEHRLEDVLhrDIDRVILMERGEIVADMTPDEIL 232
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTIL--DADLVLVLSRGILVECDTPENLL 242
|
...
gi 1382220129 233 ASK 235
Cdd:cd03288 243 AQE 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-241 |
9.66e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 84.26 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYES-LDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgeVTGSLEINGKNIsefsmhdY 81
Cdd:PLN03232 615 ISIKNGYFSWDSkTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA----ETSSVVIRGSVA-------Y 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDT-------DSQFVGLSIGEDI-AFALENQLmsniDMYPlvkstakMVDLADMLERSPhDLSGGQKQRVSL 153
Cdd:PLN03232 684 VPQVSWIFNATvrenilfGSDFESERYWRAIdVTALQHDL----DLLP-------GRDLTEIGERGV-NISGGQKQRVSM 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 154 AGILVDDVDILLFDEPLASLDPKTGKATIE--IIDQLHnetNKTIVIIEHRLEdvLHRDIDRVILMERGEI-----VADM 226
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK---GKTRVLVTNQLH--FLPLMDRIILVSEGMIkeegtFAEL 826
|
250
....*....|....*
gi 1382220129 227 TPDEILASKLLDTHG 241
Cdd:PLN03232 827 SKSGSLFKKLMENAG 841
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
264-492 |
1.54e-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: 82.54 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 264 LSNLKALDyKRFRPAVQAWFADRPAPAAeKQYQPLlEVHGLTYSYDGEKnalEDVSFKIG-------KGEFVSILGKNGS 336
Cdd:COG4615 296 LRKIEELE-LALAAAEPAAADAAAPPAP-ADFQTL-ELRGVTYRYPGED---GDEGFTLGpidltirRGELVFIVGGNGS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 337 GKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNpnhmisHHMiFDEIAfglrnrNIAEELITEKVEHV 416
Cdd:COG4615 370 GKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSD------FHL-FDRLL------GLDGEADPARAREL 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 417 LELCGLS-KFRhwpIE-------ALSYGQKKRVtiASIL-VLE--PeLLILDEPTAGQD--YRN--YTSMLafiQKLnRD 481
Cdd:COG4615 437 LERLELDhKVS---VEdgrfsttDLSQGQRKRL--ALLVaLLEdrP-ILVFDEWAADQDpeFRRvfYTELL---PEL-KA 506
|
250
....*....|.
gi 1382220129 482 LGITVVIISHD 492
Cdd:COG4615 507 RGKTVIAISHD 517
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
10-238 |
1.86e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.45 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 10 FRYESLDkpTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQVGTVL 89
Cdd:PRK15112 21 FRRQTVE--AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-----SGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 90 QDTDSQfvgLSIGEDIAFALENQLMSNIDMYPL-----VKSTAKMVDL-ADMLERSPHDLSGGQKQRVSLAGILVDDVDI 163
Cdd:PRK15112 94 QDPSTS---LNPRQRISQILDFPLRLNTDLEPEqrekqIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 164 LLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEILASKLLD 238
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHIS-DQVLVMHQGEVVERGSTADVLASPLHE 244
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-233 |
2.45e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.58 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKnIS---EFS--MH-DYT--EQV---GTV 88
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE-----PTSGRVEVNGR-VSallELGagFHpELTgrENIylnGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 89 L----QDTDSQFvglsigEDI-AFA-LENQlmsnIDMyPlVKStakmvdladmlersphdLSGGQKQRVSLAGILVDDVD 162
Cdd:COG1134 116 LglsrKEIDEKF------DEIvEFAeLGDF----IDQ-P-VKT-----------------YSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEILA 233
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAV--RRLcDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
296-506 |
2.81e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.90 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSylngedlSELSIFERS-QK 374
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQ-ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAG-------SHIELLGRTvQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMQNPNHMISHH-MIFDEiaFGLRNR-NIAEELI---------------------TEKVEHVLELCGLSKFRHWPIE 431
Cdd:PRK09984 74 EGRLARDIRKSRANTgYIFQQ--FNLVNRlSVLENVLigalgstpfwrtcfswftreqKQRALQALTRVGMVHFAHQRVS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 432 ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVI 506
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
297-524 |
3.08e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.85 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGV------IDADSgsSYLNGEDLSELS 367
Cdd:PRK15093 2 PLLDIRNLTIEFktsDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrVTADR--MRFDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 368 IFERSQKVGvvmqnpnHMIShhMIFDEIAFGLR-NRNIAEELIT-------------------EKVEHVLELCGLSK--- 424
Cdd:PRK15093 80 PRERRKLVG-------HNVS--MIFQEPQSCLDpSERVGRQLMQnipgwtykgrwwqrfgwrkRRAIELLHRVGIKDhkd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 425 -FRHWPIEaLSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRS 503
Cdd:PRK15093 151 aMRSFPYE-LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
250 260
....*....|....*....|.
gi 1382220129 504 IVIADSKLIANAAMTEVFSQP 524
Cdd:PRK15093 230 NVLYCGQTVETAPSKELVTTP 250
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
298-461 |
3.56e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDgEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELsifeRSQKVGV 377
Cdd:PRK13538 1 MLEARNLACERD-ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ----RDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMqnpnhMISHHM-IFDE------IAFGLRnrnIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLE 450
Cdd:PRK13538 76 LL-----YLGHQPgIKTEltalenLRFYQR---LHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTR 147
|
170
....*....|..
gi 1382220129 451 PELLILDEP-TA 461
Cdd:PRK13538 148 APLWILDEPfTA 159
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-218 |
3.58e-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: 78.22 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 27 IEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISefsmhdYTEQvgTVLQDTDSQFVGLSIGEDI 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLkPDE------GDIEIELDTVS------YKPQ--YIKADYEGTVRDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 106 AFALENQLMSNIdMYPLvkstakmvDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEII 185
Cdd:cd03237 88 DFYTHPYFKTEI-AKPL--------QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1382220129 186 DQLHNETNKTIVIIEHrleDVLHRDI--DRVILME 218
Cdd:cd03237 159 RRFAENNEKTAFVVEH---DIIMIDYlaDRLIVFE 190
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
299-512 |
3.88e-16 |
|
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: 81.71 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVV 378
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPnhMISHHMIFDEIAFGlRNRNIAEELITEKVEHV---LELCGLSKFRHWPIEA----LSYGQKKRVTIASILVLEP 451
Cdd:TIGR01193 554 PQEP--YIFSGSILENLLLG-AKENVSQDEIWAACEIAeikDDIENMPLGYQTELSEegssISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 452 ELLILDEPTAGQDYRNYTSMLAFIQKLNRDlgiTVVIISHDMHlVLEYTTRSIVIADSKLI 512
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKII 687
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
299-524 |
4.43e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.20 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEknALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD----SGSSYLNGEDLSELSIfeRSQK 374
Cdd:PRK10418 5 IELRNIALQAAQP--LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCAL--RGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMQNPN------HMISHHMIFDEIAFGLRNRN-----IAEELITEKVEHVLELcglskfrhWPIEaLSYGQKKRVTI 443
Cdd:PRK10418 81 IATIMQNPRsafnplHTMHTHARETCLALGKPADDatltaALEAVGLENAARVLKL--------YPFE-MSGGMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 444 ASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQ 523
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
.
gi 1382220129 524 P 524
Cdd:PRK10418 232 P 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
298-491 |
4.51e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.91 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDgEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL-SELSIFERS---- 372
Cdd:PRK13540 1 MLDVIELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQlcfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 -QKVGVvmqNPNHMISHHMIFDeIAFGLRNRNIAEELITEKVEHVLEL-CGLskfrhwpieaLSYGQKKRVTIASILVLE 450
Cdd:PRK13540 80 gHRSGI---NPYLTLRENCLYD-IHFSPGAVGITELCRLFSLEHLIDYpCGL----------LSSGQKRQVALLRLWMSK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1382220129 451 PELLILDEPTAGQDYRNYTSMLAFIQKlNRDLGITVVIISH 491
Cdd:PRK13540 146 AKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-227 |
6.72e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.16 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 6 SNFSFRYE--SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiphaiKGEVTGSLEINGKNISEFSMHDYTE 83
Cdd:PRK11629 9 DNLCKRYQegSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 84 ----QVGTVLQdtdsqFVGLSigEDIAfALENQLMsnidmyPLV---KSTAKMVDLA-DML------ERSPH---DLSGG 146
Cdd:PRK11629 84 lrnqKLGFIYQ-----FHHLL--PDFT-ALENVAM------PLLigkKKPAEINSRAlEMLaavgleHRANHrpsELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 147 QKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEdvLHRDIDRVILMERGEIVADM 226
Cdd:PRK11629 150 ERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ--LAKRMSRQLEMRDGRLTAEL 227
|
.
gi 1382220129 227 T 227
Cdd:PRK11629 228 S 228
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
20-234 |
6.93e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 77.53 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAikgevtGSLEINGKNI----------------------SEF 76
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLeTPDS------GEIRVGGEEIrlkpdrdgelvpadrrqlqrirTRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 77 SM---------HdyteqvGTVLQD---TDSQFVGLSIGEDIAFALENqlmsnidmypLVKstakmVDLADMLERSPHDLS 144
Cdd:COG4598 98 GMvfqsfnlwsH------MTVLENvieAPVHVLGRPKAEAIERAEAL----------LAK-----VGLADKRDAYPAHLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHrlEDVLHRDI-DRVILMERGEIV 223
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTH--EMGFARDVsSHVVFLHQGRIE 233
|
250
....*....|.
gi 1382220129 224 ADMTPDEILAS 234
Cdd:COG4598 234 EQGPPAEVFGN 244
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
308-493 |
7.22e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.90 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 308 YDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITK-------LIMGVidADSGSSYLNGEDL--SELSIFERSQKVGVV 378
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHGKNLyaPDVDPVEVRRRIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 379 MQNPNHMISHhmIFDEIAFGLR------------NRNIAEELITEKVEHVLELCGLSkfrhwpieaLSYGQKKRVTIASI 446
Cdd:PRK14243 97 FQKPNPFPKS--IYDNIAYGARingykgdmdelvERSLRQAALWDEVKDKLKQSGLS---------LSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHDM 493
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM 210
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-236 |
7.53e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.99 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 17 KPTLKNINLRIEKGEkIV-IIGPSGSGKSTLGQCLNGLIPHAiKGEVTgsleINGKNISEFSMHdyteQ-----VGTVLQ 90
Cdd:COG1137 16 RTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPD-SGRIF----LDGEDITHLPMH----KrarlgIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 91 DTdSQFVGLSIGEDIAFALEnqlMSNIDmyplvkSTAKMVDLADMLE--------RSP-HDLSGGQKQRVSLAGILVDDV 161
Cdd:COG1137 86 EA-SIFRKLTVEDNILAVLE---LRKLS------KKEREERLEELLEefgithlrKSKaYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 162 DILLFDEPLASLDPktgKATIEIIDQLHNETNKTI-VII-EHRLEDVLhrDI-DRVILMERGEIVADMTPDEILASKL 236
Cdd:COG1137 156 KFILLDEPFAGVDP---IAVADIQKIIRHLKERGIgVLItDHNVRETL--GIcDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-511 |
7.78e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaIKGEVTGSLEINGKNISeFSMHDYTEQVGTVLQDTDSQFVG- 98
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTG-----IYTRDAGSILYLGKEVT-FNGPKSSQEAGIGIIHQELNLIPq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 LSIGEDIAFALE-NQLMSNIDMyplvkstAKMVDLADML------ERSPH----DLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:PRK10762 94 LTIAENIFLGREfVNRFGRIDW-------KKMYAEADKLlarlnlRFSSDklvgELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 168 EPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEIlasklldthgirepl 246
Cdd:PRK10762 167 EPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIF--EIcDDVTVFRDGQFIAEREVADL--------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 247 ylsalkaakapltCEDKLSNL---KALD--YKRFRpavqawfadrpAPAAEKQyqplLEVHGLTYSydgeknALEDVSFK 321
Cdd:PRK10762 229 -------------TEDSLIEMmvgRKLEdqYPRLD-----------KAPGEVR----LKVDNLSGP------GVNDVSFT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 322 IGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS-----------IFERSQKVGVVMQ---NPNHMIS 387
Cdd:PRK10762 275 LRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglangivyISEDRKRDGLVLGmsvKENMSLT 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 388 HHMIFDEIAFGLRNrniAEELITekVEHVLELCGL-SKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYR 466
Cdd:PRK10762 355 ALRYFSRAGGSLKH---ADEQQA--VSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVG 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1382220129 467 NYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK10762 430 AKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
308-524 |
8.63e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.19 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 308 YDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD-----SGSSYLNGEDL--SELSIFERSQKVGVVMQ 380
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 381 NPNHMiSHHMIFDEIAFGLRNRNIA--EELITEKVEHVLELCGL-----SKFRHWPiEALSYGQKKRVTIASILVLEPEL 453
Cdd:PRK14267 93 YPNPF-PHLTIYDNVAIGVKLNGLVksKKELDERVEWALKKAALwdevkDRLNDYP-SNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 454 LILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQP 524
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
296-499 |
9.13e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.37 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDgEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMG-----VIdadSGSSYLNGEDLSELSIFE 370
Cdd:CHL00131 5 KPILEIKNLHASVN-ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykIL---EGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 371 RSQKvGVVM--QNPNHMIS-HHMIFDEIAFGLRN--RNIAE-------ELITEKvehvLELCGLS-KFRHWPI-EALSYG 436
Cdd:CHL00131 81 RAHL-GIFLafQYPIEIPGvSNADFLRLAYNSKRkfQGLPEldpleflEIINEK----LKLVGMDpSFLSRNVnEGFSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 437 QKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLvLEY 499
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQRL-LDY 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-210 |
9.37e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.68 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 12 YESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEINGKNISEFSMHDYTEQVGTVLQd 91
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLI-----SPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 92 TDSQFvGLSIGEDIAFA--LENQlmsNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEP 169
Cdd:PRK10247 89 TPTLF-GDTVYDNLIFPwqIRNQ---QPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1382220129 170 LASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRD 210
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHAD 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-223 |
9.98e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVTgsleiNGKNIsefsmhdyt 82
Cdd:COG0488 316 LELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE-PDSGTVK-----LGETV--------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 eQVGTVLQDTDsqfvglsigediAFALENQLMSNIDMYplvKSTAKMVDLADMLER---SPHD-------LSGGQKQRVS 152
Cdd:COG0488 379 -KIGYFDQHQE------------ELDPDKTVLDELRDG---APGGTEQEVRGYLGRflfSGDDafkpvgvLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 153 LAGILVDDVDILLFDEPLASLDPktgkATIEIIDQLHNETNKTIVIIEH-R--LEDVlhrdIDRVILMERGEIV 223
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHdRyfLDRV----ATRILEFEDGGVR 508
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-223 |
1.26e-15 |
|
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: 75.76 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 7 NFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKgeVTGSLEINGKNISEFSMHdYTEQVG 86
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS--VEGDIHYNGIPYKEFAEK-YPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 87 TVLQDtDSQFVGLSIGEDIAFALE---NQLMSNIdmyplvkstakmvdladmlersphdlSGGQKQRVSLAGILVDDVDI 163
Cdd:cd03233 87 YVSEE-DVHFPTLTVRETLDFALRckgNEFVRGI--------------------------SGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 164 LLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRDIDRVILMERGEIV 223
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-236 |
1.56e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.54 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEFSMHDy 81
Cdd:PRK13537 8 IDFRNVEKRYG--DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLThPDA------GSISLCGEPVPSRARHA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQ--DTDSQFvglSIGEDIA-----FALENQLMSniDMYPLVKSTAKMVDLADMLERsphDLSGGQKQRVSLA 154
Cdd:PRK13537 79 RQRVGVVPQfdNLDPDF---TVRENLLvfgryFGLSAAAAR--ALVPPLLEFAKLENKADAKVG---ELSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHnETNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEA-ERLCDRLCVIEEGRKIAEGAPHALIES 228
|
..
gi 1382220129 235 KL 236
Cdd:PRK13537 229 EI 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-532 |
1.60e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.39 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaIKGEVTGSLEINGKNISEFSMHDYTEQvgtvlqdtdsqfvGL 99
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG-----IYQKDSGSILFQGKEIDFKSSKEALEN-------------GI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 S-IGEDIAFALENQLMSNIDM--YPL----------VKSTAKMVDLADmLERSPHD----LSGGQKQRVSLAGILVDDVD 162
Cdd:PRK10982 76 SmVHQELNLVLQRSVMDNMWLgrYPTkgmfvdqdkmYRDTKAIFDELD-IDIDPRAkvatLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVLhRDIDRVILMERGEIVA-----DMTPDEILASKLL 237
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIF-QLCDEITILRDGQWIAtqplaGLTMDKIIAMMVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 238 dthgiREplylsalkaakapLTcedklsnlkaldyKRFrpavqawfadrpapaAEKQYQP---LLEVHGLTysyDGEKNA 314
Cdd:PRK10982 233 -----RS-------------LT-------------QRF---------------PDKENKPgevILEVRNLT---SLRQPS 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIF-----------ERSQKVGVVMQNP- 382
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfalvtEERRSTGIYAYLDi 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 383 --NHMISHHMIFDEIAFGLRNRNIAEEliTEKVEHVLELCGLSkfRHWPIEALSYGQKKRVTIASILVLEPELLILDEPT 460
Cdd:PRK10982 344 gfNSLISNIRNYKNKVGLLDNSRMKSD--TQWVIDSMRVKTPG--HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 461 AGQD----YRNYTSMLAFIQKlnrDLGItvVIISHDMHLVLEYTTRSIVIADSKL--IANAAMTevfSQPSLLERANL 532
Cdd:PRK10982 420 RGIDvgakFEIYQLIAELAKK---DKGI--IIISSEMPELLGITDRILVMSNGLVagIVDTKTT---TQNEILRLASL 489
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-231 |
2.70e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 75.92 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTE-------QVGTVlqdt 92
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPD-----SGSVLFGGTDLTGLDEHEIARlgigrkfQKPTV---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 93 dsqFVGLSIGE--DIAFALENQLMSNI------DMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:COG4674 97 ---FEELTVFEnlELALKGDRGVFASLfarltaEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 165 LFDEPLASLDPKTGKATIEIIDQLhnETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADMTPDEI 231
Cdd:COG4674 174 LLDEPVAGMTDAETERTAELLKSL--AGKHSVVVVEHDMEFV--RQIaRKVTVLHQGSVLAEGSLDEV 237
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-220 |
3.03e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.70 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVT------------------GSLeingKNI---- 73
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-SGRIArpagarvlflpqrpylplGTL----REAllyp 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 74 ---SEFSmhdyTEQVGTVLQDtdsqfVGLSigediafalenqlmsnidmyplvkstakmvDLADMLERS---PHDLSGGQ 147
Cdd:COG4178 450 ataEAFS----DAELREALEA-----VGLG------------------------------HLAERLDEEadwDQVLSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETnkTIVIIEHRleDVLHRDIDRVILMERG 220
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT--TVISVGHR--STLAAFHDRVLELTGD 559
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-288 |
3.19e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 77.09 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikGEVTG-SLEINGKNISEFSMHDYTEQVGT----VLQDTDSQF 96
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP--GRVMAeKLEFNGQDLQRISEKERRNLVGAevamIFQDPMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 -----VGLSIGEdiafALENQLMSN--------IDMYPLVKstakMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDI 163
Cdd:PRK11022 103 npcytVGFQIME----AIKVHQGGNkktrrqraIDLLNQVG----IPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 164 LLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMTPDEILASKlldthgiR 243
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEA-AHKIIVMYAGQVVETGKAHDIFRAP-------R 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1382220129 244 EPlYLSALKAAkAPLTCEDKlSNLKALdykrfrPAVQAWFADRPA 288
Cdd:PRK11022 247 HP-YTQALLRA-LPEFAQDK-ARLASL------PGVVPGKYDRPN 282
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
291-511 |
4.45e-15 |
|
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: 74.81 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 291 AEKQYQPLLEVHGLTYSYDG--EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSI 368
Cdd:cd03248 4 APDHLKGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 369 FERSQKVGVVMQNPnhMISHHMIFDEIAFGLRNrnIAEELITEKVEHVLELCGLSKFRHWPIEA-------LSYGQKKRV 441
Cdd:cd03248 84 KYLHSKVSLVGQEP--VLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 442 TIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISHDMHLVlEYTTRSIVIADSKL 511
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
299-508 |
4.96e-15 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 74.04 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKN----ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGedlselsifersqK 374
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMQNPNHMisHHMIFDEIAFGlrnrniaEELITEKVEHVLELCGLSK-FRHWP-----------IeALSYGQKKRVT 442
Cdd:cd03250 68 IAYVSQEPWIQ--NGTIRENILFG-------KPFDEERYEKVIKACALEPdLEILPdgdlteigekgI-NLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 443 IASILVLEPELLILDEPTAGQDyrNYTSMLAFIQKLNRDL--GITVVIISHDMHLvLEYTTRSIVIAD 508
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVD--AHVGRHIFENCILGLLlnNKTRILVTHQLQL-LPHADQIVVLDN 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
298-517 |
5.87e-15 |
|
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: 77.56 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADS--GSSYLNGEDLSELSIFERSQKV 375
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNHMISHHMIFDEIAFG----LRNRNIAEELITEKVEHVLELCGLSKFRH-WPIEALSYGQKKRVTIASILVLE 450
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 451 PELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAM 517
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDM 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-247 |
6.20e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.78 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEvtGSLEINGKNISEFSMHdytEQVGTVLQDtdSQF 96
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGS--GSVLLNGMPIDAKEMR---AISAYVQQD--DLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 97 VG-LSIGEDIAFalenqlMSNIDMYPLVKSTAKM------------VDLADMLERSPHD---LSGGQKQRVSLAGILVDD 160
Cdd:TIGR00955 111 IPtLTVREHLMF------QAHLRMPRRVTKKEKRervdevlqalglRKCANTRIGVPGRvkgLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 161 VDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHRDIDRVILMERGEIVADMTPDEilASKLLDTH 240
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ--AVPFFSDL 261
|
....*..
gi 1382220129 241 GIREPLY 247
Cdd:TIGR00955 262 GHPCPEN 268
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
299-491 |
1.13e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLT-YSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIdADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:PRK11174 350 IEAEDLEiLSPDG-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhMISHHMIFDEIAFGlrNRNIAEEliteKVEHVLELCGLSKFR-------HWPIE----ALSYGQKKRVTIASI 446
Cdd:PRK11174 428 VGQNP--QLPHGTLRDNVLLG--NPDASDE----QLQQALENAWVSEFLpllpqglDTPIGdqaaGLSVGQAQRLALARA 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLgiTVVIISH 491
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTH 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
12-221 |
1.14e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 12 YESLDKpTLKNINLRIE-----KGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTGSLEINGKniSEFSMHDYTEQVG 86
Cdd:PRK13409 343 YPDLTK-KLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVL-KPDEGEVDPELKISYK--PQYIKPDYDGTVE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 87 TVLQdtdsqfvglSIGEDIAfalENQLMSNIdMYPLvkstakmvDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PRK13409 419 DLLR---------SITDDLG---SSYYKSEI-IKPL--------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 167 DEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHrleDVLHRDI--DRVILMErGE 221
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDH---DIYMIDYisDRLMVFE-GE 530
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-228 |
1.17e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 77.68 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIPHAIKgeVTGSLEINGKNIsefsmhdY 81
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMDK--VEGHVHMKGSVA-------Y 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDtdsqfvglSIGEDIAF--ALENqlmsnidmyPLVKSTAKMVDLADMLERSPH-----------DLSGGQK 148
Cdd:TIGR00957 704 VPQQAWIQND--------SLRENILFgkALNE---------KYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQK 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKATIE-IIDQLHNETNKTIVIIEHRLEDVLHRDIdrVILMERGEIvADMT 227
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDV--IIVMSGGKI-SEMG 843
|
.
gi 1382220129 228 P 228
Cdd:TIGR00957 844 S 844
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
296-524 |
1.33e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.67 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSY---DGEKNALEDVSFKIGKGEFVSILGKNGSGKStITKL-IMGVIDAD-----SGSSYLNGEDL--- 363
Cdd:PRK15134 3 QPLLAIENLSVAFrqqQTVRTVVNDVSLQIEAGETLALVGESGSGKS-VTALsILRLLPSPpvvypSGDIRFHGESLlha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 364 SELSIFE-RSQKVGVVMQNPnhMISH---HMIFDEIAFGLR-NRNIAEELITEKVEHVLELCG-------LSKFRHwpie 431
Cdd:PRK15134 82 SEQTLRGvRGNKIAMIFQEP--MVSLnplHTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGirqaakrLTDYPH---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 432 ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
250
....*....|...
gi 1382220129 512 IANAAMTEVFSQP 524
Cdd:PRK15134 236 VEQNRAATLFSAP 248
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-460 |
1.92e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgevtgslEINGKnisEFSMHDYTeqVGTVLQD---T 92
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-----------EFEGE---ARPAPGIK--VGYLPQEpqlD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 93 DSQFVGLSIGE---DIAFALE--NQLMSNI-----DMYPLVKSTAKM------VDLADM---LERS-------PHD---- 142
Cdd:PRK11819 83 PEKTVRENVEEgvaEVKAALDrfNEIYAAYaepdaDFDALAAEQGELqeiidaADAWDLdsqLEIAmdalrcpPWDakvt 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 143 -LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTgkatIEIIDQ-LHNETNkTIVIIEHrledvlhrdiDRVIL---- 216
Cdd:PRK11819 163 kLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLEQfLHDYPG-TVVAVTH----------DRYFLdnva 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 217 -----MERGEIVadmtPDEILASKLLDTHGIRepLYLSALKAAKAPLTCEDKL----SNLKALDYK------RFRPAVQA 281
Cdd:PRK11819 228 gwileLDRGRGI----PWEGNYSSWLEQKAKR--LAQEEKQEAARQKALKRELewvrQSPKARQAKskarlaRYEELLSE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 282 WFADRPA------PAAEKQYQPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGs 355
Cdd:PRK11819 302 EYQKRNEtneifiPPGPRLGDKVIEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 356 sylngedlsELSIFErSQKVGVVMQNPNHMISHHMIFDEIAFGLrnrniaEELITEKVE-----HVlelcglSKF----- 425
Cdd:PRK11819 380 ---------TIKIGE-TVKLAYVDQSRDALDPNKTVWEEISGGL------DIIKVGNREipsraYV------GRFnfkgg 437
|
490 500 510
....*....|....*....|....*....|....*.
gi 1382220129 426 -RHWPIEALSYGQKKRVTIASILVLEPELLILDEPT 460
Cdd:PRK11819 438 dQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
296-529 |
2.36e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSelsiF---ERS 372
Cdd:PRK10762 2 QALLQLKGIDKAFPGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT----FngpKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 373 QK--VGVVMQNPNhMISHHMIFDEIAFGLRNRN----IAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:PRK10762 77 QEagIGIIHQELN-LIPQLTIAENIFLGREFVNrfgrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVfSQPSL 526
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL-TEDSL 233
|
...
gi 1382220129 527 LER 529
Cdd:PRK10762 234 IEM 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-251 |
2.40e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGL--IPHAIKGEVTgsleINGKNISEFSMH 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSM---LNALfrIVELEKGRIM----IDDCDVAKFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 DyTEQVGTVLQDTDSQFVGLSIGEDIAFALENqlmsNIDMYPLVKSTakmvDLADMLERSPHDL-----------SGGQK 148
Cdd:PLN03232 1307 D-LRRVLSIIPQSPVLFSGTVRFNIDPFSEHN----DADLWEALERA----HIKDVIDRNPFGLdaevseggenfSVGQR 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 149 QRVSLAGILVDDVDILLFDEPLASLDPKTGKatieIIDQLHNETNK--TIVIIEHRLEDVLhrDIDRVILMERGEIVADM 226
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDS----LIQRTIREEFKscTMLVIAHRLNTII--DCDKILVLSSGQVLEYD 1451
|
250 260 270
....*....|....*....|....*....|.
gi 1382220129 227 TPDEILA------SKLLDTHGIREPLYLSAL 251
Cdd:PLN03232 1452 SPQELLSrdtsafFRMVHSTGPANAQYLSNL 1482
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-223 |
2.62e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.52 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 9 SFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIPHAikgEVT-GSLEINGKNISEFSMHDYTEQVGT 87
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTL---LSLIQRHF---DVSeGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 88 VLQdTDSQFVGlSIGEDIAFALENQLMSNIDmyplvkSTAKMVDLADMLERSPHD-----------LSGGQKQRVSLAGI 156
Cdd:PRK10789 394 VSQ-TPFLFSD-TVANNIALGRPDATQQEIE------HVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 157 LVDDVDILLFDEPLASLDpktGKATIEIidqLHN----ETNKTIVIIEHRLEDVLhrDIDRVILMERGEIV 223
Cdd:PRK10789 466 LLLNAEILILDDALSAVD---GRTEHQI---LHNlrqwGEGRTVIISAHRLSALT--EASEILVMQHGHIA 528
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-246 |
3.22e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.22 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESL-DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCL----------NGLIPHAIKGEVTGSLEING- 70
Cdd:PTZ00265 1166 IEIMDVNFRYISRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhHIVFKNEHTNDMTNEQDYQGd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 71 -------KNISEFSM-------HDYT--EQVGTVLQD--------------------TDSQFVGLSIGEDIAFALENQLM 114
Cdd:PTZ00265 1246 eeqnvgmKNVNEFSLtkeggsgEDSTvfKNSGKILLDgvdicdynlkdlrnlfsivsQEPMLFNMSIYENIKFGKEDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 115 SNidmyplVKSTAKMVDLADMLERSPH-----------DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIE 183
Cdd:PTZ00265 1326 ED------VKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 184 IIDQLHNETNKTIVIIEHRLEDVLHRDidrvilmergEIVADMTPDEilASKLLDTHGIREPL 246
Cdd:PTZ00265 1400 TIVDIKDKADKTIITIAHRIASIKRSD----------KIVVFNNPDR--TGSFVQAHGTHEEL 1450
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
128-237 |
5.61e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.37 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 128 KMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVL 207
Cdd:PRK11144 114 ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEIL 193
|
90 100 110
....*....|....*....|....*....|
gi 1382220129 208 hRDIDRVILMERGEIVADMTPDEILASKLL 237
Cdd:PRK11144 194 -RLADRVVVLEQGKVKAFGPLEEVWASSAM 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
298-512 |
5.87e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.44 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADS--GSSYLNGEdLSELSIFERSQKV 375
Cdd:NF040905 1 ILEMRGITKTFPGVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE-VCRFKDIRDSEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVmqnpnhmISH-------HM-----IF--DEIA-FGLRNRNI----AEELItEKVehvlelcGLSKFRHWPIEALSYG 436
Cdd:NF040905 79 GIV-------IIHqelalipYLsiaenIFlgNERAkRGVIDWNEtnrrARELL-AKV-------GLDESPDTLVTDIGVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 437 QKKRVTIASILVLEPELLILDEPTAG---QDYRNytsMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLI 512
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAAlneEDSAA---LLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-222 |
6.10e-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: 70.15 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQ-VGTVLQDTDSQ 95
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA-----SGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 --FVGLSIGEDIAFalenqlmsnidmyplvkstakmvdladmlersPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:cd03215 88 glVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 174 DPKTgKATI-EIIDQLHNEtNKTIVIIEHRLEDVLHrdI-DRVILMERGEI 222
Cdd:cd03215 136 DVGA-KAEIyRLIRELADA-GKAVLLISSELDELLG--LcDRILVMYEGRI 182
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-221 |
6.53e-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: 74.44 E-value: 6.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 10 FRYESLDKpTLKNINLRIE-----KGEKIVIIGPSGSGKSTLGQCLNGLI-PHaiKGEVTGSLEINGK--NISefsmHDY 81
Cdd:COG1245 342 VEYPDLTK-SYGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLkPD--EGEVDEDLKISYKpqYIS----PDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTDSQFVGLSIgediafaLENQLMSnidmyPLvkstakmvDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:COG1245 415 DGTVEEFLRSANTDDFGSSY-------YKTEIIK-----PL--------GLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHrleDVLHRDI--DRVILMErGE 221
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH---DIYLIDYisDRLMVFE-GE 532
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
297-520 |
6.77e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQ-KV 375
Cdd:PRK09700 4 PYISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNhmishhmIFDEIAFgLRNRNIAeELITEKV---------------EHVLELCGLSKFRHWPIEALSYGQKKR 440
Cdd:PRK09700 83 GIIYQELS-------VIDELTV-LENLYIG-RHLTKKVcgvniidwremrvraAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 441 VTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-220 |
7.57e-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: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqclngLIphAIKGE---VTGSLEINGKNISE--FSMHDYTEQVGTVLQ 90
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSL------LL--AILGEmqtLEGKVHWSNKNESEpsFEATRSRNRYSVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 91 DTDSQFVGLSIGEDIAFA--LENQ----------LMSNIDMYPLVKSTakmvdlaDMLERSPhDLSGGQKQRVSLAGILV 158
Cdd:cd03290 85 AQKPWLLNATVEENITFGspFNKQrykavtdacsLQPDIDLLPFGDQT-------EIGERGI-NLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 159 DDVDILLFDEPLASLDPKTGKATI-EIIDQLHNETNKTIVIIEHRLEDVLHrdIDRVILMERG 220
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPH--ADWIIAMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-284 |
1.01e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.39 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGL--IPHAIKGEVTgsleINGKNISEFSMHD 80
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSM---LNALfrIVELERGRIL----IDGCDISKFGLMD 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQdTDSQFVGLsigedIAFALE--NQlMSNIDMYplvkSTAKMVDLADMLERSPHDL-----------SGGQ 147
Cdd:PLN03130 1311 LRKVLGIIPQ-APVLFSGT-----VRFNLDpfNE-HNDADLW----ESLERAHLKDVIRRNSLGLdaevseagenfSVGQ 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKatieIIDQLHNETNK--TIVIIEHRLEDVLhrDIDRVILMERGEIVAD 225
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVDVRTDA----LIQKTIREEFKscTMLIIAHRLNTII--DCDRILVLDAGRVVEF 1453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 226 MTPDEILA------SKLLDTHGIREPLYLSALKAAKApltcEDKLSNL--KALDYKR-----FRPAVQAWFA 284
Cdd:PLN03130 1454 DTPENLLSnegsafSKMVQSTGAANAQYLRSLVFGGD----EDRLAREesKALDGQRkwlasSRWAAAAQFA 1521
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-235 |
1.07e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.08 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQVGTVLQDTDSQFVGL 99
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD-----AGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAFALE--------------NQLMSNIDMyplvkstakmVDLADMLERSphdLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK10895 94 SVYDNLMAVLQirddlsaeqredraNELMEEFHI----------EHLRDSMGQS---LSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 166 FDEPLASLDPKTGKATIEIIDQLHnETNKTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEILASK 235
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETL--AVcERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
3-221 |
1.20e-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: 71.43 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFryesLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQClngliphaikgeVTGSLEINGKNISEFSMHDYT 82
Cdd:cd03291 40 LFFSNLCL----VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLML------------ILGELEPSEGKIKHSGRISFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTdsqfvglsIGEDIAFAL---ENQLMSNIDMYPLVKSTAKMVDLAD-MLERSPHDLSGGQKQRVSLAGILV 158
Cdd:cd03291 104 SQFSWIMPGT--------IKENIIFGVsydEYRYKSVVKACQLEEDITKFPEKDNtVLGEGGITLSGGQRARISLARAVY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 159 DDVDILLFDEPLASLDPKTGKatiEIIDQLHNE--TNKTIVIIEHRLEDVlhRDIDRVILMERGE 221
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEK---EIFESCVCKlmANKTRILVTSKMEHL--KKADKILILHEGS 235
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
309-504 |
1.34e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.39 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 309 DGEKN-ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSG-------------SSYLNGedlsELSIFERSQK 374
Cdd:PRK13545 33 DGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGtvdikgsaaliaiSSGLNG----QLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 375 VGVVMqnpnhmishhmifdeiafGLRNRNIAEelITEKvehVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13545 109 KGLMM------------------GLTKEKIKE--IIPE---IIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 455 ILDEPTAGQDyRNYTSMLafIQKLN--RDLGITVVIISHDMHLVLEYTTRSI 504
Cdd:PRK13545 166 VIDEALSVGD-QTFTKKC--LDKMNefKEQGKTIFFISHSLSQVKSFCTKAL 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-220 |
1.37e-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: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 5 FSNFSFryesLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHaiKGEVTGSLEINgknisefsmhdYTE 83
Cdd:TIGR01271 431 FSNFSL----YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPS--EGKIKHSGRIS-----------FSP 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 84 QVGTVLQDT--DSQFVGLSIGEDIAFALEN--QLMSNIDMYPLVKSTakmvdladMLERSPHDLSGGQKQRVSLAGILVD 159
Cdd:TIGR01271 494 QTSWIMPGTikDNIIFGLSYDEYRYTSVIKacQLEEDIALFPEKDKT--------VLGEGGITLSGGQRARISLARAVYK 565
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 160 DVDILLFDEPLASLDPKTGKATIE-IIDQLHneTNKTIVIIEHRLEDVlhRDIDRVILMERG 220
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKEIFEsCLCKLM--SNKTRILVTSKLEHL--KKADKILLLHEG 623
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
133-496 |
1.40e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 73.74 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 133 ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDpktgkatieiidqLHN----ET-----NKTIVIIEHRL 203
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD-------------LHAvlwlETyllkwPKTFIVVSHAR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 204 E-------DVLHRDIDRVILMERGEIVADMTPDEILASK----------------LLDT---HGIREPLYLSALKAAkap 257
Cdd:PLN03073 402 EflntvvtDILHLHGQKLVTYKGDYDTFERTREEQLKNQqkafesnersrshmqaFIDKfryNAKRASLVQSRIKAL--- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 258 ltceDKLSNLKAL----DYKRFRPAVQawfaDRPAPaaekqyqPLLEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGK 333
Cdd:PLN03073 479 ----DRLGHVDAVvndpDYKFEFPTPD----DRPGP-------PIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGP 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 334 NGSGKSTITKLIMGVIDADSGSSYlngedlselsifeRSQKVGVVMQNPNHMISHHMIFDEIAFGLRNRNIAEElitEKV 413
Cdd:PLN03073 544 NGIGKSTILKLISGELQPSSGTVF-------------RSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPE---QKL 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 414 EHVLELCGLS-KFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTagqDYRNYTSMLAFIQKLNRDLGiTVVIISHD 492
Cdd:PLN03073 608 RAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS---NHLDLDAVEALIQGLVLFQG-GVLMVSHD 683
|
....
gi 1382220129 493 MHLV 496
Cdd:PLN03073 684 EHLI 687
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-232 |
1.44e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.17 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 1 MTIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAIKGEVTGSLEINGKNISEfsmh 79
Cdd:PRK13536 40 VAIDLAGVSKSYG--DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTsPDAGKITVLGVPVPARARLAR---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 dytEQVGTVlqdtdSQFVGLsigeDIAFAL-ENQL-------MSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRV 151
Cdd:PRK13536 114 ---ARIGVV-----PQFDNL----DLEFTVrENLLvfgryfgMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 152 SLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEI 231
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEA-ERLCDRLCVLEAGRKIAEGRPHAL 259
|
.
gi 1382220129 232 L 232
Cdd:PRK13536 260 I 260
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-234 |
2.05e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.90 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 35 IIGPSGSGKSTLGQCLNGLIPHAIKGEVTGSLEINGKNISEF-SMHDYTEQVGTVLQDTDSqfVGLSIGEDI-AFALENQ 112
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNP--FPMSIMDNVlAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 113 LMSNIDMYPLVKSTAKMVDL----ADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQL 188
Cdd:PRK14271 130 LVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1382220129 189 HNETnkTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK14271 210 ADRL--TVIIVTHNLAQAA-RISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
304-487 |
2.10e-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: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 304 LTYSYD---GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLI-----MGVIdadSGSSYLNGEDLSElsIFERSqkV 375
Cdd:cd03232 9 LNYTVPvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPLDK--NFQRS--T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNHmishhmifdeiafglrnrniaEELITekVEHVLELCGLskfrhwpIEALSYGQKKRVTIASILVLEPELLI 455
Cdd:cd03232 82 GYVEQQDVH---------------------SPNLT--VREALRFSAL-------LRGLSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190
....*....|....*....|....*....|..
gi 1382220129 456 LDEPTAGQDYRNYTSMLAFIQKLNRDlGITVV 487
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLADS-GQAIL 162
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-234 |
2.27e-13 |
|
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: 72.52 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESLDKP---TLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAikgevtGSLEINGKNISEFS 77
Cdd:COG4615 327 TLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLyRPES------GEILLDGQPVTADN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 78 MHDYTEQVGTVLQDtdsqfvglsigediaFALENQLMsNIDMYPLVKstakmvDLADMLER--------------SPHDL 143
Cdd:COG4615 401 REAYRQLFSAVFSD---------------FHLFDRLL-GLDGEADPA------RARELLERleldhkvsvedgrfSTTDL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 144 SGGQKQRVSLAGILVDDVDILLFDEPLASLDPkTGKATI--EIIDQLHnETNKTIVIIEH--RLEDVlhrdIDRVILMER 219
Cdd:COG4615 459 SQGQRKRLALLVALLEDRPILVFDEWAADQDP-EFRRVFytELLPELK-ARGKTVIAISHddRYFDL----ADRVLKMDY 532
|
250
....*....|....*
gi 1382220129 220 GEIVADMTPDEILAS 234
Cdd:COG4615 533 GKLVELTGPAALAAS 547
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
310-491 |
2.39e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD---SGSSYLNGEDLSELSIFERSqkvGVVMQN----P 382
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS---AYVQQDdlfiP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 383 NHMISHHMIFDEIafgLR-NRNIAEELITEKVEHVLELCGLSKFRHWPI------EALSYGQKKRVTIASILVLEPELLI 455
Cdd:TIGR00955 113 TLTVREHLMFQAH---LRmPRRVTKKEKRERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1382220129 456 LDEPTAGQDyrnytSMLAF--IQKLnRDL---GITVVIISH 491
Cdd:TIGR00955 190 CDEPTSGLD-----SFMAYsvVQVL-KGLaqkGKTIICTIH 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-493 |
2.94e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.13 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHaikGEVTGSLEINGKnISEFS-MHDyTEQVGTVLQDTDSQFV- 97
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH---GSYEGEILFDGE-VCRFKdIRD-SEALGIVIIHQELALIp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 98 GLSIGEDIAFALENQLMSNIDMYPLVKSTAKMvdLADM-LERSPH----DLSGGQKQRVSLAGILVDDVDILLFDEPLAS 172
Cdd:NF040905 92 YLSIAENIFLGNERAKRGVIDWNETNRRAREL--LAKVgLDESPDtlvtDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 173 LDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLhRDIDRVILMERGEIVadmtpdeilasklldthgireplylSALK 252
Cdd:NF040905 170 LNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIR-RVADSITVLRDGRTI-------------------------ETLD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 253 AAKAPLTcEDKLsnlkaldykrFRPAVQAWFADRPAPAAEKQYQPLLEVHGLT--YSYDGEKNALEDVSFKIGKGEFVSI 330
Cdd:NF040905 223 CRADEVT-EDRI----------IRGMVGRDLEDRYPERTPKIGEVVFEVKNWTvyHPLHPERKVVDDVSLNVRRGEIVGI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 331 LGKNGSGKstiTKLIMGV--------IdadSGSSYLNGE--DLSELS---------IFERSQKVGVVMQNP---N----- 383
Cdd:NF040905 292 AGLMGAGR---TELAMSVfgrsygrnI---SGTVFKDGKevDVSTVSdaidaglayVTEDRKGYGLNLIDDikrNitlan 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 384 -HMISHHMIFDEIafglRNRNIAEELITE---KVEHVLELCGlskfrhwpieALSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:NF040905 366 lGKVSRRGVIDEN----EEIKVAEEYRKKmniKTPSVFQKVG----------NLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
490 500 510
....*....|....*....|....*....|....*...
gi 1382220129 460 TAGQD----YRNYTsmlaFIQKLnRDLGITVVIISHDM 493
Cdd:NF040905 432 TRGIDvgakYEIYT----IINEL-AAEGKGVIVISSEL 464
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
296-521 |
4.03e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.14 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKV 375
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNHMISHHMIFDEIAFGlrNRNIAEELITEKVEHVLELCG-LSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG--GFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRS-------IVIADS--KLIANAAMTEVF 521
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGyvlenghVVLEDTgdALLANEAVRSAY 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
296-520 |
4.25e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 296 QPLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELS-------- 367
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASttaalaag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 368 ---IFERSQKVG--VVMQN------PNhmishhmifdeiAFGLRNRNIAEELITEKVEHVlelcGLSKFRHWPIEALSYG 436
Cdd:PRK11288 81 vaiIYQELHLVPemTVAENlylgqlPH------------KGGIVNRRLLNYEAREQLEHL----GVDIDPDTPLKYLSIG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 437 QKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIAN-A 515
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfD 223
|
....*
gi 1382220129 516 AMTEV 520
Cdd:PRK11288 224 DMAQV 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-222 |
4.76e-13 |
|
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: 69.50 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVTGSLEINGKNISEFSMHDYT 82
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL------NTEGDIQIDGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTdsqfvglsigediaFALENQLMSNIDMYPLVKS-----TAKMVDLADMLERSPHDL-----------SGG 146
Cdd:cd03289 77 KAFGVIPQKV--------------FIFSGTFRKNLDPYGKWSDeeiwkVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 147 QKQRVSLAGILVDDVDILLFDEPLASLDPktgkATIEIIDQL--HNETNKTIVIIEHRLEDVLhrDIDRVILMERGEI 222
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDP----ITYQVIRKTlkQAFADCTVILSEHRIEAML--ECQRFLVIEENKV 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-233 |
5.71e-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: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 8 FSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVtgslEINGKNISEFSMhDYTEQVGT 87
Cdd:COG4586 28 FRREYR--EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIL-VPTSGEV----RVLGYVPFKRRK-EFARRIGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 88 V------------LQDTdsqfvglsigediaFAL--------ENQLMSNIDMYplvkstAKMVDLADMLERSPHDLSGGQ 147
Cdd:COG4586 100 VfgqrsqlwwdlpAIDS--------------FRLlkaiyripDAEYKKRLDEL------VELLDLGELLDTPVRQLSLGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVADM 226
Cdd:COG4586 160 RMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDI--EALcDRVIVIDHGRIIYDG 237
|
....*..
gi 1382220129 227 TPDEILA 233
Cdd:COG4586 238 SLEELKE 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
311-491 |
1.04e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.68 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 311 EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADS--GSSYLNGEDLSELSIfersQKVGVVMQN----PNH 384
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL----KRTGFVTQDdilyPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 385 MISHHMIFDEIafgLR-NRNIAEELITEKVEHVLELCGLSKFRHWP-----IEALSYGQKKRVTIASILVLEPELLILDE 458
Cdd:PLN03211 156 TVRETLVFCSL---LRlPKSLTKQEKILVAESVISELGLTKCENTIignsfIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|....*..
gi 1382220129 459 PTAGQD----YRNYTSMLAFIQKlnrdlGITVVIISH 491
Cdd:PLN03211 233 PTSGLDataaYRLVLTLGSLAQK-----GKTIVTSMH 264
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-234 |
1.16e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.60 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikGEVTgsleINGKNISefsmhdyteqvgtvlqDTDS 94
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPDS--GEVL----WDGEPLD----------------PEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 QFVG-----------LSIGEDIA-FAlenQL--MSnidmyplvKSTAKM--------VDLADMLERSPHDLSGGQKQRVS 152
Cdd:COG4152 71 RRIGylpeerglypkMKVGEQLVyLA---RLkgLS--------KAEAKRradewlerLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 153 LAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVlHRDIDRVILMERGEIVADMTPDEIL 232
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELV-EELCDRIVIINKGRKVLSGSVDEIR 217
|
..
gi 1382220129 233 AS 234
Cdd:COG4152 218 RQ 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-235 |
1.19e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESLDkpTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEVTgsleINGKNISEFSMHDYT 82
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIV----FDGKDITDWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 EQVGTVLQDTDSQFVGLSIGEDIA----FALENQLMSNI----DMYPlvkstakmvDLADMLERSPHDLSGGQKQRVSLA 154
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAmggfFAERDQFQERIkwvyELFP---------RLHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 155 GILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLhRDIDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQAL-KLADRGYVLENGHVVLEDTGDALLAN 227
|
.
gi 1382220129 235 K 235
Cdd:PRK11614 228 E 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-225 |
1.21e-12 |
|
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: 67.56 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHA-----IKGEVTGSLEINGKNISEFSMHDYTEQVGTVLq 90
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDsgtvtVRGRVSSLLGLGGGFNPELTGRENIYLNGRLL- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 91 dtdsqfvGLS---IGEDIAFALE-NQLMSNIDMyPlVKStakmvdladmlersphdLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:cd03220 113 -------GLSrkeIDEKIDEIIEfSELGDFIDL-P-VKT-----------------YSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 167 DEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVlhRDI-DRVILMERGEIVAD 225
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSI--KRLcDRALVLEKGKIRFD 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
302-492 |
1.22e-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: 70.35 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 302 HGLTYSYDGEKNALEDVSF------KIGkgefvsILGKNGSGKSTITKlIMGVIDADSgssylNGEDLSELSIfersqKV 375
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLsffpgaKIG------VLGLNGAGKSTLLR-IMAGVDKDF-----NGEARPQPGI-----KV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNP----------NHMISHHMI------FDEIafglrNRNIAEE------LITE--KVEHVLELCGLSKFRH---- 427
Cdd:TIGR03719 71 GYLPQEPqldptktvreNVEEGVAEIkdaldrFNEI-----SAKYAEPdadfdkLAAEqaELQEIIDAADAWDLDSqlei 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 428 -----------WPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNytsmLAFIQKLNRDLGITVVIISHD 492
Cdd:TIGR03719 146 amdalrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-242 |
1.40e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDY 81
Cdd:PRK10575 11 TFALRNVSFRVP--GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-----EGEILLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDTdSQFVGLSIGEDIAfalenqlmsnIDMYPL--------------VKSTAKMVDLADMLERSPHDLSGGQ 147
Cdd:PRK10575 84 ARKVAYLPQQL-PAAEGMTVRELVA----------IGRYPWhgalgrfgaadrekVEEAISLVGLKPLAHRLVDSLSGGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 148 KQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVADMT 227
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDI-NMAARYCDYLVALRGGEMIAQGT 231
|
250
....*....|....*.
gi 1382220129 228 PDEILASKLL-DTHGI 242
Cdd:PRK10575 232 PAELMRGETLeQIYGI 247
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-511 |
1.48e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 70.20 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESldKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVT--GSLEINGKNIS----EF 76
Cdd:PRK10636 2 IVFSSLQIRRGV--RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEI-SADGGSYTfpGNWQLAWVNQEtpalPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 77 SMHDYT-------EQVGTVLQDTDSQFVGLSIgediafALENQLMSNIDMYPLVKSTAKMVD----LADMLERSPHDLSG 145
Cdd:PRK10636 79 PALEYVidgdreyRQLEAQLHDANERNDGHAI------ATIHGKLDAIDAWTIRSRAASLLHglgfSNEQLERPVSDFSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKtgkATIEIIDQLHNETNkTIVIIEHRlEDVLHRDIDRVILMER---GEI 222
Cdd:PRK10636 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHD-RDFLDPIVDKIIHIEQqslFEY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 223 VADMTPDEIL-ASKLLDTHGIREP-----LYLSAL------KAAKApltcEDKLSNLKALD-YKRFRPAvqawFADRP-- 287
Cdd:PRK10636 228 TGNYSSFEVQrATRLAQQQAMYESqqervAHLQSYidrfraKATKA----KQAQSRIKMLErMELIAPA----HVDNPfh 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 288 ----APaaEKQYQPLLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLngedl 363
Cdd:PRK10636 300 fsfrAP--ESLPNPLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 364 selsifERSQKVGVVMQnpnhmisHHMIF---DEIAFGLRNRnIAEELITEKVEHVLELCGLSKFR-HWPIEALSYGQKK 439
Cdd:PRK10636 372 ------AKGIKLGYFAQ-------HQLEFlraDESPLQHLAR-LAPQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKA 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 440 RVTIASILVLEPELLILDEPTAGQDyrnytsmLAFIQKLNR---DLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK10636 438 RLVLALIVWQRPNLLLLDEPTNHLD-------LDMRQALTEaliDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
288-491 |
1.70e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.13 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 288 APAAEKQYQPLLEVHGL------TYSYDG-EKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNG 360
Cdd:PRK10789 297 APVVKDGSEPVPEGRGEldvnirQFTYPQtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 361 EDLSELSIFERSQKVGVVMQNPnhmishhMIF-DEIAfglrnRNIA---EELITEKVEHVLELCGLskfrHWPI------ 430
Cdd:PRK10789 377 IPLTKLQLDSWRSRLAVVSQTP-------FLFsDTVA-----NNIAlgrPDATQQEIEHVARLASV----HDDIlrlpqg 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 431 ---------EALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRdlGITVVIISH 491
Cdd:PRK10789 441 ydtevgergVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAH 508
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-228 |
1.92e-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: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 12 YESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGKNIsEFSMHDYTEQVGTVLQD 91
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP-----PTSGTVLVGGKDI-ETNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 92 tDSQFVGLSIGEDIAFALE----NQLMSNIDMYPLVKSTAkmvdLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:TIGR01257 1012 -NILFHHLTVAEHILFYAQlkgrSWEEAQLEMEAMLEDTG----LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 168 EPLASLDPKTGKATIEIIdqLHNETNKTIVIIEHRLEDVlhrDI--DRVILMERGEIVADMTP 228
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEA---DLlgDRIAIISQGRLYCSGTP 1144
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-231 |
1.96e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.66 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 17 KPTLKNINLRIEKGEkIV-IIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQ-VGTVLQDTDS 94
Cdd:COG1129 265 GGVVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPAD-----SGEIRLDGKPVRIRSPRDAIRAgIAYVPEDRKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 Q--FVGLSIGEDIAFALENQLMSNIdmyplVKSTAKMVDLA-DMLER------SPHD----LSGGQKQRVSLAGILVDDV 161
Cdd:COG1129 339 EglVLDLSIRENITLASLDRLSRGG-----LLDRRRERALAeEYIKRlriktpSPEQpvgnLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 162 DILLFDEPLASLDPKTgKATI-EIIDQLHNEtNKTIVIIEHRLEDVLHrdI-DRVILMERGEIVADMTPDEI 231
Cdd:COG1129 414 KVLILDEPTRGIDVGA-KAEIyRLIRELAAE-GKAVIVISSELPELLG--LsDRILVMREGRIVGELDREEA 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
299-522 |
2.12e-12 |
|
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: 69.45 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID--ADSGSSYLNGEDLSELSIFERSQKVG 376
Cdd:TIGR03269 1 IEVKNLTKKFDG-KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHVALCEKCGYVERPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 --------------VVMQNPNHMISHHM-----IFDEIAFGLRNR-----NIAEEL------ITEKVEHVLELCGLSKFR 426
Cdd:TIGR03269 80 epcpvcggtlepeeVDFWNLSDKLRRRIrkriaIMLQRTFALYGDdtvldNVLEALeeigyeGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 427 HWPIEA---LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRS 503
Cdd:TIGR03269 160 HRITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*....
gi 1382220129 504 IVIADSKLIANAAMTEVFS 522
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVA 258
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
330-526 |
2.24e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.36 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 330 ILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDL--SELSIF---ERsQKVGVVMQNpNHMISHHMIFDEIAFGLRNRNi 404
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKGIClppEK-RRIGYVFQD-ARLFPHYKVRGNLRYGMAKSM- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 405 aeeliTEKVEHVLELCG----LSKFrhwPIeALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNR 480
Cdd:PRK11144 106 -----VAQFDKIVALLGieplLDRY---PG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1382220129 481 DLGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQPSL 526
Cdd:PRK11144 177 EINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAM 222
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-241 |
3.17e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlipHAIKGEVTGSLEINGKNISE-----------FSMHDYTEQ 84
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---HPAYKILEGDILFKGESILDlepeerahlgiFLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 85 VGTVlqdTDSQFVGLSIGEDIAFALENQLmSNIDMYPLVKSTAKMVDL-ADMLERSPHD-LSGGQKQRVSLAGILVDDVD 162
Cdd:CHL00131 96 IPGV---SNADFLRLAYNSKRKFQGLPEL-DPLEFLEIINEKLKLVGMdPSFLSRNVNEgFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNeTNKTIVIIEH--RLEDVLHRDIdrVILMERGEIVadMTPDEILAsKLLDTH 240
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGINKLMT-SENSIILITHyqRLLDYIKPDY--VHVMQNGKII--KTGDAELA-KELEKK 245
|
.
gi 1382220129 241 G 241
Cdd:CHL00131 246 G 246
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
17-512 |
3.91e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.77 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 17 KPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAikGEVtgSLEIN---GK-NISEFSMHDY---------- 81
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEPSA--GNV--SLDPNerlGKlRQDQFAFEEFtvldtvimgh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 -------------------TEQVGTVLQDTDSQFV------------GLSIGEDIAFALENQLMSNIdmyplvkstakmv 130
Cdd:PRK15064 90 telwevkqerdriyalpemSEEDGMKVADLEVKFAemdgytaearagELLLGVGIPEEQHYGLMSEV------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 131 dladmlerSPhdlsgGQKQRVSLAGILVDDVDILLFDEPLASLDPKTgkatIEIIDQLHNETNKTIVIIEHrledvlhrd 210
Cdd:PRK15064 157 --------AP-----GWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISH--------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 211 iDRVILMERGEIVADMTPDEI-----------LASKLldthgIREPLyLSALKAAKApltcedKLSNLKALdYKRFRP-A 278
Cdd:PRK15064 211 -DRHFLNSVCTHMADLDYGELrvypgnydeymTAATQ-----ARERL-LADNAKKKA------QIAELQSF-VSRFSAnA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 279 VQAWFADRPAPAAEK-------------------QYQPL----LEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNG 335
Cdd:PRK15064 277 SKAKQATSRAKQIDKikleevkpssrqnpfirfeQDKKLhrnaLEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 336 SGKSTITKLIMGVIDADSGSSylngeDLSElsiferSQKVGVVMQNPNHMISHHM-IFDEIAfGLRNRNIAEELitekVE 414
Cdd:PRK15064 356 VGKTTLLRTLVGELEPDSGTV-----KWSE------NANIGYYAQDHAYDFENDLtLFDWMS-QWRQEGDDEQA----VR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 415 HVLE--LCGLSKFRHwPIEALSYGQKKRVTIASILVLEPELLILDEPTagqdyrNYTSMLAfIQKLNRDLGI---TVVII 489
Cdd:PRK15064 420 GTLGrlLFSQDDIKK-SVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT------NHMDMES-IESLNMALEKyegTLIFV 491
|
570 580
....*....|....*....|...
gi 1382220129 490 SHDMHLVLEYTTRSIVIADSKLI 512
Cdd:PRK15064 492 SHDREFVSSLATRIIEITPDGVV 514
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-207 |
4.73e-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: 69.17 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 7 NFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikgEVTGSLEINGKNISEFSMHDYTEQVG 86
Cdd:TIGR01271 1222 GLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL------STEGEIQIDGVSWNSVTLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 87 TVLQDTdsqfvglsigediaFALENQLMSNIDMYPL-----VKSTAKMVDLADMLERSPHDL-----------SGGQKQR 150
Cdd:TIGR01271 1296 VIPQKV--------------FIFSGTFRKNLDPYEQwsdeeIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQL 1361
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 151 VSLAGILVDDVDILLFDEPLASLDPktgkATIEIIDQL--HNETNKTIVIIEHRLEDVL 207
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDP----VTLQIIRKTlkQSFSNCTVILSEHRVEALL 1416
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
314-511 |
5.48e-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: 68.89 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLsELSIFERSQKVGVVMQNpNHMISHHMIFD 393
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQH-NILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 394 EIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLA 473
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*...
gi 1382220129 474 FIQKLNRdlGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:TIGR01257 1103 LLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-176 |
5.58e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 65.07 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 18 PTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVtgslEINGKNISEFSMHdYTEQVgTVLQDTDSQFV 97
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPD-SGEV----RWNGTPLAEQRDE-PHENI-LYLGHLPGLKP 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 98 GLSIGEDIAFAleNQLMSNIDMYPLvKSTAKmVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPK 176
Cdd:TIGR01189 87 ELSALENLHFW--AAIHGGAQRTIE-DALAA-VGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-201 |
5.97e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLiPHAIKGEVtgslEINGKNIsefsmHDYTEQVGTVLQDTDSQFVGL 99
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGL-DDGSSGEV----SLVGQPL-----HQMDEEARAKLRAKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SigediaF-------ALEN-QL------MSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK10584 96 S------FmliptlnALENvELpallrgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1382220129 166 FDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEH 201
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-229 |
7.28e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.52 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAIKGEVTGSLEINgknisefsmhdYTEQ---VGTVLQDTDSQ 95
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVIKRNGKLRIG-----------YVPQklyLDTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVGLSIG---EDIAFALenqlmsnidmyplvkstaKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLAS 172
Cdd:PRK09544 89 FLRLRPGtkkEDILPAL------------------KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 173 LDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHRdIDRVILMERgEIVADMTPD 229
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAK-TDEVLCLNH-HICCSGTPE 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-505 |
1.32e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHAikgevtGSLEINGKNISEFSMHDYTEQ-VGTVLQDTdsQFV 97
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDA------GSILIDGQEMRFASTTAALAAgVAIIYQEL--HLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 98 -GLSIGEDIafaLENQLMSNIDMyplVKSTAKMVDLADMLER-----SPH----DLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:PRK11288 92 pEMTVAENL---YLGQLPHKGGI---VNRRLLNYEAREQLEHlgvdiDPDtplkYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 168 EPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLhRDIDRVILMERGEIV------ADMTPDEILAS----KLL 237
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIF-ALCDAITVFKDGRYVatfddmAQVDRDQLVQAmvgrEIG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 238 DTHGireplYlsalkaakapltcedklsnlkaldykrfrpavqawfadRPAPAAEkqyqPLLEVHGLtysyDGEKNAlED 317
Cdd:PRK11288 244 DIYG-----Y--------------------------------------RPRPLGE----VRLRLDGL----KGPGLR-EP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 318 VSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFErSQKVGVVM----QNPNHMISHHMIFD 393
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD-AIRAGIMLcpedRKAEGIIPVHSVAD 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 394 EIAFGLRNRNI-AEELITEKVE------HVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYR 466
Cdd:PRK11288 351 NINISARRHHLrAGCLINNRWEaenadrFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
490 500 510
....*....|....*....|....*....|....*....
gi 1382220129 467 NYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTRSIV 505
Cdd:PRK11288 431 AKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVV 468
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
304-491 |
2.21e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.06 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 304 LTYS--YDGEKNA-LEDVSFKIGKGEFVSILGKNGSGKSTI-----TKLIMGVIDadSGSSYLNGEDLSelSIFERSqkV 375
Cdd:TIGR00956 765 LTYEvkIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTLlnvlaERVTTGVIT--GGDRLVNGRPLD--SSFQRS--I 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPNHmISHHMIFDEIAFGLRNRNIAEELITEK---VEHVLELCGLSKFRH----WPIEALSYGQKKRVTIASILV 448
Cdd:TIGR00956 839 GYVQQQDLH-LPTSTVRESLRFSAYLRQPKSVSKSEKmeyVEEVIKLLEMESYADavvgVPGEGLNVEQRKRLTIGVELV 917
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1382220129 449 LEPELLI-LDEPTAGQDYRNYTSMLAFIQKLNrDLGITVVIISH 491
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 960
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-224 |
2.30e-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: 63.82 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTL--------GQ--CLNGLIPHA--------------IKGeVTGSLEINGKNISe 75
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaeGQrrYVESLSAYArqflgqmdkpdvdsIEG-LSPAIAIDQKTTS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 76 fsmHDYTEQVGTVLQDTDsqFVGLsigediafalenqLMSNIdmyPLVKSTAKMVDLAD---MLERSPHDLSGGQKQRVS 152
Cdd:cd03270 89 ---RNPRSTVGTVTEIYD--YLRL-------------LFARV---GIRERLGFLVDVGLgylTLSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 153 LAGILVDDVD--ILLFDEPLASLDPKTGKATIEIIDQLHNETNkTIVIIEHRLEDVLHrdIDRVILM------ERGEIVA 224
Cdd:cd03270 148 LATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRA--ADHVIDIgpgagvHGGEIVA 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-223 |
2.62e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.36 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 11 RYESLDKP------TLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaIKGEVTGSLEINGKNISEFSMHD---Y 81
Cdd:PRK10908 3 RFEHVSKAylggrqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-----IERPSAGKIWFSGHDITRLKNREvpfL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQDtDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK10908 78 RRQIGMIFQD-HHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDVLHRDIdRVILMERGEIV 223
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSY-RMLTLSDGHLH 216
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-496 |
2.72e-11 |
|
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: 66.57 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 136 LERSPHDLSGGQKQRVSLA--------GILVddvdILlfDEPLASLDPKTGKATIEIIDQLHNETNkTIVIIEHRLEDVL 207
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLAtqigsgltGVLY----VL--DEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHDEDTIR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 208 HrdIDRVILM------ERGEIVADMTPDEILASKLLDThgirePLYLSALKAAKAPltcedklsnlkaldyKRFRPAVQA 281
Cdd:TIGR00630 555 A--ADYVIDIgpgageHGGEVVASGTPEEILANPDSLT-----GQYLSGRKKIEVP---------------AERRPGNGK 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 282 WfadrpapaaekqyqplLEVHGltysydGEKNALEDVSFKIGKGEFVSILGKNGSGKSTitkLIMGVIdADSGSSYLNG- 360
Cdd:TIGR00630 613 F----------------LTLKG------ARENNLKNITVSIPLGLFTCITGVSGSGKST---LINDTL-YPALANRLNGa 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 361 --EDLSELSI--FERSQKVGVVMQ---------NPNHMIShhmIFDEI-------------------------------A 396
Cdd:TIGR00630 667 ktVPGRYTSIegLEHLDKVIHIDQspigrtprsNPATYTG---VFDEIrelfaetpeakvrgytpgrfsfnvkggrceaC 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 397 FGL----------------------------------RNRNIAEEL---ITE---------KVEHVLE-LC--GLSKFR- 426
Cdd:TIGR00630 744 QGDgvikiemhflpdvyvpcevckgkrynretlevkyKGKNIADVLdmtVEEayeffeavpSISRKLQtLCdvGLGYIRl 823
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1382220129 427 HWPIEALSYGQKKRVTIASIL---VLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLV 496
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVI 895
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
319-523 |
3.22e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 319 SFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSiFERSQKvgVVMQ----NPNHMISHhmifDE 394
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS-FEQLQK--LVSDewqrNNTDMLSP----GE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 395 IAFGLRNRNIAEELI--TEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSML 472
Cdd:PRK10938 96 DDTGRTTAEIIQDEVkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 473 AFIQKLNRDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEVFSQ 523
Cdd:PRK10938 176 ELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
297-464 |
6.63e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 297 PLLEVHGLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELsifERSQKVG 376
Cdd:PRK13543 10 PLLAAHALAFSRNEEP-VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQNPNhMISHHMIFDEIAF--GLRNRNiAEELITekveHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK13543 86 YLGHLPG-LKADLSTLENLHFlcGLHGRR-AKQMPG----SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|
gi 1382220129 455 ILDEPTAGQD 464
Cdd:PRK13543 160 LLDEPYANLD 169
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-223 |
7.32e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 11 RYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLngliphaikgevTGSLEIN-GKNISEFSMHdYTEQVGTVL 89
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL------------LSQFEISeGRVWAERSIA-YVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 90 QDTdsqfvglsIGEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLE----RSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PTZ00243 734 NAT--------VRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLEteigEKGVNLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 166 FDEPLASLDPKTGKATIE--IIDQLHnetNKTIVIIEHRLEDVLHrdIDRVILMERGEIV 223
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVEecFLGALA---GKTRVLATHQVHVVPR--ADYVVALGDGRVE 860
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-233 |
1.39e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.67 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNgLIPHAIKGEvtgsLEINGKNISEfsmHDYTEQ------VGTVLQDTd 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETPTGGE----LYYQGQDLLK---ADPEAQkllrqkIQIVFQNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 94 sqFVGLSIGEDIAFALENQLMSNIDMyplvKSTAKMVDLADMLE----------RSPHDLSGGQKQRVSLAGILVDDVDI 163
Cdd:PRK11308 102 --YGSLNPRKKVGQILEEPLLINTSL----SAAERREKALAMMAkvglrpehydRYPHMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 164 LLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEDVLHrdI-DRVILMERGEIVADMTPDEILA 233
Cdd:PRK11308 176 VVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEH--IaDEVMVMYLGRCVEKGTKEQIFN 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
298-505 |
1.50e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSsylngedlselSIFERSQKVGV 377
Cdd:PRK11147 3 LISIHGAWLSF-SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGR-----------IIYEQDLIVAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNP--------------------NHMISHHMIFDEIAFGLRNRNIAE-ELITEKVEH------------VLELCGLSK 424
Cdd:PRK11147 71 LQQDPprnvegtvydfvaegieeqaEYLKRYHDISHLVETDPSEKNLNElAKLQEQLDHhnlwqlenrineVLAQLGLDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 425 frHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIqklnRDLGITVVIISHDMHLVLEYTTRsI 504
Cdd:PRK11147 151 --DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHDRSFIRNMATR-I 223
|
.
gi 1382220129 505 V 505
Cdd:PRK11147 224 V 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-206 |
2.02e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESL-DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEIN-GKNISEFSMHD 80
Cdd:PTZ00265 383 IQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY-----DPTEGDIIINdSHNLKDINLKW 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 81 YTEQVGTVLQDtdSQFVGLSIGEDIAF---------ALENQLMSN-------------------IDMYPLVKSTA----- 127
Cdd:PTZ00265 458 WRSKIGVVSQD--PLLFSNSIKNNIKYslyslkdleALSNYYNEDgndsqenknkrnscrakcaGDLNDMSNTTDsneli 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 128 ------KMVDLADMLERSP----HD-------------------LSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTG 178
Cdd:PTZ00265 536 emrknyQTIKDSEVVDVSKkvliHDfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260
....*....|....*....|....*...
gi 1382220129 179 KATIEIIDQLHNETNKTIVIIEHRLEDV 206
Cdd:PTZ00265 616 YLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-220 |
2.29e-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: 59.95 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIPHAIKGEVTGSLEINGKNISEfsmhDYTEQVGTVLQdTDSQ 95
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTL---LDVLAGRKTAGVITGEILINGRPLDK----NFQRSTGYVEQ-QDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVGLSIGEDIAFalenqlmsnidmyplvksTAKMvdladmlerspHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:cd03232 91 SPNLTVREALRF------------------SALL-----------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1382220129 176 KTGKATIEIIDQLhNETNKTIVIIEHRLEDVLHRDIDRVILMERG 220
Cdd:cd03232 142 QAAYNIVRFLKKL-ADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-175 |
2.65e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVtgslEINGKNIS--EFSMH-DYTEQVGTVLQDt 92
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLL-HVESGQI----QIDGKTATrgDRSRFmAYLGHLPGLKAD- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 93 dsqfvgLSIGEDIAF--ALENQLMSNIDmyplvKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:PRK13543 97 ------LSTLENLHFlcGLHGRRAKQMP-----GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....*
gi 1382220129 171 ASLDP 175
Cdd:PRK13543 166 ANLDL 170
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-250 |
3.06e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTL-----GQCLNGLIPHAIKgeVTGSLEINGKNISEFSMHDYTEQVGTVLQDTDS 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLlkalaGDLTGGGAPRGAR--VTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 qfvglsigediAFALENQLMSNIDMYPLVKSTAKMV----DLAD-MLERSPHD---------LSGGQKQRVSLAGILVD- 159
Cdd:PRK13547 95 -----------AFAFSAREIVLLGRYPHARRAGALThrdgEIAWqALALAGATalvgrdvttLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 160 --------DVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIVAD------ 225
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDP-NLAARHADRIAMLADGAIVAHgapadv 242
|
250 260 270
....*....|....*....|....*....|
gi 1382220129 226 MTPDEI-----LASKLLDTHGIREPLYLSA 250
Cdd:PRK13547 243 LTPAHIarcygFAVRLVDAGDGVPPVIVPA 272
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
315-506 |
3.15e-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: 63.43 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPnhmishhMIFde 394
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDP-------VLF-- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 395 iAFGLR-NRNIAEELITEKVEHVLELCGLSKF-RHWPI----------EALSYGQKKRVTIASILVLEPELLILDEPTAG 462
Cdd:TIGR00957 1373 -SGSLRmNLDPFSQYSDEEVWWALELAHLKTFvSALPDkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1382220129 463 QDYRNYTSMLAFIQKLNRDlgITVVIISHDMHLVLEYtTRSIVI 506
Cdd:TIGR00957 1452 VDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDY-TRVIVL 1492
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-203 |
4.97e-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: 60.46 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 30 GEKIVIIGPSGSGKSTLGQCLNG-LIPHAIKGEVTGSL-EIngknISEF---SMHDYTEQV--GTVLQDTDSQFVGL--- 99
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPNLGKFDDPPDWdEI----LDEFrgsELQNYFTKLleGDVKVIVKPQYVDLipk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 ----SIGEdiafalenqLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDP 175
Cdd:cd03236 102 avkgKVGE---------LLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 1382220129 176 KTGKATIEIIDQLhNETNKTIVIIEHRL 203
Cdd:cd03236 173 KQRLNAARLIREL-AEDDNYVLVVEHDL 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
298-502 |
5.63e-10 |
|
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: 62.72 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGEKN-ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSElSIFERSQKVG 376
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQnpnhmishhmiFDEIAFGL----------RNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASI 446
Cdd:TIGR01257 2016 YCPQ-----------FDAIDDLLtgrehlylyaRLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 447 LVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRDlGITVVIISHDMHLVLEYTTR 502
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTR 2139
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-174 |
6.14e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 7 NFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVTGSLEINgknisefsmhdyteqVG 86
Cdd:PRK15064 324 NLTKGFD--NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPD-SGTVKWSENAN---------------IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 87 TVLQDTDSQFvglsiGEDIA-FALENQLMSNIDMYPLVKST-AKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDIL 164
Cdd:PRK15064 386 YYAQDHAYDF-----ENDLTlFDWMSQWRQEGDDEQAVRGTlGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170
....*....|
gi 1382220129 165 LFDEPLASLD 174
Cdd:PRK15064 461 VMDEPTNHMD 470
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
314-511 |
6.15e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.21 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 314 ALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEdLSELSIFE--RSQKVGVvmqnpnhmishhmi 391
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIAISAglSGQLTGI-------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 392 fDEIAFGLRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSM 471
Cdd:PRK13546 104 -ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1382220129 472 LAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PRK13546 183 LDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
20-208 |
7.76e-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: 59.33 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIphaikGEVTGSLEINGKNISEFSMHDyteqVGtVLQDTDSQFVGL 99
Cdd:TIGR03740 16 VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGIL-----RPTSGEIIFDGHPWTRKDLHK----IG-SLIESPPLYENL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGED--IAFALENQLMSNIDmyplvkSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKT 177
Cdd:TIGR03740 86 TARENlkVHTTLLGLPDSRID------EVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIG 159
|
170 180 190
....*....|....*....|....*....|.
gi 1382220129 178 GKATIEIIdQLHNETNKTIVIIEHRLEDVLH 208
Cdd:TIGR03740 160 IQELRELI-RSFPEQGITVILSSHILSEVQQ 189
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-240 |
1.48e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKgEVTGSLEINGKNISEFSMHDYTeqVGTVLQDTDSQ 95
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVR-QTAGRVLLDGKPVAPCALRGRK--IATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVGL-SIGediAFALENQL----MSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPL 170
Cdd:PRK10418 92 FNPLhTMH---THARETCLalgkPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 171 ASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLeDVLHRDIDRVILMERGEIV--ADM-----TPDEILASKLLDTH 240
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDM-GVVARLADDVAVMSHGRIVeqGDVetlfnAPKHAVTRSLVSAH 244
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
16-223 |
1.50e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGevtGSLEINGKNISEFSMHDYT-EQVGTVLQ---- 90
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTG---GTVEFKGKDLLELSPEDRAgEGIFMAFQypve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 91 --DTDSQFVGLSIGEDIAFALENQLMSNIDMYPLVKSTAKMVDL-ADMLERSPH-DLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:PRK09580 90 ipGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 167 DEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEH--RLEDVLHRDIdrVILMERGEIV 223
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHyqRILDYIKPDY--VHVLYQGRIV 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-206 |
1.55e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.13 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTgSLEINGKNISEFSMHDYTEQVgtvlQDTDSQFVGL 99
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV-RLASGKIS-ILGQPTRQALQKNLVAYVPQS----EEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SigEDIAFALENQLMSNIDM-----YPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLD 174
Cdd:PRK15056 97 V--EDVVMMGRYGHMGWLRRakkrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190
....*....|....*....|....*....|..
gi 1382220129 175 PKTGKATIEIIDQLHNEtNKTIVIIEHRLEDV 206
Cdd:PRK15056 175 VKTEARIISLLRELRDE-GKTMLVSTHNLGSV 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-201 |
1.63e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 57.89 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAiKGEVtgsleingknisefsmhdyteqvgtVLQDTDSQFVGL 99
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL-AGRV-------------------------LLNGGPLDFQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGEDIAF-----ALENQL--MSNIDMYPLVKSTAKMVD-LADM----LERSP-HDLSGGQKQRVSLAGILVDDVDILLF 166
Cdd:cd03231 70 SIARGLLYlghapGIKTTLsvLENLRFWHADHSDEQVEEaLARVglngFEDRPvAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1382220129 167 DEPLASLDpKTGKATIEIIDQLHNETNKTIVIIEH 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 |
2.35e-09 |
|
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: 57.27 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDAD---SGSSYLNGEDLSELSIFERSQKVGVVmQNPNHMishhmi 391
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVS-EEDVHF------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 392 fdeiafglrnrniAEELITEKVEHVLELCGLSKFRhwpieALSYGQKKRVTIASILVLEPELLILDEPTAGQDyrnytSM 471
Cdd:cd03233 96 -------------PTLTVRETLDFALRCKGNEFVR-----GISGGERKRVSIAEALVSRASVLCWDNSTRGLD-----SS 152
|
170 180
....*....|....*....|...
gi 1382220129 472 LAF-----IQKLNRDLGITVVII 489
Cdd:cd03233 153 TALeilkcIRTMADVLKTTTFVS 175
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
302-492 |
2.47e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 302 HGLTYSYDGEKNALEDV--SF----KIGkgefvsILGKNGSGKSTITKlIMGVIDADSgssylNGEdlselSIFERSQKV 375
Cdd:PRK11819 10 NRVSKVVPPKKQILKDIslSFfpgaKIG------VLGLNGAGKSTLLR-IMAGVDKEF-----EGE-----ARPAPGIKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNP----------NHMISHHMI------FDEIafglrNRNIAE------ELITE--KVEHVLELCGLSKFRH---- 427
Cdd:PRK11819 73 GYLPQEPqldpektvreNVEEGVAEVkaaldrFNEI-----YAAYAEpdadfdALAAEqgELQEIIDAADAWDLDSqlei 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 428 -----------WPIEALSYGQKKRVTIASILVLEPELLILDEPTagqdyrNY---TSMLAFIQKLNRDLGiTVVIISHD 492
Cdd:PRK11819 148 amdalrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT------NHldaESVAWLEQFLHDYPG-TVVAVTHD 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-236 |
3.71e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 14 SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQ-VGTVlqdT 92
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA-----GGEIRLNGKDISPRSPLDAVKKgMAYI---T 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 93 DSQ-----FVGLSIGEDIAFA--LENQ-------LMSNIDMYPLVKSTAKMVDL-ADMLERSPHDLSGGQKQRVSLAGIL 157
Cdd:PRK09700 345 ESRrdngfFPNFSIAQNMAISrsLKDGgykgamgLFHEVDEQRTAENQRELLALkCHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 158 VDDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHRdIDRVILMERGEIVA------DMTPDEI 231
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITV-CDRIAVFCEGRLTQiltnrdDMSEEEI 502
|
....*
gi 1382220129 232 LASKL 236
Cdd:PRK09700 503 MAWAL 507
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-231 |
4.60e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.88 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 17 KPTLKNINLRIEKGEkIV-IIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQ-VGTVLQdtDS 94
Cdd:COG3845 271 VPALKDVSLEVRAGE-ILgIAGVAGNGQSELAEALAGLRPPA-----SGSIRLDGEDITGLSPRERRRLgVAYIPE--DR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 QFVGLSIGEDIAfalENQLMSNIDMYPLVK----STAKMVDLA-DMLER------SPHD----LSGGQKQRVSLAGILVD 159
Cdd:COG3845 343 LGRGLVPDMSVA---ENLILGRYRRPPFSRggflDRKAIRAFAeELIEEfdvrtpGPDTparsLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 160 DVDILLFDEPLASLDPktgKATIEIIDQLHNETN--KTIVIIEHRLEDVLhrDI-DRVILMERGEIVADMTPDEI 231
Cdd:COG3845 420 DPKLLIAAQPTRGLDV---GAIEFIHQRLLELRDagAAVLLISEDLDEIL--ALsDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-209 |
5.27e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVT------GSLE----INgKNISEFS--MH-DYt 82
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTlfgrrrGSGEtiwdIK-KHIGYVSssLHlDY- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 83 eQVGTVLQDTD-SQFVGlSIG--EDIAFALENQLMSNIDMYPLVKSTAKmvdladmlerSP-HDLSGGQKQRVSLAGILV 158
Cdd:PRK10938 350 -RVSTSVRNVIlSGFFD-SIGiyQAVSDRQQKLAQQWLDILGIDKRTAD----------APfHSLSWGQQRLALIVRALV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLED----VLHR 209
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDapacITHR 472
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-202 |
5.90e-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: 55.24 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFrYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEF-SMHDY 81
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-----SGRIGMPEGEDLLFlPQRPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQvGTvlqdtdsqfvglsigediafaLENQLmsnidMYPLvkstaKMVdladmlersphdLSGGQKQRVSLAGILVDDV 161
Cdd:cd03223 75 LPL-GT---------------------LREQL-----IYPW-----DDV------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHnetnKTIVIIEHR 202
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGHR 147
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-220 |
7.09e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIPHAIKGEVTGSLEINGKNISEFSMhdytEQVGTVLQDtDSQ 95
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTL---LNALAGRIQGNNFTGTILANNRKPTKQIL----KRTGFVTQD-DIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 96 FVGLSIGEDIAFA----LENQLM---------SNIDMYPLVKSTAKMVdlADMLERSphdLSGGQKQRVSLAGILVDDVD 162
Cdd:PLN03211 152 YPHLTVRETLVFCsllrLPKSLTkqekilvaeSVISELGLTKCENTII--GNSFIRG---ISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 163 ILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHRDIDRVILMERG 220
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
298-464 |
7.11e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 298 LLEVHGLTYSYDGeKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVID--ADSGSSYLNGEDLSELSIFERSQKv 375
Cdd:PRK09580 1 MLSIKDLHVSVED-KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRAGE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVM--QNPNHM--ISHHMIFDEIAFGLR--------NRNIAEELITEKVEhVLELCGLSKFRHWPIeALSYGQKKRVTI 443
Cdd:PRK09580 79 GIFMafQYPVEIpgVSNQFFLQTALNAVRsyrgqeplDRFDFQDLMEEKIA-LLKMPEDLLTRSVNV-GFSGGEKKRNDI 156
|
170 180
....*....|....*....|.
gi 1382220129 444 ASILVLEPELLILDEPTAGQD 464
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLD 177
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
299-530 |
8.66e-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: 58.77 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNA-LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADsGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAvLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQ-------------NPNHMISHHMIF---DEIafGLRNrniAEELITEKVEHVLELCGLskfrhwpieALSYGQKKRV 441
Cdd:TIGR01271 1297 IPQkvfifsgtfrknlDPYEQWSDEEIWkvaEEV--GLKS---VIEQFPDKLDFVLVDGGY---------VLSNGHKQLM 1362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 442 TIASILVLEPELLILDEPTAGQDYRNYtsmlafiQKLNRDL-----GITVVIISHDMHLVLEyTTRSIVIADSKLIANAA 516
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTL-------QIIRKTLkqsfsNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDS 1434
|
250
....*....|....
gi 1382220129 517 MTEVFSQPSLLERA 530
Cdd:TIGR01271 1435 IQKLLNETSLFKQA 1448
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-218 |
1.00e-08 |
|
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: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 27 IEKGEKIVIIGPSGSGKSTLGQCLngliphaikgevTGSLEINGKNISefsmhdyteqvgtvlqdtdsqfvglsigedia 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKIL------------AGQLIPNGDNDE-------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 107 falenqlmsnidmYPLVKSTAKmvdladmlersPH--DLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEI 184
Cdd:cd03222 58 -------------WDGITPVYK-----------PQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|....*.
gi 1382220129 185 IDQLHNETNKTIVIIEHrleDVLHRDI--DRVILME 218
Cdd:cd03222 114 IRRLSEEGKKTALVVEH---DLAVLDYlsDRIHVFE 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-252 |
1.16e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLgqclngLIPHAIKGEVT-GSLEINGKNIS------ 74
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTL------LLTFMRMVEVCgGEIRVNGREIGayglre 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 75 ---EFSM--HDYTEQVGTVLQDTDSqFVGLSIGEDIAfALEnqlmsNIDMYPLVKSTAKMVDlADMLErSPHDLSGGQKQ 149
Cdd:PTZ00243 1382 lrrQFSMipQDPVLFDGTVRQNVDP-FLEASSAEVWA-ALE-----LVGLRERVASESEGID-SRVLE-GGSNYSVGQRQ 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 150 RVSLA-GILVDDVDILLFDEPLASLDP---KTGKATIeiidqLHNETNKTIVIIEHRLEDVLHrdIDRVILMERGeIVAD 225
Cdd:PTZ00243 1453 LMCMArALLKKGSGFILMDEATANIDPaldRQIQATV-----MSAFSAYTVITIAHRLHTVAQ--YDKIIVMDHG-AVAE 1524
|
250 260
....*....|....*....|....*...
gi 1382220129 226 M-TPDEILASKLLDTHGIREPLYLSALK 252
Cdd:PTZ00243 1525 MgSPRELVMNRQSIFHSMVEALGRSEAK 1552
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
299-523 |
1.32e-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: 56.07 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGE-KNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03288 20 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhmishhMIFD-EIAFGL------RNRNIAEELITEKVEHVLELC--GLSKFRHWPIEALSYGQKKRVTIASILV 448
Cdd:cd03288 100 ILQDP-------ILFSgSIRFNLdpeckcTDDRLWEALEIAQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 449 LEPELLILDEPTAGQDYR-----NYTSMLAFIQKlnrdlgiTVVIISHDMHLVLEyTTRSIVIADSKLIANAAMTEVFSQ 523
Cdd:cd03288 173 RKSSILIMDEATASIDMAtenilQKVVMTAFADR-------TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
299-530 |
1.42e-08 |
|
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: 56.02 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSY-DGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADsGSSYLNGEDLSELSIFERSQKVGV 377
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQ-------------NPNHMISHHMIF---DEIafGLRNrniAEELITEKVEHVLELCGLskfrhwpieALSYGQKKRV 441
Cdd:cd03289 82 IPQkvfifsgtfrknlDPYGKWSDEEIWkvaEEV--GLKS---VIEQFPGQLDFVLVDGGC---------VLSHGHKQLM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 442 TIASILVLEPELLILDEPTAGQDYRNYtsmlafiQKLNRDL-----GITVVIISHDMHLVLEyTTRSIVIADSKLIANAA 516
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITY-------QVIRKTLkqafaDCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDS 219
|
250
....*....|....
gi 1382220129 517 MTEVFSQPSLLERA 530
Cdd:cd03289 220 IQKLLNEKSHFKQA 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-232 |
1.94e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.70 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPHAikgevtGSLEINGKNISEFSMHDYTEQVGTVLQDTDSQFV--- 97
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDA------GEVHYRMRDGQLRDLYALSEAERRRLLRTEWGFVhqh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 98 -----------GLSIGEdiafalenQLMSNIDM-YPLVKSTAkmvdlADMLER----------SPHDLSGGQKQRVSLAG 155
Cdd:PRK11701 98 prdglrmqvsaGGNIGE--------RLMAVGARhYGDIRATA-----GDWLERveidaariddLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 156 ILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEdVLHRDIDRVILMERGEIVADMTPDEIL 232
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLA-VARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-496 |
2.08e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.53 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 136 LERSPHDLSGGQKQRVSLAGILVDDVD--ILLFDEPLASLDPKTGKATIEIIDQLHNETNkTIVIIEHrlEDVLHRDIDR 213
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEH--DEQMISLADR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 214 VILMER------GEIVADMTPDEILASKlldthgireplylSALKAAKapltcedkLSNLKALDYKRFRPAVQAWfadrp 287
Cdd:PRK00635 547 IIDIGPgagifgGEVLFNGSPREFLAKS-------------DSLTAKY--------LRQELTIPIPEKRTNSLGT----- 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 288 apaaekqyqpllevhgLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKS-----TITKLIMGVIDADSGSS-YLNGE 361
Cdd:PRK00635 601 ----------------LTLSK-ATKHNLKDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFIEQGFCSNlSIQWG 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 362 DLSEL-------------SI-------FE----------RSQKVGV------------------------VMQNPN---- 383
Cdd:PRK00635 664 AISRLvhitrdlpgrsqrSIpltyikaFDdlrelfaeqpRSKRLGLtkshfsfntplgacaecqglgsitTTDNRTsipc 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 384 ---HMISHHMIFDEIAFglRNRNIAEEL----------------ITEKVEhvlELCGLsKFRHWPI----EALSYGQKKR 440
Cdd:PRK00635 744 pscLGKRFLPQVLEVRY--KGKNIADILemtayeaekffldepsIHEKIH---ALCSL-GLDYLPLgrplSSLSGGEIQR 817
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 441 VTIASIL---VLEPELLILDEPTAGQDYRNYTSMLAFIQKLNrDLGITVVIISHDMHLV 496
Cdd:PRK00635 818 LKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLT-HQGHTVVIIEHNMHVV 875
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-239 |
3.85e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhAIKGEVT--GSlEINGKNIS----------EFSMhdYTEQvgTVL 89
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP-ASEGEAWlfGQ-PVDAGDIAtrrrvgymsqAFSL--YGEL--TVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 90 QDTD--SQFVGLSiGEDIAfalenqlmsnidmyPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFD 167
Cdd:NF033858 358 QNLElhARLFHLP-AAEIA--------------ARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 168 EPLASLDPKTGKATIEIIDQLHNETNKTIVIIEH------RledvlhrdIDRVILMERGEIVADMTPDEILASKLLDT 239
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSREDGVTIFISTHfmneaeR--------CDRISLMHAGRVLASDTPAALVAARGAAT 492
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
315-513 |
5.04e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPnhmishhMIFDe 394
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP-------VLFD- 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 395 iafGLRNRNIAE--ELITEKVEHVLELCGLSKFRHWPIEAL-----------SYGQKKRVTIASILVLEPELLIL-DEPT 460
Cdd:PTZ00243 1398 ---GTVRQNVDPflEASSAEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKGSGFILmDEAT 1474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 461 AGQDYR-----NYTSMLAFIqklnrdlGITVVIISHDMHLVLEYTtrSIVIADSKLIA 513
Cdd:PTZ00243 1475 ANIDPAldrqiQATVMSAFS-------AYTVITIAHRLHTVAQYD--KIIVMDHGAVA 1523
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-183 |
5.95e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 3 IAFSNFSFRYESldKPTL-KNINLRIEKGEKIVIIGPSGSGKSTLGQCLNG-LIPhaIKGEVTGSLEIngkNISEFSMH- 79
Cdd:PLN03073 509 ISFSDASFGYPG--GPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQP--SSGTVFRSAKV---RMAVFSQHh 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 80 -DYTEQVGTVLQDTDSQFVGlsigediafALENQLMSNIDMYPLVKSTAkmvdLADMlerspHDLSGGQKQRVSLAGILV 158
Cdd:PLN03073 582 vDGLDLSSNPLLYMMRCFPG---------VPEQKLRAHLGSFGVTGNLA----LQPM-----YTLSGGQKSRVAFAKITF 643
|
170 180
....*....|....*....|....*
gi 1382220129 159 DDVDILLFDEPLASLDPKTGKATIE 183
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDAVEALIQ 668
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
299-493 |
6.27e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNA--LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLN-GEDLSELSIFERSQKV 375
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 376 GVVMQNPnhMISHHMIFDEIAFGL--------------------------RNRNIAE---------------ELITEKVE 414
Cdd:PTZ00265 463 GVVSQDP--LLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkRNSCRAKcagdlndmsnttdsnELIEMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 415 HVL----ELCGLSK--FRHWPIEA---------------LSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLA 473
Cdd:PTZ00265 541 YQTikdsEVVDVSKkvLIHDFVSAlpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260
....*....|....*....|
gi 1382220129 474 FIQKLNRDLGITVVIISHDM 493
Cdd:PTZ00265 621 TINNLKGNENRITIIIAHRL 640
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
300-464 |
8.95e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 300 EVHGLTYSYdGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSE-------------- 365
Cdd:NF033858 3 RLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADarhrravcpriaym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 366 -----------LSIFERSQKVGVVmqnpnhmishhmifdeiaFGL----RNRNIAEelitekvehVLELCGLSKFRHWPI 430
Cdd:NF033858 82 pqglgknlyptLSVFENLDFFGRL------------------FGQdaaeRRRRIDE---------LLRATGLAPFADRPA 134
|
170 180 190
....*....|....*....|....*....|....
gi 1382220129 431 EALSYGQKKRVTIASILVLEPELLILDEPTAGQD 464
Cdd:NF033858 135 GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
131-234 |
9.77e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.04 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 131 DLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIVIIEHRLEdVLHRD 210
Cdd:PRK15093 147 DHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQ-MLSQW 225
|
90 100
....*....|....*....|....
gi 1382220129 211 IDRVILMERGEIVADMTPDEILAS 234
Cdd:PRK15093 226 ADKINVLYCGQTVETAPSKELVTT 249
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-223 |
1.03e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVTGSLEINGKNISEFSMHdY 81
Cdd:TIGR00956 59 TRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNT-DGFHIGVEGVITYDGITPEEIKKH-Y 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 82 TEQVGTVLQdTDSQFVGLSIGEDIAFALENQLMSN-IDMYPLVKSTAKMVDLA----------------DMLErsphDLS 144
Cdd:TIGR00956 137 RGDVVYNAE-TDVHFPHLTVGETLDFAARCKTPQNrPDGVSREEYAKHIADVYmatyglshtrntkvgnDFVR----GVS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 145 GGQKQRVSLAGILVDDVDILLFDEPLASLDPKTgkaTIEIIDQLH---NETNKTIVIIEHRLEDVLHRDIDRVILMERGE 221
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSAT---ALEFIRALKtsaNILDTTPLVAIYQCSQDAYELFDKVIVLYEGY 288
|
..
gi 1382220129 222 IV 223
Cdd:TIGR00956 289 QI 290
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
303-513 |
1.22e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 303 GLTYSYDGEKnALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSelsiFERSQK-----VGV 377
Cdd:PRK10982 3 NISKSFPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID----FKSSKEalengISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPNhMISHHMIFDEIAFG---LRNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELL 454
Cdd:PRK10982 78 VHQELN-LVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1382220129 455 ILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLVLEYTTRSIVIADSKLIA 513
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-237 |
1.87e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 14 SLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGliphaIKGEVTGSLEINGKNISEFSMHDYTEQvGTVLQDTD 93
Cdd:PRK10982 258 SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG-----IREKSAGTITLHGKKINNHNANEAINH-GFALVTEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 94 SQFVGLSIGEDIAFaleNQLMSNIDMY---------PLVKSTAKMVdLADMLERSPH------DLSGGQKQRVSLAGILV 158
Cdd:PRK10982 332 RRSTGIYAYLDIGF---NSLISNIRNYknkvglldnSRMKSDTQWV-IDSMRVKTPGhrtqigSLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 159 DDVDILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHRdIDRVILMERGEIV-----ADMTPDEI-- 231
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGI-TDRILVMSNGLVAgivdtKTTTQNEIlr 485
|
....*.
gi 1382220129 232 LASKLL 237
Cdd:PRK10982 486 LASLHL 491
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
315-491 |
2.34e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTItkliMGVIDADSGSSYLNGEdlSELSIFERSQKV-----GVVMQN----PNHM 385
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTL----MDVLAGRKTGGYIEGD--IRISGFPKKQETfarisGYCEQNdihsPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 386 ISHHMIFDeiAFGLRNRNIAEELITEKVEHVLELCGLSKFRH----WP-IEALSYGQKKRVTIASILVLEPELLILDEPT 460
Cdd:PLN03140 970 VRESLIYS--AFLRLPKEVSKEEKMMFVDEVMELVELDNLKDaivgLPgVTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170 180 190
....*....|....*....|....*....|....
gi 1382220129 461 AGQDYRnytsMLAFIQKLNR---DLGITVVIISH 491
Cdd:PLN03140 1048 SGLDAR----AAAIVMRTVRntvDTGRTVVCTIH 1077
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
306-505 |
2.69e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 52.03 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 306 YSYDGEKNALEDVSFKIGKGEF-----VSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLS----ELSIFERSQKVG 376
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 VVMQNPNHMISHHMIFDEIAFGLRNRNIAEELITEkvehvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPELLIL 456
Cdd:cd03237 81 LLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPE---------------------LSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1382220129 457 DEPTAGQDYRNYTSMLAFIQKLNRDLGITVVIISHDMHLVLEYTTRSIV 505
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
290-464 |
3.07e-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: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 290 AAEKQYQPLLE---VHGLTYSYDGEKNALEDVSFKIGK--------GEFVSILGKNGSGKSTITKLIMG-----VIDADS 353
Cdd:TIGR00956 41 AADSDYQPTFPnalLKILTRGFRKLKKFRDTKTFDILKpmdglikpGELTVVLGRPGSGCSTLLKTIASntdgfHIGVEG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 354 GSSYlNGEDLSELsifeRSQKVGVVM---QNPNHmISHHMIFDEIAF-------GLRNRNIAEELITEKVEHV-LELCGL 422
Cdd:TIGR00956 121 VITY-DGITPEEI----KKHYRGDVVynaETDVH-FPHLTVGETLDFaarcktpQNRPDGVSREEYAKHIADVyMATYGL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1382220129 423 SKFRHWP-----IEALSYGQKKRVTIASILVLEPELLILDEPTAGQD 464
Cdd:TIGR00956 195 SHTRNTKvgndfVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-202 |
4.30e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 7 NFSFRYEslDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHaikgevTGSLEINGKNISEfSMHDYTEQV 85
Cdd:PRK13540 6 ELDFDYH--DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPE------KGEILFERQSIKK-DLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 86 GTVLQDTDSQfVGLSIGEDIAFALENQlMSNIDMYPLVKstakMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK13540 77 CFVGHRSGIN-PYLTLRENCLYDIHFS-PGAVGITELCR----LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 1382220129 166 FDEPLASLDPKTGKATIEIIdQLHNETNKTIVIIEHR 202
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKI-QEHRAKGGAVLLTSHQ 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
299-491 |
5.80e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNA--LEDVSFKIGKGEFVSILGKNGSGKSTITKLIM------------------------------ 346
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 347 -----GVIDADSGSSYLNGEDLSELSIFERSQKV-------------------GVVMQNPnhMISHHMIFDEIAFGlrnr 402
Cdd:PTZ00265 1246 eeqnvGMKNVNEFSLTKEGGSGEDSTVFKNSGKIlldgvdicdynlkdlrnlfSIVSQEP--MLFNMSIYENIKFG---- 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 403 niAEELITEKVEHVLELCGLSKFrhwpIEAL---------------SYGQKKRVTIASILVLEPELLILDEPTAGQDYRN 467
Cdd:PTZ00265 1320 --KEDATREDVKRACKFAAIDEF----IESLpnkydtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
250 260
....*....|....*....|....
gi 1382220129 468 YTSMLAFIQKLNRDLGITVVIISH 491
Cdd:PTZ00265 1394 EKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-239 |
8.61e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 10 FRYESLDKPTLKN-INLRIEKGEKIVIIGPSGSGKSTLGQCLNGLI-PHAikgevtGSLEINGKNISEFSMHDYTEQvGT 87
Cdd:PRK11288 258 LRLDGLKGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATrRTA------GQVYLDGKPIDIRSPRDAIRA-GI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 88 VLQDTDSQFVGL----SIGEDIafalenqlmsNIDMYPLvKSTAKMV-------DLAD-----MLERSPH------DLSG 145
Cdd:PRK11288 331 MLCPEDRKAEGIipvhSVADNI----------NISARRH-HLRAGCLinnrweaENADrfirsLNIKTPSreqlimNLSG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 146 GQKQRVSLAGILVDDVDILLFDEPLASLDpkTGkATIEIIDQLHN--ETNKTIVIIEHRLEDVLHRDiDRVILMERGEIV 223
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGID--VG-AKHEIYNVIYElaAQGVAVLFVSSDLPEVLGVA-DRIVVMREGRIA 475
|
250 260
....*....|....*....|.
gi 1382220129 224 -----ADMTPDEILASKLLDT 239
Cdd:PRK11288 476 gelarEQATERQALSLALPRT 496
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
310-494 |
9.04e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGS-SYLNGEDLSELS----IFERSQKVGVVMQNPNH 384
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNvSLDPNERLGKLRqdqfAFEEFTVLDTVIMGHTE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 385 MISHHMIFDEI--------AFGLRnrniAEELITEKVEH------------VLELcGLSKFRHW-PIEALSYGQKKRVTI 443
Cdd:PRK15064 92 LWEVKQERDRIyalpemseEDGMK----VADLEVKFAEMdgytaearagelLLGV-GIPEEQHYgLMSEVAPGWKLRVLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 444 ASILVLEPELLILDEPTAGQDYrNYTSMLAfiQKLN-RDlgITVVIISHDMH 494
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDI-NTIRWLE--DVLNeRN--STMIIISHDRH 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-183 |
1.19e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEfSMHDYteqvgtvLQDTdsQFVG--- 98
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPD-----AGEVLWQGEPIRR-QRDEY-------HQDL--LYLGhqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 -----LSIGEDIAFALenQLMSNIDMYPLVKSTAKmVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASL 173
Cdd:PRK13538 84 gikteLTALENLRFYQ--RLHGPGDDEALWEALAQ-VGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170
....*....|
gi 1382220129 174 DpKTGKATIE 183
Cdd:PRK13538 161 D-KQGVARLE 169
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-204 |
1.52e-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: 48.47 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIPHAIKGEVTGSLEINGKNISefsmhdyteqvgtvlqdtdsqfvgL 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---VNEGLYASGKARLISFLPKFSRNKL------------------------I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 SIGediafalenQLMSNIDMyplvkstakmvDLADM-LERSPHDLSGGQKQRVSLAGILVDDVD--ILLFDEPLASLDPK 176
Cdd:cd03238 64 FID---------QLQFLIDV-----------GLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180
....*....|....*....|....*...
gi 1382220129 177 TGKATIEIIDQLHNETNkTIVIIEHRLE 204
Cdd:cd03238 124 DINQLLEVIKGLIDLGN-TVILIEHNLD 150
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-230 |
1.84e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 22 NINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGEVTgsleINGKNISEFSMHDYTEQvGTVLQDTDSQFVG--- 98
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIF----IDGKPVKIRNPQQAIAQ-GIAMVPEDRKRDGivp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 99 -LSIGEDIAFALENQL--MSNIDmyplvkSTAKMVDLADMLER------SPH----DLSGGQKQRVSLAGILVDDVDILL 165
Cdd:PRK13549 355 vMGVGKNITLAALDRFtgGSRID------DAAELKTILESIQRlkvktaSPElaiaRLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 166 FDEPLASLDpkTG-KATI-EIIDQLHNEtNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDE 230
Cdd:PRK13549 429 LDEPTRGID--VGaKYEIyKLINQLVQQ-GVAIIVISSELPEVLGLS-DRVLVMHEGKLKGDLINHN 491
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
312-496 |
2.38e-06 |
|
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: 49.15 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 312 KNALEDVSFKIGKGEFVSILGKNGSGKST-ITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQ---------N 381
Cdd:cd03271 8 ENNLKNIDVDIPLGVLTCVTGVSGSGKSSlINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQspigrtprsN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 382 PNHMIShhmIFDEI------------------AFGLRNRNIAEEL---ITE---------KVEHVLE-LC--GLSKFR-H 427
Cdd:cd03271 88 PATYTG---VFDEIrelfcevckgkrynretlEVRYKGKSIADVLdmtVEEaleffenipKIARKLQtLCdvGLGYIKlG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1382220129 428 WPIEALSYGQKKRVTIASILVLE---PELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHDMHLV 496
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVI 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
315-491 |
3.59e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEDLSELSIFERSQKVGVVMQNPNhMISHHMIFDE 394
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPV-LFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 395 IAFGLRN-RNIAEELITEKVEHVLEL--CGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYtsm 471
Cdd:PLN03130 1334 DPFNEHNdADLWESLERAHLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD--- 1410
|
170 180
....*....|....*....|..
gi 1382220129 472 lAFIQKLNRD--LGITVVIISH 491
Cdd:PLN03130 1411 -ALIQKTIREefKSCTMLIIAH 1431
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
315-459 |
4.25e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSsylngedlselsiFERSQKVGVVMQNPnhMISHHMIFDE 394
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK-------------IKHSGRISFSPQTS--WIMPGTIKDN 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 395 IAFGL-----RNRNIA-----EELIT---EKVEHVLELCGLSkfrhwpieaLSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:TIGR01271 507 IIFGLsydeyRYTSVIkacqlEEDIAlfpEKDKTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSP 575
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
315-492 |
5.04e-06 |
|
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: 48.02 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTitkLIMGVIDADSGSSYLNGedlseLSIFERsQKVGVvMQNPN----------- 383
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSS---LAFDTIYAEGQRRYVES-----LSAYAR-QFLGQ-MDKPDvdsieglspai 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 384 ----HMISHH----------------MIFDEIafGLRNRniAEELITEKVEHvlelcgLSKFRHwpIEALSYGQKKRVTI 443
Cdd:cd03270 81 aidqKTTSRNprstvgtvteiydylrLLFARV--GIRER--LGFLVDVGLGY------LTLSRS--APTLSGGEAQRIRL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1382220129 444 ASIL--VLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHD 492
Cdd:cd03270 149 ATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD 198
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-46 |
5.25e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 49.64 E-value: 5.25e-06
10 20
....*....|....*....|....*..
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
308-492 |
9.06e-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: 46.16 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 308 YDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMgvidADSGSSYLNgedlSELSIFERsQKVGVVMQNPNHmis 387
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLI----SFLPKFSR-NKLIFIDQLQFL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 388 hhmifdeIAFGLRNRNIAEELITekvehvlelcglskfrhwpieaLSYGQKKRVTIASILVLEPE--LLILDEPTAGQDY 465
Cdd:cd03238 72 -------IDVGLGYLTLGQKLST----------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180
....*....|....*....|....*..
gi 1382220129 466 RNYTSMLAFIQKLnRDLGITVVIISHD 492
Cdd:cd03238 123 QDINQLLEVIKGL-IDLGNTVILIEHN 148
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
299-491 |
9.73e-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: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 299 LEVHGLTYSYDGEKNALEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGS-SYLNGEDLselsIFersqkvgv 377
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRiGMPEGEDL----LF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 378 VMQNPnhmishhmifdEIAFGlrnrNIAEELItekvehvlelcglskfRHWPiEALSYGQKKRVTIASILVLEPELLILD 457
Cdd:cd03223 69 LPQRP-----------YLPLG----TLREQLI----------------YPWD-DVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 1382220129 458 EPTAGQDyrnyTSMLAFIQKLNRDLGITVVIISH 491
Cdd:cd03223 117 EATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
315-459 |
1.06e-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: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 315 LEDVSFKIGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGEdlselsiFERSQKVGVVMQNpnhmishhMIFDE 394
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------ISFSSQFSWIMPG--------TIKEN 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 395 IAFGL-----RNRNIA-----EELIT---EKVEHVLELCGLSkfrhwpieaLSYGQKKRVTIASILVLEPELLILDEP 459
Cdd:cd03291 118 IIFGVsydeyRYKSVVkacqlEEDITkfpEKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSP 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-221 |
1.32e-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: 45.44 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 29 KGEKIVIIGPSGSGKSTLGQCLNGLiphaikgevtgsLEINGKNISEFSMHDYTEQVGTVLQDTDsqfvglsigediafa 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE------------LGPPGGGVIYIDGEDILEEVLDQLLLII--------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 109 lenqlmsnidmyplvkstakmvdladmLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIID-- 186
Cdd:smart00382 54 ---------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1382220129 187 ---QLHNETNKTIVIIEHRLEDVLHRDI----DRVILMERGE 221
Cdd:smart00382 107 lllLLKSEKNLTVILTTNDEKDLGPALLrrrfDRRIVLLLIL 148
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-206 |
1.54e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 2 TIAFSNFSFRYESLDKP------------------TLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGL-IPHaikgev 62
Cdd:PRK13545 4 KVKFEHVTKKYKMYNKPfdklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPN------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 63 TGSLEINGknisefsmhdyTEQVGTVLQDTDSQFVGLsigEDIAFaleNQLMSNIDMYPLVKSTAKMVDLADM---LERS 139
Cdd:PRK13545 78 KGTVDIKG-----------SAALIAISSGLNGQLTGI---ENIEL---KGLMMGLTKEKIKEIIPEIIEFADIgkfIYQP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1382220129 140 PHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKATIEIIDQLhNETNKTIVIIEHRLEDV 206
Cdd:PRK13545 141 VKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQV 206
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-204 |
2.34e-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: 44.66 E-value: 2.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382220129 141 HDLSGGQKQRVSLAGIL----VDDVDILLFDEPLASLDPKTGKATIEIIDQLHNETNKTIViIEHRLE 204
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPE 142
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-46 |
4.65e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 4.65e-05
10 20
....*....|....*....|....*..
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
15-219 |
9.07e-05 |
|
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: 43.75 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 15 LDKPTLKNI-----NLRIEKGEKI-VIIGPSGSGKSTLGQCL--------------NGLIPHAI-KGEVTGSLEINgknI 73
Cdd:cd03240 1 IDKLSIRNIrsfheRSEIEFFSPLtLIVGQNGAGKTTIIEALkyaltgelppnskgGAHDPKLIrEGEVRAQVKLA---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 74 SEFSMHDYTeqvgtVLQDtdsqfvgLSIGEDIAFALENQLMSnidmyPLVkstakmvdlaDMLERsphdLSGGQKQ---- 149
Cdd:cd03240 78 ENANGKKYT-----ITRS-------LAILENVIFCHQGESNW-----PLL----------DMRGR----CSGGEKVlasl 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 150 --RVSLAGILVDDVDILLFDEPLASLDP-KTGKATIEIIDQLHNETNKTIVIIEH--RLEDVlhrdIDRVILMER 219
Cdd:cd03240 127 iiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHdeELVDA----ADHIYRVEK 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-237 |
9.95e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.99 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 13 ESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAikgevTGSLEINGKNISEFSMHDYTEQvGTVLQDT 92
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT-----SGYVTLDGHEVVTRSPQDGLAN-GIVYISE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 93 DSQ----FVGLSIGEDIAF-ALE--NQLMSNIDMYPLVKSTAKMVDLADM----LERSPHDLSGGQKQRVSLAGILVDDV 161
Cdd:PRK10762 335 DRKrdglVLGMSVKENMSLtALRyfSRAGGSLKHADEQQAVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 162 DILLFDEPLASLDPKTGKATIEIIDQLHNEtNKTIVIIEHRLEDVLHRDiDRVILMERGEIVADMTPDEILASKLL 237
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMS-DRILVMHEGRISGEFTREQATQEKLM 488
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-349 |
1.22e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 136 LERSPHDLSGGQKQRVSLAG-I---LVDDVDILlfDEPLASLDPK-TGKaTIEIIDQLHNETNkTIVIIEHRlEDVLhRD 210
Cdd:COG0178 479 LDRSAGTLSGGEAQRIRLATqIgsgLVGVLYVL--DEPSIGLHQRdNDR-LIETLKRLRDLGN-TVIVVEHD-EDTI-RA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 211 IDRVILM-----ERG-EIVADMTPDEILASKllDTHGIReplYLSALKAAKAPLtcedklsnlkaldyKRfRPAVQAWfa 284
Cdd:COG0178 553 ADYIIDIgpgagEHGgEVVAQGTPEEILKNP--DSLTGQ---YLSGRKRIPVPK--------------KR-RKGNGKF-- 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1382220129 285 drpapaaekqyqplLEVHGLTysydgeKNALEDVSFKIGKGEFVSILGKNGSGKSTitkLIMGVI 349
Cdd:COG0178 611 --------------LTIKGAR------ENNLKNVDVEIPLGVLTCVTGVSGSGKST---LVNDIL 652
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
132-231 |
1.81e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 132 LADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGKatiEIIDQLHN--ETNKTIVIIEHRLEDVlHR 209
Cdd:NF000106 134 LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN---EVWDEVRSmvRDGATVLLTTQYMEEA-EQ 209
|
90 100
....*....|....*....|..
gi 1382220129 210 DIDRVILMERGEIVADMTPDEI 231
Cdd:NF000106 210 LAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
20-228 |
2.15e-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: 43.37 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLgqcLNGLIPHAIKGEVTGSLEINGknisEFSMHDYTEQVGTVLQDTDS----- 94
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSL---INDTLYPALARRLHLKKEQPG----NHDRIEGLEHIDKVIVIDQSpigrt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 95 ------QFVG----------------------LSI---GEDIAFALEnqlMSNIDMYPLVKSTAKMVDLADMLE------ 137
Cdd:cd03271 84 prsnpaTYTGvfdeirelfcevckgkrynretLEVrykGKSIADVLD---MTVEEALEFFENIPKIARKLQTLCdvglgy 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 138 ----RSPHDLSGGQKQRVSLAGILVDDVD---ILLFDEPLASLDPKTGKATIEIIDQLHNETNkTIVIIEHRLeDVLhRD 210
Cdd:cd03271 161 iklgQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNL-DVI-KC 237
|
250 260
....*....|....*....|....
gi 1382220129 211 IDRVILM-----ER-GEIVADMTP 228
Cdd:cd03271 238 ADWIIDLgpeggDGgGQVVASGTP 261
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-230 |
2.23e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 16 DKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGlipHAIKGEVTGSLEINGKNISEFSMHD-------Y-TEqvgt 87
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG---RSYGRNISGTVFKDGKEVDVSTVSDaidaglaYvTE---- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 88 vlqdtDSQFVGLSIGEDIAFalenqlmsNIDMYPLVK-STAKMVDL-----------ADMLERSPH------DLSGGQKQ 149
Cdd:NF040905 345 -----DRKGYGLNLIDDIKR--------NITLANLGKvSRRGVIDEneeikvaeeyrKKMNIKTPSvfqkvgNLSGGNQQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 150 RVSLAGILVDDVDILLFDEPLASLDpkTG-KATI-EIIDQLHNEtNKTIVIIEHRLEDVLHRdIDRVILMERGEIVADMT 227
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGID--VGaKYEIyTIINELAAE-GKGVIVISSELPELLGM-CDRIYVMNEGRITGELP 487
|
...
gi 1382220129 228 PDE 230
Cdd:NF040905 488 REE 490
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-46 |
2.25e-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: 2.25e-04
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
400-520 |
2.33e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 400 RNRNIAEELITEKVEHVLELCGLSKFRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLN 479
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1382220129 480 RDlGITVVIISHDMHLVLEYTTRSIVIADSKLIANAAMTEV 520
Cdd:NF000106 192 RD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-231 |
4.10e-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: 43.46 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 143 LSGGQKQRVSLAGILVDDVD---ILLFDEPLASLDPKTGKATIEIIDQLHNETNkTIVIIEHRLeDVLhRDIDRVILM-- 217
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNL-DVI-KTADYIIDLgp 906
|
90
....*....|....*...
gi 1382220129 218 ---ER-GEIVADMTPDEI 231
Cdd:TIGR00630 907 eggDGgGTVVASGTPEEV 924
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
355-492 |
7.10e-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: 42.69 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 355 SSYLNGE---DLSELSIFErsqkvgvvmqnpnhmiSHHMiFDEIAFGLRNRNIAEELITEKVEHV-------LELCGLSK 424
Cdd:TIGR00630 422 AVTVGGKsiaDVSELSIRE----------------AHEF-FNQLTLTPEEKKIAEEVLKEIRERLgflidvgLDYLSLSR 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 425 frhwPIEALSYGQKKRVTIASIL--VLEPELLILDEPTAGQDYRNYTSMLAFIQKLnRDLGITVVIISHD 492
Cdd:TIGR00630 485 ----AAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD 549
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
310-561 |
7.75e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 310 GEKNALEDVSFKIGKGEFVSILGKNGSGKSTITK-LIMGVIDADSGSSYL-------NGEDLSEL-----SIFERSQkvg 376
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRyMAMHAIDGIPKNCQIlhveqevVGDDTTALqcvlnTDIERTQ--- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 377 vVMQNPNHMISHHMIFDEIAF-----GLRNRNIAEELITEKVEHV---LE--------------LCGLS---KFRHWPIE 431
Cdd:PLN03073 265 -LLEEEAQLVAQQRELEFETEtgkgkGANKDGVDKDAVSQRLEEIykrLElidaytaearaasiLAGLSftpEMQVKATK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 432 ALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRdlgiTVVIISHDMHLVLEYTTRSIVIADSKL 511
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1382220129 512 IANAAMTEVFsqpsllERanlctTSIYELATMMKIDDTN----AFMQYFIDYER 561
Cdd:PLN03073 420 VTYKGDYDTF------ER-----TREEQLKNQQKAFESNersrSHMQAFIDKFR 462
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-206 |
8.34e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPhaikgEVTGSLEINGknisEFSmhdyteqVGTVLQDTDSQFVGL 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS-----PTVGKVDRNG----EVS-------VIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 100 sigEDIAFALENQLMSNIDMYPLVKSTAKMVDLADMLERSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLASLDPKTGK 179
Cdd:PRK13546 104 ---ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180
....*....|....*....|....*..
gi 1382220129 180 ATIEIIDQLhNETNKTIVIIEHRLEDV 206
Cdd:PRK13546 181 KCLDKIYEF-KEQNKTIFFVSHNLGQV 206
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-46 |
1.05e-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: 1.05e-03
10 20
....*....|....*....|....*..
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTL 650
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-46 |
1.97e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 1.97e-03
10 20
....*....|....*....|....*..
gi 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-201 |
2.17e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 12 YESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIpHAIKGEVtgsleingknisefsmhdyteQVGTVLqd 91
Cdd:PRK11147 327 YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQL-QADSGRI---------------------HCGTKL-- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 92 tdsqfvglsigeDIAF------AL--ENQLMSNIdmyplvkSTAK---MVD---------LADML-----ERSP-HDLSG 145
Cdd:PRK11147 383 ------------EVAYfdqhraELdpEKTVMDNL-------AEGKqevMVNgrprhvlgyLQDFLfhpkrAMTPvKALSG 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1382220129 146 GQKQRVSLAGILVDDVDILLFDEPLASLDPKtgkaTIEIIDQLHNETNKTIVIIEH 201
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVE----TLELLEELLDSYQGTVLLVSH 495
|
|
| 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 1382220129 20 LKNINLRIEKGEKIVIIGPSGSGKSTL 46
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTL 651
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
322-506 |
2.67e-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: 39.09 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 322 IGKGEFVSILGKNGSGKSTITKLIMGVIDADSGSSYLNGedlseLSIFERSQKVgvvmqnpnhmishhmifdeiafglrn 401
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-----ITPVYKPQYI-------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 402 rniaeelitekvehvlelcglskfrhwpieALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLAFIQKLNRD 481
Cdd:cd03222 71 ------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*
gi 1382220129 482 LGITVVIISHDMhLVLEYTTRSIVI 506
Cdd:cd03222 121 GKKTALVVEHDL-AVLDYLSDRIHV 144
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
143-235 |
2.71e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 143 LSGGQKQRVSLAGILVdDVD----ILLFDEplasldPKTG------KATIEIIDQLHNETNkTIVIIEHRLeDVlhrdI- 211
Cdd:COG0178 827 LSGGEAQRVKLASELS-KRStgktLYILDE------PTTGlhfhdiRKLLEVLHRLVDKGN-TVVVIEHNL-DV----Ik 893
|
90 100 110
....*....|....*....|....*....|..
gi 1382220129 212 --DRVILM-----ER-GEIVADMTPDEILASK 235
Cdd:COG0178 894 taDWIIDLgpeggDGgGEIVAEGTPEEVAKVK 925
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-188 |
2.93e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.22 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 33 IVIIGPSGSGKSTL---------------GQCLNGLIPH-AIKGEVTGSLEINGKN---------ISEFSMHDYTEqvgt 87
Cdd:COG0419 26 NLIVGPNGAGKSTIleairyalygkarsrSKLRSDLINVgSEEASVELEFEHGGKRyrierrqgeFAEFLEAKPSE---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 88 vLQDTDSQFVGLSIGEDI---AFALENQLMSNIDMYPLVKsTAKMVDLADMLE-RSPHDLSGGQKQRVSLAgilvdDVDI 163
Cdd:COG0419 102 -RKEALKRLLGLEIYEELkerLKELEEALESALEELAELQ-KLKQEILAQLSGlDPIETLSGGERLRLALA-----DLLS 174
|
170 180
....*....|....*....|....*
gi 1382220129 164 LLFDepLASLDPKTGKATIEIIDQL 188
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEEL 197
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
35-137 |
2.98e-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: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 35 IIGPSGSGKSTLG-Q-CLNGLIPHAIKGEVTGSLEIN---GKNISEFSMHDYTEQVGTVL-------QDTDsqfVGLSIG 102
Cdd:cd19492 6 ICGVPGVGKTQLCmQlAVNVQIPKCFGGLAGEAIYIDtegSFNIHYFRVHDYVELLALINslpkfleDHPK---VKLIVV 82
|
90 100 110
....*....|....*....|....*....|....*.
gi 1382220129 103 EDIAFALENQLMSNIDMYPLVKSTA-KMVDLADMLE 137
Cdd:cd19492 83 DSIAFPFRHDFDDLAQRTRLLNGLAqLLHSLARQHN 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
324-498 |
3.05e-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: 38.51 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 324 KGEFVSILGKNGSGKSTITKLIMGVIDADSGSS-YLNGEDLSELSIFERSQKVGVVMQnpnhmishhmifdeiafglrnr 402
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 403 niaeelitekvehvlelcglskfrhwpiEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNY-----TSMLAFIQK 477
Cdd:smart00382 59 ----------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLLLL 110
|
170 180
....*....|....*....|.
gi 1382220129 478 LNRDLGITVVIISHDMHLVLE 498
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGP 131
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
34-201 |
3.37e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.17 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 34 VIIGPSGSGKSTLGQClnglIPHAIKGEVTGSLEINgknisefsmhdyteqvgtvlqDTDSQFvglSIGEDIA-----FA 108
Cdd:cd03279 32 LICGPTGAGKSTILDA----ITYALYGKTPRYGRQE---------------------NLRSVF---APGEDTAevsftFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 109 LENQLMSNIDMYPLVKSTAKMV------DLADMLERSPHDLSGGQKQRVSLA-GILVDDV---------DILLFDEPLAS 172
Cdd:cd03279 84 LGGKKYRVERSRGLDYDQFTRIvllpqgEFDRFLARPVSTLSGGETFLASLSlALALSEVlqnrggarlEALFIDEGFGT 163
|
170 180
....*....|....*....|....*....
gi 1382220129 173 LDPKTGKATIEIIDQLHNEtNKTIVIIEH 201
Cdd:cd03279 164 LDPEALEAVATALELIRTE-NRMVGVISH 191
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
316-492 |
3.53e-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: 38.49 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 316 EDVSFkiGKGEFVSILGKNGSGKSTITKLImgvidadsgssylngedlselsifersqKVGVVMQNPNHMIShhmifdei 395
Cdd:cd03227 14 NDVTF--GEGSLTIITGPNGSGKSTILDAI----------------------------GLALGGAQSATRRR-------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382220129 396 AFGLRNRNIAeeliTEKVEHVLELCGLSKfrhwpiealsyGQKKRVTIASILVLEPE----LLILDEPTAGQDYRNyTSM 471
Cdd:cd03227 56 SGVKAGCIVA----AVSAELIFTRLQLSG-----------GEKELSALALILALASLkprpLYILDEIDRGLDPRD-GQA 119
|
170 180
....*....|....*....|.
gi 1382220129 472 LAFIQKLNRDLGITVVIISHD 492
Cdd:cd03227 120 LAEAILEHLVKGAQVIVITHL 140
|
|
| |
