|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-474 |
1.24e-111 |
|
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: 339.57 E-value: 1.24e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyEGKLEGDVLLDGKSVSDTPLYD 80
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPA-VDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPH--GGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLL 160
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 161 PGIMVLDEPSSNLDMA-AIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFDSLSDGTRKE 239
Cdd:COG1123 161 PDLLIADEPTTALDVTtQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 240 IGLRPFSLSKLKPAnqyqAHTAKQMEFQNFCFAYKKREPESLHI---PSAELPVGETIAIIGLNGAGKSTLARCICGLEK 316
Cdd:COG1123 241 PRLGAARGRAAPAA----AAAEPLLEVRNLSKRYPVRGKGGVRAvddVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 317 -KCGFLQVEGKTL------DWKARLKHCYMVMQDTSHQLF-TESVADEV-----LLSMDNKDETV--VDKILKQFDL-LE 380
Cdd:COG1123 317 pTSGSILFDGKDLtklsrrSLRELRRRVQMVFQDPYSSLNpRMTVGDIIaeplrLHGLLSRAERRerVAELLERVGLpPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 381 YKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVV 459
Cdd:COG1123 397 LADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVA 476
|
490
....*....|....*
gi 933767453 460 HMEKGQVKESYPLDE 474
Cdd:COG1123 477 VMYDGRIVEDGPTEE 491
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-219 |
2.33e-81 |
|
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: 251.23 E-value: 2.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 4 FQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTPLYDLAA 83
Cdd:cd03225 2 LKNLSFSYPDGARPA-LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDLTKLSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 84 MVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGI 163
Cdd:cd03225 76 KVGLVFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 164 MVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGE 219
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
268-467 |
6.08e-81 |
|
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: 249.87 E-value: 6.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 268 NFCFAYKkREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDWKARLKHCYMVMQDTSH 346
Cdd:cd03226 4 NISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESsGSILLNGKPIKAKERRKSIGYVMQDVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 347 QLFTESVADEVLLSMDNKDE--TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHM 424
Cdd:cd03226 83 QLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 933767453 425 REVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVK 467
Cdd:cd03226 163 ERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-229 |
6.54e-74 |
|
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: 232.61 E-value: 6.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDL 81
Cdd:COG1122 1 IELENLSFSYPGGTPA--LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT-----SGEVLVDGKDITKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLP 161
Cdd:COG1122 74 RRKVGLVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 162 GIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEF 229
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
265-465 |
4.10e-70 |
|
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: 222.34 E-value: 4.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGK---TLDWKARLKHCYMV 340
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTsGEVLVDGKdltKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTSHQLFTESVADEVLLSMDN------KDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDE 414
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVAFGLENlglpeeEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 933767453 415 PTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQ 465
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
265-466 |
7.99e-66 |
|
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: 211.81 E-value: 7.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKrEPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLD----WKARlKHCYM 339
Cdd:COG1122 2 ELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKpTSGEVLVDGKDITkknlRELR-RKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 VMQDTSHQLFTESVADEVLLSMDN----KDE--TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFD 413
Cdd:COG1122 80 VFQNPDDQLFAPTVEEDVAFGPENlglpREEirERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 933767453 414 EPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
265-471 |
4.21e-45 |
|
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: 158.75 E-value: 4.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEG-KTLD----WKARlKHCY 338
Cdd:TIGR04520 2 EVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLpTSGKVTVDGlDTLDeenlWEIR-KKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 MVMQDTSHQLFTESVADEVLLSMDNK----DETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVF 412
Cdd:TIGR04520 81 MVFQNPDNQFVGATVEDDVAFGLENLgvprEEMRkrVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 413 DEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDP-ELVMAgcSYVVHMEKGQV-KESYP 471
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMeEAVLA--DRVIVMNKGKIvAEGTP 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
264-466 |
2.78e-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: 155.97 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGK---TLDWKARLKHCYM 339
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRdlaSLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 VMQDTSHQlFTESVADEVLL----------SMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREI 409
Cdd:COG1120 80 VPQEPPAP-FGLTVRELVALgryphlglfgRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLA-DQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
265-474 |
4.77e-43 |
|
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: 161.93 E-value: 4.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEG---KTLDWKARLKHCYMV 340
Cdd:COG2274 475 ELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRILIDGidlRQIDPASLRRQIGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTshQLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHPL-----------SLSGGQKQRVAIASAIVSNREI 409
Cdd:COG2274 555 LQDV--FLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELVMAgCSYVVHMEKGQVKESYPLDE 474
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEE 695
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-253 |
1.42e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 152.48 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYgEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDL 81
Cdd:PRK13635 6 IRVEHISFRY-PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL-----PEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLP 161
Cdd:PRK13635 80 RRQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 162 GIMVLDEPSSNLD-------MAAIDDLRQvlslwkKQGKTIL-IAehrlyylHDL-----ADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13635 160 DIIILDEATSMLDprgrrevLETVRQLKE------QKGITVLsIT-------HDLdeaaqADRVIVMNKGEILEEGTPEE 226
|
250 260
....*....|....*....|....*.
gi 933767453 229 FDSLSDGTRkEIGLR-PFSLsKLKPA 253
Cdd:PRK13635 227 IFKSGHMLQ-EIGLDvPFSV-KLKEL 250
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
265-464 |
2.26e-42 |
|
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: 149.61 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPesLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDwKARLKHCYMVMQD 343
Cdd:cd03235 1 EVEDLTVSYGGHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTsGSIRVFGKPLE-KERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 344 TSHQLFTESVADEVLLSMDN----------KDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFD 413
Cdd:cd03235 78 SIDRDFPISVRDVVLMGLYGhkglfrrlskADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 933767453 414 EPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKG 464
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
271-474 |
4.95e-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: 149.95 E-value: 4.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 271 FAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTL---DWKARLKHCYMVMQD--T 344
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGRPVtrrRRKAFRRRVQMVFQDpyA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 345 S-HQLFT-ESVADEVLLSMDNKDETV-VDKILKQFDL-LEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD 420
Cdd:COG1124 91 SlHPRHTvDRILAEPLRIHGLPDREErIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 421 LKHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:COG1124 171 VSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
265-466 |
6.20e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.47 E-value: 6.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKR---EPESLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDwKARLKHCYMV 340
Cdd:COG1121 8 ELENLTVSYGGRpvlEDVSLTIPP-----GEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFGKPPR-RARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTSHQLFTESVADEVLLSMDN----------KDETVVDKILKQFDLLEYKDRhPLS-LSGGQKQRVAIASAIVSNREI 409
Cdd:COG1121 82 QRAEVDWDFPITVRDVVLMGRYGrrglfrrpsrADREAVDEALERVGLEDLADR-PIGeLSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-259 |
6.62e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 150.52 E-value: 6.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSVSD-TPL 78
Cdd:PRK13644 1 MIRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQ------KGKVLVSGIDTGDfSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSV 158
Cdd:PRK13644 73 QGIRKLVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 159 LLPGIMVLDEPSSNLDM-AAIDDLRQVLSLWKKqGKTILIAEHRLYYLHDlADRVLYVKDGEIEREYTPAEFdsLSDGTR 237
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPdSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENV--LSDVSL 228
|
250 260
....*....|....*....|..
gi 933767453 238 KEIGLRPFSLSKLkpANQYQAH 259
Cdd:PRK13644 229 QTLGLTPPSLIEL--AENLKMH 248
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
265-465 |
1.24e-40 |
|
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: 143.15 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGK---TLDWKARLKHCYMV 340
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPtSGEILIDGKdiaKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQdtshqlftesvadevllsmdnkdetvvdkilkqfdlleykdrhplsLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD 420
Cdd:cd00267 79 PQ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 933767453 421 LKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQ 465
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
265-466 |
2.03e-39 |
|
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: 140.65 E-value: 2.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLdwkarlkhcymvmQD 343
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSsGEILLDGKDL-------------AS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 344 TSHQLFTESVAdevllsmdnkdetVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKH 423
Cdd:cd03214 66 LSPKELARKIA-------------YVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 933767453 424 MREVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03214 133 QIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
265-486 |
3.97e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.82 E-value: 3.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDW----KARlKHCYM 339
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKpQSGEIKIDGITISKenlkEIR-KKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 VMQDTSHQLFTESVADEVLLSMDNKDET------VVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFD 413
Cdd:PRK13632 88 IFQNPDNQFIGATVEDDIAFGLENKKVPpkkmkdIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 414 EPTSGLDLKHMREVARSLKSLADQG-KTLLVITHDPELVMAgCSYVVHMEKGQ-VKESYPLDESGSKKVLDFFRI 486
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAIL-ADKVIVFSEGKlIAQGKPKEILNNKEILEKAKI 241
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
258-469 |
5.10e-39 |
|
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: 149.14 E-value: 5.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 258 AHTAKQMEFQNFCFAYKKREPeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEG---KTLDWKAR 333
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGfLPPYSGSILINGvdlSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 334 LKHCYMVMQDTshQLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQRVAIASA 402
Cdd:COG4988 410 RRQIAWVPQNP--YLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 403 IVSNREIIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELVMAgCSYVVHMEKGQVKES 469
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.35e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 141.28 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSVSDTPLY 79
Cdd:PRK13632 7 MIKVENVSFSYPNSENNA-LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQ------SGEIKIDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVL 159
Cdd:PRK13632 80 EIRKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 160 LPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAehrlyYLHD-----LADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIS-----ITHDmdeaiLADKVIVFSEGKLIAQGKPKE 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-251 |
3.57e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 140.61 E-value: 3.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYD 80
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF-----EGKVKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLL 160
Cdd:PRK13642 79 LRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 161 PGIMVLDEPSSNLDMAAIDDLRQVLSLWK-KQGKTILIAEHRLYYLHDlADRVLYVKDGEIEREYTPAEFDSLSDGTrKE 239
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDM-VE 236
|
250
....*....|...
gi 933767453 240 IGLR-PFSLSKLK 251
Cdd:PRK13642 237 IGLDvPFSSNLMK 249
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
264-468 |
3.99e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 138.64 E-value: 3.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPES--LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGK---TLDWKA----R 333
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRpTSGEVLIDGQdisSLSERElarlR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 334 LKHCYMVMQdtSHQLFTE-SVADEVLLSM------DNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSN 406
Cdd:COG1136 85 RRHIGFVFQ--FFNLLPElTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 407 REIIVFDEPTSGLDLKHMREVARSLKSLADQ-GKTLLVITHDPELvMAGCSYVVHMEKGQVKE 468
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPEL-AARADRVIRLRDGRIVS 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
264-465 |
4.13e-38 |
|
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: 136.74 E-value: 4.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCG---FLQVEGKTLDWKARLKHCYM 339
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLyDPTSGeilIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 VMQDTshQLFTESVADEVLlsmdnkdetvvdkilkqfdlleykdrhplslSGGQKQRVAIASAIVSNREIIVFDEPTSGL 419
Cdd:cd03228 81 VPQDP--FLFSGTIRENIL-------------------------------SGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 933767453 420 DLKHMREVARSLKSLAdQGKTLLVITHDPELVMAgCSYVVHMEKGQ 465
Cdd:cd03228 128 DPETEALILEALRALA-KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
265-466 |
8.70e-38 |
|
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: 137.62 E-value: 8.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPES--LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKT---LDWKA----RL 334
Cdd:cd03255 2 ELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRpTSGEVRVDGTDiskLSEKElaafRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 335 KHCYMVMQdtSHQLFTE-SVADEVLLSM------DNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNR 407
Cdd:cd03255 82 RHIGFVFQ--SFNLLPDlTALENVELPLllagvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 408 EIIVFDEPTSGLDLKHMREVARSLKSLADQ-GKTLLVITHDPELVMAgCSYVVHMEKGQV 466
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-242 |
2.97e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 138.26 E-value: 2.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEES--SGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSVSDT-- 76
Cdd:PRK13637 3 IKIENLTHIYMEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPT------SGKIIIDGVDITDKkv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLYDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVS----DYhiEDLMGRSVFALSGGEKQKIA 152
Cdd:PRK13637 77 KLSDIRKKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNivglDY--EDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLDMAAIDD-LRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE-FD 230
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEiLNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREvFK 234
|
250
....*....|..
gi 933767453 231 SLSdgTRKEIGL 242
Cdd:PRK13637 235 EVE--TLESIGL 244
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-219 |
8.42e-37 |
|
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: 133.28 E-value: 8.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV-LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-----SGEILIDGVDLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFFNvDTdseLAfacENLgypqedilkridrtvsdyhiedlmgrsvfaLSGGEKQKIACAssSVLL- 160
Cdd:cd03228 75 RKNIAYVPQDP--FLFS-GT---IR---ENI------------------------------LSGGQRQRIAIA--RALLr 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 161 -PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKqGKTILIAEHRLYYLhDLADRVLYVKDGE 219
Cdd:cd03228 114 dPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
264-466 |
2.06e-36 |
|
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: 133.80 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKK---REPESLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKARLKHCY 338
Cdd:cd03259 1 LELKGLSKTYGSvraLDDLSLTVEP-----GEFLALLGPSGCGKTTLLRLIAGLERpDSGEILIDGRDVtGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 MVMQDTShqLFTE-SVADEVLLSMDNKD------ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIV 411
Cdd:cd03259 76 MVFQDYA--LFPHlTVAENIAFGLKLRGvpkaeiRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 412 FDEPTSGLDLKhMREVARS-LKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03259 154 LDEPLSALDAK-LREELREeLKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
264-468 |
3.52e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.14 E-value: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLD----WKARlKHCY 338
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLlLPEAGTITVGGMVLSeetvWDVR-RQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 MVMQDTSHQLFTESVADEVLLSMDN----KDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVF 412
Cdd:PRK13635 85 MVFQNPDNQFVGATVQDDVAFGLENigvpREEMVerVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 413 DEPTSGLDLKHMREVARSLKSLADQGK-TLLVITHDPELVmAGCSYVVHMEKGQVKE 468
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEA-AQADRVIVMNKGEILE 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
265-474 |
3.95e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 133.65 E-value: 3.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTL-----DWKARLkhCY 338
Cdd:COG1131 2 EVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtSGEVRVLGEDVardpaEVRRRI--GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 MVMQDTSHQLFTesvADEVLLSM-------DNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIV 411
Cdd:COG1131 78 VPQEPALYPDLT---VRENLRFFarlyglpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 412 FDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-221 |
4.18e-36 |
|
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: 133.03 E-value: 4.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEEssgGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03259 1 LELKGLSKTYGSV---RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER-----PDSGEILIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AamVGSVFQNP-----KSQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASS 156
Cdd:cd03259 73 N--IGMVFQDYalfphLTVAENI------AFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAAIDDLR-QVLSLWKKQGKTIliaehrLYYLHD------LADRVLYVKDGEIE 221
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELReELKELQRELGITT------IYVTHDqeealaLADRIAVMNEGRIV 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-228 |
4.61e-36 |
|
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: 134.02 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyegkLEGDVLLDGKSVSDTPLYD 80
Cdd:COG1120 1 MLEAENLSVGYGGRPV---LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP-----SSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNPKSQF-FNVdtdSELAFacenLG-YP---------QEDIlKRIDRTVSDYHIEDLMGRSVFALSGGEKQ 149
Cdd:COG1120 73 LARRIAYVPQEPPAPFgLTV---RELVA----LGrYPhlglfgrpsAEDR-EAVEEALERTGLEHLADRPVDELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 150 K--IACAsssvlL---PGIMVLDEPSSNLDMA-AIDDLRQVLSLWKKQGKTILIAehrlyyLHDL------ADRVLYVKD 217
Cdd:COG1120 145 RvlIARA-----LaqePPLLLLDEPTSHLDLAhQLEVLELLRRLARERGRTVVMV------LHDLnlaaryADRLVLLKD 213
|
250
....*....|.
gi 933767453 218 GEIEREYTPAE 228
Cdd:COG1120 214 GRIVAQGPPEE 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-469 |
6.77e-36 |
|
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: 139.82 E-value: 6.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 21 RNVNLTINTGEFVLLTGESGCGKTtITRL-VNGLVPhYYEGKLEGDVLLDGKSVSDTPLYDLAAM----VGSVFQ----- 90
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKS-VTALsILRLLP-DPAAHPSGSILFDGQDLLGLSERELRRIrgnrIAMIFQepmts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 91 -NPksqFFNVDTdsELAfacENL----GYPQEDILKRI----DRTvsdyHI---EDLMGRSVFALSGGEKQKI----ACA 154
Cdd:COG4172 105 lNP---LHTIGK--QIA---EVLrlhrGLSGAAARARAlellERV----GIpdpERRLDAYPHQLSGGQRQRVmiamALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 155 SSsvllPGIMVLDEPSSNLDM---AAIDDLrqVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI-EREYTPAEFD 230
Cdd:COG4172 173 NE----PDLLIADEPTTALDVtvqAQILDL--LKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIvEQGPTAELFA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 231 SLSDG-TRKEIGLRPfslSKLKPANQYQAHTAkqMEFQNFCFAYK------KREPEslHIP-----SAELPVGETIAIIG 298
Cdd:COG4172 247 APQHPyTRKLLAAEP---RGDPRPVPPDAPPL--LEARDLKVWFPikrglfRRTVG--HVKavdgvSLTLRRGETLGLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 299 LNGAGKSTLARCICGLEKKCGFLQVEGK---TLDWKARL---KHCYMVMQD---------TSHQLFTES-VADEVLLSMD 362
Cdd:COG4172 320 ESGSGKSTLGLALLRLIPSEGEIRFDGQdldGLSRRALRplrRRMQVVFQDpfgslsprmTVGQIIAEGlRVHGPGLSAA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 363 NKDETVVDkILKQFDLL-EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDlkhmrevaRS--------LKS 433
Cdd:COG4172 400 ERRARVAE-ALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD--------VSvqaqildlLRD 470
|
490 500 510
....*....|....*....|....*....|....*..
gi 933767453 434 L-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKES 469
Cdd:COG4172 471 LqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQ 507
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
265-482 |
8.67e-36 |
|
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: 133.06 E-value: 8.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTL--DWKARLKH-CYMV 340
Cdd:COG4555 3 EVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPdSGSILIDGEDVrkEPREARRQiGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTSHQLFTesvADEVLL-------SMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFD 413
Cdd:COG4555 81 DERGLYDRLT---VRENIRyfaelygLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 414 EPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDESGSKKVLD 482
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
277-450 |
1.46e-35 |
|
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: 130.62 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 277 EPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTLDWK-----ARLKHCYMVMQDTSHQLFT 350
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQSGAVLIDGEPLDYSrkgllERRQRVGLVFQDPDDQLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 351 ESVADEV---LLSMDNKDETV---VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHM 424
Cdd:TIGR01166 84 ADVDQDVafgPLNLGLSEAEVerrVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|....*.
gi 933767453 425 REVARSLKSLADQGKTLLVITHDPEL 450
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-229 |
6.38e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 130.57 E-value: 6.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESsggGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLyDL 81
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT-----SGEVRVLGEDVARDPA-EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksqffNVDTD---SE-LAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQK--IACAs 155
Cdd:COG1131 72 RRRIGYVPQEP-----ALYPDltvREnLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRlgLALA- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 156 ssvLL--PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEF 229
Cdd:COG1131 146 ---LLhdPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-222 |
9.52e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.40 E-value: 9.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNG-LVPhyyegkLEGDVLLDGKSVSDTPLY 79
Cdd:COG2884 1 MIRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERP------TSGQVLVNGQDLSRLKRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAM---VGSVFQNPK-----SQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKI 151
Cdd:COG2884 73 EIPYLrrrIGVVFQDFRllpdrTVYENV------ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 152 ACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIER 222
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
285-468 |
9.63e-35 |
|
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: 129.55 E-value: 9.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTL------DWKARLKHCYMVMQDTSHQL-FTESVAD- 355
Cdd:cd03257 25 SFSIKKGETLGLVGESGSGKSTLARAILGLLKPtSGSIIFDGKDLlklsrrLRKIRRKEIQMVFQDPMSSLnPRMTIGEq 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 356 --EVLLS--MDNKDE---TVVDKILKQFDLLE-YKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREV 427
Cdd:cd03257 105 iaEPLRIhgKLSKKEarkEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933767453 428 ARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:cd03257 185 LDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-220 |
1.78e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESsggGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDL 81
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFF--NVDTDSELAFACENLGYPQEDI---LKRIDRTvsdyhiEDLMGRSVFALSGGEKQKIACASS 156
Cdd:COG4619 73 RRQVAYVPQEP--ALWggTVRDNLPFPFQLRERKFDRERAlelLERLGLP------PDILDKPVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 157 SVLLPGIMVLDEPSSNLD---MAAIDDLrqVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDpenTRRVEEL--LREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-246 |
2.04e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 130.24 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyegkLE---GDVLLDGKSVSDTP 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--------LEaesGQIIIDGDLLTEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSS 157
Cdd:PRK13650 76 VWDIRHKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 158 VLLPGIMVLDEPSSNLDMAAIDDL-RQVLSLWKKQGKTILIAEHRLYYLHdLADRVLYVKDGEIEREYTPAEFDSLSDGT 236
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELiKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
250
....*....|.
gi 933767453 237 rKEIGL-RPFS 246
Cdd:PRK13650 235 -LQLGLdIPFT 244
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
264-465 |
2.10e-34 |
|
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: 127.30 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKRE---PESLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDWKARL----- 334
Cdd:cd03229 1 LELKNVSKRYGQKTvlnDVSLNIEA-----GEIVALLGPSGSGKSTLLRCIAGLEEPDsGSILIDGEDLTDLEDElpplr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 335 KHCYMVMQDtsHQLFTesvadevllSMdnkdeTVVDKILkqfdlleykdrhpLSLSGGQKQRVAIASAIVSNREIIVFDE 414
Cdd:cd03229 76 RRIGMVFQD--FALFP---------HL-----TVLENIA-------------LGLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 933767453 415 PTSGLDLKHMREVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQ 465
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-228 |
2.10e-34 |
|
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: 136.89 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDL 81
Cdd:COG2274 474 IELENVSFRYPGDSPPV-LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT-----SGRILIDGIDLRQIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFFNvDTDSE-LAFACENLgyPQEDILKRIDRT-VSDYhIEDL----------MGRSvfaLSGGEKQ 149
Cdd:COG2274 548 RRQIGVVLQDV--FLFS-GTIREnITLGDPDA--TDEEIIEAARLAgLHDF-IEALpmgydtvvgeGGSN---LSGGQRQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 150 KIACASSsvLL--PGIMVLDEPSSNLD-------MAAIDDLRqvlslwkkQGKTILIAEHRLYYLhDLADRVLYVKDGEI 220
Cdd:COG2274 619 RLAIARA--LLrnPRILILDEATSALDaeteaiiLENLRRLL--------KGRTVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
....*...
gi 933767453 221 EREYTPAE 228
Cdd:COG2274 688 VEDGTHEE 695
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
291-469 |
4.44e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 128.19 E-value: 4.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-----DWKARLKHCYMVMQdtSHQLFTE-SVADEVLLS--- 360
Cdd:COG1126 27 GEVVVIIGPSGSGKSTLLRCINLLEEpDSGTITVDGEDLtdskkDINKLRRKVGMVFQ--QFNLFPHlTVLENVTLApik 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 ---MDNKD-ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAD 436
Cdd:COG1126 105 vkkMSKAEaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAK 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 933767453 437 QGKTLLVITHDpelvMA----GCSYVVHMEKGQVKES 469
Cdd:COG1126 185 EGMTMVVVTHE----MGfareVADRVVFMDGGRIVEE 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-220 |
4.51e-34 |
|
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: 126.99 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 6 NVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKsvsDTPLYDLAAMV 85
Cdd:cd03226 4 NISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES-----SGSILLNGK---PIKAKERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 86 GSVFQNPKSQFFNVDTDSELAFACENLGYPQEDIlkridRTV-SDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIM 164
Cdd:cd03226 74 GYVMQDVDYQLFTDSVREELLLGLKELDAGNEQA-----ETVlKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 165 VLDEPSSNLD---MAAIDDLrqVLSLwKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:cd03226 149 IFDEPTSGLDyknMERVGEL--IREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-242 |
6.64e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 129.05 E-value: 6.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGG---GIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL-VPHyyegklEGDVLLDGKSVSDT 76
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlIPS------EGKVYVDGLDTSDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 P-LYDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACAS 155
Cdd:PRK13633 78 EnLWDIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 156 SSVLLPGIMVLDEPSSNLD-------MAAIDDLRqvlslwKKQGKTILIAEHrlyYLHDL--ADRVLYVKDGEIEREYTP 226
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDpsgrrevVNTIKELN------KKYGITIILITH---YMEEAveADRIIVMDSGKVVMEGTP 228
|
250
....*....|....*..
gi 933767453 227 AE-FDSLSdgTRKEIGL 242
Cdd:PRK13633 229 KEiFKEVE--MMKKIGL 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
265-468 |
2.59e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.55 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPE----SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLdwkARLKH--- 336
Cdd:COG2884 3 RFENVSKRYPGGREAlsdvSLEIEK-----GEFVFLTGPSGAGKSTLLKLLYGEERpTSGQVLVNGQDL---SRLKRrei 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 337 CY------MVMQDtsHQLFTE-SVADEVLLSM------DNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAI 403
Cdd:COG2884 75 PYlrrrigVVFQD--FRLLPDrTVYENVALPLrvtgksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 404 VSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-200 |
2.67e-33 |
|
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: 124.46 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSV--SDTPLYDLAAMVGSVFQNPKSQF 96
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLrPQ------SGAVLIDGEPLdySRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 97 FNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMA 176
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....
gi 933767453 177 AIDDLRQVLSLWKKQGKTILIAEH 200
Cdd:TIGR01166 162 GREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
291-466 |
2.94e-33 |
|
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: 125.33 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDWKARL-----KHCYMVMQdtSHQLFTE-SVADEVLLS--- 360
Cdd:cd03262 26 GEVVVIIGPSGSGKSTLLRCINLLEEpDSGTIIIDGLKLTDDKKNinelrQKVGMVFQ--QFNLFPHlTVLENITLApik 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 ---MDNKD-ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAD 436
Cdd:cd03262 104 vkgMSKAEaEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAE 183
|
170 180 190
....*....|....*....|....*....|
gi 933767453 437 QGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03262 184 EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-228 |
3.05e-33 |
|
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: 132.57 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEEssGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDL 81
Cdd:COG4988 337 IELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFFNvDTdseLAfacENL--GYPQ---EDILKRIDRT-VSDYhIEDL-------MGRSVFALSGGEK 148
Cdd:COG4988 410 RRQIAWVPQNP--YLFA-GT---IR---ENLrlGRPDasdEELEAALEAAgLDEF-VAALpdgldtpLGEGGRGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 149 QKIACAssSVLL--PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKqGKTILIAEHRLyYLHDLADRVLYVKDGEIEREYTP 226
Cdd:COG4988 480 QRLALA--RALLrdAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTH 555
|
..
gi 933767453 227 AE 228
Cdd:COG4988 556 EE 557
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
280-466 |
3.47e-33 |
|
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: 126.80 E-value: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDWKARL------KHCYMVMQDTSHQLFTES 352
Cdd:TIGR04521 25 SLTIED-----GEFVAIIGHTGSGKSTLIQHLNGLLKPTsGTVTIDGRDITAKKKKklkdlrKKVGLVFQFPEHQLFEET 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 353 VADEV---LLSMDNKDETV---VDKILKQFDL-LEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMR 425
Cdd:TIGR04521 100 VYKDIafgPKNLGLSEEEAeerVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933767453 426 EVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:TIGR04521 180 EILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
265-466 |
3.71e-33 |
|
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: 123.48 E-value: 3.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEG---KTLDWKARLKHCYMV 340
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTsGRVRLDGadiSQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTshQLFTESVADEVLlsmdnkdetvvdkilkqfdlleykdrhplslSGGQKQRVAIASAIVSNREIIVFDEPTSGLD 420
Cdd:cd03246 82 PQDD--ELFSGSIAENIL-------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 933767453 421 LKHMREVARSLKSLADQGKTLLVITHDPELVmAGCSYVVHMEKGQV 466
Cdd:cd03246 129 VEGERALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-219 |
4.75e-33 |
|
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: 122.74 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 4 FQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDLAA 83
Cdd:cd00267 2 IENLSFRYGGRTA---LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 84 MVGSVFQnpksqffnvdtdselafacenlgypqedilkridrtvsdyhiedlmgrsvfaLSGGEKQKIACASSSVLLPGI 163
Cdd:cd00267 74 RIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 164 MVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGE 219
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
265-469 |
5.45e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.83 E-value: 5.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPE----SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGlekkcgFLQVEG----------KTLDW 330
Cdd:COG1132 341 EFENVSFSYPGDRPVlkdiSLTIPP-----GETVALVGPSGSGKSTLVNLLLR------FYDPTSgrilidgvdiRDLTL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 331 KARLKHCYMVMQDTshQLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQRVAI 399
Cdd:COG1132 410 ESLRRQIGVVPQDT--FLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 400 ASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELVMAgCSYVVHMEKGQVKES 469
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
265-466 |
6.64e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.16 E-value: 6.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLD----WKARLKHCYm 339
Cdd:COG4619 2 ELEGLSFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTsGEIYLDGKPLSamppPEWRRQVAY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 VMQDTshQLFTESVADEVLLSMDNK----DETVVDKILKQFDL-LEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDE 414
Cdd:COG4619 79 VPQEP--ALWGGTVRDNLPFPFQLRerkfDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 933767453 415 PTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG4619 157 PTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-219 |
7.58e-33 |
|
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: 123.07 E-value: 7.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03229 1 LELKNVSKRYGQKTV---LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE-----PDSGSILIDGEDLTDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAM--VGSVFQNPksqffnvdtdselafaceNLgYPQEDILKRIdrtvsdyhiedlmgrsVFALSGGEKQKIACASSSVL 159
Cdd:cd03229 73 PLRrrIGMVFQDF------------------AL-FPHLTVLENI----------------ALGLSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 160 LPGIMVLDEPSSNLDMAAIDDLRQVL-SLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGE 219
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLkSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-228 |
7.94e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.88 E-value: 7.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTP--- 77
Cdd:COG3839 3 SLELENVSKSYGGVEA---LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL-----EDPTSGEILIGGRDVTDLPpkd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 -----------LYDlaAMvgSVFQNpksqffnvdtdseLAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGG 146
Cdd:COG3839 75 rniamvfqsyaLYP--HM--TVYEN-------------IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 147 EKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLS-LWKKQGKTIliaehrLYYLHD------LADRVLYVKDGE 219
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKrLHRRLGTTT------IYVTHDqveamtLADRIAVMNDGR 211
|
....*....
gi 933767453 220 IEREYTPAE 228
Cdd:COG3839 212 IQQVGTPEE 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
280-474 |
9.08e-33 |
|
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: 124.62 E-value: 9.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDW-------KARlKHCYMVMQdtsH-QLFT 350
Cdd:cd03258 25 SLSVPK-----GEIFGIIGRSGAGKSTLIRCINGLERpTSGSVLVDGTDLTLlsgkelrKAR-RRIGMIFQ---HfNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 351 -ESVADEVLLSM------DNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKH 423
Cdd:cd03258 96 sRTVFENVALPLeiagvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 933767453 424 MREVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:cd03258 176 TQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
265-466 |
9.68e-33 |
|
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: 122.51 E-value: 9.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTL--DWKARLKHCYMVM 341
Cdd:cd03230 2 EVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdSGEIKVLGKDIkkEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 342 QDTShqLFtesvadevllsmdnKDETVvdkilkqfdlLEYkdrhpLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL 421
Cdd:cd03230 80 EEPS--LY--------------ENLTV----------REN-----LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 933767453 422 KHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03230 129 ESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-228 |
1.28e-32 |
|
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: 124.53 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGGGI-RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLY 79
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVlKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW-----SGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFQNPKSQF---FNVDTDSELAFACENLGypqeDILKRIDRTVSDYHI-EDLMGRSVFALSGGEKQKIACAS 155
Cdd:COG1124 76 AFRRRVQMVFQDPYASLhprHTVDRILAEPLRIHGLP----DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 156 SSVLLPGIMVLDEPSSNLDMA--AiddlrQVLSLWKKqgktiLIAEHRLYYL---HDLA------DRVLYVKDGEIEREY 224
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSvqA-----EILNLLKD-----LREERGLTYLfvsHDLAvvahlcDRVAVMQNGRIVEEL 221
|
....
gi 933767453 225 TPAE 228
Cdd:COG1124 222 TVAD 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
2.40e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 124.42 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyYEGKlEGDVLLDGKSV--SDTPL 78
Cdd:PRK13639 1 ILETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGI----LKPT-SGEVLIKGEPIkyDKKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSV 158
Cdd:PRK13639 74 LEVRKTVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 159 LLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFDSLSDGTRK 238
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRK 233
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-228 |
2.92e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.90 E-value: 2.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESsgGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDL 81
Cdd:COG1132 340 IEFENVSFSYPGDR--PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-----SGRILIDGVDIRDLTLESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFFNvDTdseLAfacENLGY-----PQEDILK-----RIDRTVS------DYHIEDlmgRSVfALSG 145
Cdd:COG1132 413 RRQIGVVPQDT--FLFS-GT---IR---ENIRYgrpdaTDEEVEEaakaaQAHEFIEalpdgyDTVVGE---RGV-NLSG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 146 GEKQKIACAssSVLL--PGIMVLDEPSSNLD-------MAAIDDLRqvlslwkkQGKT-ILIAeHRLYYLHDlADRVLYV 215
Cdd:COG1132 480 GQRQRIAIA--RALLkdPPILILDEATSALDtetealiQEALERLM--------KGRTtIVIA-HRLSTIRN-ADRILVL 547
|
250
....*....|...
gi 933767453 216 KDGEIEREYTPAE 228
Cdd:COG1132 548 DDGRIVEQGTHEE 560
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
265-465 |
2.97e-32 |
|
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: 122.36 E-value: 2.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKkREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLdwkARLKHCYM---- 339
Cdd:TIGR02673 3 EFHNVSKAYP-GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSrGQVRIAGEDV---NRLRGRQLpllr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 -----VMQDtSHQLFTESVADEVLLSM--DNKDETV----VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNRE 408
Cdd:TIGR02673 79 rrigvVFQD-FRLLPDRTVYENVALPLevRGKKEREiqrrVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 409 IIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQ 465
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-228 |
5.29e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 125.60 E-value: 5.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSVSDTPLY 79
Cdd:COG3842 5 ALELENVSKRYGDVTA---LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFEtPD------SGRILLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DlaAMVGSVFQNPksQFF-------NVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIA 152
Cdd:COG3842 76 K--RNVGMVFQDY--ALFphltvaeNV------AFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVL-SLWKKQGKTILIAEhrlyylHD------LADRVLYVKDGEIEREYT 225
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELrRLQRELGITFIYVT------HDqeealaLADRIAVMNDGRIEQVGT 219
|
...
gi 933767453 226 PAE 228
Cdd:COG3842 220 PEE 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-223 |
5.67e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.07 E-value: 5.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGeesSGGG----IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL-VPHyyegklEGDVLLDGKSVSD 75
Cdd:COG1136 4 LLELRNLTKSYG---TGEGevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPT------SGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 76 TPLYDLAAM----VGSVFqnpksQFFN-VDTDSelafACENL-------GYPQEDILKRIDRTVSDYHIEDLMGRSVFAL 143
Cdd:COG1136 75 LSERELARLrrrhIGFVF-----QFFNlLPELT----ALENValplllaGVSRKERRERARELLERVGLGDRLDHRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 144 SGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVL-SLWKKQGKTILIAEH--RLYylhDLADRVLYVKDGEI 220
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLrELNRELGTTIVMVTHdpELA---ARADRVIRLRDGRI 222
|
...
gi 933767453 221 ERE 223
Cdd:COG1136 223 VSD 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-220 |
1.12e-31 |
|
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: 119.85 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAM 84
Cdd:cd03214 3 ENLSVGYGGRTV---LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK-----PSSGEILLDGKDLASLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 85 VGSVFQnpksqffnvdtdselafACENLGypqedilkridrtvsdyhIEDLMGRSVFALSGGEKQKIACASSSVLLPGIM 164
Cdd:cd03214 75 IAYVPQ-----------------ALELLG------------------LAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 165 VLDEPSSNLDMA-AIDDLRQVLSLWKKQGKTILIAehrlyyLHDL------ADRVLYVKDGEI 220
Cdd:cd03214 120 LLDEPTSHLDIAhQIELLELLRRLARERGKTVVMV------LHDLnlaaryADRVILLKDGRI 176
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
265-468 |
1.17e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 121.66 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLE-KKCGFLQVEGKTLDWKARLKH------- 336
Cdd:COG4161 4 QLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLEtPDSGQLNIAGHQFDFSQKPSEkairllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 337 --CYMVMQD-------TSHQLFTEsvADEVLLSMdNKDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVS 405
Cdd:COG4161 82 qkVGMVFQQynlwphlTVMENLIE--APCKVLGL-SKEQARekAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 406 NREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-221 |
1.42e-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: 120.44 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03301 1 VELENVTKRFGNVTA---LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-----EEPTSGRIYIGGRDVTDLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 -AAMVgsvFQN----P-KSQFFNvdtdseLAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACAS 155
Cdd:cd03301 73 dIAMV---FQNyalyPhMTVYDN------IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 156 SSVLLPGIMVLDEPSSNLDMAAIDDLRQVLS-LWKKQGKTIliaehrLYYLHD------LADRVLYVKDGEIE 221
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKrLQQRLGTTT------IYVTHDqveamtMADRIAVMNDGQIQ 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-466 |
1.47e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.67 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 21 RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVS-DTPLYDLAAMVGSVFQ--------- 90
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD-----SGEILLDGEPVRfRSPRDAQAAGIAIIHQelnlvpnls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 91 --------NPKSQFFNVDTDSELAFAcenlgypqEDILKRI------DRTVSDyhiedlmgrsvfaLSGGEKQKIACASS 156
Cdd:COG1129 96 vaeniflgREPRRGGLIDWRAMRRRA--------RELLARLgldidpDTPVGD-------------LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAAIDDL-RQVLSLwKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFdslsdg 235
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLfRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 236 TRKEI-----GlRPFSlsklkpaNQYQAHTAKQ----MEFQNFCFaykkrePESLHIPSAELPVGETIAIIGLNGAGKST 306
Cdd:COG1129 228 TEDELvrlmvG-RELE-------DLFPKRAAAPgevvLEVEGLSV------GGVVRDVSFSVRAGEILGIAGLVGAGRTE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 307 LARCICGLEKK-CGFLQVEGKTLDWK---ARLKH--CYmVMQDTSHQ-LFTE-SVADEVLLS----------MDNKDET- 367
Cdd:COG1129 294 LARALFGADPAdSGEIRLDGKPVRIRsprDAIRAgiAY-VPEDRKGEgLVLDlSIRENITLAsldrlsrgglLDRRRERa 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 368 VVDKILKQFDLleyKDRHP----LSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLV 443
Cdd:COG1129 373 LAEEYIKRLRI---KTPSPeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIV 449
|
490 500
....*....|....*....|...
gi 933767453 444 ITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG1129 450 ISSELPELLGLSDRILVMREGRI 472
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
1.63e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.74 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGeeSSGGG---IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTP 77
Cdd:COG1116 7 ALELRGVSKRFP--TGGGGvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT-----SGEVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 lydlaAMVGSVFQNP-----KSQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIA 152
Cdd:COG1116 80 -----PDRGVVFQEPallpwLTVLDNV------ALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLDMAAIDDLRQ-VLSLWKKQGKTILIAEhrlyylHD------LADRVL 213
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDeLLRLWQETGKTVLFVT------HDvdeavfLADRVV 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
285-474 |
2.19e-31 |
|
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: 120.68 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKtlDW----KARL----KHCYMVMQDTShqLFTE-SVA 354
Cdd:cd03261 20 DLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPdSGEVLIDGE--DIsglsEAELyrlrRRMGMLFQSGA--LFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEV---LLSMDNKDETVVDKI----LKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREV 427
Cdd:cd03261 96 ENVafpLREHTRLSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 933767453 428 ARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:cd03261 176 DDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-228 |
3.00e-31 |
|
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: 120.42 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGeesSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGlvphyYEGKLEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-----FETPTSGEILLDGKDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AamVGSVFQNpKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLP 161
Cdd:cd03300 73 P--VNTVFQN-YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 162 GIMVLDEPSSNLDMAAIDDLRQVLS-LWKKQGKTIliaehrLYYLHD------LADRVLYVKDGEIEREYTPAE 228
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKrLQKELGITF------VFVTHDqeealtMSDRIAVMNKGKIQQIGTPEE 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-219 |
3.35e-31 |
|
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: 119.66 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGeessGG--GIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGlvphyYEGKLEGDVLLDGKSVSDTPL 78
Cdd:TIGR02673 1 MIEFHNVSKAYP----GGvaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYG-----ALTPSRGQVRIAGEDVNRLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAM---VGSVFQNPK-----SQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQK 150
Cdd:TIGR02673 72 RQLPLLrrrIGVVFQDFRllpdrTVYENV------ALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 151 IACASSSVLLPGIMVLDEPSSNLDmaaiDDL-RQVLSLWK---KQGKTILIAEHRLYYLHDLADRVLYVKDGE 219
Cdd:TIGR02673 146 VAIARAIVNSPPLLLADEPTGNLD----PDLsERILDLLKrlnKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-229 |
3.87e-31 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 120.48 E-value: 3.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyegkLEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03295 1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP-----TSGEIFIDGEDIREQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQN----PK---SQffNVDTDSELafacenLGYPQEDILKRIDRTVSDYHIED--LMGRSVFALSGGEKQKIA 152
Cdd:cd03295 74 RRKIGYVIQQiglfPHmtvEE--NIALVPKL------LKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLDMAAIDDL-RQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEF 229
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLqEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
260-469 |
5.49e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.99 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 260 TAKQMEFQNFCFAYKK-REPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLD----WKAR 333
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLlEAESGQIIIDGDLLTeenvWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 334 lKHCYMVMQDTSHQLFTESVADEVLLSMDNK----DETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNR 407
Cdd:PRK13650 81 -HKIGMVFQNPDNQFVGATVEDDVAFGLENKgiphEEMKerVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 408 EIIVFDEPTSGLDLKHMREVARSLKSLADQ-GKTLLVITHDPELVmAGCSYVVHMEKGQVKES 469
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVEST 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
280-484 |
6.23e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 122.11 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGK---TLD----WKARlKHCYMVMQdtsH-QLFT 350
Cdd:COG1135 25 SLTIEK-----GEIFGIIGYSGAGKSTLIRCINLLERpTSGSVLVDGVdltALSerelRAAR-RKIGMIFQ---HfNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 351 E-SVADEVLLSMD----NKDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKH 423
Cdd:COG1135 96 SrTVAENVALPLEiagvPKAEIRkrVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 424 MREVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQVKesypldESGSkkVLDFF 484
Cdd:COG1135 176 TRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIV------EQGP--VLDVF 229
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
280-466 |
6.48e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 119.78 E-value: 6.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGK---TLDWKARLKH---CYMVMQDtsHQLFTE- 351
Cdd:COG3638 23 SLEIER-----GEFVALIGPSGAGKSTLLRCLNGLVEpTSGEILVDGQdvtALRGRALRRLrrrIGMIFQQ--FNLVPRl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 352 SVADEVL-------------LSMDNKDETV-VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTS 417
Cdd:COG3638 96 SVLTNVLagrlgrtstwrslLGLFPPEDRErALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 933767453 418 GLDLKHMREVARSLKSLA-DQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG3638 176 SLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
252-469 |
8.36e-31 |
|
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: 125.26 E-value: 8.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 252 PANQYQAHTAKQMEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEG---KT 327
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRfLDPQSGSITLGGvdlRD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 328 LDWKARLKHCYMVMQDTsHqLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQR 396
Cdd:COG4987 402 LDEDDLRRRIAVVPQRP-H-LFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 397 VAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELvMAGCSYVVHMEKGQVKES 469
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAG-LERMDRILVLEDGRIVEQ 550
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-466 |
8.73e-31 |
|
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: 124.91 E-value: 8.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL------------------------VPHYY-------EGKLEGDVLl 68
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvalcekcgyveRPSKVgepcpvcGGTLEPEEV- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 69 DGKSVSDTPLYDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEK 148
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 149 QKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVL-SLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPA 227
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 228 E--------FDSLSDGTRKEIG---LRPFSLSKlkpaNQYQAHTAKQMEFQNFCFAYKKrepeslhipsaelpvGETIAI 296
Cdd:TIGR03269 255 EvvavfmegVSEVEKECEVEVGepiIKVRNVSK----RYISVDRGVVKAVDNVSLEVKE---------------GEIFGI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 297 IGLNGAGKSTLARCICG-LEKKCGFLQVE---------GKTLDWKARLKHcYMVMQDTSHQLFTESVADEVL---LSMDN 363
Cdd:TIGR03269 316 VGTSGAGKTTLSKIIAGvLEPTSGEVNVRvgdewvdmtKPGPDGRGRAKR-YIGILHQEYDLYPHRTVLDNLteaIGLEL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 KDETVVDK---ILKQFDLLEYK-----DRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARS-LKSL 434
Cdd:TIGR03269 395 PDELARMKaviTLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSiLKAR 474
|
490 500 510
....*....|....*....|....*....|..
gi 933767453 435 ADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:TIGR03269 475 EEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-220 |
1.58e-30 |
|
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: 116.34 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGeesSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPlydl 81
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-----PDSGEIKVLGKDIKKEP---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 aamvgsvfqnpksqffnvdtdselAFACENLGY-PQEDILkridrtvsdyhIEDLMGRSVFALSGGEKQKIACASSSVLL 160
Cdd:cd03230 69 ------------------------EEVKRRIGYlPEEPSL-----------YENLTVRENLKLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 161 PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-220 |
1.90e-30 |
|
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: 117.59 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGeessGGG-----IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL-VPHyyegklEGDVLLDGKSVSD 75
Cdd:cd03255 1 IELKNLSKTYG----GGGekvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPT------SGEVRVDGTDISK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 76 TPLYDLAAM----VGSVFQNPK-----SQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGG 146
Cdd:cd03255 71 LSEKELAAFrrrhIGFVFQSFNllpdlTALENV------ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 147 EKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVL-SLWKKQGKTILIAEHRLyYLHDLADRVLYVKDGEI 220
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-230 |
1.93e-30 |
|
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: 117.99 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSV---SDTPL 78
Cdd:cd03261 1 IELRGLTKSFGGRTV---LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR-----PDSGEVLIDGEDIsglSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVGSVFQNP-----KSQFFNVdtdselAFAC-ENLGYPQEDILKRID---RTVSDYHIEDLMGRSvfaLSGGEKQ 149
Cdd:cd03261 73 YRLRRRMGMLFQSGalfdsLTVFENV------AFPLrEHTRLSEEEIREIVLeklEAVGLRGAEDLYPAE---LSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 150 KIACASSSVLLPGIMVLDEPSSNLD---MAAIDDLrqVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTP 226
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDpiaSGVIDDL--IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
....
gi 933767453 227 AEFD 230
Cdd:cd03261 222 EELR 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-245 |
3.10e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 119.13 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYgEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNG-LVPHyyeGKLEGDVLLDGKSVSDTPLYD 80
Cdd:PRK13640 6 VEFKHVSFTY-PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPD---DNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLL 160
Cdd:PRK13640 82 IREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 161 PGIMVLDEPSSNLDMAAIDD-LRQVLSLWKKQGKTILIAEHRLYYLhDLADRVLYVKDGEIEREYTPAE-FDSLSdgTRK 238
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQiLKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEiFSKVE--MLK 238
|
....*...
gi 933767453 239 EIGLR-PF 245
Cdd:PRK13640 239 EIGLDiPF 246
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
285-484 |
7.17e-30 |
|
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: 116.62 E-value: 7.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGK---TLDWKARL---KHCYMVMQDTShqLFTE-SVADE 356
Cdd:COG1127 25 SLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpDSGEILVDGQditGLSEKELYelrRRIGMLFQGGA--LFDSlTVFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 357 VLLSMD---NKDETVVDKI----LKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVAR 429
Cdd:COG1127 103 VAFPLRehtDLSEAEIRELvlekLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 430 SLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE---SGSKKVLDFF 484
Cdd:COG1127 183 LIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEllaSDDPWVRQFL 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-213 |
8.31e-30 |
|
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: 116.03 E-value: 8.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGG-GIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPlyd 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT-----SGEVLVDGEPVTGPG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 laAMVGSVFQNP-----KSQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACAS 155
Cdd:cd03293 73 --PDRGYVFQQDallpwLTVLDNV------ALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 156 SSVLLPGIMVLDEPSSNLDMAAIDDLRQ-VLSLWKKQGKTI-LIAehrlyylHD------LADRVL 213
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEeLLDIWRETGKTVlLVT-------HDideavfLADRVV 203
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-228 |
2.05e-29 |
|
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: 115.02 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03254 3 IEFENVNFSYDEKKPV--LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-----KGQILIDGIDIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNP----KSQFFNVDTDSELAfacenlgyPQEDILKRIDRTVSDYHIEDL-------MGRSVFALSGGEKQK 150
Cdd:cd03254 76 RSMIGVVLQDTflfsGTIMENIRLGRPNA--------TDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 151 IACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQvlSLWK-KQGKTILIAEHRLYYLHDlADRVLYVKDGEIEREYTPAE 228
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTETEKLIQE--ALEKlMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDE 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
265-466 |
2.09e-29 |
|
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: 114.99 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEG---KTLDWKARLKHCYMV 340
Cdd:cd03245 4 EFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLDGtdiRQLDPADLRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTShqLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHPL-----------SLSGGQKQRVAIASAIVSNREI 409
Cdd:cd03245 84 PQDVT--LFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELvMAGCSYVVHMEKGQV 466
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSL-LDLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
264-473 |
2.47e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.00 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKcgflqVEGKTL---------DWKARL 334
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKV-----KSGEIFynnqaitddNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 335 KHCYMVMQDTSHQLFTESVADEVLLSMDN------KDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNRE 408
Cdd:PRK13648 83 KHIGIVFQNPDNQFVGSIVKYDVAFGLENhavpydEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 409 IIVFDEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDPELVMAGcSYVVHMEKGQV-KESYPLD 473
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAMEA-DHVIVMNKGTVyKEGTPTE 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
280-466 |
2.65e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 117.89 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKARLKHCYMVMQDtsHQLFTE-SVADE 356
Cdd:COG3842 25 SLSIEP-----GEFVALLGPSGCGKTTLLRMIAGFETpDSGRILLDGRDVtGLPPEKRNVGMVFQD--YALFPHlTVAEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 357 VL--LSMDNKDETV----VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLK---HMR-E 426
Cdd:COG3842 98 VAfgLRMRGVPKAEirarVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKlreEMReE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933767453 427 VARSLKSLadqGKTLLVITHDPE--LVMAGcsYVVHMEKGQV 466
Cdd:COG3842 178 LRRLQREL---GITFIYVTHDQEeaLALAD--RIAVMNDGRI 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
264-466 |
3.82e-29 |
|
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: 114.04 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLdwkARLK------- 335
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDV---SDLRgraipyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 336 --HCYMVMQDtSHQLFTESVADEVLLSM---DNKDETVVDKILKQFDLLEYKDRH---PLSLSGGQKQRVAIASAIVSNR 407
Cdd:cd03292 77 rrKIGVVFQD-FRLLPDRNVYENVAFALevtGVPPREIRKRVPAALELVGLSHKHralPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 408 EIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
265-466 |
4.62e-29 |
|
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: 121.13 E-value: 4.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEG---KTLDWKARLKHCYMV 340
Cdd:TIGR03375 465 EFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLyQPTEGSVLLDGvdiRQIDPADLRRNIGYV 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDtsHQLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQRVAIASAIVSNREI 409
Cdd:TIGR03375 545 PQD--PRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPI 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELvMAGCSYVVHMEKGQV 466
Cdd:TIGR03375 623 LLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSL-LDLVDRIIVMDNGRI 677
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-228 |
5.97e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 115.10 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSV--SDTP 77
Cdd:PRK13638 1 MLATSDLWFRYQDEPV---LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ------KGAVLWQGKPLdySKRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSS 157
Cdd:PRK13638 72 LLALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 158 VLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
262-471 |
1.06e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 114.42 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 262 KQMEFQNFCFAYKKR-EPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLD----WKARLK 335
Cdd:PRK13642 3 KILEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFEGKVKIDGELLTaenvWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 336 hCYMVMQDTSHQLFTESVADEVLLSMDN----KDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREI 409
Cdd:PRK13642 83 -IGMVFQNPDNQFVGATVEDDVAFGMENqgipREEMIkrVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLADQGK-TLLVITHDPELVmAGCSYVVHMEKGQ-VKESYP 471
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEA-ASSDRILVMKAGEiIKEAAP 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
281-417 |
1.30e-28 |
|
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: 110.43 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTL---DWKARLKHCYMVMQDtsHQLF-TESVAD 355
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPtEGTILLDGQDLtddERKSLRKEIGYVFQD--PQLFpRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 356 EVLLS------MDNKDETVVDKILKQFDLLEYKDRH----PLSLSGGQKQRVAIASAIVSNREIIVFDEPTS 417
Cdd:pfam00005 79 NLRLGlllkglSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
261-467 |
1.52e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.03 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 261 AKQMEFQNFCFAYKKREPESLHIP----SAELPVGETIAIIGLNGAGKSTLARCICGLekkcgFLQVEGK-------TLD 329
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEESTEKLAlddvNLEVKKGEFLVILGRNGSGKSTIAKHMNAL-----LIPSEGKvyvdgldTSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 330 ----WKARLKhCYMVMQDTSHQLFTESVADEVLLSMDN----KDE--TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAI 399
Cdd:PRK13633 77 eenlWDIRNK-AGMVFQNPDNQIVATIVEEDVAFGPENlgipPEEirERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 400 ASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ-GKTLLVITHDPELVmAGCSYVVHMEKGQVK 467
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKVV 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
277-474 |
1.59e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 113.53 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 277 EPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTL----DWKARLK------------HCYM 339
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSeGSIVVNGQTInlvrDKDGQLKvadknqlrllrtRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 VMQDT---SHQLFTESVAD---EVL-LSMDNKDETVVdKILKQFDLLEY-KDRHPLSLSGGQKQRVAIASAIVSNREIIV 411
Cdd:PRK10619 97 VFQHFnlwSHMTVLENVMEapiQVLgLSKQEARERAV-KYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 412 FDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-220 |
1.77e-28 |
|
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: 112.30 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYgEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyYEGKlEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03245 3 IEFRNVSFSY-PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL----YKPT-SGSVLLDGTDIRQLDPADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQnpksqffnvdtDSELAFAC--EN--LGYP---QEDILKRIDRT-VSDY-----HIEDLM-GRSVFALSGGE 147
Cdd:cd03245 77 RRNIGYVPQ-----------DVTLFYGTlrDNitLGAPladDERILRAAELAgVTDFvnkhpNGLDLQiGERGRGLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 148 KQKIACASSSVLLPGIMVLDEPSSNLDMAA----IDDLRQVLSlwkkqGKTILIAEHRLYYLhDLADRVLYVKDGEI 220
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSeerlKERLRQLLG-----DKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-228 |
2.28e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 113.69 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSY--GEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL-VPHyyegklEGDVLLDGKSVSDTP- 77
Cdd:PRK13649 3 INLQNVSYTYqaGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVPT------QGSVRVDDTLITSTSk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 ---LYDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHI-EDLMGRSVFALSGGEKQKIAC 153
Cdd:PRK13649 77 nkdIKQIRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 154 ASSSVLLPGIMVLDEPSSNLDMAAiddLRQVLSLWKK---QGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKG---RKELMTLFKKlhqSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
291-474 |
2.39e-28 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 112.97 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDWK-------------------ARLKhcyMVMQDT---SHQ 347
Cdd:COG4598 34 GDVISIIGSSGSGKSTFLRCINLLETPDsGEIRVGGEEIRLKpdrdgelvpadrrqlqrirTRLG---MVFQSFnlwSHM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 348 LFTESVAdEV---LLSMDnKDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLK 422
Cdd:COG4598 111 TVLENVI-EApvhVLGRP-KAEAIerAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933767453 423 HMREVARSLKSLADQGKTLLVITHdpELVMAG--CSYVVHMEKGQVKESYPLDE 474
Cdd:COG4598 189 LVGEVLKVMRDLAEEGRTMLVVTH--EMGFARdvSSHVVFLHQGRIEEQGPPAE 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
264-474 |
4.02e-28 |
|
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: 111.50 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGK-TLDWKARLKHCY---- 338
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEvLLDGKDIYDLDVdvle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 ------MVMQDTShqLFTESVADEV-----LLSMDNKDE--TVVDKILKQFDLLEY-KDR-HPLSLSGGQKQRVAIASAI 403
Cdd:cd03260 79 lrrrvgMVFQKPN--PFPGSIYDNVayglrLHGIKLKEEldERVEEALRKAALWDEvKDRlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 404 VSNREIIVFDEPTSGLDLKHMREVARSLKSLADQgKTLLVITHDPELVmAGCS-YVVHMEKGQVKESYPLDE 474
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQA-ARVAdRTAFLLNGRLVEFGPTEQ 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-228 |
4.35e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.95 E-value: 4.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSY--GEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYeGKLEGDVLLDGKSVSDTPLY 79
Cdd:PRK13646 3 IRFDNVSYTYqkGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTT-GTVTVDDITITHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIE-DLMGRSVFALSGGEKQKIACASSSV 158
Cdd:PRK13646 82 PVRKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 159 LLPGIMVLDEPSSNLDMAAiddLRQVLSLWKK----QGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQS---KRQVMRLLKSlqtdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
291-474 |
4.37e-28 |
|
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: 112.10 E-value: 4.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKC--GFLQVEGKTL------DWKARLKHCYMVMQDTSHQlfTESVADeVLLS-- 360
Cdd:COG1119 29 GEHWAILGPNGAGKSTLLSLITGDLPPTygNDVRLFGERRggedvwELRKRIGLVSPALQLRFPR--DETVLD-VVLSgf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 ---------MDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSL 431
Cdd:COG1119 106 fdsiglyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 933767453 432 KSLADQG-KTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:COG1119 186 DKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEE 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-247 |
6.08e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.15 E-value: 6.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTPLYD 80
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-----EKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLL 160
Cdd:PRK13648 81 LRKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 161 PGIMVLDEPSSNLDMAAIDDLrqvLSLWK--KQGKTILIaehrLYYLHDL-----ADRVLYVKDGEIEREYTPAE-FDSL 232
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNL---LDLVRkvKSEHNITI----ISITHDLseameADHVIVMNKGTVYKEGTPTEiFDHA 233
|
250
....*....|....*.
gi 933767453 233 SDGTrkEIGLR-PFSL 247
Cdd:PRK13648 234 EELT--RIGLDlPFPI 247
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
280-473 |
6.66e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 111.72 E-value: 6.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLdwKARLKHCYMVMQDtsHQLF---TesVAD 355
Cdd:COG1116 31 SLTVAA-----GEFVALVGPSGCGKSTLLRLIAGLEKPTsGEVLVDGKPV--TGPGPDRGVVFQE--PALLpwlT--VLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 356 EVLLSMDNKD------ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD--LK-HMRE 426
Cdd:COG1116 100 NVALGLELRGvpkaerRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDalTReRLQD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 933767453 427 VARSLksLADQGKTLLVITHDPE--LVMAgcSYVVHMEK--GQVKESYPLD 473
Cdd:COG1116 180 ELLRL--WQETGKTVLFVTHDVDeaVFLA--DRVVVLSArpGRIVEEIDVD 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
7.03e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.20 E-value: 7.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYgeESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYD 80
Cdd:PRK13652 3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK-----PTSGSVLIRGEPITKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLL 160
Cdd:PRK13652 76 VRKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 161 PGIMVLDEPSSNLDMAAIDDL-RQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELiDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-228 |
8.53e-28 |
|
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: 110.78 E-value: 8.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTitrLVNgLVPHYYEGKlEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV-LRDISLDIPAGETVALVGPSGSGKST---LVN-LIPRFYDVD-SGRILIDGHDVRDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFFNvDTDSE-LAFAceNLGYPQEDILKR---------IDRTVSDYH--IEDlmgRSVfALSGGEKQ 149
Cdd:cd03251 75 RRQIGLVSQDV--FLFN-DTVAEnIAYG--RPGATREEVEEAaraanahefIMELPEGYDtvIGE---RGV-KLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 150 KIACASSSVLLPGIMVLDEPSSNLD-------MAAIDDLrqvlslwkKQGKTILIAEHRLYYLHDlADRVLYVKDGEIER 222
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDteserlvQAALERL--------MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVE 216
|
....*.
gi 933767453 223 EYTPAE 228
Cdd:cd03251 217 RGTHEE 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
291-485 |
9.55e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.95 E-value: 9.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEG-KTLDWKA--RL--KHCYMVMQdtSHQLFTESVADEVLL----- 359
Cdd:PRK09493 27 GEVVVIIGPSGSGKSTLLRCINKLEEiTSGDLIVDGlKVNDPKVdeRLirQEAGMVFQ--QFYLFPHLTALENVMfgplr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 --SMDNKD-ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD--LKHmrEVARSLKSL 434
Cdd:PRK09493 105 vrGASKEEaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpeLRH--EVLKVMQDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 435 ADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYP----LDESGSKKVLDFFR 485
Cdd:PRK09493 183 AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDpqvlIKNPPSQRLQEFLQ 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-228 |
1.07e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.89 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTPLYDl 81
Cdd:PRK09452 15 VELRGISKSFDGKEV---ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-----ETPDSGRIMLDGQDITHVPAEN- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 aAMVGSVFQN----PK-SQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASS 156
Cdd:PRK09452 86 -RHVNTVFQSyalfPHmTVFENV------AFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 157 SVLLPGIMVLDEPSSNLDMaaidDLRQVL-----SLWKKQGKTIliaehrLYYLHD------LADRVLYVKDGEIEREYT 225
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDY----KLRKQMqnelkALQRKLGITF------VFVTHDqeealtMSDRIVVMRDGRIEQDGT 228
|
...
gi 933767453 226 PAE 228
Cdd:PRK09452 229 PRE 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
281-477 |
1.15e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 111.32 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTL------DWKARLKHCYMVMQDT-----SHQL 348
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSqGNVSWRGEPLaklnraQRKAFRRDIQMVFQDSisavnPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 349 FTESVADEV--LLSMDNKDETV-VDKILKQFDL-LEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHM 424
Cdd:PRK10419 108 VREIIREPLrhLLSLDKAERLArASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933767453 425 REVARSLKSLADQGKT-LLVITHDPELVMAGCSYVVHMEKGQVKESYPLDESGS 477
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.41e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.48 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSV--SDTPL 78
Cdd:PRK13636 5 ILKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK-----PSSGRILFDGKPIdySRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSV 158
Cdd:PRK13636 78 MKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 159 LLPGIMVLDEPSSNLDMAAIDDLRQ-VLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKlLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKE 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
285-466 |
1.64e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 110.59 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTL-DWKAR-LKHCYMVMQDTSHQLFTESVADEVLL-- 359
Cdd:COG4559 21 SLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLNGRPLaAWSPWeLARRRAVLPQHSSLAFPFTVEEVVALgr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 ----SMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAI------VSNREIIVF-DEPTSGLDLKHMREVA 428
Cdd:COG4559 101 aphgSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRWLFlDEPTSALDLAHQHAVL 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 933767453 429 RSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG4559 181 RLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
291-471 |
1.94e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.94 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTLDW------KARlKHCYMVMQDTSHQLFTESVADEVL----- 358
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGEPIKYdkksllEVR-KTVGIVFQNPDDQLFAPTVEEDVAfgpln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 --LSMDNKDETVVDKiLKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAD 436
Cdd:PRK13639 107 lgLSKEEVEKRVKEA-LKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 933767453 437 QGKTLLVITHDPELVMAGCSYVVHMEKGQ-VKESYP 471
Cdd:PRK13639 186 EGITIIISTHDVDLVPVYADKVYVMSDGKiIKEGTP 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
280-466 |
1.96e-27 |
|
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: 109.97 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLE---------KKCGFLQVEGKTLDwKARlKHCYMVMQDtsHQLFT 350
Cdd:cd03256 21 SLSINP-----GEFVALIGPSGAGKSTLLRCLNGLVeptsgsvliDGTDINKLKGKALR-QLR-RQIGMIFQQ--FNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 351 E-SVADEVLLSMDNKDETV---------VDK-----ILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEP 415
Cdd:cd03256 92 RlSVLENVLSGRLGRRSTWrslfglfpkEEKqralaALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 933767453 416 TSGLDLKHMREVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03256 172 VASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
261-461 |
2.04e-27 |
|
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: 115.08 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 261 AKQMEFQNFCFAYKKREPeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTL---DWKARLKH 336
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIAVNGVPLadaDADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 337 CYMVMQdtSHQLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYK-----------DRHPLSLSGGQKQRVAIASAIVS 405
Cdd:TIGR02857 398 IAWVPQ--HPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVaalpqgldtpiGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 406 NREIIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELvMAGCSYVVHM 461
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLAL-AALADRIVVL 529
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
280-466 |
2.12e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.55 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL--DWKARLKHCYMVMQDtsHQLF---TesV 353
Cdd:COG1118 22 SLEIAS-----GELVALLGPSGSGKTTLLRIIAGLETpDSGRIVLNGRDLftNLPPRERRVGFVFQH--YALFphmT--V 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 ADEVLLSMDNKD------ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL---KHM 424
Cdd:COG1118 93 AENIAFGLRVRPpskaeiRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKEL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933767453 425 REVARSLksLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG1118 173 RRWLRRL--HDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
279-468 |
2.41e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 109.72 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 279 ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLE-KKCGFLQVEGKTLDWKARL---------KHCYMVMQD----- 343
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEmPRSGTLNIAGNHFDFSKTPsdkairelrRNVGMVFQQynlwp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 344 --TSHQLFTEsvADEVLLSMDnKDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGL 419
Cdd:PRK11124 96 hlTVQQNLIE--APCRVLGLS-KDQALarAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 933767453 420 DLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:PRK11124 173 DPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-468 |
2.67e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 4 FQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLD-GKSVS----DTPL 78
Cdd:COG0488 1 LENLSKSFGGRPL---LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD-----SGEVSIPkGLRIGylpqEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDlaamVGSVFQNpksqFFNVDTD-----SELAFACENLGYPQEDILK------------------RIDRTVSDYHI-ED 134
Cdd:COG0488 73 DD----DLTVLDT----VLDGDAElraleAELEELEAKLAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFpEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 135 LMGRSVFALSGGEKQKIACASssVLL--PGIMVLDEPSSNLDMAAIDDLRQVLslwKKQGKTILIAEHRLYYLHDLADRV 212
Cdd:COG0488 145 DLDRPVSELSGGWRRRVALAR--ALLsePDLLLLDEPTNHLDLESIEWLEEFL---KNYPGTVLVVSHDRYFLDRVATRI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 213 LYVKDGEI---------------------EREYtpAEFDslsdgtrKEIG-----LRPFSlsklkpanqYQAHTAKQ--- 263
Cdd:COG0488 220 LELDRGKLtlypgnysayleqraerleqeAAAY--AKQQ-------KKIAkeeefIRRFR---------AKARKAKQaqs 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 -------MEFQnfcfAYKKREPE-SLHIPSAE----------------------------LPVGETIAIIGLNGAGKSTL 307
Cdd:COG0488 282 rikalekLERE----EPPRRDKTvEIRFPPPErlgkkvleleglsksygdktllddlslrIDRGDRIGLIGPNGAGKSTL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 308 ARCICGLEKkcgflQVEGkTLDWKARLKHCYMvmqDTSHQLF--TESVADEVLLSMDNKDETVVDKILKQFdLLEYKDRH 385
Cdd:COG0488 358 LKLLAGELE-----PDSG-TVKLGETVKIGYF---DQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLGRF-LFSGDDAF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 386 -PLS-LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLkHMREVarsLKS-LAD-QGkTLLVITHDPELVMAGCSYVVHM 461
Cdd:COG0488 428 kPVGvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI-ETLEA---LEEaLDDfPG-TVLLVSHDRYFLDRVATRILEF 502
|
....*..
gi 933767453 462 EKGQVKE 468
Cdd:COG0488 503 EDGGVRE 509
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
265-468 |
4.11e-27 |
|
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: 108.86 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEG---KTLDWKARLKHCYMV 340
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFyDVDSGRILIDGhdvRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTShqLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQRVAIASAIVSNREI 409
Cdd:cd03251 82 SQDVF--LFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELVMAGCSYVVhMEKGQVKE 468
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENADRIVV-LEDGKIVE 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
281-453 |
4.46e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.70 E-value: 4.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLekkcgfLQVEGKTLDWKARLKHCYMVMQDTSHQLFTESVADEVLLS 360
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGV------LRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 ----------MDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARS 430
Cdd:NF040873 82 rwarrglwrrLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161
|
170 180
....*....|....*....|...
gi 933767453 431 LKSLADQGKTLLVITHDPELVMA 453
Cdd:NF040873 162 LAEEHARGATVVVVTHDLELVRR 184
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
288-466 |
4.62e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.32 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 288 LPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTLDWKAR-----LKHCYMVMQDTSHQLFTESVADEVLLSM 361
Cdd:PRK13636 29 IKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKPIDYSRKglmklRESVGMVFQDPDNQLFSASVYQDVSFGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 362 DN----KDET--VVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLA 435
Cdd:PRK13636 109 VNlklpEDEVrkRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQ 188
|
170 180 190
....*....|....*....|....*....|..
gi 933767453 436 DQ-GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK13636 189 KElGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-468 |
4.83e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.03 E-value: 4.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYgeeSSGGGIR----NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEGKLEGDVLLDGKSVSDT 76
Cdd:PRK15134 5 LLAIENLSVAF---RQQQTVRtvvnDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLYDLAAMVGS----VFQNPKSQFFNVDT-DSELAfacENL----GYPQE----DILKRIDRT--------VSDY-Hied 134
Cdd:PRK15134 82 SEQTLRGVRGNkiamIFQEPMVSLNPLHTlEKQLY---EVLslhrGMRREaargEILNCLDRVgirqaakrLTDYpH--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 135 lmgrsvfALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAiddLRQVLSLWK--KQ--GKTILIAEHRLYYLHDLAD 210
Cdd:PRK15134 156 -------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSV---QAQILQLLRelQQelNMGLLFITHNLSIVRKLAD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 211 RVLYVKDGE-IEREYTPAEFDSLSDG-TRKEIGLRPFSLsklkpANQYQAHTAKQMEFQNFCFAYKKR---------EPE 279
Cdd:PRK15134 226 RVAVMQNGRcVEQNRAATLFSAPTHPyTQKLLNSEPSGD-----PVPLPEPASPLLDVEQLQVAFPIRkgilkrtvdHNV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGKTLD-WKAR----LKH-CYMVMQDTSH----QLF 349
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHnLNRRqllpVRHrIQVVFQDPNSslnpRLN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 350 TESVADEVL------LSMDNKDETVVdKILKQFDL-LEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLK 422
Cdd:PRK15134 381 VLQIIEEGLrvhqptLSAAQREQQVI-AVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 933767453 423 HMREVARSLKSLADQGK-TLLVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:PRK15134 460 VQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
285-466 |
4.99e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.48 E-value: 4.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTL-DWKAR-LKHCYMVMQDTSHQLFTESVADEVLL-- 359
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLNGRPLaDWSPAeLARRRAVLPQHSSLSFPFTVEEVVAMgr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 ----SMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIV-----SNREIIVF-DEPTSGLDLKHMREVAR 429
Cdd:PRK13548 102 aphgLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepDGPPRWLLlDEPTSALDLAHQHHVLR 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 933767453 430 SLKSLA-DQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK13548 182 LARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-218 |
9.59e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.05 E-value: 9.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphYYEGKleGDVLLDGKSVSDTPLYDL 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI---YLPQR--GRVKVMGREVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLP 161
Cdd:PRK13647 78 RSKVGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 162 GIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDG 218
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-230 |
9.88e-27 |
|
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: 108.14 E-value: 9.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESsgggI-RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLY 79
Cdd:COG1127 5 MIEVRNLTKSFGDRV----VlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR-----PDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAM---VGSVFQNP-----KSQFFNVdtdselAFAC-ENLGYPQEDILKRIDRTVSD---YHIEDLMGRSvfaLSGGE 147
Cdd:COG1127 76 ELYELrrrIGMLFQGGalfdsLTVFENV------AFPLrEHTDLSEAEIRELVLEKLELvglPGAADKMPSE---LSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 148 KQKIACASSSVLLPGIMVLDEPSSNLD---MAAIDDLrqVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREY 224
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDpitSAVIDEL--IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
....*.
gi 933767453 225 TPAEFD 230
Cdd:COG1127 225 TPEELL 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-228 |
1.14e-26 |
|
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: 107.63 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITrlvnGLVPHYYEgKLEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVV----SLLERFYD-PTSGEILLDGVDIRDLNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksqffnvdtdseLAFAC---ENLGYPQED-ILKRIDRTVSDYHIED-----------LMGRSVFALSGG 146
Cdd:cd03249 76 RSQIGLVSQEP------------VLFDGtiaENIRYGKPDaTDEEVEEAAKKANIHDfimslpdgydtLVGERGSQLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 147 EKQKIACASSSVLLPGIMVLDEPSSNLD-------MAAIDDLRqvlslwkkQGKTILIAEHRLYYLHDlADRVLYVKDGE 219
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDaeseklvQEALDRAM--------KGRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
....*....
gi 933767453 220 IEREYTPAE 228
Cdd:cd03249 215 VVEQGTHDE 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
285-474 |
1.30e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.53 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLarcicgLEKKCGFLQVEGKTLDWKAR-LKHCY-------MVMQDtsHQLFTE-SVAD 355
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTL------LNLIAGFLPPDSGRILWNGQdLTALPpaerpvsMLFQE--NNLFPHlTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 356 EVLLSMD-----NKDETV-VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD--LKH-M-- 424
Cdd:COG3840 91 NIGLGLRpglklTAEQRAqVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpaLRQeMld 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 933767453 425 --REVARslkslaDQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:COG3840 171 lvDELCR------ERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
281-474 |
1.45e-26 |
|
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: 107.13 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKCG---FLQ---VEGKTLDWKARLKHCYmVMQDtsHQLFTE-SV 353
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSgsiRFDgrdITGLPPHERARAGIGY-VPEG--RRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 ADEVLLSM----DNKDETVVDKILKQFDLLEYKdRHPL--SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREV 427
Cdd:cd03224 93 EENLLLGAyarrRAKRKARLERVYELFPRLKER-RKQLagTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 933767453 428 ARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:cd03224 172 FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
263-466 |
1.67e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.79 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 263 QMEFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKAR--LKHCY 338
Cdd:PRK11231 2 TLRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTpQSGTVFLGDKPIsMLSSRqlARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 MVMQdtsHQLFTESVADEVLLS------------MDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSN 406
Cdd:PRK11231 80 LLPQ---HHLTPEGITVRELVAygrspwlslwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 407 REIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
291-466 |
1.73e-26 |
|
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: 106.61 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDwKARLKHC---------YMVMQdtsHQLFTE-SVADEVLL 359
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKpDGGTIVLNGTVLF-DSRKKINlppqqrkigLVFQQ---YALFPHlNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 SM----DNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDlKHMREVARSL--KS 433
Cdd:cd03297 99 GLkrkrNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD-RALRLQLLPElkQI 177
|
170 180 190
....*....|....*....|....*....|...
gi 933767453 434 LADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-216 |
1.89e-26 |
|
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: 106.46 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 4 FQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPlydlaA 83
Cdd:cd03235 2 VEDLTVSYGGHPV---LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK-----PTSGSIRVFGKPLEKER-----K 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 84 MVGSVfqnpkSQFFNVDTDSEL-----------AFACENLGYPQEDIlKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIA 152
Cdd:cd03235 69 RIGYV-----PQRRSIDRDFPIsvrdvvlmglyGHKGLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVK 216
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-228 |
3.18e-26 |
|
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: 106.65 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESsgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVsdTPLYDL 81
Cdd:cd03299 1 LKVENLSKDWKEFK----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK-----PDSGKILLNGKDI--TNLPPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNpKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLP 161
Cdd:cd03299 70 KRDISYVPQN-YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 162 GIMVLDEPSSNLDMAAIDDLRQVLSLWKKQ-GKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
281-448 |
3.24e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 105.64 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKCG---FLQVEGKTLDWKARLKHCYMVmqdtSHQ--LFTE-SVA 354
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAgevLWNGEPIRDAREDYRRRLAYL----GHAdgLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEVLLSMDNK----DETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARS 430
Cdd:COG4133 94 ENLRFWAALYglraDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAEL 173
|
170
....*....|....*...
gi 933767453 431 LKSLADQGKTLLVITHDP 448
Cdd:COG4133 174 IAAHLARGGAVLLTTHQP 191
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-220 |
3.63e-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: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPV-LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR-----PTSGRVRLDGADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVfqnpksqffnvdtdselafacenlgyPQEDILkrIDRTVSDyHIedlmgrsvfaLSGGEKQKIACASSSVLLP 161
Cdd:cd03246 75 GDHVGYL--------------------------PQDDEL--FSGSIAE-NI----------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 162 GIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLhDLADRVLYVKDGEI 220
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
265-468 |
4.10e-26 |
|
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: 106.16 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEG---KTLDWKARLKHCYMV 340
Cdd:cd03253 2 EFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFyDVSSGSILIDGqdiREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTShqLFTESVADEVLLSMDN-KDETVV---------DKILKQFDLLEYK--DRHpLSLSGGQKQRVAIASAIVSNRE 408
Cdd:cd03253 81 PQDTV--LFNDTIGYNIRYGRPDaTDEEVIeaakaaqihDKIMRFPDGYDTIvgERG-LKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 409 IIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELVMaGCSYVVHMEKGQVKE 468
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIV-NADKIIVLKDGRIVE 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
264-481 |
4.22e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.56 E-value: 4.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREP---ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDWKARLKHCY- 338
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTtGTVTVDDITITHKTKDKYIRp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 ------MVMQDTSHQLFTESVADEVLLSMDNKDETVVDKILKQFDLL-------EYKDRHPLSLSGGQKQRVAIASAIVS 405
Cdd:PRK13646 83 vrkrigMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLmdlgfsrDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 406 NREIIVFDEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQ-VKESYPLDESGSKKVL 481
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSiVSQTSPKELFKDKKKL 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
264-473 |
4.81e-26 |
|
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: 105.63 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAY--KKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLdwKARLKHCYMV 340
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERpTSGEVLVDGEPV--TGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDtsHQLFT-ESVADEVLLSMDNKD------ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFD 413
Cdd:cd03293 79 FQQ--DALLPwLTVLDNVALGLELQGvpkaeaRERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 414 EPTSGLDlKHMREVARS--LKSLADQGKTLLVITHDPE--LVMAGCSYVVHMEKGQVKESYPLD 473
Cdd:cd03293 157 EPFSALD-ALTREQLQEelLDIWRETGKTVLLVTHDIDeaVFLADRVVVLSARPGRIVAEVEVD 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
280-450 |
5.35e-26 |
|
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: 105.00 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGK-TLDWKARLKHCYMvmQDTSHQLF-------T 350
Cdd:TIGR03608 18 NLTIEK-----GKMYAIIGESGSGKSTLLNIIGLLEKFdSGQVYLNGQeTPPLNSKKASKFR--REKLGYLFqnfalieN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 351 ESVADEVLLSMDNKDETVVDK------ILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHM 424
Cdd:TIGR03608 91 ETVEENLDLGLKYKKLSKKEKrekkkeALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNR 170
|
170 180
....*....|....*....|....*.
gi 933767453 425 REVARSLKSLADQGKTLLVITHDPEL 450
Cdd:TIGR03608 171 DEVLDLLLELNDEGKTIIIVTHDPEV 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-481 |
7.05e-26 |
|
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: 110.30 E-value: 7.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyeGKLEGDVLLDG-----KSVSDTPLYDLAAMVGSVFQNPK- 93
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPH---GTWDGEIYWSGsplkaSNIRDTERAGIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 94 SQFFNVDTDSELAFACENLGYPQedILKRIDRTVSDYHIEDL-MGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSN 172
Cdd:TIGR02633 94 SVAENIFLGNEITLPGGRMAYNA--MYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 173 LDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEiEREYTPAEFDSLSDGTRKEIGLRPFSLSKLKP 252
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ-HVATKDMSTMSEDDIITMMVGREITSLYPHEP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 253 anqyqaHTAKQ--MEFQNF-CFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKC-GFLQVEGKT 327
Cdd:TIGR02633 251 ------HEIGDviLEARNLtCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFeGNVFINGKP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 328 LDWKARLKH----CYMVMQDTSH----------QLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHPL----SL 389
Cdd:TIGR02633 325 VDIRNPAQAiragIAMVPEDRKRhgivpilgvgKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigRL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 390 SGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKES 469
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
490
....*....|..
gi 933767453 470 YPLDESGSKKVL 481
Cdd:TIGR02633 485 FVNHALTQEQVL 496
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-242 |
9.64e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.64 E-value: 9.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEES--SGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHYYEGKLEGDVLLDGKSVSDtpL 78
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTSGTVTIGERVITAGKKNKK--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHI-EDLMGRSVFALSGGEKQKIACASSS 157
Cdd:PRK13634 81 KPLRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 158 VLLPGIMVLDEPSSNLDMAAIDDLRQVL-SLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFdsLSDGT 236
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFyKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI--FADPD 238
|
....*..
gi 933767453 237 R-KEIGL 242
Cdd:PRK13634 239 ElEAIGL 245
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-228 |
1.26e-25 |
|
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: 104.57 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESsggGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEGKLEGDVLLDGKSV--SDTPLY 79
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFQNP----KSQFFNVdtdselAFACENLGYPQEDILKRIDRTV-SDYHIEDLMGRSVFA--LSGGEKQKIA 152
Cdd:cd03260 78 ELRRRVGMVFQKPnpfpGSIYDNV------AYGLRLHGIKLKEELDERVEEAlRKAALWDEVKDRLHAlgLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLD---MAAIDDLrqVLSLwkKQGKTILIAEHRLYYLHDLADRVLYVKDGEIeREYTPAE 228
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDpisTAKIEEL--IAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL-VEFGPTE 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-250 |
1.37e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 106.25 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEES--SGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEGKLEGDVLLDGKSVSDTPLY 79
Cdd:PRK13645 7 IILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHI-EDLMGRSVFALSGGEKQKIACASSSV 158
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 159 LLPGIMVLDEPSSNLDMAAIDDLRQV-LSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFDSLSDGTR 237
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLfERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLT 246
|
250
....*....|...
gi 933767453 238 KeIGLRPFSLSKL 250
Cdd:PRK13645 247 K-IEIDPPKLYQL 258
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
285-474 |
1.43e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.17 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTL-DWK----AR----LKhcymvmQDTSHQL-FTesV 353
Cdd:COG4604 21 SLTIPKGGITALIGPNGAGKSTLLSMISRLlPPDSGEVLVDGLDVaTTPsrelAKrlaiLR------QENHINSrLT--V 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 ADevLLS----------MDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKH 423
Cdd:COG4604 93 RE--LVAfgrfpyskgrLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKH 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933767453 424 MREVARSLKSLAD-QGKTLLVITHDpeLVMAGC--SYVVHMEKGQVKESYPLDE 474
Cdd:COG4604 171 SVQMMKLLRRLADeLGKTVVIVLHD--INFASCyaDHIVAMKDGRVVAQGTPEE 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
264-466 |
1.46e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.04 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL----EKKCGFLQVEGKTLD----WKARLK 335
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpdDNPNSKITVDGITLTaktvWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 336 hCYMVMQDTSHQLFTESVADEVLLSMDNKD------ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREI 409
Cdd:PRK13640 86 -VGIVFQNPDNQFVGATVGDDVAFGLENRAvprpemIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLA-DQGKTLLVITHD-PELVMAgcSYVVHMEKGQV 466
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDiDEANMA--DQVLVLDDGKL 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
291-467 |
1.96e-25 |
|
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: 103.74 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKtlDWKARLKHCYM----VMQDTShqLFTESVADEVLLSM---- 361
Cdd:cd03263 28 GEIFGLLGHNGAGKTTTLKMLTGELRPtSGTAYINGY--SIRTDRKAARQslgyCPQFDA--LFDELTVREHLRFYarlk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 362 ---DNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAdQG 438
Cdd:cd03263 104 glpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KG 182
|
170 180
....*....|....*....|....*....
gi 933767453 439 KTLLVITHDPELVMAGCSYVVHMEKGQVK 467
Cdd:cd03263 183 RSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
281-467 |
2.60e-25 |
|
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: 103.56 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDWKARL------KHCYMVMQdtSHQLFTESV 353
Cdd:TIGR02982 21 LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSvQEGSLKVLGQELHGASKKqlvqlrRRIGYIFQ--AHNLLGFLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 ADE-VLLSMDNKDET-------VVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMR 425
Cdd:TIGR02982 99 ARQnVQMALELQPNLsyqeareRARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 933767453 426 EVARSLKSLA-DQGKTLLVITHDPE-LVMAgcSYVVHMEKGQVK 467
Cdd:TIGR02982 179 DVVELMQKLAkEQGCTILMVTHDNRiLDVA--DRILQMEDGKLL 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
280-466 |
2.74e-25 |
|
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: 103.86 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKARLKHCYMVMQdtSHQLFTE-SVADE 356
Cdd:cd03300 20 SLDIKE-----GEFFTLLGPSGCGKTTLLRLIAGFETpTSGEILLDGKDItNLPPHKRPVNTVFQ--NYALFPHlTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 357 VL--LSMDNKDETV----VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARS 430
Cdd:cd03300 93 IAfgLRLKKLPKAEikerVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLE 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 933767453 431 LKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03300 173 LKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-468 |
3.38e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 108.33 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyYEGKlEGDVLLDGKSVsDTPLYDLAAMVG------------- 86
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI----HEPT-KGTITINNINY-NKLDHKLAAQLGigiiyqelsvide 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 87 -SVFQN------PKSQFFNVDTdselaFACENLGYPQEDILKRIDRTVSdyhiedlMGRSVFALSGGEKQKIACASSSVL 159
Cdd:PRK09700 95 lTVLENlyigrhLTKKVCGVNI-----IDWREMRVRAAMMLLRVGLKVD-------LDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 160 LPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGeiereyTPAEFDSLSDGTRKE 239
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG------SSVCSGMVSDVSNDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 240 IgLRPFSLSKLK---PANQYQAHTAKQ---MEFQNFcfayKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG 313
Cdd:PRK09700 237 I-VRLMVGRELQnrfNAMKENVSNLAHetvFEVRNV----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 314 LEK-KCGFLQVEGKTLDWKARLKH-----CYMVMQDTSHQLFTE-SVADEVLLS--------------MDNKDETVVDKi 372
Cdd:PRK09700 312 VDKrAGGEIRLNGKDISPRSPLDAvkkgmAYITESRRDNGFFPNfSIAQNMAISrslkdggykgamglFHEVDEQRTAE- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 373 lKQFDLLEYK----DRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHD- 447
Cdd:PRK09700 391 -NQRELLALKchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEl 469
|
490 500
....*....|....*....|.
gi 933767453 448 PELvMAGCSYVVHMEKGQVKE 468
Cdd:PRK09700 470 PEI-ITVCDRIAVFCEGRLTQ 489
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
264-466 |
4.95e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.11 E-value: 4.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREpESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTLDwKARLKHCY---- 338
Cdd:PRK13652 4 IETRDLCYSYSGSK-EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGiLKPTSGSVLIRGEPIT-KENIREVRkfvg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 MVMQDTSHQLFTESVADEVLLSMDN---KDETV---VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVF 412
Cdd:PRK13652 82 LVFQNPDDQIFSPTVEQDIAFGPINlglDEETVahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 413 DEPTSGLDLKHMREVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
5.59e-25 |
|
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: 103.04 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGG-GIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTP-- 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-----ERPTSGSVLVDGTDLTLLSgk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 -LYDLAAMVGSVFQN-----PKSQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKI 151
Cdd:cd03258 76 eLRKARRRIGMIFQHfnllsSRTVFENV------ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 152 ACASSSVLLPGIMVLDEPSSNLDMAAIDD-LRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIERE 223
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
285-466 |
6.41e-25 |
|
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: 102.90 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKA-RLKHCYMVM--QDTshQLFTE-SVADEVL 358
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRpTSGSVLFDGEDItGLPPhEIARLGIGRtfQIP--RLFPElTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 L--------------SMDNKDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLK 422
Cdd:cd03219 98 VaaqartgsglllarARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 933767453 423 HMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03219 178 ETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-234 |
8.23e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 104.40 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL-------------------VPHYYEGKLEGDVLLDGKSVSDTPLYD 80
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdeknkkKTKEKEKVLEKLVIQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHI-EDLMGRSVFALSGGEKQKIACASSSVL 159
Cdd:PRK13651 103 IRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 160 LPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPaeFDSLSD 234
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT--YDILSD 255
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
287-474 |
8.88e-25 |
|
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: 105.18 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTL-DWKARL------KHCYMVMQDTShqLF-TESVADEV 357
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsGRIRLGGEVLqDSARGIflpphrRRIGYVFQEAR--LFpHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 358 LLSMDNKD--------ETVVDkILKQFDLLeykDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVAR 429
Cdd:COG4148 99 LYGRKRAPraerrisfDEVVE-LLGIGHLL---DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 933767453 430 SLKSLADQGKT-LLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:COG4148 175 YLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
291-447 |
9.22e-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: 104.36 E-value: 9.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKCGflQVEGK---------TLDWKA----RLKHCYMVMQD--TS-HQLFT--ES 352
Cdd:COG0444 31 GETLGLVGESGSGKSTLARAILGLLPPPG--ITSGEilfdgedllKLSEKElrkiRGREIQMIFQDpmTSlNPVMTvgDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 353 VADEVLLSMDNKDETVVDKILKQFDLL------EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD------ 420
Cdd:COG0444 109 IAEPLRIHGGLSKAEARERAIELLERVglpdpeRRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqaq 188
|
170 180
....*....|....*....|....*...
gi 933767453 421 -LKHMREVARSLksladqGKTLLVITHD 447
Cdd:COG0444 189 iLNLLKDLQREL------GLAILFITHD 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
264-466 |
9.42e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.28 E-value: 9.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKrEPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLE-KKCGFLQVEGK-----TLDWkARLKhC 337
Cdd:PRK13647 5 IEVEDLHFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYlPQRGRVKVMGRevnaeNEKW-VRSK-V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 338 YMVMQDTSHQLFTESVADEVLLSMDN----KDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIV 411
Cdd:PRK13647 82 GLVFQDPDDQVFSSTVWDDVAFGPVNmgldKDEVErrVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 412 FDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
285-466 |
9.69e-25 |
|
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: 101.59 E-value: 9.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTLDWKARLKHCYMVMQDTSHQlfTESVADEVL----L 359
Cdd:cd03269 20 SFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDSGEVLFDGKPLDIAARNRIGYLPEERGLYP--KMKVIDQLVylaqL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 SMDNKDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ 437
Cdd:cd03269 98 KGLKKEEARrrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA 177
|
170 180
....*....|....*....|....*....
gi 933767453 438 GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03269 178 GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-228 |
1.38e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.37 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESS--GGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSV----S 74
Cdd:PRK13641 3 IKFENVDYIYSPGTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPS------SGTITIAGYHItpetG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 75 DTPLYDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDI----LKRIDRTVSDyhiEDLMGRSVFALSGGEKQK 150
Cdd:PRK13641 77 NKNLKKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAkekaLKWLKKVGLS---EDLISKSPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 151 IACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKE 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
264-474 |
1.45e-24 |
|
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: 101.79 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEG---KTLDWKARLKHCYM 339
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGhdlALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 VMQDTShqLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHPL-----------SLSGGQKQRVAIASAIVSNRE 408
Cdd:cd03252 81 VLQENV--LFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 409 IIVFDEPTSGLDLKHMREVARSLKSLADqGKTLLVITHDPELVMAGCSYVVhMEKGQVKESYPLDE 474
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIV-MEKGRIVEQGSHDE 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
296-466 |
1.53e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.78 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 296 IIGLNGAGKSTLARCICGLEK-KCGFLQVEG-------------------KTLDWKARLKHCYMVMQDTSHQLFTESVAD 355
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKsKYGTIQVGDiyigdkknnhelitnpyskKIKNFKELRRRVSMVFQFPEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 356 EVL---LSMDNKDETVVDKILKQFDLL----EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVA 428
Cdd:PRK13631 137 DIMfgpVALGVKKSEAKKLAKFYLNKMglddSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM 216
|
170 180 190
....*....|....*....|....*....|....*...
gi 933767453 429 RSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK13631 217 QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-220 |
1.72e-24 |
|
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: 100.82 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03269 1 LEVENVTKRFGRVTA---LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-----SGEVLFDGKPLDIAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMvgsvfqnPKSQ--FFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVL 159
Cdd:cd03269 73 GYL-------PEERglYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 160 LPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
280-466 |
1.74e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.38 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGK---TLDWKARlkHCYMVMQdtSHQLF-TESVA 354
Cdd:COG3839 23 DLDIED-----GEFLVLLGPSGCGKSTLLRMIAGLEDpTSGEILIGGRdvtDLPPKDR--NIAMVFQ--SYALYpHMTVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEVLLSMDN----KDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKhMREVA 428
Cdd:COG3839 94 ENIAFPLKLrkvpKAEIDrrVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK-LRVEM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 933767453 429 RS-LKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG3839 173 RAeIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
285-469 |
1.89e-24 |
|
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: 100.73 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGeTIAIIGLNGAGKSTLARCICGL-EKKCG---FLQVEGKTLDWKARLKHCYMVMQDTSHQLFT--ESVADEVL 358
Cdd:cd03264 20 SLTLGPG-MYGLLGPNGAGKTTLMRILATLtPPSSGtirIDGQDVLKQPQKLRRRIGYLPQEFGVYPNFTvrEFLDYIAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 LS--MDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHmREVARSLksLAD 436
Cdd:cd03264 99 LKgiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEE-RIRFRNL--LSE 175
|
170 180 190
....*....|....*....|....*....|....*
gi 933767453 437 QGKTLLVI--THDPELVMAGCSYVVHMEKGQVKES 469
Cdd:cd03264 176 LGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-230 |
2.30e-24 |
|
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: 101.49 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGeeSSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03256 1 IEVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-----PTSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAM---VGSVFQnpksQFFNVDTDSelafACEN-----LGY-----------PQEDI------LKRIDrtvsdyhIEDLM 136
Cdd:cd03256 74 RQLrrqIGMIFQ----QFNLIERLS----VLENvlsgrLGRrstwrslfglfPKEEKqralaaLERVG-------LLDKA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 137 GRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIddlRQVLSLWKK----QGKTILIAEHRLYYLHDLADRV 212
Cdd:cd03256 139 YQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASS---RQVMDLLKRinreEGITVIVSLHQVDLAREYADRI 215
|
250
....*....|....*...
gi 933767453 213 LYVKDGEIEREYTPAEFD 230
Cdd:cd03256 216 VGLKDGRIVFDGPPAELT 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
281-471 |
2.53e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 101.75 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK------KCGFLQVEG-KTLDWKARL-----KHCYMVMQdtSHQL 348
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtiRVGDITIDTaRSLSQQKGLirqlrQHVGFVFQ--NFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 349 FTESVADE------VLLSMDNKDETVV--DKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD 420
Cdd:PRK11264 97 FPHRTVLEniiegpVIVKGEPKEEATAraRELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 933767453 421 LKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYP 471
Cdd:PRK11264 177 PELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
273-474 |
2.78e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 101.84 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 273 YKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL---DWKARLKHCYMVMQDTSH-- 346
Cdd:COG4167 21 FRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEpTSGEILINGHKLeygDYKYRCKHIRMIFQDPNTsl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 347 --QLFTESVADEVLL---SMDNKD-ETVVDKILKQFDLL-EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGL 419
Cdd:COG4167 101 npRLNIGQILEEPLRlntDLTAEErEERIFATLRLVGLLpEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAAL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 420 DLkhmrevarSLKS---------LADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:COG4167 181 DM--------SVRSqiinlmlelQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-228 |
3.40e-24 |
|
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: 100.77 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNglvpHYYEgKLEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03253 1 IEFENVTFAYDPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF----RFYD-VSSGSILIDGQDIREVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNpkSQFFNVDTDSELAFACENLGypQEDILK-----RIDRTVSD----YhiEDLMGRSVFALSGGEKQKIA 152
Cdd:cd03253 74 RRAIGVVPQD--TVLFNDTIGYNIRYGRPDAT--DEEVIEaakaaQIHDKIMRfpdgY--DTIVGERGLKLSGGEKQRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLD-------MAAIDDLRqvlslwkkQGKTILIAEHRLYYLHDlADRVLYVKDGEIEREYT 225
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDthtereiQAALRDVS--------KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
...
gi 933767453 226 PAE 228
Cdd:cd03253 219 HEE 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
118-447 |
3.41e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 106.05 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 118 DILKRID-RTVSDYHIEDL-----MGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLD----MAAIDDLRQVLsl 187
Cdd:PRK13409 182 ELLKKVDeRGKLDEVVERLgleniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNVARLIRELA-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 188 wkkQGKTILIAEHRLYYLHDLADRV--LYvkdGEiereytPAEFDSLSD--GTRKEIG-------------LRPFSLSKL 250
Cdd:PRK13409 260 ---EGKYVLVVEHDLAVLDYLADNVhiAY---GE------PGAYGVVSKpkGVRVGINeylkgylpeenmrIRPEPIEFE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 251 KPANQYQAHTAKQMEFQNFcfaYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKcgflqVEGKtLDW 330
Cdd:PRK13409 328 ERPPRDESERETLVEYPDL---TKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKP-----DEGE-VDP 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 331 KARL--KHCYMVM-QDTSHQLFTESVADEVLLSMDNKDetvvdkILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNR 407
Cdd:PRK13409 399 ELKIsyKPQYIKPdYDGTVEDLLRSITDDLGSSYYKSE------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 933767453 408 EIIVFDEPTSGLDLKHMREVARSLKSLAD-QGKTLLVITHD 447
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDHD 513
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-220 |
4.45e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.57 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 4 FQNVSFSYGEESSGggiRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTPLYDLAa 83
Cdd:PRK11000 6 LRNVTKAYGDVVIS---KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL-----EDITSGDLFIGEKRMNDVPPAERG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 84 mVGSVFQNpKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGI 163
Cdd:PRK11000 77 -VGMVFQS-YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 164 MVLDEPSSNLDMAAIDDLR-QVLSLWKKQGKTIliaehrLYYLHD------LADRVLYVKDGEI 220
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRiEISRLHKRLGRTM------IYVTHDqveamtLADKIVVLDAGRV 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-228 |
4.65e-24 |
|
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: 100.49 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTPLYDl 81
Cdd:cd03296 3 IEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-----ERPDSGTILFGGEDATDVPVQE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 aAMVGSVFQNpKSQFFNVDTDSELAFACE----NLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSS 157
Cdd:cd03296 74 -RNVGFVFQH-YALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 158 VLLPGIMVLDEPSSNLDMAAIDDLRQVL-SLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLrRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-220 |
1.08e-23 |
|
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: 99.12 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEessGGG----IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSV--- 73
Cdd:cd03257 1 LLEVKNLSVSFPT---GGGsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-----PTSGSIIFDGKDLlkl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 74 SDTPLYDLAAMVGSVFQNPKS----------------QFFNVDTDSELafacenlgypQEDILKRIDRTVSDYhiEDLMG 137
Cdd:cd03257 73 SRRLRKIRRKEIQMVFQDPMSslnprmtigeqiaeplRIHGKLSKKEA----------RKEAVLLLLVGVGLP--EEVLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 138 RSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDM---AAIddLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLY 214
Cdd:cd03257 141 RYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVsvqAQI--LDLLKKLQEELGLTLLFITHDLGVVAKIADRVAV 218
|
....*.
gi 933767453 215 VKDGEI 220
Cdd:cd03257 219 MYAGKI 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
287-481 |
1.08e-23 |
|
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: 102.11 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKARL------KHCYMVMQDTShqLFTE-SVADEV 357
Cdd:TIGR02142 19 TLPGQGVTAIFGRSGSGKTTLIRLIAGLTRpDEGEIVLNGRTLfDSRKGIflppekRRIGYVFQEAR--LFPHlSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 358 LLSM---DNKDETVV-DKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKS 433
Cdd:TIGR02142 97 RYGMkraRPSERRISfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLER 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 933767453 434 LADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDESGSKKVL 481
Cdd:TIGR02142 177 LHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
280-466 |
1.20e-23 |
|
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: 98.48 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKARLKHCYMVMQdtSHQLFTE-SVADE 356
Cdd:cd03301 20 NLDIAD-----GEFVVLLGPSGCGKTTTLRMIAGLEEpTSGRIYIGGRDVtDLPPKDRDIAMVFQ--NYALYPHmTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 357 VLLSM-------DNKDETV--VDKILKQFDLLeykDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKhMREV 427
Cdd:cd03301 93 IAFGLklrkvpkDEIDERVreVAELLQIEHLL---DRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK-LRVQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933767453 428 ARS-LKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03301 169 MRAeLKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-220 |
1.32e-23 |
|
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: 98.37 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTP--LY 79
Cdd:cd03262 1 IEIKNLHKSFGDFHV---LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD-----SGTIIIDGLKLTDDKknIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFQNpksqfFNVdtdselaF----ACENLGYPQEDILKRIDRTVSD--YHIEDLMGRSVFA------LSGGE 147
Cdd:cd03262 73 ELRQKVGMVFQQ-----FNL-------FphltVLENITLAPIKVKGMSKAEAEEraLELLEKVGLADKAdaypaqLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 148 KQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
285-466 |
1.43e-23 |
|
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: 96.73 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTLD----WKARLKHCYMVMQdtshqlftesvadevll 359
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVDGKEVSfaspRDARRAGIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 smdnkdetvvdkilkqfdlleykdrhplsLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGK 439
Cdd:cd03216 83 -----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGV 133
|
170 180
....*....|....*....|....*..
gi 933767453 440 TLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03216 134 AVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
267-466 |
1.43e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.12 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 267 QNFCFAYKKREP---ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKARL----KHC 337
Cdd:PRK13637 6 ENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVDItDKKVKLsdirKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 338 YMVMQDTSHQLFTESVADEVLLSMDN---KDETVVDKILKQFDLL-----EYKDRHPLSLSGGQKQRVAIASAIVSNREI 409
Cdd:PRK13637 86 GLVFQYPEYQLFEETIEKDIAFGPINlglSEEEIENRVKRAMNIVgldyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLADQGK-TLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
118-447 |
1.91e-23 |
|
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: 103.71 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 118 DILKRID-RTVSDYHIEDL-----MGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLD----MAAIDDLRQVLsl 187
Cdd:COG1245 182 ELLEKVDeRGKLDELAEKLgleniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELA-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 188 wkKQGKTILIAEHRLYYLHDLADRV--LYvkdGEiereytPAEFDSLSD--GTRKEIG-------------LRPFSLSKL 250
Cdd:COG1245 260 --EEGKYVLVVEHDLAILDYLADYVhiLY---GE------PGVYGVVSKpkSVRVGINqyldgylpeenvrIRDEPIEFE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 251 KPANQYQAHTAKQMEFQNFcfaYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKcgflqVEGKtLDW 330
Cdd:COG1245 329 VHAPRREKEEETLVEYPDL---TKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKP-----DEGE-VDE 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 331 KARL--KHCYmVMQDtshqlFTESVadEVLLSMDNKDET----VVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIV 404
Cdd:COG1245 400 DLKIsyKPQY-ISPD-----YDGTV--EEFLRSANTDDFgssyYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLS 471
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 933767453 405 SNREIIVFDEPTSGLDLKHMREVARSLKSLAD-QGKTLLVITHD 447
Cdd:COG1245 472 RDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEnRGKTAMVVDHD 515
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-217 |
2.01e-23 |
|
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: 97.93 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESsggGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTP--L 78
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS-----AGEVLWNGEPIRDARedY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVG---------SVFQNpksqffnvdtdseLAFACENLGYPQEDIlkRIDRTVSDYHIEDLMGRSVFALSGGEKQ 149
Cdd:COG4133 74 RRRLAYLGhadglkpelTVREN-------------LRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 150 KIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLyyLHDLADRVLYVKD 217
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP--LELAAARVLDLGD 204
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-228 |
2.10e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.99 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESsggGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSV-SDTPLYD 80
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPD-----SGRIVLNGRDLfTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAamVGSVFQNPksQFF-------NVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIAC 153
Cdd:COG1118 75 RR--VGFVFQHY--ALFphmtvaeNI------AFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 154 ASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLS-LWKKQGKTILIAEhrlyylHD------LADRVLYVKDGEIEREYTP 226
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRrLHDELGGTTVFVT------HDqeealeLADRVVVMNQGRIEQVGTP 218
|
..
gi 933767453 227 AE 228
Cdd:COG1118 219 DE 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
271-469 |
2.26e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.03 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 271 FAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGK---TLDWK----ARlKHCYMVMQ 342
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTsGRVLVDGQdltALSEKelrkAR-RQIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 343 dtsH--QLFTESVADEVLLSM--DNKD----ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDE 414
Cdd:PRK11153 90 ---HfnLLSSRTVFDNVALPLelAGTPkaeiKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 415 PTSGLD-------LKHMREVARSLksladqGKTLLVITHDPELVMAGCSYVVHMEKGQVKES 469
Cdd:PRK11153 167 ATSALDpattrsiLELLKDINREL------GLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
280-473 |
2.53e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 99.19 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDWKARLKHCYMVMQ----DTSHQLFTESVA 354
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKISILGQPTRQALQKNLVAYVPQseevDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DE-------VLLSMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREV 427
Cdd:PRK15056 102 MMgryghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 933767453 428 ARSLKSLADQGKTLLVITHDPELVMAGCSYVVhMEKGQVKESYPLD 473
Cdd:PRK15056 182 ISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTE 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
291-466 |
2.60e-23 |
|
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: 98.52 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLDwKARLK-------HCYMVMQDtsHQLFTE-SVADEVL--- 358
Cdd:TIGR02315 28 GEFVAIIGPSGAGKSTLLRCINRLvEPSSGSILLEGTDIT-KLRGKklrklrrRIGMIFQH--YNLIERlTVLENVLhgr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 ----------LSMDNKDETVVDK-ILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREV 427
Cdd:TIGR02315 105 lgykptwrslLGRFSEEDKERALsALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 933767453 428 ARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:TIGR02315 185 MDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-228 |
3.90e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.04 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEES--SGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEGKLEGDVLLDGKSvSDTPL 78
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS-KQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHI-EDLMGRSVFALSGGEKQKIACASSS 157
Cdd:PRK13643 80 KPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 158 VLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSD 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
291-466 |
3.99e-23 |
|
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: 96.47 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGL---EKKCGFLQVEGKTLDWKARLKHCYMVMQDtshqlftesvadEVLLSMDNKDET 367
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGRrtgLGVSGEVLINGRPLDKRSFRKIIGYVPQD------------DILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 368 vvdkilkqfdlLEY--KDRhplSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVIT 445
Cdd:cd03213 103 -----------LMFaaKLR---GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSI 168
|
170 180
....*....|....*....|..
gi 933767453 446 HDP-ELVMAGCSYVVHMEKGQV 466
Cdd:cd03213 169 HQPsSEIFELFDKLLLLSQGRV 190
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
264-469 |
6.99e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.55 E-value: 6.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREP---ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTL-------DWKA 332
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTsGTVTIGERVItagkknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 333 RLKHCYMVMQDTSHQLFTESVADEVLLSMDN---KDETVVDKILKQFDLL----EYKDRHPLSLSGGQKQRVAIASAIVS 405
Cdd:PRK13634 83 LRKKVGIVFQFPEHQLFEETVEKDICFGPMNfgvSEEDAKQKAREMIELVglpeELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 406 NREIIVFDEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKES 469
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
265-446 |
7.06e-23 |
|
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: 96.91 E-value: 7.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL---EKKCGFLQ-VEGKTLDWKARLKHCYMV 340
Cdd:cd03254 4 EFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFydpQKGQILIDgIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTShqLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQRVAIASAIVSNREI 409
Cdd:cd03254 83 LQDTF--LFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITH 446
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAH 196
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-228 |
7.16e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.53 E-value: 7.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGeessgGG---IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSD-T 76
Cdd:PRK11650 3 GLKLQAVRKSYD-----GKtqvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL-----ERITSGEIWIGGRVVNElE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLYDLAAMvgsVFQN----PK-SQFFNvdtdseLAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKI 151
Cdd:PRK11650 73 PADRDIAM---VFQNyalyPHmSVREN------MAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 152 ACASSSVLLPGIMVLDEPSSNLDMAaiddLR-----QVLSLWKKQGKTiliaehRLYYLHD------LADRVLYVKDGEI 220
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDAK----LRvqmrlEIQRLHRRLKTT------SLYVTHDqveamtLADRVVVMNGGVA 213
|
....*...
gi 933767453 221 EREYTPAE 228
Cdd:PRK11650 214 EQIGTPVE 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
8.80e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 101.21 E-value: 8.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYgeESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDL 81
Cdd:TIGR02857 322 LEFSGVSVAY--PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFFNVDTDSELAFACenLGYPQEDILKRIDRTVSDYHIEDL-------MGRSVFALSGGEKQKIACA 154
Cdd:TIGR02857 395 RDQIAWVPQHP--FLFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALpqgldtpIGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 155 SSSVLLPGIMVLDEPSSNLDMAA----IDDLRQVLslwkkQGKTILIAEHRLYYLHdLADRVL 213
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETeaevLEALRALA-----QGRTVLLVTHRLALAA-LADRIV 527
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-247 |
8.90e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.41 E-value: 8.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTPLY--DLA 82
Cdd:PRK11432 10 KNITKRFGSNTV---IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL-----EKPTEGQIFIDGEDVTHRSIQqrDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 83 AmvgsVFQNpKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSdyhIEDLMG---RSVFALSGGEKQKIACASSSVL 159
Cdd:PRK11432 82 M----VFQS-YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALE---LVDLAGfedRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 160 LPGIMVLDEPSSNLD------M-AAIDDLRQVLSLwkkqgktiliaeHRLYYLHD------LADRVLYVKDGEIereytp 226
Cdd:PRK11432 154 KPKVLLFDEPLSNLDanlrrsMrEKIRELQQQFNI------------TSLYVTHDqseafaVSDTVIVMNKGKI------ 215
|
250 260
....*....|....*....|.
gi 933767453 227 aefdsLSDGTRKEIGLRPFSL 247
Cdd:PRK11432 216 -----MQIGSPQELYRQPASR 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
280-483 |
1.07e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.00 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTLD-WKARLKHCYMVMQDtsHQLFTE-SVADE 356
Cdd:PRK10851 22 SLDIPS-----GQMVALLGPSGSGKTTLLRIIAGLEHQtSGHIRFHGTDVSrLHARDRKVGFVFQH--YALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 357 VL--LSMDNKDE--------TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMRE 426
Cdd:PRK10851 95 IAfgLTVLPRRErpnaaaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 427 VARSLKSLADQGK-TLLVITHDPELVMAGCSYVVHMEKGQVKE-SYPLD---ESGSKKVLDF 483
Cdd:PRK10851 175 LRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQaGTPDQvwrEPATRFVLEF 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
1.12e-22 |
|
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: 95.90 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGG-GIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSVSDTPL 78
Cdd:cd03266 1 MITADALTKRFRDVKKTVqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePD------AGFATVDGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 yDLAAMVGSVFQNpksqffnvDTDSELAFACENLGY--------PQEdILKRIDRTVSDYHIEDLMGRSVFALSGGEKQK 150
Cdd:cd03266 75 -EARRRLGFVSDS--------TGLYDRLTARENLEYfaglyglkGDE-LTARLEELADRLGMEELLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 151 IACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
286-474 |
1.56e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 98.41 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 286 AELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLdWKARLKHC---------YmVMQDtsHQLFTE-SVA 354
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRpQKGRIVLNGRVL-FDAEKGIClppekrrigY-VFQD--ARLFPHyKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEVLLSMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSL 434
Cdd:PRK11144 95 GNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933767453 435 ADQGKT-LLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:PRK11144 175 AREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-228 |
1.76e-22 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 96.19 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAM 84
Cdd:TIGR04406 5 ENLIKSYKKRKV---VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVR-----PDAGKILIDGQDITHLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 85 -VGSVFQNPkSQFfnvdtdSELAFAcENL--------GYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACAS 155
Cdd:TIGR04406 77 gIGYLPQEA-SIF------RKLTVE-ENImavleirkDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 156 SSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:TIGR04406 149 ALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAE 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
285-466 |
1.92e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 95.82 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDWK-----ARLKHCYmVMQDtsHQLFTE-SVADEV 357
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRsGSIRFDGEDITGLpphriARLGIGY-VPEG--RRIFPSlTVEENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 358 LL-----SMDNKDETVVDKILKQF-DLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSL 431
Cdd:COG0410 100 LLgayarRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEII 179
|
170 180 190
....*....|....*....|....*....|....*
gi 933767453 432 KSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG0410 180 RRLNREGVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-222 |
2.23e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 100.48 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSY-GEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNglvpHYYEGKlEGDVLLDGKSVSDTPLYD 80
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPA--LRNINFKIPAGKTVALVGRSGSGKSTIANLLT----RFYDID-EGEILLDGHDLRDYTLAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNpkSQFFNVDTDSELAFACENLgYPQEDILKR---------IDRTvsDYHIEDLMGRSVFALSGGEKQKI 151
Cdd:PRK11176 415 LRNQVALVSQN--VHLFNDTIANNIAYARTEQ-YSREQIEEAarmayamdfINKM--DNGLDTVIGENGVLLSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 152 ACASSsvLL---PgIMVLDEPSSNLD-------MAAIDDLrqvlslwkKQGKTILIAEHRLYYLHDlADRVLYVKDGEI- 220
Cdd:PRK11176 490 AIARA--LLrdsP-ILILDEATSALDteseraiQAALDEL--------QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIv 557
|
..
gi 933767453 221 ER 222
Cdd:PRK11176 558 ER 559
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-220 |
2.51e-22 |
|
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: 94.78 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSD-----T 76
Cdd:cd03292 1 IEFINVTKTYPNGTAA--LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-----ELPTSGTIRVNGQDVSDlrgraI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLydLAAMVGSVFQNPK-----SQFFNVdtdselAFACENLGYPQEDILKRID---RTVSDYHIEDLMGRSvfaLSGGEK 148
Cdd:cd03292 74 PY--LRRKIGVVFQDFRllpdrNVYENV------AFALEVTGVPPREIRKRVPaalELVGLSHKHRALPAE---LSGGEQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 149 QKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
285-466 |
2.68e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.92 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEG---KTLDWKARLKHCYMVMQDTshQLFTESVADEVLLSM 361
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGielRELDPESWRKHLSWVGQNP--QLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 362 DNKDETVVDKILKQFDLLEYKDRHPL-----------SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARS 430
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190
....*....|....*....|....*....|....*.
gi 933767453 431 LKSlADQGKTLLVITHDPElVMAGCSYVVHMEKGQV 466
Cdd:PRK11174 528 LNA-ASRRQTTLMVTHQLE-DLAQWDQIWVMQDGQI 561
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-229 |
3.65e-22 |
|
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: 94.92 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAM-VGSVFQNPkSQFFN 98
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGKILLDGQDITKLPMHKRARLgIGYLPQEA-SIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 VDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAI 178
Cdd:cd03218 90 LTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 933767453 179 DDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEF 229
Cdd:cd03218 170 QDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-171 |
4.17e-22 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 92.33 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDLAAMVGSVFQNPkSQFFNV 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-----EGTILLDGQDLTDDERKSLRKEIGYVFQDP-QLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 100 DTDSELAFACENLGYPQEDILKRIDR---TVSDYHIED-LMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSS 171
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKDARAEEaleKLGLGDLADrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
264-469 |
4.68e-22 |
|
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: 99.82 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTL-----DWKARlkHC 337
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLyTPQHGQVLVDGVDLaiadpAWLRR--QM 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 338 YMVMQDTShqLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQRVAIASAIVSN 406
Cdd:TIGR01846 534 GVVLQENV--LFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIAIARALVGN 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 407 REIIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELVmAGCSYVVHMEKGQVKES 469
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTV-RACDRIIVLEKGQIAES 672
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
280-468 |
5.84e-22 |
|
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: 94.71 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKARLKHCYMVMQDtsHQLFTE-SVADE 356
Cdd:cd03296 22 SLDIPS-----GELVALLGPSGSGKTTLLRLIAGLERpDSGTILFGGEDAtDVPVQERNVGFVFQH--YALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 357 VLL--------SMDNKDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMRE 426
Cdd:cd03296 95 VAFglrvkprsERPPEAEIRakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 933767453 427 VARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:cd03296 175 LRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-228 |
6.87e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 94.39 E-value: 6.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNglvphyyegKLE----GDVLLDGKSVSDt 76
Cdd:PRK09493 1 MIEFKNVSKHFGPTQV---LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCIN---------KLEeitsGDLIVDGLKVND- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLYDLAAM---VGSVFQnpksQF--FNVDTdselafACENL--------GYPQEDILKRIDRTVSDYHIEDLMGRSVFAL 143
Cdd:PRK09493 68 PKVDERLIrqeAGMVFQ----QFylFPHLT------ALENVmfgplrvrGASKEEAEKQARELLAKVGLAERAHHYPSEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 144 SGGEKQKIACASSSVLLPGIMVLDEPSSNLDmaaiDDLRQ-VLSLWK---KQGKTILIAEHRLYYLHDLADRVLYVKDGE 219
Cdd:PRK09493 138 SGGQQQRVAIARALAVKPKLMLFDEPTSALD----PELRHeVLKVMQdlaEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
....*....
gi 933767453 220 IEREYTPAE 228
Cdd:PRK09493 214 IAEDGDPQV 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
291-467 |
6.96e-22 |
|
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: 93.77 E-value: 6.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTLDWKARLKHCY-MVMQDtsHQLFTESVADEVL-------LSM 361
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGfIEPASGSIKVNDQSHTGLAPYQRPVsMLFQE--NNLFAHLTVRQNIglglhpgLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 362 DNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGK-T 440
Cdd:TIGR01277 102 NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQrT 181
|
170 180
....*....|....*....|....*..
gi 933767453 441 LLVITHDPELVMAGCSYVVHMEKGQVK 467
Cdd:TIGR01277 182 LLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-202 |
8.44e-22 |
|
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: 98.20 E-value: 8.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 4 FQNVSFSYgeESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAA 83
Cdd:TIGR02868 337 LRDLSAGY--PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-----PLQGEVTLDGVPVSSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 84 MVGSVFQNPksQFFNVDTDSELAFACENLgyPQEDILKRIDRTVSDYHIEDL-------MGRSVFALSGGEKQKIACASS 156
Cdd:TIGR02868 410 RVSVCAQDA--HLFDTTVRENLRLARPDA--TDEELWAALERVGLADWLRALpdgldtvLGEGGARLSGGERQRLALARA 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAA----IDDLRQVLSlwkkqGKTILIAEHRL 202
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETadelLEDLLAALS-----GRTVVLITHHL 530
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
288-466 |
1.05e-21 |
|
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: 92.94 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 288 LPVGETIAIIGLNGAGKSTLARCICGLE-KKCGFLQVEG---KTLDWKARlkHCYMVMQDtsHQLFTE-SVADEVLLS-- 360
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFEtPQSGRVLINGvdvTAAPPADR--PVSMLFQE--NNLFAHlTVEQNVGLGls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 ----MDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD--LKH-MREVArsLKS 433
Cdd:cd03298 97 pglkLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpaLRAeMLDLV--LDL 174
|
170 180 190
....*....|....*....|....*....|...
gi 933767453 434 LADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-481 |
1.25e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 97.69 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 18 GGIR---NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyeGKLEGDVLLDG-----KSVSDTP------LYDLAA 83
Cdd:PRK13549 16 GGVKaldNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPH---GTYEGEIIFEGeelqaSNIRDTEragiaiIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 84 MVG--SVFQNpksQF-------FNVDTDSELAFACENLgypqediLKRIDRTVSDYhiedlmgRSVFALSGGEKQKIACA 154
Cdd:PRK13549 93 LVKelSVLEN---IFlgneitpGGIMDYDAMYLRAQKL-------LAQLKLDINPA-------TPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 155 SSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGeiereytpaefdslsd 234
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG---------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 235 gtrKEIGLRPFS---------------LSKLKPanqYQAHTAKQ--MEFQNFCfAYkkrEPESLHIP-----SAELPVGE 292
Cdd:PRK13549 220 ---RHIGTRPAAgmteddiitmmvgreLTALYP---REPHTIGEviLEVRNLT-AW---DPVNPHIKrvddvSFSLRRGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 293 TIAIIGLNGAGKSTLARCICGL--EKKCGFLQVEGKtldwKARLKHCY--------MVMQD-TSHQLFTE-SVADEVLLS 360
Cdd:PRK13549 290 ILGIAGLVGAGRTELVQCLFGAypGRWEGEIFIDGK----PVKIRNPQqaiaqgiaMVPEDrKRDGIVPVmGVGKNITLA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 M-----------DNKDETVVDKILKQfdlLEYKDRHPL----SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMR 425
Cdd:PRK13549 366 AldrftggsridDAAELKTILESIQR---LKVKTASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 426 EVARSLKSLADQGKTLLVITHD-PElVMAGCSYVVHMEKGQVKESYPLDESGSKKVL 481
Cdd:PRK13549 443 EIYKLINQLVQQGVAIIVISSElPE-VLGLSDRVLVMHEGKLKGDLINHNLTQEQVM 498
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
291-466 |
1.43e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.28 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDWKARL----KHCYMVMQDTSHQLFTESVADEVLLSMDN-- 363
Cdd:PRK13644 28 GEYIGIIGKNGSGKSTLALHLNGLLRpQKGKVLVSGIDTGDFSKLqgirKLVGIVFQNPETQFVGRTVEEDLAFGPENlc 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 ----KDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGK 439
Cdd:PRK13644 108 lppiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK 187
|
170 180
....*....|....*....|....*..
gi 933767453 440 TLLVITHDPELVMAGCSYVVhMEKGQV 466
Cdd:PRK13644 188 TIVYITHNLEELHDADRIIV-MDRGKI 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
263-466 |
2.07e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.38 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 263 QMEFQNFCFAYKKREP---ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-----------------EKKCGFLQ 322
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdeknKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 323 VE------GKTLDWKARL-----KHCYMVMQDTSHQLFTESVADEVL---LSMD-NKDET--VVDKILKQFDL-LEYKDR 384
Cdd:PRK13651 82 KVleklviQKTRFKKIKKikeirRRVGVVFQFAEYQLFEQTIEKDIIfgpVSMGvSKEEAkkRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 385 HPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKG 464
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
..
gi 933767453 465 QV 466
Cdd:PRK13651 242 KI 243
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-222 |
2.34e-21 |
|
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: 97.20 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRL------VNGlvphyyegkleGDVLLDGKSVSD 75
Cdd:COG5265 358 VRFENVSFGYDPERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLlfrfydVTS-----------GRILIDGQDIRD 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 76 TPLYDLAAMVGSVFQNPksQFFNvDTdseLAFaceNLGY-----PQEDILKRIDRTvsdyHIED-----------LMGRS 139
Cdd:COG5265 425 VTQASLRAAIGIVPQDT--VLFN-DT---IAY---NIAYgrpdaSEEEVEAAARAA----QIHDfieslpdgydtRVGER 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 140 VFALSGGEKQKIACAssSVLL--PGIMVLDEPSSNLDMA---AI-DDLRQVlslwkKQGKTILIAEHRLYYLHDlADRVL 213
Cdd:COG5265 492 GLKLSGGEKQRVAIA--RTLLknPPILIFDEATSALDSRterAIqAALREV-----ARGRTTLVIAHRLSTIVD-ADEIL 563
|
250
....*....|
gi 933767453 214 YVKDGEI-ER 222
Cdd:COG5265 564 VLEAGRIvER 573
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-228 |
2.64e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.30 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGeessggG---IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTP 77
Cdd:PRK13548 2 MLEARNLSVRLG------GrtlLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-----SGEVRLNGRPLADWS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAMVGSVFQNpksqffnvdtdSELAFACE-----NLG-YPQEDILKRIDRTVSDY----HIEDLMGRSVFALSGGE 147
Cdd:PRK13548 71 PAELARRRAVLPQH-----------SSLSFPFTveevvAMGrAPHGLSRAEDDALVAAAlaqvDLAHLAGRDYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 148 KQKIACASssVLL--------PGIMVLDEPSSNLDMA-AIDDLRQVLSLWKKQGKTILIAehrlyyLHDL------ADRV 212
Cdd:PRK13548 140 QQRVQLAR--VLAqlwepdgpPRWLLLDEPTSALDLAhQHHVLRLARQLAHERGLAVIVV------LHDLnlaaryADRI 211
|
250
....*....|....*.
gi 933767453 213 LYVKDGEIEREYTPAE 228
Cdd:PRK13548 212 VLLHQGRLVADGTPAE 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
285-474 |
2.72e-21 |
|
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: 96.74 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLD-W-KARL-KHC-YMVmQDTshQLFTESVADEVLL 359
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPpTAGSVRLDGADLSqWdREELgRHIgYLP-QDV--ELFDGTIAENIAR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 SMDNKDETVV---------DKILKqfdlLE--YKDR---HPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMR 425
Cdd:COG4618 429 FGDADPEKVVaaaklagvhEMILR----LPdgYDTRigeGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEA 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 933767453 426 EVARSLKSLADQGKTLLVITHDPELvMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:COG4618 505 ALAAAIRALKARGATVVVITHRPSL-LAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
280-474 |
3.22e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.63 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTLDWKARLKHCYM-----------VMqdtsHQ 347
Cdd:COG4152 21 SFTVPK-----GEIFGLLGPNGAGKTTTIRIILGiLAPDSGEVLWDGEPLDPEDRRRIGYLpeerglypkmkVG----EQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 348 L--FTEsvadevLLSMDNKD-ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD---L 421
Cdd:COG4152 92 LvyLAR------LKGLSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpvnV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 933767453 422 KHMREVarsLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:COG4152 166 ELLKDV---IRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
20-224 |
3.97e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.90 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGlvphyYEGKLEGDVLLDGKSVSDTPLYDLAamVGSVFQNpKSQFFNV 99
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-----FEQPTAGQIMLDGVDLSHVPPYQRP--INMMFQS-YALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 100 DTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAID 179
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 933767453 180 DLR-QVLSLWKKQGKTILIAEHRLYYLHDLADRVL------YVKDGEIEREY 224
Cdd:PRK11607 187 RMQlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAimnrgkFVQIGEPEEIY 238
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-220 |
4.13e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.28 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEGKLEGDVLLDGKSVSDTPLYDL 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEV---LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPK-----SQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASS 156
Cdd:PRK14247 81 RRRVQMVFQIPNpipnlSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 157 SVLLPGIMVLDEPSSNLD---MAAIDDLrqVLSLwkKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDpenTAKIESL--FLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
291-449 |
4.46e-21 |
|
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: 92.71 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGK---TLDWKA----RLKHCYMVMQdtSHQLFTE-SVADEVLLSM 361
Cdd:cd03294 50 GEIFVIMGLSGSGKSTLLRCINRLiEPTSGKVLIDGQdiaAMSRKElrelRRKKISMVFQ--SFALLPHrTVLENVAFGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 362 D------NKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSL- 434
Cdd:cd03294 128 EvqgvprAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLq 207
|
170
....*....|....*
gi 933767453 435 ADQGKTLLVITHDPE 449
Cdd:cd03294 208 AELQKTIVFITHDLD 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
280-446 |
5.16e-21 |
|
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: 91.12 E-value: 5.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEK----KCGFLQVEgkTLDWKARLKHCYMVMQdtSHQLFTESVAD 355
Cdd:cd03268 20 SLHVKK-----GEIYGFLGPNGAGKTTTMKIILGLIKpdsgEITFDGKS--YQKNIEALRRIGALIE--APGFYPNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 356 EVLLSMDN---KDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLK 432
Cdd:cd03268 91 ENLRLLARllgIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELIL 170
|
170
....*....|....
gi 933767453 433 SLADQGKTLLVITH 446
Cdd:cd03268 171 SLRDQGITVLISSH 184
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-220 |
5.24e-21 |
|
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: 91.78 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL-VPHyyegklEGDVLLDGKSVSDTPLYD 80
Cdd:cd03252 1 ITFEHVRFRYKPDGPVI-LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPE------NGRVLVDGHDLALADPAW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQnpKSQFFNVDTDSELAFAceNLGYPQEDILKRIdrTVSDYH---------IEDLMGRSVFALSGGEKQKI 151
Cdd:cd03252 74 LRRQVGVVLQ--ENVLFNRSIRDNIALA--DPGMSMERVIEAA--KLAGAHdfiselpegYDTIVGEQGAGLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 152 ACASSSVLLPGIMVLDEPSSNLDM----AAIDDLRQVLSlwkkqGKTILIAEHRLYYLHDlADRVLYVKDGEI 220
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYesehAIMRNMHDICA-----GRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
291-471 |
5.28e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.91 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGK---TLDWKARLKHCYMVMQDTSHQlFTESVADEV--------- 357
Cdd:PRK09536 29 GSLVGLVGPNGAGKTTLLRAINGtLTPTAGTVLVAGDdveALSARAASRRVASVPQDTSLS-FEFDVRQVVemgrtphrs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 358 -LLSMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAD 436
Cdd:PRK09536 108 rFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVD 187
|
170 180 190
....*....|....*....|....*....|....*
gi 933767453 437 QGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYP 471
Cdd:PRK09536 188 DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-200 |
5.35e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 92.23 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGeessGGG-----IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSd 75
Cdd:COG4525 3 MLTVRHVSVRYP----GGGqpqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA-----PSSGEITLDGVPVT- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 76 TPlydlAAMVGSVFQN----P-KSQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQK 150
Cdd:COG4525 73 GP----GADRGVVFQKdallPwLNVLDNV------AFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 151 IACASSSVLLPGIMVLDEPssnldMAAIDDL-RQ-----VLSLWKKQGKTILIAEH 200
Cdd:COG4525 143 VGIARALAADPRFLLMDEP-----FGALDALtREqmqelLLDVWQRTGKGVFLITH 193
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
264-465 |
6.22e-21 |
|
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: 90.61 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPES---LHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTldwkarlkhCYm 339
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSVSVPGSI---------AY- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 vmqdTSHQ--LFTESVADEVL--LSMDNKD-ETVVD--------KILKQFDLLEYKDRHpLSLSGGQKQRVAIASAIVSN 406
Cdd:cd03250 71 ----VSQEpwIQNGTIRENILfgKPFDEERyEKVIKacalepdlEILPDGDLTEIGEKG-INLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 407 REIIVFDEPTSGLDlkhmREVARSL------KSLADqGKTLLVITHDPELVMAgCSYVVHMEKGQ 465
Cdd:cd03250 146 ADIYLLDDPLSAVD----AHVGRHIfencilGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-234 |
6.79e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.80 E-value: 6.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGeeSSGGGIRNVNLTINTGEFVLLTGESGCGKTTitrLVNgLVPHYYEGKlEGDVLLDGKSVSDTPLYDL 81
Cdd:PRK13657 335 VEFDDVSFSYD--NSRQGVEDVSFEAKPGQTVAIVGPTGAGKST---LIN-LLQRVFDPQ-SGRILIDGTDIRTVTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFFNVD------------TDSELAFACEnLGYPQEDILKRIDRTvsDYHIEDlMGRSvfaLSGGEKQ 149
Cdd:PRK13657 408 RRNIAVVFQDA--GLFNRSiednirvgrpdaTDEEMRAAAE-RAQAHDFIERKPDGY--DTVVGE-RGRQ---LSGGERQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 150 KIACASSSVLLPGIMVLDEPSSNLDM-------AAIDDLRqvlslwkkQGKTILIAEHRLYYLHDlADRVLYVKDGE-IE 221
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVeteakvkAALDELM--------KGRTTFIIAHRLSTVRN-ADRILVFDNGRvVE 549
|
250
....*....|...
gi 933767453 222 ReytpAEFDSLSD 234
Cdd:PRK13657 550 S----GSFDELVA 558
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
285-466 |
7.89e-21 |
|
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: 91.64 E-value: 7.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCIcglekkCGFLQ-------VEGKTLDwkaRLKhcymvmqdtSHQ---------- 347
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNLI------TGFYRptsgrilFDGRDIT---GLP---------PHRiarlgiartf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 348 ----LFTE-SVADEVLLSMDNKD---------------------ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIAS 401
Cdd:COG0411 86 qnprLFPElTVLENVLVAAHARLgrgllaallrlprarreereaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 402 AIVSNREIIVFDEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-471 |
9.91e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.31 E-value: 9.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 6 NVSFSYgEESSGGGIRNVNLTINTGEFVLLTGESGCGKTtITRLVNGLVPHYYEGKLEGDVLL---------DGKSVSDT 76
Cdd:PRK10261 19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKS-VTALALMRLLEQAGGLVQCDKMLlrrrsrqviELSEQSAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLYDL-AAMVGSVFQNPKSQFFNVDTDSELAFACENL--GYPQEDILKRIDRTVSDYHI---EDLMGRSVFALSGGEKQK 150
Cdd:PRK10261 97 QMRHVrGADMAMIFQEPMTSLNPVFTVGEQIAESIRLhqGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 151 IACASSSVLLPGIMVLDEPSSNLDM---AAIDDLRQVLSlwKKQGKTILIAEHRLYYLHDLADRVLY------VKDGEIE 221
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVtiqAQILQLIKVLQ--KEMSMGVIFITHDMGVVAEIADRVLVmyqgeaVETGSVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 222 R-------EYTPAEFDSLSD-GTRKEIGL-RPFSLSKLKPANQYQAHTAKQ--------MEFQNFC---------FAYKK 275
Cdd:PRK10261 255 QifhapqhPYTRALLAAVPQlGAMKGLDYpRRFPLISLEHPAKQEPPIEQDtvvdgepiLQVRNLVtrfplrsglLNRVT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 276 REPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLD------WKARLKHCYMVMQDTSHQL 348
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLvESQGGEIIFNGQRIDtlspgkLQALRRDIQFIFQDPYASL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 349 FT-ESVADEVL-------LSMDNKDETVVDKILKQFDLL-EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGL 419
Cdd:PRK10261 415 DPrQTVGDSIMeplrvhgLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 933767453 420 DLKHMREVARSLKSLA-DQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYP 471
Cdd:PRK10261 495 DVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
291-466 |
1.44e-20 |
|
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: 90.12 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEG-----KTLDWKARLKhcymVMQDtSHQLFTESVADEVL-----L 359
Cdd:cd03266 31 GEVTGLLGPNGAGKTTTLRMLAGLlEPDAGFATVDGfdvvkEPAEARRRLG----FVSD-STGLYDRLTARENLeyfagL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 SMDNKDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ 437
Cdd:cd03266 106 YGLKGDELTarLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL 185
|
170 180
....*....|....*....|....*....
gi 933767453 438 GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03266 186 GKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
291-487 |
1.49e-20 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 90.30 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTldwkARLKHCYMVMQDTSHQL---FTESVADEVLLSMDNK-- 364
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAkGTVKVAGAS----PGKGWRHIGYVPQRHEFawdFPISVAHTVMSGRTGHig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 365 --------DETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAD 436
Cdd:TIGR03771 82 wlrrpcvaDFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 933767453 437 QGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDESGSKKVLDFFRIR 487
Cdd:TIGR03771 162 AGTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
281-481 |
1.72e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 90.28 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLD-----WKARLKHCYmVMQdtSHQLFTE-SV 353
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPvKSGSIRLDGEDITklpphERARAGIAY-VPQ--GREIFPRlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 ADEVLLSMDN---KDETVVDKILKQFDLL-EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVAR 429
Cdd:TIGR03410 93 EENLLTGLAAlprRSRKIPDEIYELFPVLkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 430 SLKSLADQGK-TLLVITHDPELVMAGCSYVVHMEKGQVKESYP---LDESGSKKVL 481
Cdd:TIGR03410 173 VIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAgdeLDEDKVRRYL 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-228 |
2.35e-20 |
|
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: 89.80 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 18 GGIR---NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDLAAM-VGSVFQNPK 93
Cdd:cd03219 11 GGLValdDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-----SGSVLFDGEDITGLPPHEIARLgIGRTFQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 94 -----SQFFNVDT----DSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQK----IACASSsvll 160
Cdd:cd03219 86 lfpelTVLENVMVaaqaRTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRleiaRALATD---- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 161 PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVlYVKD-GEIEREYTPAE 228
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRV-TVLDqGRVIAEGTPDE 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-228 |
2.40e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITrlvnGLVPHYYEgKLEGDVLLDGKSVSDTPLYDL 81
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVA----ALLQNLYQ-PTGGQVLLDGVPLVQYDHHYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFFNVDTDSELAFACENlgYPQEDILKR---------IDRTVSDYHIEdlMGRSVFALSGGEKQKIA 152
Cdd:TIGR00958 554 HRQVALVGQEP--VLFSGSVRENIAYGLTD--TPDEEIMAAakaanahdfIMEFPNGYDTE--VGEKGSQLSGGQKQRIA 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLDMAAiddlRQVLSLWKK-QGKTILIAEHRLYYLHDlADRVLYVKDGEIEREYTPAE 228
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAEC----EQLLQESRSrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQ 699
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-228 |
2.58e-20 |
|
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: 90.40 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 19 GIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAM----VGSVFQN--- 91
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE-----PTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSfal 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 92 -P-KSQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEP 169
Cdd:cd03294 114 lPhRTVLENV------AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 170 SSNLDMAAIDDLR-QVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:cd03294 188 FSALDPLIRREMQdELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
287-468 |
2.77e-20 |
|
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: 89.42 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-----DWKARL--KHCYMVMQdtSHQL---FT--ESV 353
Cdd:COG4181 34 EVEAGESVAIVGASGSGKSTLLGLLAGLDRpTSGTVRLAGQDLfaldeDARARLraRHVGFVFQ--SFQLlptLTalENV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 ADEVLLSMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKS 433
Cdd:COG4181 112 MLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFE 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 933767453 434 L-ADQGKTLLVITHDPELVmAGCSYVVHMEKGQVKE 468
Cdd:COG4181 192 LnRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
2.78e-20 |
|
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: 87.48 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGeessggGI---RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVS-DTP 77
Cdd:cd03216 1 LELRGITKRFG------GVkalDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-----SGEILVDGKEVSfASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAMVGSVFQnpksqffnvdtdselafacenlgypqedilkridrtvsdyhiedlmgrsvfaLSGGEKQKIACASSS 157
Cdd:cd03216 70 RDARRAGIAMVYQ----------------------------------------------------LSVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 158 VLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
278-448 |
3.69e-20 |
|
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: 93.19 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 278 PESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEG---KTLDWKARLKHCYMVMQDtSHqLFTESV 353
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDGvpvSSLDQDEVRRRVSVCAQD-AH-LFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 ADEVLLSMDNKDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLK 422
Cdd:TIGR02868 426 RENLRLARPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170 180
....*....|....*....|....*.
gi 933767453 423 HMREVARSLKSlADQGKTLLVITHDP 448
Cdd:TIGR02868 506 TADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
264-469 |
4.21e-20 |
|
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: 87.75 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGK-TLDWKARLKHCYMVM 341
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVpVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 342 QDTSHqLFtesvadevllsmdnkDETVVDKILKQFdlleykdrhplslSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL 421
Cdd:cd03247 81 NQRPY-LF---------------DTTLRNNLGRRF-------------SGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 933767453 422 KHMREVARSLKSLAdQGKTLLVITHDpelvMAGCSY---VVHMEKGQVKES 469
Cdd:cd03247 132 ITERQLLSLIFEVL-KDKTLIWITHH----LTGIEHmdkILFLENGKIIMQ 177
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
270-448 |
4.38e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.19 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 270 CFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLE----KKCGFLQVEGKTLD-WKARLKHCYmVMQDt 344
Cdd:TIGR00955 30 CFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgvKGSGSVLLNGMPIDaKEMRAISAY-VQQD- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 345 shQLFTESV-ADEVL-----LSMDN---KDETV--VDKILKQFDLLEYKD-------RHPlSLSGGQKQRVAIASAIVSN 406
Cdd:TIGR00955 108 --DLFIPTLtVREHLmfqahLRMPRrvtKKEKRerVDEVLQALGLRKCANtrigvpgRVK-GLSGGERKRLAFASELLTD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933767453 407 REIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDP 448
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQP 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-221 |
4.63e-20 |
|
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: 88.51 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINtGEFVLLTGESGCGKTTITRLVNGLV-PHYYEGKLEGDVLLDGKSVSDTPLYDLAamVGSVFQNpKSQFFNVD 100
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEkPDGGTIVLNGTVLFDSRKKINLPPQQRK--IGLVFQQ-YALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 101 TDSELAFACEnlGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDD 180
Cdd:cd03297 92 VRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933767453 181 LRQVLSLWKKQ-GKTILIAEHRLYYLHDLADRVLYVKDGEIE 221
Cdd:cd03297 170 LLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
264-466 |
7.48e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREP---ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQV-------EGKTLDWKA 332
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGKVTVgdivvssTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 333 RLKHCYMVMQDTSHQLFTESVADEVLLSMDN------KDETVVDKILKQFDLL-EYKDRHPLSLSGGQKQRVAIASAIVS 405
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQNfgipkeKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 406 NREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-223 |
8.42e-20 |
|
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: 86.60 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTITRLVNG-LVPhyyegkLEGDVLLDGKSVSDtplyd 80
Cdd:cd03247 1 LSINNVSFSYPEQEQQV-LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKP------QQGEITLDGVPVSD----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 laamvgsvFQNPKSQFFNVDTDSELAFAC---ENLGYPqedilkridrtvsdyhiedlmgrsvfaLSGGEKQKIACAssS 157
Cdd:cd03247 69 --------LEKALSSLISVLNQRPYLFDTtlrNNLGRR---------------------------FSGGERQRLALA--R 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 158 VLLPG--IMVLDEPSSNLDmaAIDDlRQVLSLWKKQ--GKTILIAEHRLYYLHDlADRVLYVKDGEIERE 223
Cdd:cd03247 112 ILLQDapIVLLDEPTVGLD--PITE-RQLLSLIFEVlkDKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-228 |
8.83e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.91 E-value: 8.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEGKLEGDVLLDGKSVSDTPLYD-----------LAAMVGSV 88
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 89 FQNPKSQFFNVDTDSELAFACENLGYPQEDILKRidrtvSDYHIE------DLMGRSVFALSGGEKQKIACASSSVLLPG 162
Cdd:PRK13631 122 FQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKL-----AKFYLNkmglddSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 163 IMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
252-469 |
9.42e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.20 E-value: 9.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 252 PANQYQAHTAKQMEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCIC-GLEKKCGFLQVEGKTL-D 329
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNGQPIaD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 330 WK-ARLKHCYMVMQDTSHqLFTESVADEVLLSMDNKDETVVDKILKQF---DLLEykDRHPLS---------LSGGQKQR 396
Cdd:PRK11160 407 YSeAALRQAISVVSQRVH-LFSATLRDNLLLAAPNASDEALIEVLQQVgleKLLE--DDKGLNawlgeggrqLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 397 VAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHdpELV-MAGCSYVVHMEKGQVKES 469
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH--RLTgLEQFDRICVMDNGQIIEQ 554
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-229 |
9.74e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.16 E-value: 9.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDLAAM-VG------SVFQNp 92
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-----SGRIFLDGEDITHLPMHKRARLgIGylpqeaSIFRK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 93 ksqfFNVDtDSELAFAcENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQK--IA--CASSsvllPGIMVLDE 168
Cdd:COG1137 93 ----LTVE-DNILAVL-ELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRveIAraLATN----PKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 169 PSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEF 229
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
265-465 |
9.80e-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: 85.58 E-value: 9.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKR---EPESLHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEKkcgflQVEGkTLDWKARLKHCYMvm 341
Cdd:cd03221 2 ELENLSKTYGGKlllKDISLTINP-----GDRIGLVGRNGAGKSTLLKLIAGELE-----PDEG-IVTWGSTVKIGYF-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 342 qdtsHQLftesvadevllsmdnkdetvvdkilkqfdlleykdrhplslSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL 421
Cdd:cd03221 69 ----EQL-----------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 933767453 422 KHMREVARSLKSLadQGkTLLVITHDPELVMAGCSYVVHMEKGQ 465
Cdd:cd03221 104 ESIEALEEALKEY--PG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-218 |
1.14e-19 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 87.91 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVsDTPLYDlaAMVgsVFQN----Pksq 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-----AQPTSGGVILEGKQI-TEPGPD--RMV--VFQNysllP--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 96 FFNVDTDSELAFACENLGYPQEDilkriDRTVSDYHIeDLMGRSVFA------LSGGEKQKIACASSSVLLPGIMVLDEP 169
Cdd:TIGR01184 68 WLTVRENIALAVDRVLPDLSKSE-----RRAIVEEHI-ALVGLTEAAdkrpgqLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 933767453 170 SSNLDMAAIDDLR-QVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDG 218
Cdd:TIGR01184 142 FGALDALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
1.31e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.22 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTT----ITRLVnglvphyyeGKLEGDVLLDGKSVSDT 76
Cdd:COG4604 1 MIEIKNVSKRYGGKVV---LDDVSLTIPKGGITALIGPNGAGKSTllsmISRLL---------PPDSGEVLVDGLDVATT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLYDLAAMVGSVFQNPksqFFNVD-TDSEL-AFacenlG-YP-------QEDiLKRIDRTVSDYHIEDLMGRSVFALSGG 146
Cdd:COG4604 69 PSRELAKRLAILRQEN---HINSRlTVRELvAF-----GrFPyskgrltAED-REIIDEAIAYLDLEDLADRYLDELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 147 EKQK--IAcasssvllpgiMV---------LDEPSSNLDMA-AIDDLRQVLSLWKKQGKTILIAehrlyyLHDL------ 208
Cdd:COG4604 140 QRQRafIA-----------MVlaqdtdyvlLDEPLNNLDMKhSVQMMKLLRRLADELGKTVVIV------LHDInfascy 202
|
250 260
....*....|....*....|
gi 933767453 209 ADRVLYVKDGEIEREYTPAE 228
Cdd:COG4604 203 ADHIVAMKDGRVVAQGTPEE 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
261-466 |
1.37e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 261 AKQMEFQNFCFAYKKREP---ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLekkcgFLQVEGKTL--DWK--AR 333
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL-----IISETGQTIvgDYAipAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 334 LKHCY----------MVMQDTSHQLFTESVADEVL---LSMDNKDETVVDKILKQFDLL----EYKDRHPLSLSGGQKQR 396
Cdd:PRK13645 79 LKKIKevkrlrkeigLVFQFPEYQLFQETIEKDIAfgpVNLGENKQEAYKKVPELLKLVqlpeDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 397 VAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
264-473 |
1.61e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.65 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREP---ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLE-KKCGFLQVEG-------KTLDWKA 332
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRVDDtlitstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 333 RLKHCYMVMQDTSHQLFTESVADEVLLSMDN---KDETVVDKILKQFDLL----EYKDRHPLSLSGGQKQRVAIASAIVS 405
Cdd:PRK13649 83 IRKKVGLVFQFPESQLFEETVLKDVAFGPQNfgvSQEEAEALAREKLALVgiseSLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 406 NREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQ-VKESYPLD 473
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKlVLSGKPKD 231
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
287-466 |
1.70e-19 |
|
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: 88.99 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDWKARL--KHCYMVMQDTShqlftesvADEVLLSMDN 363
Cdd:TIGR01188 15 KVREGEVFGFLGPNGAGKTTTIRMLTTLLRpTSGTARVAGYDVVREPRKvrRSIGIVPQYAS--------VDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 -----------KD--ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARS 430
Cdd:TIGR01188 87 lemmgrlyglpKDeaEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 933767453 431 LKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:TIGR01188 167 IRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRI 202
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
265-468 |
1.85e-19 |
|
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: 91.42 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYkkrEPES--LHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEG---KTLDWKARLKHCY 338
Cdd:COG5265 359 RFENVSFGY---DPERpiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFyDVTSGRILIDGqdiRDVTQASLRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 MVMQDTShqLFTESVA------------DEV------------LLSMDNKDETVV-DKILKqfdlleykdrhplsLSGGQ 393
Cdd:COG5265 436 IVPQDTV--LFNDTIAyniaygrpdaseEEVeaaaraaqihdfIESLPDGYDTRVgERGLK--------------LSGGE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 394 KQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHdpELvmagcSYVVH------MEKGQVK 467
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAH--RL-----STIVDadeilvLEAGRIV 571
|
.
gi 933767453 468 E 468
Cdd:COG5265 572 E 572
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-249 |
1.89e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 87.68 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 23 VNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyegklEGDVLLDGKSVSDTPLYDLAAMVGSVFQNpKSQFFNVDTD 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG------SGSIQFAGQPLEAWSAAELARHRAYLSQQ-QTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 103 SELAfacenLGYPQ----EDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASssVLL---PGI------MVLDEP 169
Cdd:PRK03695 88 QYLT-----LHQPDktrtEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAA--VVLqvwPDInpagqlLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 170 SSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIereytpaefdsLSDGTRKEIgLRPFSLSK 249
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKL-----------LASGRRDEV-LTPENLAQ 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
291-466 |
1.96e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.62 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKARLKHCYMVMQdtSHQLFTE-SVADEVL--LSMDN-- 363
Cdd:PRK09452 40 GEFLTLLGPSGCGKTTVLRLIAGFETpDSGRIMLDGQDItHVPAENRHVNTVFQ--SYALFPHmTVFENVAfgLRMQKtp 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 KDE--TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ-GKT 440
Cdd:PRK09452 118 AAEitPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGIT 197
|
170 180
....*....|....*....|....*.
gi 933767453 441 LLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK09452 198 FVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
291-466 |
2.06e-19 |
|
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: 85.56 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDWK----ARLKHCYMVMQDTSHQ-LF-TESVADEVLLsmdn 363
Cdd:cd03215 26 GEIVGIAGLVGNGQTELAEALFGLRPPAsGEITLDGKPVTRRsprdAIRAGIAYVPEDRKREgLVlDLSVAENIAL---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 kdetvvdkilkqfdlleykdrhPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLV 443
Cdd:cd03215 102 ----------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLL 159
|
170 180
....*....|....*....|...
gi 933767453 444 ITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03215 160 ISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-220 |
2.25e-19 |
|
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: 86.39 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESsgggiRNVNLTINTGEFVLLTGESGCGKTTITRLVNGlvphyYEGKLEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAG-----FETPQSGRVLINGVDVTAAPPADR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AamVGSVFQ-NPKSQFFNVDTDSELAFAcENLGYPQEDiLKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLL 160
Cdd:cd03298 71 P--VSMLFQeNNLFAHLTVEQNVGLGLS-PGLKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 161 PGIMVLDEPSSNLDMAAIDDLRQ-VLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDlVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
265-474 |
2.39e-19 |
|
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: 86.82 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKRePESLHIP--SAELPVGETIAIIGLNGAGKSTlarCICGLEK----KCGFLQVEG---KTLDWKARLK 335
Cdd:cd03249 2 EFKNVSFRYPSR-PDVPILKglSLTIPPGKTVALVGSSGCGKST---VVSLLERfydpTSGEILLDGvdiRDLNLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 336 HCYMVMQDTshQLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQRVAIASAIV 404
Cdd:cd03249 78 QIGLVSQEP--VLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 405 SNREIIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELVM-AGCSYVvhMEKGQVKESYPLDE 474
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRnADLIAV--LQNGQVVEQGTHDE 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
291-466 |
2.48e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.47 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTLDWK----ARLKHCYMVmqdtsHQLFT--E--SVADEVLLSM 361
Cdd:COG3845 31 GEIHALLGENGAGKSTLMKILYGLYQPdSGEILIDGKPVRIRsprdAIALGIGMV-----HQHFMlvPnlTVAENIVLGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 362 DNKDETVVD--KILKQfdLLEYKDRHPL---------SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARS 430
Cdd:COG3845 106 EPTKGGRLDrkAARAR--IRELSERYGLdvdpdakveDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEI 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 933767453 431 LKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG3845 184 LRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
265-474 |
2.65e-19 |
|
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: 91.17 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGK---TLDWKARLKHCYMV 340
Cdd:TIGR03797 453 EVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETpESGSVFYDGQdlaGLDVQAVRRQLGVV 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTshQLFTESVADEVL----LSMDNKDETvvdkiLKQFDLLEYKDRHPL-----------SLSGGQKQRVAIASAIVS 405
Cdd:TIGR03797 533 LQNG--RLMSGSIFENIAggapLTLDEAWEA-----ARMAGLAEDIRAMPMgmhtvisegggTLSGGQRQRLLIARALVR 605
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 406 NREIIVFDEPTSGLDLKHMREVARSLKSLAdqgKTLLVITHDPELVMaGCSYVVHMEKGQVKESYPLDE 474
Cdd:TIGR03797 606 KPRILLFDEATSALDNRTQAIVSESLERLK---VTRIVIAHRLSTIR-NADRIYVLDAGRVVQQGTYDE 670
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-228 |
3.28e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.01 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEGKLEGDVLLDGKSV--SDTPLY 79
Cdd:COG1117 12 IEVRNLNVYYGDKQA---LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFQNP----KSQFFNVdtdselAFACENLGYPQEDILKRIDRT----------VSDyhieDLmGRSVFALSG 145
Cdd:COG1117 89 ELRRRVGMVFQKPnpfpKSIYDNV------AYGLRLHGIKSKSELDEIVEEslrkaalwdeVKD----RL-KKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 146 GEKQK--IACA---SSSVLLpgimvLDEPSSNLD---MAAIDDLrqVLSLwkKQGKTILIAEH------RlyylhdLADR 211
Cdd:COG1117 158 GQQQRlcIARAlavEPEVLL-----MDEPTSALDpisTAKIEEL--ILEL--KKDYTIVIVTHnmqqaaR------VSDY 222
|
250
....*....|....*..
gi 933767453 212 VLYVKDGEIErEYTPAE 228
Cdd:COG1117 223 TAFFYLGELV-EFGPTE 238
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-223 |
3.39e-19 |
|
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: 85.71 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGeesSGGGIRNVNLTINTGEFVLLtGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYdL 81
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTP-----PSSGTIRIDGQDVLKQPQK-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPkSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLP 161
Cdd:cd03264 71 RRRIGYLPQEF-GVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 162 GIMVLDEPSSNLDMAAIDDLRQVLS-LwkKQGKTILIAEHRLYYLHDLADRVLYVKDGEIERE 223
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSeL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
296-466 |
3.71e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.37 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 296 IIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDWKAR-----LKHCYMVMQDTSHQLFTESVADEVLLSMDN----KD 365
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRpQKGAVLWQGKPLDYSKRgllalRQQVATVFQDPEQQIFYTDIDSDIAFSLRNlgvpEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 366 ETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLV 443
Cdd:PRK13638 112 EITrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVII 191
|
170 180
....*....|....*....|...
gi 933767453 444 ITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK13638 192 SSHDIDLIYEISDAVYVLRQGQI 214
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
288-447 |
3.93e-19 |
|
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: 86.65 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 288 LPV---GETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGktlDWKARLKHcymvMQDTSHQLFTESVADE------- 356
Cdd:cd03236 20 LPVpreGQVLGLVGPNGIGKSTALKILAGkLKPNLGKFDDPP---DWDEILDE----FRGSELQNYFTKLLEGdvkvivk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 357 --------------VLLSMDNKDET-VVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL 421
Cdd:cd03236 93 pqyvdlipkavkgkVGELLKKKDERgKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*.
gi 933767453 422 KHMREVARSLKSLADQGKTLLVITHD 447
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-220 |
5.05e-19 |
|
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: 85.99 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDtplYD- 80
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ-----PQGGQVLLDGKPISQ---YEh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 --LAAMVGSVFQNPksQFFNVDTDSELAFACEnlGYPQEDILKRIDRTVSDYHIEDL-------MGRSVFALSGGEKQKI 151
Cdd:cd03248 84 kyLHSKVSLVGQEP--VLFARSLQDNIAYGLQ--SCSFECVKEAAQKAHAHSFISELasgydteVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 152 ACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWkKQGKTILIAEHRLYYLHDlADRVLYVKDGEI 220
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDW-PERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
291-466 |
5.26e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.17 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGK---TLDWKA----RLKHCYMVMQdTSHQLFTESVADEVLL--- 359
Cdd:PRK10535 34 GEMVAIVGASGSGKSTLMNILGCLDKpTSGTYRVAGQdvaTLDADAlaqlRREHFGFIFQ-RYHLLSHLTAAQNVEVpav 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 ---SMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAD 436
Cdd:PRK10535 113 yagLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD 192
|
170 180 190
....*....|....*....|....*....|
gi 933767453 437 QGKTLLVITHDPElVMAGCSYVVHMEKGQV 466
Cdd:PRK10535 193 RGHTVIIVTHDPQ-VAAQAERVIEIRDGEI 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-231 |
5.89e-19 |
|
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: 85.56 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDLAAM 84
Cdd:cd03224 4 ENLNAGYGKSQI---LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR-----SGSIRFDGRDITGLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 85 -VGSVFQNPksQFF---NVDtdselafacENL-----GYPQEDILKRIDRtVSDY--HIEDLMGRSVFALSGGEKQKIAC 153
Cdd:cd03224 76 gIGYVPEGR--RIFpelTVE---------ENLllgayARRRAKRKARLER-VYELfpRLKERRKQLAGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 154 ASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFDS 231
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-234 |
6.47e-19 |
|
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: 87.86 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 23 VNLTINTGEFVLLTGESGCGKTTITRLVNGLVpHYYEGKLE--GDVLLDGKSVSDTPLYDLAamVGSVFQNpKSQFFNVD 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLT-RPDEGEIVlnGRTLFDSRKGIFLPPEKRR--IGYVFQE-ARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 101 TDSELAFACENLGYPQEDIlkRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDD 180
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRI--SFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 181 LRQVL-SLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFDSLSD 234
Cdd:TIGR02142 170 ILPYLeRLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
285-471 |
9.62e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 9.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEK------------KCGFLQ-----VEGKTL------------DWKARLK 335
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEpdsgevsipkglRIGYLPqepplDDDLTVldtvldgdaelrALEAELE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 336 HCYMVMQDTSHQLFTESVADEVLLSMDNKD-ETVVDKILKQFDLLEYKDRHPLS-LSGGQKQRVAIASAIVSNREIIVFD 413
Cdd:COG0488 98 ELEAKLAEPDEDLERLAELQEEFEALGGWEaEARAEEILSGLGFPEEDLDRPVSeLSGGWRRRVALARALLSEPDLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 414 EPTSGLDLkhmrEVARSLKS-LADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKeSYP 471
Cdd:COG0488 178 EPTNHLDL----ESIEWLEEfLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLT-LYP 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
291-447 |
1.03e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.39 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDWKARLKHCY-MVMQdtSHQLFTE-SVADEVL--LSMDNKD 365
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLFIGEKRMNDVPPAERGVgMVFQ--SYALYPHlSVAENMSfgLKLAGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 366 ETVVDK-------ILKQFDLLeykDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD--LK-HMR-EVARSLKSL 434
Cdd:PRK11000 107 KEEINQrvnqvaeVLQLAHLL---DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaaLRvQMRiEISRLHKRL 183
|
170
....*....|...
gi 933767453 435 adqGKTLLVITHD 447
Cdd:PRK11000 184 ---GRTMIYVTHD 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-220 |
1.05e-18 |
|
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: 84.12 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTitrLVNGLVPHYYEGKLEGDVLLDGKSVSDTPLYDLAAM-VGSVFQNPKsqffn 98
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKST---LAKTIMGHPKYEVTEGEILFKGEDITDLPPEERARLgIFLAFQYPP----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 vdtdselafacenlgypqedilkridrTVSDYHIEDLMgRSVFA-LSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAA 177
Cdd:cd03217 88 ---------------------------EIPGVKNADFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 933767453 178 IDDLRQVLSLWKKQGKTILIAEHRLYYL-HDLADRVLYVKDGEI 220
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHYQRLLdYIKPDRVHVLYDGRI 183
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
287-468 |
1.06e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.83 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPV--GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDW-------KARLKHCYMVMQD-----TSHQLftE 351
Cdd:PRK10584 30 ELVVkrGETIALIGESGSGKSTLLAILAGLDDgSSGEVSLVGQPLHQmdeearaKLRAKHVGFVFQSfmlipTLNAL--E 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 352 SVADEVLL--SMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVAR 429
Cdd:PRK10584 108 NVELPALLrgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 933767453 430 SLKSL-ADQGKTLLVITHDPELVmAGCSYVVHMEKGQVKE 468
Cdd:PRK10584 188 LLFSLnREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQE 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
285-447 |
1.27e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 86.71 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTL------DWKARLKHCYMVMQD---------TSHQL 348
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTsGEILFDGQDItglsgrELRPLRRRMQMVFQDpyaslnprmTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 349 FTESVADEVLLSMDNKDETVVDkILKQFDLL-EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLkhmrev 427
Cdd:COG4608 118 IAEPLRIHGLASKAERRERVAE-LLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV------ 190
|
170 180
....*....|....*....|....*....
gi 933767453 428 arS--------LKSLADQ-GKTLLVITHD 447
Cdd:COG4608 191 --SiqaqvlnlLEDLQDElGLTYLFISHD 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-220 |
1.35e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTITRLVNglvpHYYEGKlEGDVLLDGKSVSDTPLYDL 81
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPV-LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT----RAWDPQ-QGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFFNVDTDSELAFACENlgyPQEDILKRIDRTVS-DYHIEDLM---------GRsvfALSGGEKQKI 151
Cdd:PRK11160 413 RQAISVVSQRV--HLFSATLRDNLLLAAPN---ASDEALIEVLQQVGlEKLLEDDKglnawlgegGR---QLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 152 ACAssSVLL---PgIMVLDEPSSNLDMaaiDDLRQVLSLWKK--QGKTILIAEHRLYYLHDLaDRVLYVKDGEI 220
Cdd:PRK11160 485 GIA--RALLhdaP-LLLLDEPTEGLDA---ETERQILELLAEhaQNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
264-466 |
1.50e-18 |
|
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: 84.69 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYK--KREPESLHIPSaelpvGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTL-DWKARLKHCYM 339
Cdd:cd03299 1 LKVENLSKDWKefKLKNVSLEVER-----GDYFVILGPTGSGKSVLLETIAGfIKPDSGKILLNGKDItNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 VMQDtsHQLFTE-SVADEVLLSMDNK------DETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVF 412
Cdd:cd03299 76 VPQN--YALFPHmTVYKNIAYGLKKRkvdkkeIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 413 DEPTSGLDLKhMREVARS-LKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03299 154 DEPFSALDVR-TKEKLREeLKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
296-466 |
1.64e-18 |
|
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: 86.39 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 296 IIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-DWKARLKHCYMVMQdtSHQLFTE-SVADEVL--LSMDNKD-ETV- 368
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQpDSGSIMLDGEDVtNVPPHLRHINMVFQ--SYALFPHmTVEENVAfgLKMRKVPrAEIk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 369 --VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ-GKTLLVIT 445
Cdd:TIGR01187 79 prVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFVFVT 158
|
170 180
....*....|....*....|.
gi 933767453 446 HDPELVMAGCSYVVHMEKGQV 466
Cdd:TIGR01187 159 HDQEEAMTMSDRIAIMRKGKI 179
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-222 |
1.65e-18 |
|
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: 88.17 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLD------------GKSVSDTPlYDLAAMVGS 87
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP-----PTSGSVRLDgadlkqwdretfGKHIGYLP-QDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 88 VFQNPKSqfFNVDTDSELAFACENLGYPQEDILKRIDRTVSDyhiedlMGRSVFALSGGEKQKIACASSSVLLPGIMVLD 167
Cdd:TIGR01842 408 VAENIAR--FGENADPEKIIEAAKLAGVHELILRLPDGYDTV------IGPGGATLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 168 EPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLhDLADRVLYVKDGEIER 222
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLL-GCVDKILVLQDGRIAR 533
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-228 |
1.76e-18 |
|
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: 83.96 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHYYEGKLEG-DVLLDGKSVSDTply 79
Cdd:cd03265 1 IEVENLVKKYGDFEA---VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRATVAGhDVVREPREVRRR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 dlaamVGSVFQNPKsqffnvdTDSELAfACENL-------GYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIA 152
Cdd:cd03265 75 -----IGIVFQDLS-------VDDELT-GWENLyiharlyGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLDMAAIDDL-RQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVwEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
259-466 |
2.31e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 84.06 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 259 HTAKQMEFQNFCFAYKKRePESLHIP--SAELPVGETIAIIGLNGAGKSTlarCICGLEKkcgFLQVEGKT--LDWK--A 332
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTR-PDTLVLQdvSFTLHPGEVTALVGPSGSGKST---VVALLEN---FYQPQGGQvlLDGKpiS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 333 RLKHCY------MVMQDTshQLFTESVADEVLLSMDNK-DETVV--------DKILKQFDLLEYKD--RHPLSLSGGQKQ 395
Cdd:cd03248 80 QYEHKYlhskvsLVGQEP--VLFARSLQDNIAYGLQSCsFECVKeaaqkahaHSFISELASGYDTEvgEKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 396 RVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSlADQGKTLLVITHDPELVMAGCSYVVhMEKGQV 466
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVERADQILV-LDGGRI 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
264-471 |
2.33e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.27 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREP---ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTL-------DWKA 332
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIAGYHItpetgnkNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 333 RLKHCYMVMQDTSHQLFTESVADEVLLS------MDNKDETVVDKILKQFDLLE-YKDRHPLSLSGGQKQRVAIASAIVS 405
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVLKDVEFGpknfgfSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 406 NREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQ-VKESYP 471
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKlIKHASP 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
291-473 |
2.68e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.04 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDWKARL--KHCYMVMQ-DTSHQLFTesvADEVLL------S 360
Cdd:PRK13536 67 GECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPARARLarARIGVVPQfDNLDLEFT---VRENLLvfgryfG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 MDNKD-ETVVDKILkQFDLLEYKDRHPLS-LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDlKHMRE-VARSLKSLADQ 437
Cdd:PRK13536 144 MSTREiEAVIPSLL-EFARLESKADARVSdLSGGMKRRLTLARALINDPQLLILDEPTTGLD-PHARHlIWERLRSLLAR 221
|
170 180 190
....*....|....*....|....*....|....*..
gi 933767453 438 GKTLLVITHDPELVMAGCSYVVHMEKG-QVKESYPLD 473
Cdd:PRK13536 222 GKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHA 258
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-220 |
2.69e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.34 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDvLLDGKsvsdTPLYDLAAM 84
Cdd:PRK11247 16 NAVSKRYGERTV---LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-----ETPSAGE-LLAGT----APLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 85 VGSVFQNP-----KSQFFNVdtdselafaceNLGYP---QEDILKRIDrTVSdyhIEDLMGRSVFALSGGEKQKIACASS 156
Cdd:PRK11247 83 TRLMFQDArllpwKKVIDNV-----------GLGLKgqwRDAALQALA-AVG---LADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAAIDDLRQVL-SLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIeSLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
265-466 |
3.91e-18 |
|
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: 83.50 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIpSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGK-TLDW---KARLKHCYm 339
Cdd:cd03295 2 EFENVTKRYGGGKKAVNNL-NLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPTSGEIFIDGEdIREQdpvELRRKIGY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 VMQDTS---HQLFTESVAdeVLLSMDN----KDETVVDKILKQFDL--LEYKDRHPLSLSGGQKQRVAIASAIVSNREII 410
Cdd:cd03295 80 VIQQIGlfpHMTVEENIA--LVPKLLKwpkeKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 411 VFDEPTSGLDLKHMREVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-481 |
5.25e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 5.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGL-VPHyyegklEGDVLLDGKSVSDTPLYD-LAAMVGSVFQN----Pksq 95
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPD------AGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 96 ffnvdtdsELAFAcEN--LG-YPQEdiLKRIDRTVSDYHIEDLMGR---------SVFALSGGEKQKIACASSSVLLPGI 163
Cdd:PRK11288 93 --------EMTVA-ENlyLGqLPHK--GGIVNRRLLNYEAREQLEHlgvdidpdtPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 164 MVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREytpaeFDSLSDGTRKEI--- 240
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT-----FDDMAQVDRDQLvqa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 241 ----------GLRPfslsklkpanqyQAHTAKQMEFQNFcFAYKKREPESLHIPSaelpvGETIAIIGLNGAGKSTLARC 310
Cdd:PRK11288 237 mvgreigdiyGYRP------------RPLGEVRLRLDGL-KGPGLREPISFSVRA-----GEIVGLFGLVGAGRSELMKL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 311 ICGLEKKC-GFLQVEGKTLDWKArlkhcymvMQDTSHQ---LFTE-----------SVADEVLLS-----------MDNK 364
Cdd:PRK11288 299 LYGATRRTaGQVYLDGKPIDIRS--------PRDAIRAgimLCPEdrkaegiipvhSVADNINISarrhhlragclINNR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 365 DETvvDKILKQFDLLEYKDRHP----LSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKT 440
Cdd:PRK11288 371 WEA--ENADRFIRSLNIKTPSReqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 933767453 441 LLVITHD-PElVMAGCSYVVHMEKGQVKESYPLDESGSKKVL 481
Cdd:PRK11288 449 VLFVSSDlPE-VLGVADRIVVMREGRIAGELAREQATERQAL 489
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-255 |
6.21e-18 |
|
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: 86.34 E-value: 6.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYgeesSGGG---IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPL 78
Cdd:COG4618 331 LSVENLTVVP----PGSKrpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP-----PTAGSVRLDGADLSQWDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVGSVFQNPksQFF------NV----DTDSE-------LAFACE-----NLGYpqedilkridrtvsDYHIedlm 136
Cdd:COG4618 402 EELGRHIGYLPQDV--ELFdgtiaeNIarfgDADPEkvvaaakLAGVHEmilrlPDGY--------------DTRI---- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 137 GRSVFALSGGEKQKIAcasssvlL-------PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLhDLA 209
Cdd:COG4618 462 GEGGARLSGGQRQRIG-------LaralygdPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLL-AAV 533
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 933767453 210 DRVLYVKDGEIEReytpaefdslsDGTRKEIglrpfsLSKLKPANQ 255
Cdd:COG4618 534 DKLLVLRDGRVQA-----------FGPRDEV------LARLARPAA 562
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
288-467 |
6.44e-18 |
|
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: 86.25 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 288 LPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLD-WKARL--KHCYMVMQDTshQLFTESVADEVLLSMDN 363
Cdd:TIGR01842 341 LQAGEALAIIGPSGSGKSTLARLIVGIWPPTsGSVRLDGADLKqWDRETfgKHIGYLPQDV--ELFPGTVAENIARFGEN 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 KDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLK 432
Cdd:TIGR01842 419 ADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIK 498
|
170 180 190
....*....|....*....|....*....|....*
gi 933767453 433 SLADQGKTLLVITHDPELvMAGCSYVVHMEKGQVK 467
Cdd:TIGR01842 499 ALKARGITVVVITHRPSL-LGCVDKILVLQDGRIA 532
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-200 |
6.76e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.21 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyYEGkleGDVLLDGKSVSDTplyd 80
Cdd:PRK11248 1 MLQISHLYADYGGKPA---LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP--YQH---GSITLDGKPVEGP---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 lAAMVGSVFQNP-----KSQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACAS 155
Cdd:PRK11248 69 -GAERGVVFQNEgllpwRNVQDNV------AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIAR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 933767453 156 SSVLLPGIMVLDEPSSNLDMAAIDDLRQ-VLSLWKKQGKTILIAEH 200
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAFTREQMQTlLLKLWQETGKQVLLITH 187
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
281-466 |
6.97e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.19 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSaelpvGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGKTLDWKARlKHCYMVMQDtSHQLFTESVADEVLLS 360
Cdd:PRK11247 33 LHIPA-----GQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-EDTRLMFQD-ARLLPWKKVIDNVGLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 MDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ-GK 439
Cdd:PRK11247 106 LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGF 185
|
170 180
....*....|....*....|....*..
gi 933767453 440 TLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK11247 186 TVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
285-450 |
7.84e-18 |
|
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: 81.80 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKkcgFLQVEGKTLdwkarLKHcymvmQDTSHQLFTESVADEVLLSMDNK 364
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMGHPK---YEVTEGEIL-----FKG-----EDITDLPPEERARLGIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 365 DEtvvdkI--LKQFDLLEYKDrhpLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLL 442
Cdd:cd03217 87 PE-----IpgVKNADFLRYVN---EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVL 158
|
....*...
gi 933767453 443 VITHDPEL 450
Cdd:cd03217 159 IITHYQRL 166
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
288-447 |
8.06e-18 |
|
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: 86.38 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 288 LPV---GETIAIIGLNGAGKSTLARCICGlEKKCGFLQVEGKtLDWKARLKHcY--MVMQD-----------TSH----- 346
Cdd:COG1245 93 LPVpkkGKVTGILGPNGIGKSTALKILSG-ELKPNLGDYDEE-PSWDEVLKR-FrgTELQDyfkklangeikVAHkpqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 347 ----QLFTESVADevLLsmDNKDET-VVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL 421
Cdd:COG1245 170 dlipKVFKGTVRE--LL--EKVDERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*.
gi 933767453 422 KHMREVARSLKSLADQGKTLLVITHD 447
Cdd:COG1245 246 YQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-228 |
9.84e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.37 E-value: 9.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvPHYYEGKLEgdvlLDGKSVSDTPLYDl 81
Cdd:PRK10851 3 IEIANIKKSFGRTQV---LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIR----FHGTDVSRLHARD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 aAMVGSVFQNpKSQFFNVDTDSELAFACENLgyPQED------ILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACAS 155
Cdd:PRK10851 74 -RKVGFVFQH-YALFRHMTVFDNIAFGLTVL--PRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 156 SSVLLPGIMVLDEPSSNLDMAAIDDLRQvlslWKKQgktiLIAEHR---LYYLHD------LADRVLYVKDGEIEREYTP 226
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRR----WLRQ----LHEELKftsVFVTHDqeeameVADRVVVMSQGNIEQAGTP 221
|
..
gi 933767453 227 AE 228
Cdd:PRK10851 222 DQ 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
287-466 |
1.46e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.00 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEKKCG---FLQVEGKTLDWKARLKHCyMVMQdtSHQLFTE-SVADEVL--LS 360
Cdd:PRK11432 28 TIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEgqiFIDGEDVTHRSIQQRDIC-MVFQ--SYALFPHmSLGENVGygLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 MDN--KDE--TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL---KHMREVARSL-K 432
Cdd:PRK11432 105 MLGvpKEErkQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrRSMREKIRELqQ 184
|
170 180 190
....*....|....*....|....*....|....
gi 933767453 433 SLadqGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK11432 185 QF---NITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
265-468 |
1.54e-17 |
|
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: 85.23 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYK-KREPESLHI-P-SAELPVGETIAIIGLNGAGKSTLARCICGL---EKkcGFLQVEGKTLDWKARlkHCY 338
Cdd:COG4615 329 ELRGVTYRYPgEDGDEGFTLgPiDLTIRRGELVFIVGGNGSGKSTLAKLLTGLyrpES--GEILLDGQPVTADNR--EAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 MvmqdtshQLFteSVA-------DEVLLSMDNKDETVVDKILKQFDL---LEYKDRH--PLSLSGGQKQRVAIASAIVSN 406
Cdd:COG4615 405 R-------QLF--SAVfsdfhlfDRLLGLDGEADPARARELLERLELdhkVSVEDGRfsTTDLSQGQRKRLALLVALLED 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 407 REIIVFDE------PTsgldLKHM--REVarsLKSLADQGKTLLVITHDPelvmagcSY------VVHMEKGQVKE 468
Cdd:COG4615 476 RPILVFDEwaadqdPE----FRRVfyTEL---LPELKARGKTVIAISHDD-------RYfdladrVLKMDYGKLVE 537
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-213 |
1.84e-17 |
|
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: 83.18 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyEGKLEGDVLLDGKSVSDTPLYDLAAMVGS----VFQNP--- 92
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPP--PGITSGEILFDGEDLLKLSEKELRKIRGReiqmIFQDPmts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 93 -------KSQFfnvdtdSELAFAceNLGYPQEDILKRIDRTVSDYHI---EDLMGRSVFALSGGEKQKIACASSSVLLPG 162
Cdd:COG0444 99 lnpvmtvGDQI------AEPLRI--HGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 163 IMVLDEPSSNLDmAAIDdlRQVLSLWKKqgktiLIAEHRLYYL---HDL------ADRVL 213
Cdd:COG0444 171 LLIADEPTTALD-VTIQ--AQILNLLKD-----LQRELGLAILfitHDLgvvaeiADRVA 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-447 |
2.13e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 21 RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSVS-DTPLYDLAAMVGSVFQNPKSqffn 98
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPD------SGEILIDGKPVRiRSPRDAIALGIGMVHQHFML---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 VDTDSelafACEN--LGYPQ--------EDILKRIDRTVSDYHIE-DLmGRSVFALSGGEKQK--IAcassSVLL--PGI 163
Cdd:COG3845 92 VPNLT----VAENivLGLEPtkggrldrKAARARIRELSERYGLDvDP-DAKVEDLSVGEQQRveIL----KALYrgARI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 164 MVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFD--SLSdgtRKEIG 241
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSeeELA---ELMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 242 lRPFSLSKLKPAnqyqAHTAKQ-MEFQNFCFAyKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCG 319
Cdd:COG3845 240 -REVLLRVEKAP----AEPGEVvLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPpASG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 320 FLQVEGKTLD-------WKARLKHcymVMQD-TSHQLFTE-SVADEVLLS------------MDNKD-ETVVDKILKQFD 377
Cdd:COG3845 314 SIRLDGEDITglsprerRRLGVAY---IPEDrLGRGLVPDmSVAENLILGryrrppfsrggfLDRKAiRAFAEELIEEFD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 378 LleyKDRHPL----SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHD 447
Cdd:COG3845 391 V---RTPGPDtparSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISED 461
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-220 |
2.13e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 85.18 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLvngLVPHYYEGklEGDVLLDGKSVSDTPLYDL 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKL---LVGFFQAR--SGEILLNGFSLKDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPkSQFFNVDTDSELAFACENLgyPQEDILKRIDRTVSDYHIEDL-------MGRSVFALSGGEKQKIACA 154
Cdd:TIGR01193 547 RQFINYLPQEP-YIFSGSILENLLLGAKENV--SQDEIWAACEIAEIKDDIENMplgyqteLSEEGSSISGGQKQRIALA 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 155 SSSVLLPGIMVLDEPSSNLDMaaIDDLRQVLSLWKKQGKTILIAEHRLyYLHDLADRVLYVKDGEI 220
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDT--ITEKKIVNNLLNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
291-474 |
2.29e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTLDWK----ARLKHCYMVMQDTShqLFTE-SVADEVLLSMDNK 364
Cdd:COG1129 30 GEVHALLGENGAGKSTLMKILSGVYQPdSGEILLDGEPVRFRsprdAQAAGIAIIHQELN--LVPNlSVAENIFLGREPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 365 DETVVD---------KILKQFDLleykDRHPL----SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLkhmREVAR-- 429
Cdd:COG1129 108 RGGLIDwramrrrarELLARLGL----DIDPDtpvgDLSVAQQQLVEIARALSRDARVLILDEPTASLTE---REVERlf 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 933767453 430 -SLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:COG1129 181 rIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAE 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
256-446 |
2.36e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 256 YQAHTAK-QMEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTL-DWK- 331
Cdd:PRK11176 333 RVIERAKgDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFyDIDEGEILLDGHDLrDYTl 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 332 ARLK-HCYMVMQDTshQLFTESVADEVLLSMDNK--DETVVD--KILKQFDLLEyKDRHPL---------SLSGGQKQRV 397
Cdd:PRK11176 413 ASLRnQVALVSQNV--HLFNDTIANNIAYARTEQysREQIEEaaRMAYAMDFIN-KMDNGLdtvigengvLLSGGQRQRI 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 933767453 398 AIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLaDQGKTLLVITH 446
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH 537
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-220 |
3.78e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.30 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYgeesSGG--GIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVS---- 74
Cdd:PRK10908 1 MIRFEHVSKAY----LGGrqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDITrlkn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 75 -DTPLydLAAMVGSVFQN-----PKSQFFNVDTDSELAfacenlGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEK 148
Cdd:PRK10908 72 rEVPF--LRRQIGMIFQDhhllmDRTVYDNVAIPLIIA------GASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 149 QKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
285-466 |
3.87e-17 |
|
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: 80.11 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDWKAR--LKHCYMVMQDTShqlftesvADEVLLSM 361
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAGHDVVREPRevRRRIGIVFQDLS--------VDDELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 362 DN-------------KDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVA 428
Cdd:cd03265 92 ENlyiharlygvpgaERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 933767453 429 RSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03265 172 EYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
4.01e-17 |
|
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: 80.90 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESsgggI-RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEGKLEgdVLldGKSVSDTPLY 79
Cdd:COG1119 3 LLELRNVTVRRGGKT----IlDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVR--LF--GERRGGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGsVFQNPKSQFFNVD-----------TDSelafacenLG----YPQEDIlKRIDRTVSDYHIEDLMGRSVFALS 144
Cdd:COG1119 75 ELRKRIG-LVSPALQLRFPRDetvldvvlsgfFDS--------IGlyrePTDEQR-ERARELLELLGLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 145 GGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQG-KTILIAEHrlyYLHDLAD---RVLYVKDGEI 220
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTH---HVEEIPPgitHVLLLKDGRV 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-228 |
4.02e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAM-VGSVFQNPkSQFFN 98
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP-----RDAGNIIIDDEDISLLPLHARARRgIGYLPQEA-SIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 VDT-DSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAA 177
Cdd:PRK10895 93 LSVyDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 933767453 178 IDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK10895 173 VIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-228 |
5.22e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGEESSGggiRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAM 84
Cdd:PRK10253 11 EQLTLGYGKYTVA---ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT-----PAHGHVWLDGEHIQHYASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 85 VGSVFQNPKSQffnvdTDSELAFACENLGYPQEDILKR--------IDRTVSDYHIEDLMGRSVFALSGGEKQKIACASS 156
Cdd:PRK10253 83 IGLLAQNATTP-----GDITVQELVARGRYPHQPLFTRwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAAIDDLRQVLS-LWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSeLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-220 |
6.56e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 81.66 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYgeESSGGGI---RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTP 77
Cdd:COG1135 1 MIELENLSKTF--PTKGGPVtalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL-----ERPTSGSVLVDGVDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAM---VGSVFQNP-----KSQFFNVdtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQ 149
Cdd:COG1135 74 ERELRAArrkIGMIFQHFnllssRTVAENV------ALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 150 KIACASSSVLLPGIMVLDEPSSNLDMAAIddlRQVLSLWK----KQGKTILIAEH-----RlyylhDLADRVLYVKDGEI 220
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETT---RSILDLLKdinrELGLTIVLITHemdvvR-----RICDRVAVLENGRI 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
268-472 |
7.10e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 7.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 268 NFCFAYK--KREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDW-----KARLKHCYM 339
Cdd:PRK11629 10 NLCKRYQegSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTpTSGDVIFNGQPMSKlssaaKAELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 VMQDTSHQL---FT--ESVADEVLLSMDNKDEtVVDKILKQFDL--LEYKDRH-PLSLSGGQKQRVAIASAIVSNREIIV 411
Cdd:PRK11629 90 GFIYQFHHLlpdFTalENVAMPLLIGKKKPAE-INSRALEMLAAvgLEHRANHrPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 412 FDEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDpeLVMAG-CSYVVHMEKGQVKESYPL 472
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHD--LQLAKrMSRQLEMRDGRLTAELSL 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-222 |
7.66e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.23 E-value: 7.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGlvphYYEGKlEGDVLLDGKSVSDTPLYDL 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMG----YYPLT-EGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNP----KSQFFNV----DTDSELAFacENLGYPQediLKRIDRTVSDyHIEDLMGRSVFALSGGEKQKIAC 153
Cdd:PRK10790 414 RQGVAMVQQDPvvlaDTFLANVtlgrDISEEQVW--QALETVQ---LAELARSLPD-GLYTPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 154 ASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAeHRLYYLHDlADRVLYVKDGE-IER 222
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLSTIVE-ADTILVLHRGQaVEQ 555
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-220 |
7.99e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.39 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYgeESSGGGI---RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGK---SVS 74
Cdd:PRK11153 1 MIELKNISKVF--PQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL-----ERPTSGRVLVDGQdltALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 75 DTPLYDLAAMVGSVFQ-----NPKSQFFNVdtdselAFACENLGYPQEDILKRIDRTVsdyhieDLMGRSVFA------L 143
Cdd:PRK11153 74 EKELRKARRQIGMIFQhfnllSSRTVFDNV------ALPLELAGTPKAEIKARVTELL------ELVGLSDKAdrypaqL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 144 SGGEKQKIACA-----SSSVLLpgimvLDEPSSNLDMAAIddlRQVLSLWKK----QGKTILIAEHRLYYLHDLADRVLY 214
Cdd:PRK11153 142 SGGQKQRVAIAralasNPKVLL-----CDEATSALDPATT---RSILELLKDinreLGLTIVLITHEMDVVKRICDRVAV 213
|
....*.
gi 933767453 215 VKDGEI 220
Cdd:PRK11153 214 IDAGRL 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-220 |
8.22e-17 |
|
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: 78.75 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGG---IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyEGKLEGDVLLDGKSVSDTPL 78
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT---GLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVgsvfqnpksqffnvdtdselafacenlgyPQEDILkrIDR-TVSdyhiEDLMgrsvFA-----LSGGEKQK-- 150
Cdd:cd03213 81 RKIIGYV-----------------------------PQDDIL--HPTlTVR----ETLM----FAaklrgLSGGERKRvs 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 151 IACAsssvLL--PGIMVLDEPSSNLD--MAAiddlrQVLSLWKK---QGKTILIAEHRL-YYLHDLADRVLYVKDGEI 220
Cdd:cd03213 122 IALE----LVsnPSLLFLDEPTSGLDssSAL-----QVMSLLRRladTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-228 |
8.46e-17 |
|
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: 81.69 E-value: 8.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyYEGKLE--GDVLLDGKSVSDTPLYDLAamVGSVFQnpksqffnv 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERP-DSGRIRlgGEVLQDSARGIFLPPHRRR--IGYVFQ--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 100 dtDSELaF----ACENLGY-----PQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQK--IACAsssvLL--PGIMVL 166
Cdd:COG4148 85 --EARL-FphlsVRGNLLYgrkraPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRvaIGRA----LLssPRLLLM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 167 DEPSSNLDMAA-------IDDLRQVLSlwkkqgktILIaehrLYYLHD------LADRVLYVKDGEIEREYTPAE 228
Cdd:COG4148 158 DEPLAALDLARkaeilpyLERLRDELD--------IPI----LYVSHSldevarLADHVVLLEQGRVVASGPLAE 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
291-451 |
9.21e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.15 E-value: 9.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLdwkARLK---------HCYMVMQDtSHQLFTESVADEV--- 357
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERpSAGKIWFSGHDI---TRLKnrevpflrrQIGMIFQD-HHLLMDRTVYDNVaip 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 358 LLSMDNKDETV---VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSL 434
Cdd:PRK10908 104 LIIAGASGDDIrrrVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF 183
|
170
....*....|....*..
gi 933767453 435 ADQGKTLLVITHDPELV 451
Cdd:PRK10908 184 NRVGVTVLMATHDIGLI 200
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
285-485 |
1.42e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKT---LDwkarlkhcymVMQDTSHQLfteSVADEV--- 357
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEpTSGRVEVNGRVsalLE----------LGAGFHPEL---TGRENIyln 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 358 --LLSMDNKD-ETVVDKILkQF-DLLEYKDRhPL-SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLK 432
Cdd:COG1134 113 grLLGLSRKEiDEKFDEIV-EFaELGDFIDQ-PVkTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 933767453 433 SLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDEsgskkVLDFFR 485
Cdd:COG1134 191 ELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE-----VIAAYE 238
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
279-469 |
1.51e-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: 82.48 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 279 ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTL---DWKARLKHCYMVMQDTShqLFTESVA 354
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFfQARSGEILLNGFSLkdiDRHTLRQFINYLPQEPY--IFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEVLLSmdNKDETVVDKILKQFDLLEYKD--------------RHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD 420
Cdd:TIGR01193 566 ENLLLG--AKENVSQDEIWAACEIAEIKDdienmplgyqtelsEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 933767453 421 LKHMREVARSLKSLADqgKTLLVITHDPElVMAGCSYVVHMEKGQVKES 469
Cdd:TIGR01193 644 TITEKKIVNNLLNLQD--KTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQ 689
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
288-447 |
1.87e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.16 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 288 LPV---GETIAIIGLNGAGKSTLARCICGlEKKCGFLQVEGKTlDWKARLKHcY--MVMQD-----------TSH----- 346
Cdd:PRK13409 93 LPIpkeGKVTGILGPNGIGKTTAVKILSG-ELIPNLGDYEEEP-SWDEVLKR-FrgTELQNyfkklyngeikVVHkpqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 347 ----QLFTESVADevLLsmDNKDET-VVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL 421
Cdd:PRK13409 170 dlipKVFKGKVRE--LL--KKVDERgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*.
gi 933767453 422 KHMREVARSLKSLAdQGKTLLVITHD 447
Cdd:PRK13409 246 RQRLNVARLIRELA-EGKYVLVVEHD 270
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-219 |
1.99e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.93 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEGKLEGDVLLDGKSVSD--TPLY 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKI---LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYErrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFqnPKSQFFNVDTDSELAFACENLGY-PQEDILKRIDRTVSDY----HIEDLMGRSVFALSGGEKQKIACA 154
Cdd:PRK14258 85 RLRRQVSMVH--PKPNLFPMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDAdlwdEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 155 SSSVLLPGIMVLDEPSSNLDMAA---IDDLRQVLSLwkKQGKTILIAEHRLYYLHDLADRVLYVKDGE 219
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRL--RSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-245 |
2.11e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGGGirnVNLTINTGEFVLLTGESGCGKTTITRLVNGLVphyyeGKLEGDVLLDGKSVSDTPLYD 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDG---VDLSVREGSLVGLVGPNGAGKTTLLRAINGTL-----TPTAGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNPKSQF-FNVDTDSELAFA--CENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSS 157
Cdd:PRK09536 75 ASRRVASVPQDTSLSFeFDVRQVVEMGRTphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 158 VLLPGIMVLDEPSSNLDMA-AIDDLRQVLSLwKKQGKTILIAEHRLyylhDLA----DRVLYVKDGEIEREYTPAefDSL 232
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINhQVRTLELVRRL-VDDGKTAVAAIHDL----DLAarycDELVLLADGRVRAAGPPA--DVL 227
|
250
....*....|....
gi 933767453 233 SDGT-RKEIGLRPF 245
Cdd:PRK09536 228 TADTlRAAFDARTA 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
291-449 |
2.65e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.09 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCIcglekkCGFLQVEGKTLdWKARLKHCY---------MVMQDtsHQLFTE-SVADEVLLS 360
Cdd:PRK10771 25 GERVAILGPSGAGKSTLLNLI------AGFLTPASGSL-TLNGQDHTTtppsrrpvsMLFQE--NNLFSHlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 MD-----NKDE-TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD-------LKHMREV 427
Cdd:PRK10771 96 LNpglklNAAQrEKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrqemLTLVSQV 175
|
170 180
....*....|....*....|..
gi 933767453 428 ARslkslaDQGKTLLVITHDPE 449
Cdd:PRK10771 176 CQ------ERQLTLLMVSHSLE 191
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-231 |
3.11e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 77.53 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTIT----RLVNGLvphyyegklEGDVLLDGKSVSDTP 77
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV-LKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVELS---------SGSILIDGVDISKIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAMVGSVFQNPksQFF------NVDTDSElafacenlgYPQEDILKRIDRTVSDYHIEDLMGR--SVFA-----LS 144
Cdd:cd03244 73 LHDLRSRISIIPQDP--VLFsgtirsNLDPFGE---------YSDEELWQALERVGLKEFVESLPGGldTVVEeggenLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 145 GGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKqGKTILIAEHRLYYLHDlADRVLYVKDGEIerey 224
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRLDTIID-SDRILVLDKGRV---- 215
|
....*..
gi 933767453 225 tpAEFDS 231
Cdd:cd03244 216 --VEFDS 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-220 |
3.43e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.17 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 3 DFQNVSFSYGEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHY-YEGKLEGDVLLDGKSVSDTPLYDL 81
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdSKIKVDGKVLYFGKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPkSQFFNVDTDSELAFACENLGYPQEDILKRID----RTVSDY-HIEDLMGRSVFALSGGEKQKIACASS 156
Cdd:PRK14246 89 RKEVGMVFQQP-NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVeeclRKVGLWkEVYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQgKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
291-470 |
3.44e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 79.37 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTL------DWKARLKHCYMVMQD---------TSHQLFTESV- 353
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATdGEVAWLGKDLlgmkddEWRAVRSDIQMIFQDplaslnprmTIGEIIAEPLr 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 -------ADEVllsmdnKDEtvVDKILKQFDLLE-YKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMR 425
Cdd:PRK15079 127 tyhpklsRQEV------KDR--VKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 426 EVARSLKSL-ADQGKTLLVITHDPE---------LVMagcsYVVH-MEKGQVKESY 470
Cdd:PRK15079 199 QVVNLLQQLqREMGLSLIFIAHDLAvvkhisdrvLVM----YLGHaVELGTYDEVY 250
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
265-474 |
4.49e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKREPESLHIPSAELPvGETIAIIGLNGAGKSTLarcICGLEK----KCGFLQVEG---KTLDWKARLKHC 337
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKP-GQTVAIVGPTGAGKSTL---INLLQRvfdpQSGRILIDGtdiRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 338 YMVMQDTShqLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHPL-----------SLSGGQKQRVAIASAIVSN 406
Cdd:PRK13657 412 AVVFQDAG--LFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 407 REIIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITHDPELVmAGCSYVVHMEKGQVKESYPLDE 474
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFDE 555
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-219 |
4.85e-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: 77.45 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 26 TINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSVSDTPLYDLAAMVGSVFQNPKSQFFNVDTDSe 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLkPD------EGDIEIELDTVSYKPQYIKADYEGTVRDLLSSITKDFYTHP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 105 lafacenlgYPQEDILKRIdrtvsdyHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLD-----MAAid 179
Cdd:cd03237 94 ---------YFKTEIAKPL-------QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlMAS-- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 933767453 180 dlRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLyVKDGE 219
Cdd:cd03237 156 --KVIRRFAENNEKTAFVVEHDIIMIDYLADRLI-VFEGE 192
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
287-469 |
5.96e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.41 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEK---KCGFLQVEGKT-LDWK----ARlKHCYMVMQD--------TSHQLFT 350
Cdd:COG0396 22 TIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyevTSGSILLDGEDiLELSpderAR-AGIFLAFQYpveipgvsVSNFLRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 351 --ESVADEVLLSMDNKDEtvVDKILKQFDL-LEYKDRhPL--SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMR 425
Cdd:COG0396 101 alNARRGEELSAREFLKL--LKEKMKELGLdEDFLDR-YVneGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 933767453 426 EVARSLKSLADQGKTLLVITHDPELVmagcSYV----VH-MEKGQVKES 469
Cdd:COG0396 178 IVAEGVNKLRSPDRGILIITHYQRIL----DYIkpdfVHvLVDGRIVKS 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
247-468 |
6.06e-16 |
|
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: 76.80 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 247 LSKLKPANQYQAHTAKQMEFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEG 325
Cdd:cd03220 6 VSKSYPTYKGGSSSLKKLGILGRKGEVGEFW--ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpDSGTVTVRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 326 KtLDWKARL-----------KHCYMVMqdtshqlftesvadeVLLSMDNKD-ETVVDKILkQF-DLLEYKDRHPLSLSGG 392
Cdd:cd03220 84 R-VSSLLGLgggfnpeltgrENIYLNG---------------RLLGLSRKEiDEKIDEII-EFsELGDFIDLPVKTYSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 393 QKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-220 |
6.25e-16 |
|
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: 76.77 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVsDTPLYDLAAMVGSVFQnpksqfFNV 99
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR-----PTSGTAYINGYSI-RTDRKAARQSLGYCPQ------FDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 100 dTDSELAfACENL-------GYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQK--IACA---SSSVLLpgimvLD 167
Cdd:cd03263 86 -LFDELT-VREHLrfyarlkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKlsLAIAligGPSVLL-----LD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 168 EPSSNLDMAAIDDLRQVLsLWKKQGKTILIAEHrlyYLHD---LADRVLYVKDGEI 220
Cdd:cd03263 159 EPTSGLDPASRRAIWDLI-LEVRKGRSIILTTH---SMDEaeaLCDRIAIMSDGKL 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
291-447 |
6.55e-16 |
|
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: 76.74 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDWKA--RLkhcyMVMQDTShqLFT-----ESVA---DEVLL 359
Cdd:TIGR01184 11 GEFISLIGHSGCGKSTLLNLISGLAQPTsGGVILEGKQITEPGpdRM----VVFQNYS--LLPwltvrENIAlavDRVLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 SMDNKD-ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLA-DQ 437
Cdd:TIGR01184 85 DLSKSErRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWeEH 164
|
170
....*....|
gi 933767453 438 GKTLLVITHD 447
Cdd:TIGR01184 165 RVTVLMVTHD 174
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-202 |
7.65e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.51 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGeesSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRL---VNGLVPHYyegKLEGDVLLDGKSV--SDTPLY 79
Cdd:PRK14243 14 ENLNVYYG---SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGF---RVEGKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFQNP----KSQFFNVdtdselAFACENLGYpQEDILKRIDRTVSDY----HIEDLMGRSVFALSGGEKQKI 151
Cdd:PRK14243 88 EVRRRIGMVFQKPnpfpKSIYDNI------AYGARINGY-KGDMDELVERSLRQAalwdEVKDKLKQSGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933767453 152 ACASSSVLLPGIMVLDEPSSNLD---MAAIDDLRQVLslwkKQGKTILIAEHRL 202
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDpisTLRIEELMHEL----KEQYTIIIVTHNM 210
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
285-447 |
7.82e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGKTL-DWKAR-LKH--CYMVMQDTS------HQLFTESVA 354
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLsDWSAAeLARhrAYLSQQQSPpfampvFQYLALHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEVllsMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIV-----SNRE--IIVFDEPTSGLDLKHMREV 427
Cdd:COG4138 96 AGA---SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLDVAQQAAL 172
|
170 180
....*....|....*....|
gi 933767453 428 ARSLKSLADQGKTLLVITHD 447
Cdd:COG4138 173 DRLLRELCQQGITVVMSSHD 192
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
263-468 |
1.02e-15 |
|
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: 75.99 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 263 QMEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTL------DWKARLK 335
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLvELSSGSILIDGVDIskiglhDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 336 hcyMVMQDTshQLFTESVADEvLLSMDNKDETVVDKILKQFDLLEYKDRHP-----------LSLSGGQKQRVAIASAIV 404
Cdd:cd03244 82 ---IIPQDP--VLFSGTIRSN-LDPFGEYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 405 SNREIIVFDEPTSGLDL---KHMREVARSlkslADQGKTLLVITHDPELVMAgCSYVVHMEKGQVKE 468
Cdd:cd03244 156 RKSKILVLDEATASVDPetdALIQKTIRE----AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
280-448 |
1.08e-15 |
|
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: 76.16 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICGL----EKKCGFLQVEGKTLDWKARLKHCYMVMQ-DTSHQLFT--ES 352
Cdd:cd03234 27 SLHVES-----GQVMAILGSSGSGKTTLLDAISGRveggGTTSGQILFNGQPRKPDQFQKCVAYVRQdDILLPGLTvrET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 353 VADEVLLSMDN-KDETVVDKILKQFDLLEYKD---RHPL--SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMRE 426
Cdd:cd03234 102 LTYTAILRLPRkSSDAIRKKRVEDVLLRDLALtriGGNLvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180
....*....|....*....|..
gi 933767453 427 VARSLKSLADQGKTLLVITHDP 448
Cdd:cd03234 182 LVSTLSQLARRNRIVILTIHQP 203
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-220 |
1.20e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.20 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL-VPHyyEGKLE-GDVLLD-GKSVSDTPL 78
Cdd:COG4161 3 IQLKNINCFYGSHQA---LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLeTPD--SGQLNiAGHQFDfSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVGSVFQnpksQF-----FNVdTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIAC 153
Cdd:COG4161 78 RLLRQKVGMVFQ----QYnlwphLTV-MENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 154 ASSSVLLPGIMVLDEPSSNLD---MAAIDDLRQVLSlwkKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELS---QTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
291-466 |
1.23e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.96 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGK---TLDWKARlkHCYMVMQDTS---HQlfteSVADEVLLSMDN 363
Cdd:PRK11650 30 GEFIVLVGPSGCGKSTLLRMVAGLERiTSGEIWIGGRvvnELEPADR--DIAMVFQNYAlypHM----SVRENMAYGLKI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 ----KDE-----TVVDKILKqfdLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLK---HMR----EV 427
Cdd:PRK11650 104 rgmpKAEieervAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKlrvQMRleiqRL 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 933767453 428 ARSLKSladqgkTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK11650 181 HRRLKT------TSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
265-474 |
1.53e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.38 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 265 EFQNFCFAYKKRepeslhipsAELPV----------GETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLdwkAR 333
Cdd:TIGR00958 480 EFQDVSFSYPNR---------PDVPVlkgltftlhpGEVVALVGPSGSGKSTVAALLQNLyQPTGGQVLLDGVPL---VQ 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 334 LKHCYM------VMQDTshQLFTESVADEVLLSMDNKDETVVDKILKQFDLLEYKDRHPLS-----------LSGGQKQR 396
Cdd:TIGR00958 548 YDHHYLhrqvalVGQEP--VLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQR 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 397 VAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSladQGKTLLVITHDPELVmAGCSYVVHMEKGQVKESYPLDE 474
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQ 699
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
285-447 |
1.64e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.31 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTL------DWKARLKHCYMVMQD---------TSHQL 348
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTgGELYYQGQDLlkadpeAQKLLRQKIQIVFQNpygslnprkKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 349 FTESVADEVLLSMDNKDETVVDkILKQFDLL-EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREV 427
Cdd:PRK11308 115 LEEPLLINTSLSAAERREKALA-MMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQV 193
|
170 180
....*....|....*....|.
gi 933767453 428 ARSLKSLADQ-GKTLLVITHD 447
Cdd:PRK11308 194 LNLMMDLQQElGLSYVFISHD 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-174 |
1.66e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSVSDTPLYDLAAMVGSVFQNPkSQFFNVD 100
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPT------SGTLLFEGEDISTLKPEIYRQQVSYCAQTP-TLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 101 TDselafaceNLGYP-----QEDILKRIDRTVSDYHI-EDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLD 174
Cdd:PRK10247 98 YD--------NLIFPwqirnQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-220 |
1.75e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.82 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL-VPHyyEGKLE--GDVLLDGKSVSDTPL 78
Cdd:PRK11124 3 IQLNGINCFYGAHQA---LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLeMPR--SGTLNiaGNHFDFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVGSVFQnpksQF-----FNVdTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIAC 153
Cdd:PRK11124 78 RELRRNVGMVFQ----QYnlwphLTV-QQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 154 ASSSVLLPGIMVLDEPSSNLD---MAAIDDLRQVLSlwkKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELA---ETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
291-448 |
1.87e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLekkcgfLQVEGKTLDWK---ARLKHCYMVMQDTSHQLF---TESVADEVLLSMD-- 362
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGL------LPPAAGTIKLDggdIDDPDVAEACHYLGHRNAmkpALTVAENLEFWAAfl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 363 NKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLL 442
Cdd:PRK13539 102 GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVI 181
|
....*.
gi 933767453 443 VITHDP 448
Cdd:PRK13539 182 AATHIP 187
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
262-447 |
2.05e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.48 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 262 KQMEFQNFCFAYKKRE----PESLhipsaELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLD---WKAR 333
Cdd:PRK10522 321 QTLELRNVTFAYQDNGfsvgPINL-----TIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGKPVTaeqPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 334 LKHCYMVMQDTshQLFTESVADEvllsMDNKDETVVDKILKQFDL---LEYKDRH--PLSLSGGQKQRVAIASAIVSNRE 408
Cdd:PRK10522 396 RKLFSAVFTDF--HLFDQLLGPE----GKPANPALVEKWLERLKMahkLELEDGRisNLKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 933767453 409 IIVFDEPTSGLDLKHMREVARS-LKSLADQGKTLLVITHD 447
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVlLPLLQEMGKTIFAISHD 509
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
271-466 |
2.23e-15 |
|
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: 75.45 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 271 FAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKtLDWKARLKHCYM---VMQDTSH 346
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTSGEVRVAGL-VPWKRRKKFLRRigvVFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 347 QLFTESVADEVLLSMDNKD------ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD 420
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDlpparfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 933767453 421 LKHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:cd03267 186 VVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
280-473 |
2.35e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.05 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSAELPVgetiaIIGLNGAGKSTLARCICGlekkcgFLQV-EGK-TLDWKA-------RlkhcYMVMQDtsHQLFT 350
Cdd:COG4525 27 SLTIESGEFVV-----ALGASGCGKTTLLNLIAG------FLAPsSGEiTLDGVPvtgpgadR----GVVFQK--DALLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 351 -ESVADEVLLSMD----NKDE--TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL-- 421
Cdd:COG4525 90 wLNVLDNVAFGLRlrgvPKAErrARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAlt 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 422 -KHMREVArsLKSLADQGKTLLVITHDPE--LVMAgcSYVVHM--EKGQVKESYPLD 473
Cdd:COG4525 170 rEQMQELL--LDVWQRTGKGVFLITHSVEeaLFLA--TRLVVMspGPGRIVERLELD 222
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
264-446 |
2.72e-15 |
|
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: 74.74 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKtlDWKARLKHCYMVMQ 342
Cdd:TIGR03740 1 LETKNLSKRFGKQT--AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGiLRPTSGEIIFDGH--PWTRKDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 343 DTShQLFTESVADE---VLLSMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGL 419
Cdd:TIGR03740 77 ESP-PLYENLTAREnlkVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180
....*....|....*....|....*..
gi 933767453 420 DLKHMREVARSLKSLADQGKTLLVITH 446
Cdd:TIGR03740 156 DPIGIQELRELIRSFPEQGITVILSSH 182
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
291-473 |
2.96e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTLDWKARLKHcyMVMQDTShQLFTESVADEVLLSMD------N 363
Cdd:PRK11248 27 GELLVVLGPSGCGKTTLLNLIAGfVPYQHGSITLDGKPVEGPGAERG--VVFQNEG-LLPWRNVQDNVAFGLQlagvekM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 KDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL---KHMREVArsLKSLADQGKT 440
Cdd:PRK11248 104 QRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAftrEQMQTLL--LKLWQETGKQ 181
|
170 180 190
....*....|....*....|....*....|....*
gi 933767453 441 LLVITHDPE--LVMAGCSYVVHMEKGQVKESYPLD 473
Cdd:PRK11248 182 VLLITHDIEeaVFMATELVLLSPGPGRVVERLPLN 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-240 |
4.01e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGE-FVLLtGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTP-- 77
Cdd:COG4152 1 MLELKGLTKRFGDKTA---VDDVSFTVPKGEiFGLL-GPNGAGKTTTIRIILGILAPD-----SGEVLWDGEPLDPEDrr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 ----------LYdlaamvgsvfqnPKSQ------FFnvdtdSELAfacenlGYPQEDILKRIDRTVSDYHIEDLMGRSVF 141
Cdd:COG4152 72 rigylpeergLY------------PKMKvgeqlvYL-----ARLK------GLSKAEAKRRADEWLERLGLGDRANKKVE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 142 ALSGGEKQKIACASSsvLL--PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGE 219
Cdd:COG4152 129 ELSKGNQQKVQLIAA--LLhdPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
250 260
....*....|....*....|.
gi 933767453 220 IereytpaefdsLSDGTRKEI 240
Cdd:COG4152 207 K-----------VLSGSVDEI 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-220 |
4.05e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEGKLEGDVLLDGKSV--SDTPLY 79
Cdd:PRK14267 5 IETVNLRVYYGSNHV---IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIysPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFQNPKS-QFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDY----HIEDLMGRSVFALSGGEKQKIACA 154
Cdd:PRK14267 82 EVRREVGMVFQYPNPfPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 155 SSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQgKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-233 |
4.88e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 77.32 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEEssGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyYEgKLEGDVLLDGKSVSDTPLYDL 81
Cdd:PRK10522 323 LELRNVTFAYQDN--GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGL----YQ-PQSGEILLDGKPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVF---------QNPKSQffnvDTDSELAfacenlgypqEDILKRIDR----TVSDYHIEDLmgrsvfALSGGEK 148
Cdd:PRK10522 396 RKLFSAVFtdfhlfdqlLGPEGK----PANPALV----------EKWLERLKMahklELEDGRISNL------KLSKGQK 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 149 QKIAcasssVLLP-----GIMVLDEpssnldMAAIDD-------LRQVLSLWKKQGKTILIAEHRLYYLhDLADRVLYVK 216
Cdd:PRK10522 456 KRLA-----LLLAlaeerDILLLDE------WAADQDphfrrefYQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEMR 523
|
250
....*....|....*..
gi 933767453 217 DGEIeREYTPAEFDSLS 233
Cdd:PRK10522 524 NGQL-SELTGEERDAAS 539
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
263-468 |
5.40e-15 |
|
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: 73.60 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 263 QMEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEG---KTLDWKARLKHCY 338
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRfLEAEEGKIEIDGidiSTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 339 MVMQDTShqLFTESVAdevlLSMDNKDETVVDKILKQFDLLEykdrHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSG 418
Cdd:cd03369 86 IIPQDPT--LFSGTIR----SNLDPFDEYSDEEIYGALRVSE----GGLNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 933767453 419 LDLKHMREVARSLKSLAdQGKTLLVITHDPELVmAGCSYVVHMEKGQVKE 468
Cdd:cd03369 156 IDYATDALIQKTIREEF-TNSTILTIAHRLRTI-IDYDKILVMDAGEVKE 203
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-233 |
8.01e-15 |
|
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: 74.46 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKsvsdtPLYDLAAMVGSVFQNPKSQFFNvdt 101
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGL-----EKPAQGTVSFRGQ-----DLYQLDRKQRRAFRRDVQLVFQ--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 102 DSELAF-----ACENLGYPQEDI--LKRIDRTVSDYHIEDLMG-RSVFA------LSGGEKQKIACASSSVLLPGIMVLD 167
Cdd:TIGR02769 96 DSPSAVnprmtVRQIIGEPLRHLtsLDESEQKARIAELLDMVGlRSEDAdklprqLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 168 EPSSNLDM---AAIddLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFDSLS 233
Cdd:TIGR02769 176 EAVSNLDMvlqAVI--LELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-220 |
8.35e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.02 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSGGGIrnvNLTINTGEFVLLTGESGCGKTTITRLVNgLVPHYYEGKLE-GDVLLDG-KSVS--DT 76
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGI---DLEVKPGEVVAIIGPSGSGKTTLLRCIN-LLEQPEAGTIRvGDITIDTaRSLSqqKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLYDLAAMVGSVFQNpksqfFNVdtdselaF----ACENL--------GYPQEDILKRIDRTVSDYHI---EDLMGRSvf 141
Cdd:PRK11264 79 LIRQLRQHVGFVFQN-----FNL-------FphrtVLENIiegpvivkGEPKEEATARARELLAKVGLagkETSYPRR-- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 142 aLSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK11264 145 -LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
288-448 |
8.47e-15 |
|
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: 72.91 E-value: 8.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 288 LPVGETIAIIGLNGAGKSTLARCICGLEKK-CGFLQVEGKTLDWKARLKHCYMVMQDTSHQLFTESVADEVL--LSMDNK 364
Cdd:cd03231 23 LAAGEALQVTGPNGSGKTTLLRILAGLSPPlAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLrfWHADHS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 365 DETVVDKiLKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVI 444
Cdd:cd03231 103 DEQVEEA-LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLT 181
|
....
gi 933767453 445 THDP 448
Cdd:cd03231 182 THQD 185
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-228 |
9.54e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.24 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 11 YGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNglvphYYEGKLEGDVLLDGKS---VSDT----------P 77
Cdd:PRK10619 15 YGEHEV---LKGVSLQANAGDVISIIGSSGSGKSTFLRCIN-----FLEKPSEGSIVVNGQTinlVRDKdgqlkvadknQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAMVGSVFQNPKSQFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIED-LMGRSVFALSGGEKQKIACASS 156
Cdd:PRK10619 87 LRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-220 |
1.02e-14 |
|
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: 73.52 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHYYEGKLEGDVLLDGKSvsdtplyDLAAMVGSVFQNPKSQFFN 98
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVRVAGLVPWKRRK-------KFLRRIGVVFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 VDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQK--IACAsssvLL--PGIMVLDEPSSNLD 174
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRaeIAAA----LLhePEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 933767453 175 MAAIDDLRQVL-SLWKKQGKTILIAEHrlyYLHD---LADRVLYVKDGEI 220
Cdd:cd03267 186 VVAQENIRNFLkEYNRERGTTVLLTSH---YMKDieaLARRVLVIDKGRL 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-221 |
1.12e-14 |
|
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: 73.24 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGeesSGGG----IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL-VPHyyegklEGDVLLDGKsvsd 75
Cdd:COG4181 8 IIELRGLTKTVG---TGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPT------SGTVRLAGQ---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 76 tplyDLAAM------------VGSVFQNpksqfF----------NVDTDSELAfacenlGYPQ-----EDILKRI---DR 125
Cdd:COG4181 75 ----DLFALdedararlrarhVGFVFQS-----FqllptltaleNVMLPLELA------GRRDararaRALLERVglgHR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 126 tVSDYHIEdlmgrsvfaLSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMA---AIDDLrqVLSLWKKQGKTILIAEHRl 202
Cdd:COG4181 140 -LDHYPAQ---------LSGGEQQRVALARAFATEPAILFADEPTGNLDAAtgeQIIDL--LFELNRERGTTLVLVTHD- 206
|
250 260
....*....|....*....|..
gi 933767453 203 yylHDLA---DRVLYVKDGEIE 221
Cdd:COG4181 207 ---PALAarcDRVLRLRAGRLV 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-212 |
1.30e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.77 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAM---VGSVFQNPksqffn 98
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE-----PTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 vdtdselaFACENLGYPQEDIL-------------KRIDRtvsdyhIEDLM----------GRSVFALSGGEKQKIACAS 155
Cdd:COG4608 105 --------YASLNPRMTVGDIIaeplrihglaskaERRER------VAELLelvglrpehaDRYPHEFSGGQRQRIGIAR 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 156 SSVLLPGIMVLDEPSSNLDM---AaiddlrQVLSLWKKqgktiLIAEHRLYYL---HDL------ADRV 212
Cdd:COG4608 171 ALALNPKLIVCDEPVSALDVsiqA------QVLNLLED-----LQDELGLTYLfisHDLsvvrhiSDRV 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-220 |
1.48e-14 |
|
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: 72.69 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyEGKLEGDVLLDGKSVSDTPLYDLAAMVgsvfqnpkSQF-FN 98
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG--GGTTSGQILFNGQPRKPDQFQKCVAYV--------RQDdIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 VD--TDSE-LAFACEN-LGYPQED-ILKRIDRTV--SDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSS 171
Cdd:cd03234 93 LPglTVREtLTYTAILrLPRKSSDaIRKKRVEDVllRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 933767453 172 NLDMAAIDDLRQVLSLWKKQGKTILIAEHR----LYylhDLADRVLYVKDGEI 220
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHQprsdLF---RLFDRILLLSSGEI 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-227 |
1.72e-14 |
|
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: 75.60 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGG--IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGL-VPHyyegklEGDVLLDGKSVSDTPL 78
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGftLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLyRPE------SGEILLDGQPVTADNR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAMVGSVFqnpkSQFF------NVDTDSELAFAcenlgypqEDILKR--IDRTVSdyhIEDlmGR-SVFALSGGEKQ 149
Cdd:COG4615 402 EAYRQLFSAVF----SDFHlfdrllGLDGEADPARA--------RELLERleLDHKVS---VED--GRfSTTDLSQGQRK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 150 KIAcasssvLL-------PgIMVLDEpssnldMAAIDD-------LRQVLSLWKKQGKTILIAEH--RlYYlhDLADRVL 213
Cdd:COG4615 465 RLA------LLvalledrP-ILVFDE------WAADQDpefrrvfYTELLPELKARGKTVIAISHddR-YF--DLADRVL 528
|
250
....*....|....
gi 933767453 214 YVKDGEIEREYTPA 227
Cdd:COG4615 529 KMDYGKLVELTGPA 542
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
264-420 |
1.88e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.15 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICG---LEKKCgflQVEGK-TLDWK-------- 331
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGA---RVEGEiLLDGEdiydpdvd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 332 -ARL-KHCYMVMQdtshQ--LFTESVADEV--------LLSMDNKDEtVVDKILKQFDLL-EYKDR---HPLSLSGGQKQ 395
Cdd:COG1117 87 vVELrRRVGMVFQ----KpnPFPKSIYDNVayglrlhgIKSKSELDE-IVEESLRKAALWdEVKDRlkkSALGLSGGQQQ 161
|
170 180
....*....|....*....|....*
gi 933767453 396 RVAIASAIVSNREIIVFDEPTSGLD 420
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALD 186
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
287-451 |
2.00e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEKKcgfLQVEGktldwkarlkhCYMVMQDTSHQlftesvadevllsmdnkDE 366
Cdd:COG2401 52 EIEPGEIVLIVGASGSGKSTLLRLLAGALKG---TPVAG-----------CVDVPDNQFGR-----------------EA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 367 TVVDKILKQFDLLE---------YKD-----RHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLK 432
Cdd:COG2401 101 SLIDAIGRKGDFKDavellnavgLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170 180
....*....|....*....|
gi 933767453 433 SLADQ-GKTLLVITHDPELV 451
Cdd:COG2401 181 KLARRaGITLVVATHHYDVI 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
285-447 |
2.44e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGKTL-DWKAR-LKH--CYMVMQDTS------HQLFTESVA 354
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLeAWSAAeLARhrAYLSQQQTPpfampvFQYLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEVLLSmdnKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIV-------SNREIIVFDEPTSGLDLKHMREV 427
Cdd:PRK03695 96 DKTRTE---AVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180
....*....|....*....|
gi 933767453 428 ARSLKSLADQGKTLLVITHD 447
Cdd:PRK03695 173 DRLLSELCQQGIAVVMSSHD 192
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
291-465 |
2.57e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.49 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTL-DWKARLKHCYMVMQdtSHQLFTESVADEVL---LSMDN-- 363
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFEQPTaGQIMLDGVDLsHVPPYQRPINMMFQ--SYALFPHMTVEQNIafgLKQDKlp 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 KDETV--VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDlKHMR-----EVARSLKSLad 436
Cdd:PRK11607 123 KAEIAsrVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD-KKLRdrmqlEVVDILERV-- 199
|
170 180
....*....|....*....|....*....
gi 933767453 437 qGKTLLVITHDPELVMAGCSYVVHMEKGQ 465
Cdd:PRK11607 200 -GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
285-447 |
2.90e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGKTL-----------DWKARLKHCYMVMQDTSHqlFTESV 353
Cdd:PRK14243 30 WLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTfhgknlyapdvDPVEVRRRIGMVFQKPNP--FPKSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 ADEVLLS------MDNKDEtVVDKILKQFDLL-EYKDR---HPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKH 423
Cdd:PRK14243 108 YDNIAYGaringyKGDMDE-LVERSLRQAALWdEVKDKlkqSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIS 186
|
170 180
....*....|....*....|....
gi 933767453 424 MREVARSLKSLADQgKTLLVITHD 447
Cdd:PRK14243 187 TLRIEELMHELKEQ-YTIIIVTHN 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
291-446 |
5.45e-14 |
|
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: 71.42 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKCG---FLQ---VEGKTLDWKARLKHCYMVmQDTShqLFTE-SVADEVLLSM-- 361
Cdd:cd03218 26 GEIVGLLGPNGAGKTTTFYMIVGLVKPDSgkiLLDgqdITKLPMHKRARLGIGYLP-QEAS--IFRKlTVEENILAVLei 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 362 --DNKDE--TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ 437
Cdd:cd03218 103 rgLSKKEreEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR 182
|
....*....
gi 933767453 438 GKTLLVITH 446
Cdd:cd03218 183 GIGVLITDH 191
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-229 |
7.86e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.35 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVN---GLVPhyyEGKLEGDVLLDGKSV----SDTp 77
Cdd:PRK14239 9 SDLSVYYNKKKA---LNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNP---EVTITGSIVYNGHNIysprTDT- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 lYDLAAMVGSVFQNPKSQFFNVdtdselafaCENLGYPQEdiLKRI-DRTVSDYHIE-------------DLMGRSVFAL 143
Cdd:PRK14239 82 -VDLRKEIGMVFQQPNPFPMSI---------YENVVYGLR--LKGIkDKQVLDEAVEkslkgasiwdevkDRLHDSALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 144 SGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQgKTILIAEHRLYYLHDLADRVLYVKDGE-IER 222
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDlIEY 228
|
....*..
gi 933767453 223 EYTPAEF 229
Cdd:PRK14239 229 NDTKQMF 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-219 |
1.04e-13 |
|
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: 68.24 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNG-LVPHyyegklEGDVLLDGKSvsdTPLYd 80
Cdd:cd03221 1 IELENLSKTYGGKLL---LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPD------EGIVTWGSTV---KIGY- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 laamvgsvfqnpksqffnvdtdselafacenlgYPQedilkridrtvsdyhiedlmgrsvfaLSGGEKQKIACASSSVLL 160
Cdd:cd03221 68 ---------------------------------FEQ--------------------------LSGGEKMRLALAKLLLEN 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 161 PGIMVLDEPSSNLDMAAIDDLRQVLSLWKkqgKTILIAEHRLYYLHDLADRVLYVKDGE 219
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEYP---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-460 |
1.05e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYgeesSGGGI-RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSD-TPL 78
Cdd:PRK15439 11 LLCARSISKQY----SGVEVlKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP-----PDSGTLEIGGNPCARlTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 ydLAAMVGS--VFQNPksqffnvdtdseLAFAceNLGYpQEDILKRIDRTVSDYH-IEDLMGrsvfALSGGEKQKIACAS 155
Cdd:PRK15439 82 --KAHQLGIylVPQEP------------LLFP--NLSV-KENILFGLPKRQASMQkMKQLLA----ALGCQLDLDSSAGS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 156 SSV-------LLPGIM------VLDEPSSNLDMAAIDDL-RQVLSLwKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIe 221
Cdd:PRK15439 141 LEVadrqiveILRGLMrdsrilILDEPTASLTPAETERLfSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTI- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 222 reytpAEFDSLSDGTRKEIglrpfsLSKLKPANQYQAHTAKQMEFQNFCFAYKKREP-------ESL------HIpSAEL 288
Cdd:PRK15439 219 -----ALSGKTADLSTDDI------IQAITPAAREKSLSASQKLWLELPGNRRQQAAgapvltvEDLtgegfrNI-SLEV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 289 PVGETIAIIGLNGAGKSTLARCICGLEK-KCG---FLQVEGKTLDWKARLKH--CYMVMQDTSHQLFTES---------V 353
Cdd:PRK15439 287 RAGEILGLAGVVGAGRTELAETLYGLRPaRGGrimLNGKEINALSTAQRLARglVYLPEDRQSSGLYLDAplawnvcalT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 ADEVLLSMDNKDET-VVDKILKQFDL-LEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSL 431
Cdd:PRK15439 367 HNRRGFWIKPARENaVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLI 446
|
490 500 510
....*....|....*....|....*....|.
gi 933767453 432 KSLADQGKTLLVITHDPELV--MAGCSYVVH 460
Cdd:PRK15439 447 RSIAAQNVAVLFISSDLEEIeqMADRVLVMH 477
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
279-468 |
1.08e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.30 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 279 ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLE----------------KKCGFLQVE----------GKTLD--- 329
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyeptsgriiyhvalcEKCGYVERPskvgepcpvcGGTLEpee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 330 ---W------KARLKHCYMVMQDTSHQLFTE-SVADEVLLSMDN---KDETVVDKILKQFDL--LEYKDRH-PLSLSGGQ 393
Cdd:TIGR03269 94 vdfWnlsdklRRRIRKRIAIMLQRTFALYGDdTVLDNVLEALEEigyEGKEAVGRAVDLIEMvqLSHRITHiARDLSGGE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 394 KQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLA-DQGKTLLVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKAIWLENGEIKE 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-225 |
1.10e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDtplydLAAMVGSVFQNPK----SQ 95
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSK-----LSSAAKAELRNQKlgfiYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 96 FFNVDTDSElafACENLGYP-------QEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDE 168
Cdd:PRK11629 95 FHHLLPDFT---ALENVAMPlligkkkPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 169 PSSNLDMAAIDDLRQVL-SLWKKQGKTILIAEHRLYYLHDLaDRVLYVKDGEIEREYT 225
Cdd:PRK11629 172 PTGNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELS 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
273-446 |
1.26e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.57 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 273 YKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCI---CGLEKKC---GFLQVEGKTL-----DWKARLKHCYMVM 341
Cdd:PRK14239 15 YNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEVtitGSIVYNGHNIysprtDTVDLRKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 342 QDTSHqlFTESVADEVLLSM---DNKDETVVD----KILKQFDLL-EYKDR---HPLSLSGGQKQRVAIASAIVSNREII 410
Cdd:PRK14239 93 QQPNP--FPMSIYENVVYGLrlkGIKDKQVLDeaveKSLKGASIWdEVKDRlhdSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 933767453 411 VFDEPTSGLDLKHMREVARSLKSLADQgKTLLVITH 446
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTR 205
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-227 |
1.44e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGlVPHYYEGKlegdVLLDGKSVSDTPLYD 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQA---LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRATSGR----IVFDGKDITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNPKSQFFNVDTDSELA---FACENLGYPQedilkRIDRTVSDY-HIEDLMGRSVFALSGGEKQKIACASS 156
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEENLAmggFFAERDQFQE-----RIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPA 227
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGD 222
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-461 |
1.51e-13 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 73.71 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 138 RSVFALSGGEKQKIACASS-SVLLPGIM-VLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLhDLADRVLYV 215
Cdd:PRK00635 472 RALATLSGGEQERTALAKHlGAELIGITyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 216 K------DGEIEREYTPAEF----DSLSDG-TRKEIGL-----RPFSLSKLKpANQYQAHTAKQMefqnfcfaykkrepe 279
Cdd:PRK00635 551 GpgagifGGEVLFNGSPREFlaksDSLTAKyLRQELTIpipekRTNSLGTLT-LSKATKHNLKDL--------------- 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 slhipSAELPVGETIAIIGLNGAGKS-----TLARCICGL--EKKCGFLQVEGKTLdwkARLKH---------------C 337
Cdd:PRK00635 615 -----TISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFieQGFCSNLSIQWGAI---SRLVHitrdlpgrsqrsiplT 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 338 YMVMQDTSHQLFTESVADEVL-------------------------LSMDNKDETVVDKIL-KQF--------------- 376
Cdd:PRK00635 687 YIKAFDDLRELFAEQPRSKRLgltkshfsfntplgacaecqglgsiTTTDNRTSIPCPSCLgKRFlpqvlevrykgknia 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 377 DLLE---YK-----------------------DRHPL-----SLSGGQKQRVAIA---SAIVSNREIIVFDEPTSGLDLK 422
Cdd:PRK00635 767 DILEmtaYEaekffldepsihekihalcslglDYLPLgrplsSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTH 846
|
410 420 430
....*....|....*....|....*....|....*....
gi 933767453 423 HMREVARSLKSLADQGKTLLVITHDPELVMAgCSYVVHM 461
Cdd:PRK00635 847 DIKALIYVLQSLTHQGHTVVIIEHNMHVVKV-ADYVLEL 884
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
280-447 |
1.75e-13 |
|
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: 70.13 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVEGKTLDWKAR-LKHCYmvmQDTSHQLFTESVADev 357
Cdd:cd03237 14 TLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKpDEGDIEIELDTVSYKPQyIKADY---EGTVRDLLSSITKD-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 358 lLSMDNKDETVVDKILKQFDLLeykDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ 437
Cdd:cd03237 89 -FYTHPYFKTEIAKPLQIEQIL---DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170
....*....|.
gi 933767453 438 G-KTLLVITHD 447
Cdd:cd03237 165 NeKTAFVVEHD 175
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
279-466 |
1.97e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 279 ESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL---EKKCG-FLQVEGKTLDWKARLKHCYMVMQDTSHQLFTE--- 351
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGsHIELLGRTVQREGRLARDIRKSRANTGYIFQQfnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 352 ----SVADEVLL----------------SMDNKDETVvdKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIV 411
Cdd:PRK09984 98 vnrlSVLENVLIgalgstpfwrtcfswfTREQKQRAL--QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 412 FDEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
281-466 |
1.99e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARcICGLEKKC--GFLQVEGKTLD-WKARL---KHCYMVMQDTSHQLFT--ES 352
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPseGEILLDAQPLEsWSSKAfarKVAYLPQQLPAAEGMTvrEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 353 VA------DEVLLSMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMRE 426
Cdd:PRK10575 106 VAigrypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933767453 427 VARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:PRK10575 186 VLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
285-425 |
2.35e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.20 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTL---DWKARLKHCYMVMQDTSHQLFTESVADEVL-- 358
Cdd:PRK15112 33 SFTLREGQTLAIIGENGSGKSTLAKMLAGMiEPTSGELLIDDHPLhfgDYSYRSQRIRMIFQDPSTSLNPRQRISQILdf 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 359 ---LSMD---NKDETVVDKILKQFDLL-EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKhMR 425
Cdd:PRK15112 113 plrLNTDlepEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS-MR 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
267-477 |
2.45e-13 |
|
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: 72.67 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 267 QNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKT--LDWKARLKHCYM---- 339
Cdd:TIGR00957 640 HNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVHMKGSVayVPQQAWIQNDSLreni 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 340 ----VMQDTSHQLFTESVAdevllsmdnkdetvvdkILKQFDLLEYKDRHPL-----SLSGGQKQRVAIASAIVSNREII 410
Cdd:TIGR00957 720 lfgkALNEKYYQQVLEACA-----------------LLPDLEILPSGDRTEIgekgvNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 411 VFDEPTSGLDL---KHMREVARSLKSLAdQGKTLLVITHdpelvmaGCSY------VVHMEKGQVKE--SYP--LDESGS 477
Cdd:TIGR00957 783 LFDDPLSAVDAhvgKHIFEHVIGPEGVL-KNKTRILVTH-------GISYlpqvdvIIVMSGGKISEmgSYQelLQRDGA 854
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-466 |
2.78e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyYEgKLEGDVLLDGKSV----SDTPLYDLAAMVG---------SV 88
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGI----YQ-KDSGSILFQGKEIdfksSKEALENGISMVHqelnlvlqrSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 89 FQN------PKSQFFnVDTDselafaceNLGYPQEDILKRIDrtvsdyhIEDLMGRSVFALSGGEKQKIACASSSVLLPG 162
Cdd:PRK10982 91 MDNmwlgryPTKGMF-VDQD--------KMYRDTKAIFDELD-------IDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 163 IMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGE-IEREytPAEFDSLSDGTRKEIG 241
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQwIATQ--PLAGLTMDKIIAMMVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 242 LrpfSLSKLKPANQyqaHTAKQM--EFQNFCfayKKREPeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKC 318
Cdd:PRK10982 233 R---SLTQRFPDKE---NKPGEVilEVRNLT---SLRQP-SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIrEKSA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 319 GFLQVEGKTLDWKARLKHCymvmqDTSHQLFTE---SVADEVLLSMD-NKDETVVDKILKQFDLLEYKD----------- 383
Cdd:PRK10982 303 GTITLHGKKINNHNANEAI-----NHGFALVTEerrSTGIYAYLDIGfNSLISNIRNYKNKVGLLDNSRmksdtqwvids 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 384 ---------RHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHD-PELvMA 453
Cdd:PRK10982 378 mrvktpghrTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEmPEL-LG 456
|
490
....*....|...
gi 933767453 454 GCSYVVHMEKGQV 466
Cdd:PRK10982 457 ITDRILVMSNGLV 469
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-217 |
3.69e-13 |
|
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: 67.18 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSygeeSSGGG--IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhYYEGKLegdvlldgksvsdtply 79
Cdd:cd03223 1 IELENLSLA----TPDGRvlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP-WGSGRI----------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVF--QNPksqFFNVDTdseLAfacENLGYPQEDIlkridrtvsdyhiedlmgrsvfaLSGGEKQKIACASSS 157
Cdd:cd03223 59 GMPEGEDLLFlpQRP---YLPLGT---LR---EQLIYPWDDV-----------------------LSGGEQQRLAFARLL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 158 VLLPGIMVLDEPSSNLDMAAIDDLRQVLslwKKQGKTILIAEHRlYYLHDLADRVLYVKD 217
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLL---KELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-231 |
4.40e-13 |
|
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: 68.21 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTIT----RLVNGLvphyyegklEGDVLLDGKSVSDTP 77
Cdd:cd03369 7 IEVENLSVRYAPDLPPV-LKNVSFKVKAGEKIGIVGRTGAGKSTLIlalfRFLEAE---------EGKIEIDGIDISTIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAMVGSVFQNP-------KSqffNVDTDSElafacenlgYPQEDILKRIdrTVSDyhiedlmgrSVFALSGGEKQK 150
Cdd:cd03369 77 LEDLRSSLTIIPQDPtlfsgtiRS---NLDPFDE---------YSDEEIYGAL--RVSE---------GGLNLSQGQRQL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 151 IACASSSVLLPGIMVLDEPSSNLDMAAiDDLRQVLSLWKKQGKTILIAEHRLYYLHDLaDRVLYVKDGEIereytpAEFD 230
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYAT-DALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEV------KEYD 205
|
.
gi 933767453 231 S 231
Cdd:cd03369 206 H 206
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-220 |
4.57e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.96 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYEgKLEGDVLLDGKSVSDTPLYdlAAMVGSVFQNPKSQFFNV 99
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVR-QTAGRVLLDGKPVAPCALR--GRKIATIMQNPRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 100 DTDSELAF-ACENLGYPQED-ILKRIDRTVSDYHIEDLMGRSVFALSGGEKQK--IACAsssvLLPG--IMVLDEPSSNL 173
Cdd:PRK10418 96 HTMHTHAReTCLALGKPADDaTLTAALEAVGLENAARVLKLYPFEMSGGMLQRmmIALA----LLCEapFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 933767453 174 DM---AAIDDLrqVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK10418 172 DVvaqARILDL--LESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-228 |
5.31e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.45 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 19 GIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDG---KSVSDTPLYDLA-AMVGSVFQNpKS 94
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGvdiAKISDAELREVRrKKIAMVFQS-FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 95 QFFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLD 174
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 175 MAAIDDLR-QVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK10070 197 PLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
247-447 |
6.95e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.52 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 247 LSKLKPAnqyqahtakqMEFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGK 326
Cdd:PRK14258 1 MSKLIPA----------IKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 327 TLDWKA----------RLKHcYMVMQDTSHQLFTESVADEV-----LLSMDNKDET--VVDKILKQFDLL-EYKDR---H 385
Cdd:PRK14258 69 VEFFNQniyerrvnlnRLRR-QVSMVHPKPNLFPMSVYDNVaygvkIVGWRPKLEIddIVESALKDADLWdEIKHKihkS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 386 PLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGK-TLLVITHD 447
Cdd:PRK14258 148 ALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHN 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
261-446 |
7.03e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 261 AKQMEFQNFCFAYKKREPESLHIpSAELPVGETIAIIGLNGAGKSTLARCICGlekkcGFLQVEGKTLDWKARLKHCYMV 340
Cdd:PLN03232 614 AISIKNGYFSWDSKTSKPTLSDI-NLEIPVGSLVAIVGGTGEGKTSLISAMLG-----ELSHAETSSVVIRGSVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 mqdtsHQLFTESVADEVLLSMDNKDETV-----VDKILKQFDLLEYKDRHPL-----SLSGGQKQRVAIASAIVSNREII 410
Cdd:PLN03232 688 -----SWIFNATVRENILFGSDFESERYwraidVTALQHDLDLLPGRDLTEIgergvNISGGQKQRVSMARAVYSNSDIY 762
|
170 180 190
....*....|....*....|....*....|....*.
gi 933767453 411 VFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITH 446
Cdd:PLN03232 763 IFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTN 798
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
287-468 |
7.92e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.37 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEKKCG------------FLQVEGKTLDwKARLKHCYMVMQD--TS------- 345
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSQTAFALMGLLAANGriggsatfngreILNLPEKELN-KLRAEQISMIFQDpmTSlnpymrv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 346 -HQLFtesvadEVLL---SMDNKD---ETVvdKILKQFDLLEYKDR---HPLSLSGGQKQRVAIASAIVSNREIIVFDEP 415
Cdd:PRK09473 117 gEQLM------EVLMlhkGMSKAEafeESV--RMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933767453 416 TSGLDLKHMREVARSLKSLADQGKT-LLVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
260-461 |
9.48e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.47 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 260 TAKQMEFQNFCFAY-KKREPESLHIpsaELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDW---KARL 334
Cdd:PRK10253 4 SVARLRGEQLTLGYgKYTVAENLTV---EIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAhGHVWLDGEHIQHyasKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 335 KHCYMVMQDTS-----------------HQ-LFTEsvadevllsMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQR 396
Cdd:PRK10253 81 RRIGLLAQNATtpgditvqelvargrypHQpLFTR---------WRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 397 VAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDpelVMAGCSYVVHM 461
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHD---LNQACRYASHL 214
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
281-476 |
1.06e-12 |
|
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: 66.19 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLarCICGLEKkcgflqvEGKTLDWKARlkhcymvmqdtshqlfteSVADEVLLS 360
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA-------SGKARLISFL------------------PKFSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 361 MDNKDETVVDKILKQFDLleykDRHPLSLSGGQKQRVAIASAIVSNRE--IIVFDEPTSGLDLKHMREVARSLKSLADQG 438
Cdd:cd03238 64 FIDQLQFLIDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLG 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 933767453 439 KTLLVITHDPElVMAGCSYVVHMEKGQVKESYPLDESG 476
Cdd:cd03238 140 NTVILIEHNLD-VLSSADWIIDFGPGSGKSGGKVVFSG 176
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
1.13e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.68 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVphyyeGKLEGDVLLDGKSVSDTPlyDL 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLV---VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT-----HPDAGSISLCGEPVPSRA--RH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAM-VGSVfqnpkSQFFNVDTDSELAfacENL-------GYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIAC 153
Cdd:PRK13537 78 ARQrVGVV-----PQFDNLDPDFTVR---ENLlvfgryfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 154 ASSSVLLPGIMVLDEPSSNLDMAA----IDDLRQVLSlwkkQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQArhlmWERLRSLLA----RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
285-465 |
1.18e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.68 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLDWKARlkHCYM----VMQ-DTSHQLFTesVADEVL 358
Cdd:PRK13537 27 SFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDAGSISLCGEPVPSRAR--HARQrvgvVPQfDNLDPDFT--VRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 -------LSMDNKDETVvdKILKQFDLLEYKDRHPLS-LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARS 430
Cdd:PRK13537 103 vfgryfgLSAAAARALV--PPLLEFAKLENKADAKVGeLSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER 180
|
170 180 190
....*....|....*....|....*....|....*
gi 933767453 431 LKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQ 465
Cdd:PRK13537 181 LRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-218 |
1.31e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 66.97 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 9 FSYGeeSSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAMV-GS 87
Cdd:cd03290 8 FSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ-----TLEGKVHWSNKNESEPSFEATRSRNrYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 88 V-FQNPKSQFFNVDTDSELAF--------------ACENlgYPQEDILKRIDRTVsdyhiedlMGRSVFALSGGEKQKIA 152
Cdd:cd03290 81 VaYAAQKPWLLNATVEENITFgspfnkqrykavtdACSL--QPDIDLLPFGDQTE--------IGERGINLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLDMAAIDDLRQ--VLSLWKKQGKTILIAEHRLYYL-HdlADRVLYVKDG 218
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLpH--ADWIIAMKDG 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
281-462 |
1.46e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 66.74 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGlekkcgFL----QVEGK-TLDWK------ARLKHCYMVMQDtsHQLF 349
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG------TLspafSASGEvLLNGRrltalpAEQRRIGILFQD--DLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 350 TE-SVADEVLLSMDNKD-----ETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDlKH 423
Cdd:COG4136 89 PHlSVGENLAFALPPTIgraqrRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD-AA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933767453 424 MREVARSL--KSLADQG-KTLLViTHDPELVMAGcSYVVHME 462
Cdd:COG4136 168 LRAQFREFvfEQIRQRGiPALLV-THDEEDAPAA-GRVLDLG 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-220 |
1.71e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.91 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 24 NLTINTGEFVLLTGESGCGKTTITRLVNG-LVPHyyegklEGDVLLDGKSVSDTPlydlaamvgsVFQNPKSQFFNVDT- 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGfLTPA------SGSLTLNGQDHTTTP----------PSRRPVSMLFQENNl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 102 DSELAFAcENLG---YP-------QEDILKRIDRTVSdyhIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSS 171
Cdd:PRK10771 83 FSHLTVA-QNIGlglNPglklnaaQREKLHAIARQMG---IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933767453 172 NLDMAaiddLRQ-VLSLWK----KQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK10771 159 ALDPA----LRQeMLTLVSqvcqERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
241-468 |
1.97e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.36 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 241 GLRPFSLSKlKPANQY----QAHTAKQMEFQNFCFAYKKREPE----SLHIPSAELpvgetIAIIGLNGAGKSTLARCIC 312
Cdd:PRK10790 315 GERVFELMD-GPRQQYgnddRPLQSGRIDIDNVSFAYRDDNLVlqniNLSVPSRGF-----VALVGHTGSGKSTLASLLM 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 313 GLEK-KCGFLQVEGK---TLDWKARLKHCYMVMQDTShqLFTESVADEVLLSMDnKDETVVDKILKQFDLLEYKDRHPL- 387
Cdd:PRK10790 389 GYYPlTEGEIRLDGRplsSLSHSVLRQGVAMVQQDPV--VLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 388 ----------SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQgKTLLVITHD-PELVMAGCS 456
Cdd:PRK10790 466 lytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRlSTIVEADTI 544
|
250
....*....|..
gi 933767453 457 YVVHmeKGQVKE 468
Cdd:PRK10790 545 LVLH--RGQAVE 554
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
267-459 |
2.74e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.46 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 267 QNFCFAYKKR---EPESLHIPSaelpvGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKT-----LDWKARLKHC 337
Cdd:PRK10895 7 KNLAKAYKGRrvvEDVSLTVNS-----GEIVGLLGPNGAGKTTTFYMVVGIvPRDAGNIIIDDEDisllpLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 338 YMVmQDTShqLFTE-SVADEVLLSMDNKDETV-------VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREI 409
Cdd:PRK10895 82 YLP-QEAS--IFRRlSVYDNLMAVLQIRDDLSaeqredrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 933767453 410 IVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGC--SYVV 459
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCerAYIV 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-185 |
3.13e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.68 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLL-DGKSV------SDTPLYDLAAMVgsVFQNP 92
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-----SGRIARpAGARVlflpqrPYLPLGTLREAL--LYPAT 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 93 KSQFfnvdTDSELAFACE--NLGypqeDILKRIDRTVSDYHIedlmgrsvfaLSGGEKQKIACAssSVLL--PGIMVLDE 168
Cdd:COG4178 452 AEAF----SDAELREALEavGLG----HLAERLDEEADWDQV----------LSLGEQQRLAFA--RLLLhkPDWLFLDE 511
|
170
....*....|....*..
gi 933767453 169 PSSNLDMAAIDDLRQVL 185
Cdd:COG4178 512 ATSALDEENEAALYQLL 528
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-228 |
3.24e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITR-LVNGLVPhyyegkLEGDVLLDGKSVSDTPLY 79
Cdd:PRK11231 2 TLRTENLTVGYGTKRI---LNDLSLSLPTGKITALIGPNGCGKSTLLKcFARLLTP------QSGTVFLGDKPISMLSSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSVFQNPKSqffnvdtdSELAFACENLGY---P---------QEDiLKRIDRTVSDYHIEDLMGRSVFALSGGE 147
Cdd:PRK11231 73 QLARRLALLPQHHLT--------PEGITVRELVAYgrsPwlslwgrlsAED-NARVNQAMEQTRINHLADRRLTDLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 148 KQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAehrlyyLHDL------ADRVLYVKDGEIE 221
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTV------LHDLnqasryCDHLVVLANGHVM 217
|
....*..
gi 933767453 222 REYTPAE 228
Cdd:PRK11231 218 AQGTPEE 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
3.72e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 21 RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAMVG---------SVFQN 91
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP-----PAAGTIKLDGGDIDDPDVAEACHYLGhrnamkpalTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 92 pksqffnvdtdseLAFACENLGYPQEDILKRIDRtVSDYHIEDLMGRsvfALSGGEKQKIACASssvLL----PgIMVLD 167
Cdd:PRK13539 94 -------------LEFWAAFLGGEELDIAAALEA-VGLAPLAHLPFG---YLSAGQKRRVALAR---LLvsnrP-IWILD 152
|
170 180 190
....*....|....*....|....*....|...
gi 933767453 168 EPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEH 200
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-449 |
3.86e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.12 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 24 NLTINTGEFVLLTGESGCGKTTITR-LVNGLVPhyyegkLEGDVLLDGKSVSDTPLYDLAAMVGSVFQNPKSQFFNVDTD 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARaLAGELPL------LSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 103 SELAFACENLgypQEDILK--RIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDD 180
Cdd:PRK10938 97 DTGRTTAEII---QDEVKDpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 181 LRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREytpaefdslsdGTRKEIgLRPFSLSKLKPANQ----- 255
Cdd:PRK10938 174 LAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAET-----------GEREEI-LQQALVAQLAHSEQlegvq 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 256 ------YQAHTA-----KQMEFQNFCFAYKKRepESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG----------- 313
Cdd:PRK10938 242 lpepdePSARHAlpanePRIVLNNGVVSYNDR--PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndlt 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 314 -LEKKCGflqvEGKTLdWKARlKHCYMVmqdtSHQLFTE-----SVADeVLLS--MDNKD--ETVVDK--ILKQ--FDLL 379
Cdd:PRK10938 320 lFGRRRG----SGETI-WDIK-KHIGYV----SSSLHLDyrvstSVRN-VILSgfFDSIGiyQAVSDRqqKLAQqwLDIL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 380 EYKDR---HPL-SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKT-LLVITHDPE 449
Cdd:PRK10938 389 GIDKRtadAPFhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAE 463
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-233 |
3.91e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGEESSGGG------IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTPL 78
Cdd:PRK10419 7 SGLSHHYAHGGLSGKhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-----ESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 YDLAAM---VGSVFQNPKSQF---FNVdtdselafaCENLGYPQEDI--LKRIDRTVSDYHIEDLMG-------RSVFAL 143
Cdd:PRK10419 82 AQRKAFrrdIQMVFQDSISAVnprKTV---------REIIREPLRHLlsLDKAERLARASEMLRAVDlddsvldKRPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 144 SGGEKQKIACASSSVLLPGIMVLDEPSSNLD-MAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIER 222
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDlVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
250
....*....|.
gi 933767453 223 EYTPAEFDSLS 233
Cdd:PRK10419 233 TQPVGDKLTFS 243
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
285-465 |
4.10e-12 |
|
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: 65.53 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPV----------GETIAIIGLNGAGKSTLARCICGlekkcGFLQVEGKTLdwkarLKHCYM---VMQDTSHQL--- 348
Cdd:COG4778 21 GKRLPVldgvsfsvaaGECVALTGPSGAGKSTLLKCIYG-----NYLPDSGSIL-----VRHDGGwvdLAQASPREIlal 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 349 ----------F--------TESVADEVLLSMDNKDETVVDKILKQFDLLEYKDR----HPLSLSGGQKQRVAIASAIVSN 406
Cdd:COG4778 91 rrrtigyvsqFlrviprvsALDVVAEPLLERGVDREEARARARELLARLNLPERlwdlPPATFSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 407 REIIVFDEPTSGLDlKHMREVARSL-KSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQ 465
Cdd:COG4778 171 PPLLLLDEPTASLD-AANRAVVVELiEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
264-477 |
4.30e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKrePESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTL-DWK-ARLKHCYMV 340
Cdd:PRK11614 6 LSFDKVSAHYGK--IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATsGRIVFDGKDItDWQtAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQDTSHQLFTESVADEVLlSMDN---KDETVVDKILKQFDLL----EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFD 413
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENL-AMGGffaERDQFQERIKWVYELFprlhERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 414 EPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPE--LVMAGCSYVvhMEKGQVKesypLDESGS 477
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqaLKLADRGYV--LENGHVV----LEDTGD 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-218 |
5.07e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyEGKLegdvlldgkSVSDTPLYDL 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAV---VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-AGKI---------TVLGVPVPAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 A----AMVGSVfqnpkSQFFNVDtdseLAFAC-ENL-------GYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQ 149
Cdd:PRK13536 109 ArlarARIGVV-----PQFDNLD----LEFTVrENLlvfgryfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKR 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 150 KIACASSSVLLPGIMVLDEPSSNLDMAA----IDDLRQVLSlwkkQGKTILIAEHRLYYLHDLADRVLYVKDG 218
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHArhliWERLRSLLA----RGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-224 |
5.71e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGlvphyyegklegdvlldgksvsdtplyD 80
Cdd:COG0488 315 VLELEGLSKSYGDKTL---LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG---------------------------E 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNPksqffNVdtdselafaceNLGY-PQE-----------DILKRIDRTVSDYHIEDLMGR---------- 138
Cdd:COG0488 365 LEPDSGTVKLGE-----TV-----------KIGYfDQHqeeldpdktvlDELRDGAPGGTEQEVRGYLGRflfsgddafk 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 139 SVFALSGGEKQKIACASssVLL--PGIMVLDEPSSNLDMAAIDDLRQVLSLWKkqGkTILIAEHRLYYLHDLADRVLYVK 216
Cdd:COG0488 429 PVGVLSGGEKARLALAK--LLLspPNVLLLDEPTNHLDIETLEALEEALDDFP--G-TVLLVSHDRYFLDRVATRILEFE 503
|
....*...
gi 933767453 217 DGEIeREY 224
Cdd:COG0488 504 DGGV-REY 510
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
158-451 |
5.88e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.61 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 158 VLL-------PGIMVLDEPSSNLDMAAIDDLRQVLSlwkKQGKTILIAEHRLYYL-----HdLADrvlyVKDGEIeREYt 225
Cdd:PRK15064 164 VLLaqalfsnPDILLLDEPTNNLDINTIRWLEDVLN---ERNSTMIIISHDRHFLnsvctH-MAD----LDYGEL-RVY- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 226 PAEFDS------------LSDGTRK--EIG-----LRPFSL--SKLKpanqyQAHT-AKQME-----------FQN--FC 270
Cdd:PRK15064 234 PGNYDEymtaatqarerlLADNAKKkaQIAelqsfVSRFSAnaSKAK-----QATSrAKQIDkikleevkpssRQNpfIR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 271 FAYKKR------EPESL----------HIPSAELPVGETIAIIGLNGAGKSTLARCICGLekkcgfLQVEGKTLDW--KA 332
Cdd:PRK15064 309 FEQDKKlhrnalEVENLtkgfdngplfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGE------LEPDSGTVKWseNA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 333 RLKHCymvMQDTSHQlFTEsvaDEVLLS-MD-----NKDETVVDKILKQfdLLEYKD---RHPLSLSGGQKQRVAIASAI 403
Cdd:PRK15064 383 NIGYY---AQDHAYD-FEN---DLTLFDwMSqwrqeGDDEQAVRGTLGR--LLFSQDdikKSVKVLSGGEKGRMLFGKLM 453
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 933767453 404 VSNREIIVFDEPTSGLDLkhmrEVARSLKSLADQGK-TLLVITHDPELV 451
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDM----ESIESLNMALEKYEgTLIFVSHDREFV 498
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-220 |
7.15e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 7.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 13 EESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVS-DTPLYDLAAmvGSVFQN 91
Cdd:PRK15439 272 EDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRP-----ARGGRIMLNGKEINaLSTAQRLAR--GLVYLP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 92 PKSQFFNVDTDSELAFACENLGYPQEDIL---KRIDRTVSDYHieDLMG-------RSVFALSGGEKQKIACASSSVLLP 161
Cdd:PRK15439 345 EDRQSSGLYLDAPLAWNVCALTHNRRGFWikpARENAVLERYR--RALNikfnhaeQAARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 162 GIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
291-464 |
7.56e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.40 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLDWKARLKHCYMVMQDTSH--QLFTESVADEVLL-------- 359
Cdd:PRK11300 31 QEIVSLIGPNGAGKTTVFNCLTGFYKPTgGTILLRGQHIEGLPGHQIARMGVVRTFQhvRLFREMTVIENLLvaqhqqlk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 -----------SMDNKDETVVDKI---LKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMR 425
Cdd:PRK11300 111 tglfsgllktpAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 933767453 426 EVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHMEKG 464
Cdd:PRK11300 191 ELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-466 |
7.71e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.50 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 19 GIR----NVNLTINTGEFVLLTGESGCGKTTITRLvnglvphyyegkLEGDVLLDGKSVS------------DTPLYDLA 82
Cdd:PRK10636 12 GVRvlldNATATINPGQKVGLVGKNGCGKSTLLAL------------LKNEISADGGSYTfpgnwqlawvnqETPALPQP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 83 AMVgsvfqnpksqfFNVDTD-------SELAFACE-NLGYPQEDILKRID---------RTVSDYH----IEDLMGRSVF 141
Cdd:PRK10636 80 ALE-----------YVIDGDreyrqleAQLHDANErNDGHAIATIHGKLDaidawtirsRAASLLHglgfSNEQLERPVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 142 ALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQvlslWKK--QGKTILIAEHRlYYLHDLADRVLYVKDG- 218
Cdd:PRK10636 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEK----WLKsyQGTLILISHDR-DFLDPIVDKIIHIEQQs 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 219 -----------EIEREYTPAEFDSLSDGTRKEIG-LRPF------SLSKLKPAnQYQAHTAKQMEF-------QNFCFAY 273
Cdd:PRK10636 224 lfeytgnyssfEVQRATRLAQQQAMYESQQERVAhLQSYidrfraKATKAKQA-QSRIKMLERMELiapahvdNPFHFSF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 274 kkREPESLHIP-------SA-------------ELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQV-EGKTLDWK 331
Cdd:PRK10636 303 --RAPESLPNPllkmekvSAgygdriildsiklNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLaKGIKLGYF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 332 ARlkhcymvmqdtsHQL-FTEsvADEVLLS-MDNKDETVVDKILKQF---------DLLEYKDRhplsLSGGQKQRVAIA 400
Cdd:PRK10636 381 AQ------------HQLeFLR--ADESPLQhLARLAPQELEQKLRDYlggfgfqgdKVTEETRR----FSGGEKARLVLA 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 401 SAIVSNREIIVFDEPTSGLDLKhMREVARslKSLADQGKTLLVITHDPELVMAGCS--YVVHmeKGQV 466
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLD-MRQALT--EALIDFEGALVVVSHDRHLLRSTTDdlYLVH--DGKV 505
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-220 |
9.30e-12 |
|
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: 63.61 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 15 SSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDLAAMvgsvfqnpks 94
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA-----SGEITLDGKPVTRRSPRDAIRA---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 95 qffnvdtdselafaceNLGYPQEDilkRIDR-TVSDYHIEDLMGRSVFaLSGGEKQKiacasssVLL-------PGIMVL 166
Cdd:cd03215 76 ----------------GIAYVPED---RKREgLVLDLSVAENIALSSL-LSGGNQQK-------VVLarwlardPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933767453 167 DEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
280-485 |
9.72e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.60 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSAELPV--GETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEG----KTLDWK---ARLKHCYMVMQdtSHQLF 349
Cdd:PRK10070 41 SLGVKDASLAIeeGEIFVIMGLSGSGKSTMVRLLNRLiEPTRGQVLIDGvdiaKISDAElreVRRKKIAMVFQ--SFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 350 TE-SVADEVLLSMD-------NKDETVVDKiLKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL 421
Cdd:PRK10070 119 PHmTVLDNTAFGMElaginaeERREKALDA-LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 422 KHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDESGSKKVLDFFR 485
Cdd:PRK10070 198 LIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
295-481 |
1.08e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 295 AIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLDWKARlKHCY-----MVMQDTShQLFTESVADEVLLSMDNKDETV 368
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIyQKDSGSILFQGKEIDFKSS-KEALengisMVHQELN-LVLQRSVMDNMWLGRYPTKGMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 369 VD---------KILKQFDL-LEYKDRhPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQG 438
Cdd:PRK10982 106 VDqdkmyrdtkAIFDELDIdIDPRAK-VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 933767453 439 KTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDESGSKKVL 481
Cdd:PRK10982 185 CGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKII 227
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-200 |
1.10e-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: 64.59 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTIT----------RLVNGLVP---HYYEGKLEGDV-LLDGKSVSdtplydLAAMV 85
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAyarQFLGQMDKPDVdSIEGLSPA------IAIDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 86 GSVFQNPKSqffNVDTDSEL-AFACenLGYPQEDILKRIDRTVS---DYhiedL-MGRSVFALSGGEKQKIACAS--SSV 158
Cdd:cd03270 85 KTTSRNPRS---TVGTVTEIyDYLR--LLFARVGIRERLGFLVDvglGY----LtLSRSAPTLSGGEAQRIRLATqiGSG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933767453 159 LLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEH 200
Cdd:cd03270 156 LTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
8-220 |
1.14e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.04 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 8 SFSYgEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLvngLVPHYYEGklEGDVLLDGKSVSDTPLYDLAAMVGS 87
Cdd:PRK10789 320 QFTY-PQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSL---IQRHFDVS--EGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 88 VFQNPksqFFNVDT-DSELAFACEN-----------LGYPQEDILkridRTVSDYHIEdlMGRSVFALSGGEKQKIACAS 155
Cdd:PRK10789 394 VSQTP---FLFSDTvANNIALGRPDatqqeiehvarLASVHDDIL----RLPQGYDTE--VGERGVMLSGGQKQRISIAR 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 156 SSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWkKQGKTILIAEHRLYYLHDlADRVLYVKDGEI 220
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTE-ASEILVMQHGHI 527
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-219 |
1.14e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGE---ESSGGgirnvnlTINTGEFVLLTGESGCGKTTITRLVNG-LVPHyyEGKLEGDVlldgkSVSDT 76
Cdd:PRK13409 340 LVEYPDLTKKLGDfslEVEGG-------EIYEGEVIGIVGPNGIGKTTFAKLLAGvLKPD--EGEVDPEL-----KISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLYDLAAMVGSVfqnpkSQFfnvdtdseLAFACENLG--YPQEDILKRIDrtvsdyhIEDLMGRSVFALSGGEKQKIACA 154
Cdd:PRK13409 406 PQYIKPDYDGTV-----EDL--------LRSITDDLGssYYKSEIIKPLQ-------LERLLDKNVKDLSGGELQRVAIA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 155 SSSVLLPGIMVLDEPSSNLD----MAAIDDLRQVLslwKKQGKTILIAEHRLYYLHDLADRVLyVKDGE 219
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRIA---EEREATALVVDHDIYMIDYISDRLM-VFEGE 530
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-223 |
1.38e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.12 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 35 LTGESGCGKTTITRLVNGLVPHYYEGKLEGDVLLDGKSVSD-TPLYDLAAMVGSVFQNPKSQFFNVdTDSELAFACENLG 113
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNyRDVLEFRRRVGMLFQRPNPFPMSI-MDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 114 YPQEDILKRIDRTVSDY----HIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVL-SLW 188
Cdd:PRK14271 131 VPRKEFRGVAQARLTEVglwdAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIrSLA 210
|
170 180 190
....*....|....*....|....*....|....*
gi 933767453 189 KKQgkTILIAEHRLYYLHDLADRVLYVKDGEIERE 223
Cdd:PRK14271 211 DRL--TVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
281-444 |
1.60e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGL------EKKCGFLQVegktldwkARL------KHCYMVMQDTSHQL 348
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGElpllsgERQSQFSHI--------TRLsfeqlqKLVSDEWQRNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 349 FTESVAD------EVLLsMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLK 422
Cdd:PRK10938 91 LSPGEDDtgrttaEIIQ-DEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180
....*....|....*....|..
gi 933767453 423 HMREVARSLKSLADQGKTLLVI 444
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVLV 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-219 |
1.62e-11 |
|
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: 66.35 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGE---ESSGGgirnvnlTINTGEFVLLTGESGCGKTTITRLVNG-LVPHyyEGKLEGDVlldgkSVSDTP 77
Cdd:COG1245 342 VEYPDLTKSYGGfslEVEGG-------EIREGEVLGIVGPNGIGKTTFAKILAGvLKPD--EGEVDEDL-----KISYKP 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAMVGSVFQNPKSQFFNVDTDSelafacenlgYPQEDILKRIDrtvsdyhIEDLMGRSVFALSGGEKQKIACASSS 157
Cdd:COG1245 408 QYISPDYDGTVEEFLRSANTDDFGSS----------YYKTEIIKPLG-------LEKLLDKNVKDLSGGELQRVAIAACL 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 158 VLLPGIMVLDEPSSNLD----MAAIDDLRQVLslwKKQGKTILIAEHRLyYLHDL-ADRVLyVKDGE 219
Cdd:COG1245 471 SRDADLYLLDEPSAHLDveqrLAVAKAIRRFA---ENRGKTAMVVDHDI-YLIDYiSDRLM-VFEGE 532
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-213 |
1.63e-11 |
|
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: 62.73 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTItrLVNGLvphYYEGKLegdvlldgKSVSDTPLY--DLAAMVGSVfqnpksQFF 97
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGL---YASGKA--------RLISFLPKFsrNKLIFIDQL------QFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 98 nVDTdselafaceNLGYpqediLKridrtvsdyhiedlMGRSVFALSGGEKQKIACAS--SSVLLPGIMVLDEPSSNLDM 175
Cdd:cd03238 72 -IDV---------GLGY-----LT--------------LGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQ 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933767453 176 aaiDDLRQVLSLWKK---QGKTILIAEHRLYYLhDLADRVL 213
Cdd:cd03238 123 ---QDINQLLEVIKGlidLGNTVILIEHNLDVL-SSADWII 159
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
383-461 |
1.80e-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: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 383 DRHPLSLSGGQKQRVAIASAIVSNRE--IIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGcSYVVH 460
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAA-DHVID 210
|
.
gi 933767453 461 M 461
Cdd:cd03270 211 I 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
291-466 |
1.84e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICG------LEkkcGFLQVEGKTLdwkarlkhCYMVMQDTSHQ-LFTE----------SV 353
Cdd:CHL00131 33 GEIHAIMGPNGSGKSTLSKVIAGhpaykiLE---GDILFKGESI--------LDLEPEERAHLgIFLAfqypieipgvSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 354 ADEVLLSMDNKDETVVDKILKQFDLLEY---------KDRHPLS------LSGGQKQRVAIASAIVSNREIIVFDEPTSG 418
Cdd:CHL00131 102 ADFLRLAYNSKRKFQGLPELDPLEFLEIineklklvgMDPSFLSrnvnegFSGGEKKRNEILQMALLDSELAILDETDSG 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 933767453 419 LDLKHMREVARSLKSLADQGKTLLVITHDPELVmagcSYV----VH-MEKGQV 466
Cdd:CHL00131 182 LDIDALKIIAEGINKLMTSENSIILITHYQRLL----DYIkpdyVHvMQNGKI 230
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
295-450 |
2.00e-11 |
|
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: 62.38 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 295 AIIGLNGAGKSTLARCICGLekkCGFLQV-EGKTLDWKARLKHCYMVMQDTShqlftesvadevllsmdnkdetvvdkIL 373
Cdd:cd03227 25 IITGPNGSGKSTILDAIGLA---LGGAQSaTRRRSGVKAGCIVAAVSAELIF--------------------------TR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 374 KQfdlleykdrhplsLSGGQKQRVAIASAI----VSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPE 449
Cdd:cd03227 76 LQ-------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPE 142
|
.
gi 933767453 450 L 450
Cdd:cd03227 143 L 143
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
383-474 |
2.12e-11 |
|
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: 65.86 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 383 DRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITHDPELV--MAgcSYVV 459
Cdd:COG4172 151 DAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVrrFA--DRVA 228
|
90
....*....|....*
gi 933767453 460 HMEKGQVKESYPLDE 474
Cdd:COG4172 229 VMRQGEIVEQGPTAE 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-224 |
2.15e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphYYEGKLEG-DVLLDGKSVSDTPLYDLAAMVGSvfqnpksqffn 98
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA---LKGTPVAGcVDVPDNQFGREASLIDAIGRKGD----------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 VDTDSELAFACeNLGYPQedilkridrtvsdyhiedLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLD---- 174
Cdd:COG2401 112 FKDAVELLNAV-GLSDAV------------------LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqta 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933767453 175 --MAaiddlRQVLSLWKKQGKTILIAEHRLYYLHDLA-DRVLYV-KDGEIEREY 224
Cdd:COG2401 173 krVA-----RNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVgYGGVPEEKR 221
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
291-466 |
2.24e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 63.98 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKC-GFLQVEGKTLdwkarLKHcymvmqdTSHQL--------------FTE-SVA 354
Cdd:COG4674 36 GELRVIIGPNGAGKTTLMDVITGKTRPDsGSVLFGGTDL-----TGL-------DEHEIarlgigrkfqkptvFEElTVF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEVLLSM--------------DNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD 420
Cdd:COG4674 104 ENLELALkgdrgvfaslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMT 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 933767453 421 LKHMREVARSLKSLAdQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG4674 184 DAETERTAELLKSLA-GKHSVVVVEHDMEFVRQIARKVTVLHQGSV 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-202 |
2.59e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyYEgKLEGDVLL-DGKSVSDTPLYD 80
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL----YD-PTEGDIIInDSHNLKDINLKW 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAMVGSVFQNP-----------------------KSQFFNVDT-----DSELAFACE-NLGYPQEDILKRID------- 124
Cdd:PTZ00265 458 WRSKIGVVSQDPllfsnsiknnikyslyslkdleaLSNYYNEDGndsqeNKNKRNSCRaKCAGDLNDMSNTTDsneliem 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 125 ----RTVSDYHI--------------------EDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDD 180
Cdd:PTZ00265 538 rknyQTIKDSEVvdvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260
....*....|....*....|...
gi 933767453 181 LRQVLSLWK-KQGKTILIAEHRL 202
Cdd:PTZ00265 618 VQKTINNLKgNENRITIIIAHRL 640
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
291-448 |
2.67e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKCGF----LQVEGKTLdwKARLKHCYMVMQDT---SHQLFTESVADEVLLSMDN 363
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFtgtiLANNRKPT--KQILKRTGFVTQDDilyPHLTVRETLVFCSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 ---KDE--TVVDKILKQFDLLEYKD-----RHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKS 433
Cdd:PLN03211 172 sltKQEkiLVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170
....*....|....*
gi 933767453 434 LADQGKTLLVITHDP 448
Cdd:PLN03211 252 LAQKGKTIVTSMHQP 266
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
291-466 |
3.41e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.34 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTlDWKARLKHCY---MVM-QDTshQLFTE-SVAD--EVLLSMD 362
Cdd:COG4586 48 GEIVGFIGPNGAGKSTTIKMLTGiLVPTSGEVRVLGYV-PFKRRKEFARrigVVFgQRS--QLWWDlPAIDsfRLLKAIY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 363 NKDETVVDKILKQF-DLLEYKD------RHpLSLsgGQKQRVAIASAIVSNREIIVFDEPTSGLDL---KHMREVARSLK 432
Cdd:COG4586 125 RIPDAEYKKRLDELvELLDLGElldtpvRQ-LSL--GQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYN 201
|
170 180 190
....*....|....*....|....*....|....
gi 933767453 433 slADQGKTLLVITHDPELVMAGCSYVVHMEKGQV 466
Cdd:COG4586 202 --RERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-481 |
3.42e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSdtplydlaamvgsvFQNPKS------- 94
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT-----RDAGSILYLGKEVT--------------FNGPKSsqeagig 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 95 ---QFFNVDtdSELAFAcEN--LGYPQEDILKRID-------------RTVSDYHIEDLMGRsvfaLSGGEKQKIACASS 156
Cdd:PRK10762 83 iihQELNLI--PQLTIA-ENifLGREFVNRFGRIDwkkmyaeadkllaRLNLRFSSDKLVGE----LSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFDslsdgt 236
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLT------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 237 rkEIGLRPFSLSKlKPANQY----QAHTAKQMEFQNFCFAykkrepeSLHIPSAELPVGETIAIIGLNGAGKSTLARCIC 312
Cdd:PRK10762 230 --EDSLIEMMVGR-KLEDQYprldKAPGEVRLKVDNLSGP-------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 313 G-LEKKCGFLQVEGKTLDWKA---------------RlKHCYMV--------MQDTSHQLFTESVAdevllSMDNKDE-T 367
Cdd:PRK10762 300 GaLPRTSGYVTLDGHEVVTRSpqdglangivyisedR-KRDGLVlgmsvkenMSLTALRYFSRAGG-----SLKHADEqQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 368 VVDKILKQFDLLEYKDRHPLS-LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITH 446
Cdd:PRK10762 374 AVSDFIRLFNIKTPSMEQAIGlLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSS 453
|
490 500 510
....*....|....*....|....*....|....*.
gi 933767453 447 D-PElVMAGCSYVVHMEKGQVKESYPLDESGSKKVL 481
Cdd:PRK10762 454 EmPE-VLGMSDRILVMHEGRISGEFTREQATQEKLM 488
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-239 |
4.42e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 3 DFQNVSFSYGEESSGGGIRNVNltintgEFVLlTGESGCGKTtitrlvnglvphYYEGKLEGDVLLDGKSVSDTPLYDLA 82
Cdd:PTZ00265 1235 DMTNEQDYQGDEEQNVGMKNVN------EFSL-TKEGGSGED------------STVFKNSGKILLDGVDICDYNLKDLR 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 83 AMVGSVFQNPksQFFNVDTDSELAFACENLgyPQEDILKRIDRTVSDYHIEDL-------MGRSVFALSGGEKQKIACAS 155
Cdd:PTZ00265 1296 NLFSIVSQEP--MLFNMSIYENIKFGKEDA--TREDVKRACKFAAIDEFIESLpnkydtnVGPYGKSLSGGQKQRIAIAR 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 156 SSVLLPGIMVLDEPSSNLDMAAIDDL-RQVLSLWKKQGKTILIAEHRLYYLHDlADRVLYVKDGE-----IEREYTPAEF 229
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIeKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNPDrtgsfVQAHGTHEEL 1450
|
250
....*....|
gi 933767453 230 DSLSDGTRKE 239
Cdd:PTZ00265 1451 LSVQDGVYKK 1460
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-228 |
4.91e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.31 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITR-----LVNGLVPHyyEGKLEGDVLLDGKSVSDTPLYDLAAMVGSVFQNPKS 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKalagdLTGGGAPR--GARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 95 QF-FNVDtdsELAFacenLG-YPQED---ILKRIDRTVSDYHIE-----DLMGRSVFALSGGEKQKIACA---------S 155
Cdd:PRK13547 95 AFaFSAR---EIVL----LGrYPHARragALTHRDGEIAWQALAlagatALVGRDVTTLSGGELARVQFArvlaqlwppH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 156 SSVLLPGIMVLDEPSSNLDMA----AIDDLRQVLSLWKKQGKTI-----LIAEHrlyylhdlADRVLYVKDGEIEREYTP 226
Cdd:PRK13547 168 DAAQPPRYLLLDEPTAALDLAhqhrLLDTVRRLARDWNLGVLAIvhdpnLAARH--------ADRIAMLADGAIVAHGAP 239
|
..
gi 933767453 227 AE 228
Cdd:PRK13547 240 AD 241
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
287-471 |
5.58e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGKT-----------LDWKARLKHCYMVMQDTS---HQLFTES 352
Cdd:PRK14267 26 KIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVrlfgrniyspdVDPIEVRREVGMVFQYPNpfpHLTIYDN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 353 VA-----DEVLLSMDNKDEtVVDKILKQFDLL-EYKDR---HPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKH 423
Cdd:PRK14267 106 VAigvklNGLVKSKKELDE-RVEWALKKAALWdEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 933767453 424 MREVARSLKSLADQgKTLLVITHDPELVMAGCSYVVHMEKGQVKESYP 471
Cdd:PRK14267 185 TAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
295-484 |
5.87e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 65.25 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 295 AIIGLNGAGKSTLARCICGlEKKCGFlqVEG--------KTLDWKARLKHcYMVMQDTSHQLFT--ESVADEVLLSMD-- 362
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG-RKTGGY--IEGdirisgfpKKQETFARISG-YCEQNDIHSPQVTvrESLIYSAFLRLPke 985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 363 -NKDETV--VDKILKQFDLLEYKDR-----HPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSL 434
Cdd:PLN03140 986 vSKEEKMmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNT 1065
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 933767453 435 ADQGKTLLVITHDPEL-VMAGCSYVVHMEK-GQVKESYPLDESgSKKVLDFF 484
Cdd:PLN03140 1066 VDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIYSGPLGRN-SHKIIEYF 1116
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-229 |
6.13e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyegklegdvlldgksvSDTPLYDL 81
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------------AETSSVVI 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPksQFFNVDTDSELAFACEnlgYPQEDILKRIDRTVSDYHIEDLMGRSV-------FALSGGEKQKIACA 154
Cdd:PLN03232 678 RGSVAYVPQVS--WIFNATVRENILFGSD---FESERYWRAIDVTALQHDLDLLPGRDLteigergVNISGGQKQRVSMA 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 155 SSSVLLPGIMVLDEPSSNLDMAAIddlRQVLSLWKK---QGKTILIAEHRLYYLhDLADRVLYVKDGEIEREYTPAEF 229
Cdd:PLN03232 753 RAVYSNSDIYIFDDPLSALDAHVA---HQVFDSCMKdelKGKTRVLVTNQLHFL-PLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-220 |
6.60e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.48 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyYEGKLegdvLLDGKSVSDTPLYDLAAMVGSVFQNPksQFF---- 97
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP--YQGSL----KINGIELRELDPESWRKHLSWVGQNP--QLPhgtl 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 98 -------NVD-TDSELAFACEnlgypQEDILKRIDRTVS--DYHIEDLMGRsvfaLSGGEKQKIACASSsVLLPG-IMVL 166
Cdd:PRK11174 440 rdnvllgNPDaSDEQLQQALE-----NAWVSEFLPLLPQglDTPIGDQAAG----LSVGQAQRLALARA-LLQPCqLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 167 DEPSSNLDMaaiDDLRQVL-SLWK-KQGKTILIAEHRLYYLHDLaDRVLYVKDGEI 220
Cdd:PRK11174 510 DEPTASLDA---HSEQLVMqALNAaSRRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-219 |
7.28e-11 |
|
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: 61.72 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGG--GIRNVNLTINTGEFVLLTGESGCGKTTitrLVNGLVphyyeGKLEgdvLLDGKSVsdtply 79
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALL-----GELE---KLSGSVS------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 dLAAMVGSVFQNPKSQF--------FNVDTDSELAF----AC---ENLgypqeDILKRIDRTVsdyhiedlMGRSVFALS 144
Cdd:cd03250 64 -VPGSIAYVSQEPWIQNgtirenilFGKPFDEERYEkvikACalePDL-----EILPDGDLTE--------IGEKGINLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 145 GGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQ--VLSLWKKqGKTILIAEHRLYYLHDlADRVLYVKDGE 219
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
291-447 |
9.38e-11 |
|
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: 60.66 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKCGflqvegktldwkarlkhcymvmQDTSHQLFTESvadevllsmdnkdetvvd 370
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNG----------------------DNDEWDGITPV------------------ 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 371 kilkqfdlleYKDRHpLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQG-KTLLVITHD 447
Cdd:cd03222 65 ----------YKPQY-IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHD 131
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
291-486 |
1.18e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGlEKKCGFLQ-----VEGKTLDWKARLKHCYMVMQDTsHqlFTESVADEVL------- 358
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAE-RVTTGVITggdrlVNGRPLDSSFQRSIGYVQQQDL-H--LPTSTVRESLrfsaylr 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 ----LSMDNKDEtVVDKILKQFDLLEYKDR----HPLSLSGGQKQRVAIASAIVSNREIIVF-DEPTSGLDLKHMREVAR 429
Cdd:TIGR00956 865 qpksVSKSEKME-YVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICK 943
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 430 SLKSLADQGKTLLVITHDPE-LVMAGCSYVVHMEKG-QVKESYPLDEsGSKKVLDFFRI 486
Cdd:TIGR00956 944 LMRKLADHGQAILCTIHQPSaILFEEFDRLLLLQKGgQTVYFGDLGE-NSHTIINYFEK 1001
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
287-474 |
1.90e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.08 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGKT-LDWKARLKHCYMVMQDTSHQLF-------TESVADEVL 358
Cdd:PRK14247 25 EIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVyLDGQDIFKMDVIELRRRVQMVFqipnpipNLSIFENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 LSM------DNKDETV--VDKILKQFDLL-EYKDR--HPL-SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMRE 426
Cdd:PRK14247 105 LGLklnrlvKSKKELQerVRWALEKAQLWdEVKDRldAPAgKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 933767453 427 VARSLKSLADQgKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:PRK14247 185 IESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
285-459 |
2.06e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTLD-------WKARLKhcyMVMQDTSHQLFTE-SVAD 355
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGqIAPDHGEILFDGENIPamsrsrlYTVRKR---MSMLFQSGALFTDmNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 356 EVLLSMDNKDE--------TVVDKiLKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEP-------TSGLD 420
Cdd:PRK11831 104 NVAYPLREHTQlpapllhsTVMMK-LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPfvgqdpiTMGVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933767453 421 LKHMREVARSLksladqGKTLLVITHD-PE-LVMAGCSYVV 459
Cdd:PRK11831 183 VKLISELNSAL------GVTCVVVSHDvPEvLSIADHAYIV 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
143-447 |
2.38e-10 |
|
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: 62.65 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 143 LSGGEKQKIA-CAsssVLL--PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKqgkTILIAEHRLYYLHDLADRVLYVKDGE 219
Cdd:TIGR03719 162 LSGGERRRVAlCR---LLLskPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHDRYFLDNVAGWILELDRGR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 220 -----------IEREYTPAEFDSLSDGTRKEIGLRPFSLSKLKP-ANQYQ--AHTAKQMEFQNFCFAyKKREPESLHIPS 285
Cdd:TIGR03719 236 gipwegnysswLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPkGRQAKskARLARYEELLSQEFQ-KRNETAEIYIPP 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 286 AE----------------------------LPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVeGKTldwkarLKH 336
Cdd:TIGR03719 315 GPrlgdkvieaenltkafgdklliddlsfkLPPGGIVGVIGPNGAGKSTLFRMITGQEQpDSGTIEI-GET------VKL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 337 CYMvmqDTSHQlftesvadevllSMDNkDETVVDKILKQFDLLEYKDRHPLS--------------------LSGGQKQR 396
Cdd:TIGR03719 388 AYV---DQSRD------------ALDP-NKTVWEEISGGLDIIKLGKREIPSrayvgrfnfkgsdqqkkvgqLSGGERNR 451
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 933767453 397 VAIASAIVSNREIIVFDEPTSGLDLkhmrEVARSLKS-LADQGKTLLVITHD 447
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEaLLNFAGCAVVISHD 499
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
285-448 |
2.39e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.06 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLekkcgfLQVEGKTLDWKARLKHcymVMQDTSHQ----------LFTESVA 354
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGL------LRPDSGEVRWNGTPLA---EQRDEPHEnilylghlpgLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEVL--LSMDNKDE-TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSL 431
Cdd:TIGR01189 91 LENLhfWAAIHGGAqRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
170
....*....|....*..
gi 933767453 432 KSLADQGKTLLVITHDP 448
Cdd:TIGR01189 171 RAHLARGGIVLLTTHQD 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
291-447 |
2.55e-10 |
|
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: 62.65 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK------------KCGFLQVEGKtLDWKARLKHcyMVMQDTSHQLFTESVADEVL 358
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKdfngearpqpgiKVGYLPQEPQ-LDPTKTVRE--NVEEGVAEIKDALDRFNEIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 LSMDNKDETVvDKILKQF----DLLEYKDRHPL---------------------SLSGGQKQRVAIASAIVSNREIIVFD 413
Cdd:TIGR03719 108 AKYAEPDADF-DKLAAEQaelqEIIDAADAWDLdsqleiamdalrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLD 186
|
170 180 190
....*....|....*....|....*....|....
gi 933767453 414 EPTSGLDLKhmrEVARSLKSLADQGKTLLVITHD 447
Cdd:TIGR03719 187 EPTNHLDAE---SVAWLERHLQEYPGTVVAVTHD 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-240 |
3.17e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGlvphYYEgKLEGDVLLDGKSVSDTPLYDLAAMvGSV--FQNPKsqFFNV 99
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTG----FYK-PTGGTILLRGQHIEGLPGHQIARM-GVVrtFQHVR--LFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 100 DTdselafACENLGYPQEDILK--------------RIDRTVSDY--HIEDLMGRSVFA------LSGGEKQKIACASSS 157
Cdd:PRK11300 95 MT------VIENLLVAQHQQLKtglfsgllktpafrRAESEALDRaaTWLERVGLLEHAnrqagnLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 158 VLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQ-GKTILIAEHRLYYLHDLADRVLYVKDGeiereyTPaefdsLSDGT 236
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG------TP-----LANGT 237
|
....
gi 933767453 237 RKEI 240
Cdd:PRK11300 238 PEEI 241
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-218 |
3.45e-10 |
|
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: 60.14 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 19 GIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGlvphYYeGKLEGDVLLDgksvSDTPLYDLAA------------MVG 86
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG----NY-LPDSGSILVR----HDGGWVDLAQaspreilalrrrTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 87 SVfqnpkSQFFNV-------DTDSELAFAcenLGYPQEDILKRIDRTVSDYHI-EDLMGRSVFALSGGEKQKIACASSSV 158
Cdd:COG4778 97 YV-----SQFLRViprvsalDVVAEPLLE---RGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 159 LLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTIL-IaehrlyyLHD------LADRVLYVKDG 218
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgI-------FHDeevreaVADRVVDVTPF 228
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-446 |
4.06e-10 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 62.34 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 136 MGRSVFALSGGEKQKIACAS---SSvlLPGIM-VLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHrlyylhD---- 207
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATqigSG--LTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH------Dedti 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 208 -LADRVLY------VKDGEIEREYTPAEF----DSLSD---GTRKEIGLRPFSLSKLKpaNQYQAHTAKQMEFQNFcfay 273
Cdd:TIGR00630 554 rAADYVIDigpgagEHGGEVVASGTPEEIlanpDSLTGqylSGRKKIEVPAERRPGNG--KFLTLKGARENNLKNI---- 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 274 kkrepeslhipSAELPVGETIAIIGLNGAGKSTL----------ARCICGLEKKCGFLQVEG------------------ 325
Cdd:TIGR00630 628 -----------TVSIPLGLFTCITGVSGSGKSTLindtlypalaNRLNGAKTVPGRYTSIEGlehldkvihidqspigrt 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 326 -------------------------KTLDWKA----------RLKHCYM--VMQDTSHQLFTESVADEV---------LL 359
Cdd:TIGR00630 697 prsnpatytgvfdeirelfaetpeaKVRGYTPgrfsfnvkggRCEACQGdgVIKIEMHFLPDVYVPCEVckgkrynreTL 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 360 SMDNKDETVVDkILKQ--FDLLEYKDRHP-----------------------LSLSGGQKQRVAIA---SAIVSNREIIV 411
Cdd:TIGR00630 777 EVKYKGKNIAD-VLDMtvEEAYEFFEAVPsisrklqtlcdvglgyirlgqpaTTLSGGEAQRIKLAkelSKRSTGRTLYI 855
|
410 420 430
....*....|....*....|....*....|....*...
gi 933767453 412 FDEPTSGL---DLKHMREVarsLKSLADQGKTLLVITH 446
Cdd:TIGR00630 856 LDEPTTGLhfdDIKKLLEV---LQRLVDKGNTVVVIEH 890
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
383-469 |
4.84e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.91 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 383 DRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ-GKTLLVITHDPELVMAGCSYVVHM 461
Cdd:PRK11022 148 DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVM 227
|
....*...
gi 933767453 462 EKGQVKES 469
Cdd:PRK11022 228 YAGQVVET 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-234 |
4.96e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.27 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYgEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITrlvngLVPHYYEGKLEGDVLLDGKSVSDTPLYDL 81
Cdd:TIGR00957 1285 VEFRNYCLRY-REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLT-----LGLFRINESAEGEIIIDGLNIAKIGLHDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNP----KSQFFNVDTDSElafacenlgYPQEDILKRIDRTvsdyHIEDLMGRSVFALS-----GGE----- 147
Cdd:TIGR00957 1359 RFKITIIPQDPvlfsGSLRMNLDPFSQ---------YSDEEVWWALELA----HLKTFVSALPDKLDhecaeGGEnlsvg 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 148 KQKIACASSSVLLPG-IMVLDEPSSNLDMAAiDDLRQVLSLWKKQGKTILIAEHRLYYLHDLAdRVLYVKDGEIereytp 226
Cdd:TIGR00957 1426 QRQLVCLARALLRKTkILVLDEATAAVDLET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV------ 1497
|
....*...
gi 933767453 227 AEFDSLSD 234
Cdd:TIGR00957 1498 AEFGAPSN 1505
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-228 |
5.36e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 13 EESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVS-DTPLYDLAAMVGSVFQN 91
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP-----RTSGYVTLDGHEVVtRSPQDGLANGIVYISED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 92 PKSQFF----NVDTDSELAfACENLGYPQEDILKRIDR-TVSDYhIEDL------MGRSVFALSGGEKQKIACASSSVLL 160
Cdd:PRK10762 336 RKRDGLvlgmSVKENMSLT-ALRYFSRAGGSLKHADEQqAVSDF-IRLFniktpsMEQAIGLLSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 161 PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
288-446 |
5.86e-10 |
|
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: 59.27 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 288 LPVGETIAIIGLNGAGKSTLARCICGLEKKcgflqVEGKTLdWKARLKHCYMVMQDTSHQ------------LFTESVAD 355
Cdd:cd03290 24 IPTGQLTMIVGQVGCGKSSLLLAILGEMQT-----LEGKVH-WSNKNESEPSFEATRSRNrysvayaaqkpwLLNATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 356 EVLL-SMDNKD--ETVVDKILKQ--FDLLEYKDR-----HPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL---K 422
Cdd:cd03290 98 NITFgSPFNKQryKAVTDACSLQpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsD 177
|
170 180
....*....|....*....|....
gi 933767453 423 HMREvARSLKSLADQGKTLLVITH 446
Cdd:cd03290 178 HLMQ-EGILKFLQDDKRTLVLVTH 200
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
281-453 |
6.47e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLekkcgfLQVEGKTLDWKARLKHCYMVMQ---DTSHQLfteSVADEV 357
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL------VAPDEGVIKRNGKLRIGYVPQKlylDTTLPL---TVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 358 LLSMDNKDETVVD--KILKQFDLLEykdrHPLS-LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHmrEVArsLKSL 434
Cdd:PRK09544 91 RLRPGTKKEDILPalKRVQAGHLID----APMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG--QVA--LYDL 162
|
170 180
....*....|....*....|....
gi 933767453 435 ADQGKT-----LLVITHDPELVMA 453
Cdd:PRK09544 163 IDQLRReldcaVLMVSHDLHLVMA 186
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
359-461 |
7.14e-10 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 61.57 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 LSMDNKDETVVDKILKQF--------DL-LEY--KDRHPLSLSGGQKQRVAIASAIVSNRE--IIVFDEPTSGLDLKHMR 425
Cdd:TIGR00630 448 LTLTPEEKKIAEEVLKEIrerlgfliDVgLDYlsLSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNR 527
|
90 100 110
....*....|....*....|....*....|....*.
gi 933767453 426 EVARSLKSLADQGKTLLVITHDPElVMAGCSYVVHM 461
Cdd:TIGR00630 528 RLINTLKRLRDLGNTLIVVEHDED-TIRAADYVIDI 562
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
285-474 |
7.15e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.33 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKS-----TLARCICGLEKKCGFLQVEGKTLDWKA-RLKHCYMVMQD-----------TSHQ 347
Cdd:PRK10418 23 SLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQTAGRVLLDGKPVAPCAlRGRKIATIMQNprsafnplhtmHTHA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 348 LFT------ESVADEVLLSMDNKDETVVDKILKqfdlleykdRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDL 421
Cdd:PRK10418 103 RETclalgkPADDATLTAALEAVGLENAARVLK---------LYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933767453 422 KHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:PRK10418 174 VAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-223 |
9.07e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.64 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 23 VNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTPLYDLAAM----VGSVFQNpksqFFN 98
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGL-----DDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQS----FML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 VDTDSELafacENLGYPQedILK-RIDRTVSDYHIEDL----MGRSVF----ALSGGEKQKIACASSSVLLPGIMVLDEP 169
Cdd:PRK10584 100 IPTLNAL----ENVELPA--LLRgESSRQSRNGAKALLeqlgLGKRLDhlpaQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 170 SSNLDMAAIDDLRQVL-SLWKKQGKTILIAEHRLyYLHDLADRVLYVKDGEIERE 223
Cdd:PRK10584 174 TGNLDRQTGDKIADLLfSLNREHGTTLILVTHDL-QLAARCDRRLRLVNGQLQEE 227
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
291-449 |
9.16e-10 |
|
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: 57.00 E-value: 9.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCIcglekkcgflqvegktldwkarlkhcymvmqdtsHQLFTESVADEVLLSMDNKDETVVD 370
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL----------------------------------ARELGPPGGGVIYIDGEDILEEVLD 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 371 KIlkqfdLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD------LKHMREVARSLKSLADQGKTLLVI 444
Cdd:smart00382 48 QL-----LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqealLLLLEELRLLLLLKSEKNLTVILT 122
|
....*
gi 933767453 445 THDPE 449
Cdd:smart00382 123 TNDEK 127
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-450 |
9.62e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyeGKLEGDVLLDGKSVSdtplydlaamvgsvFQNPKsqffnvdt 101
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH---GSYEGEILFDGEVCR--------------FKDIR-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 102 DSE----------------LAFAcEN--LGYPQEdilKR--IDRTVSDYHIEDLMGR---------SVFALSGGEKQ--K 150
Cdd:NF040905 74 DSEalgiviihqelalipyLSIA-ENifLGNERA---KRgvIDWNETNRRARELLAKvgldespdtLVTDIGVGKQQlvE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 151 IACA-SSSVLLpgiMVLDEPSSNL---DMAAIDDLrqVLSLwKKQGKTILIAEHRLYYLHDLADRVLYVKDGE-IEReyt 225
Cdd:NF040905 150 IAKAlSKDVKL---LILDEPTAALneeDSAALLDL--LLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRtIET--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 226 paeFDSLSDGTRKEIGLRPF---SLsklkpANQYQAHTAK----QMEFQNFCfAYKKREPESLHIPSAELPV--GETIAI 296
Cdd:NF040905 221 ---LDCRADEVTEDRIIRGMvgrDL-----EDRYPERTPKigevVFEVKNWT-VYHPLHPERKVVDDVSLNVrrGEIVGI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 297 IGLNGAGKSTLARCICGL---EKKCGFLQVEGKTLDWK---ARLKH--CYmVMQDTSHQ--LFTESVADEVLLSMDNK-- 364
Cdd:NF040905 292 AGLMGAGRTELAMSVFGRsygRNISGTVFKDGKEVDVStvsDAIDAglAY-VTEDRKGYglNLIDDIKRNITLANLGKvs 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 365 DETVVDKIlKQFDLLE-YKD----RHP------LSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKS 433
Cdd:NF040905 371 RRGVIDEN-EEIKVAEeYRKkmniKTPsvfqkvGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINE 449
|
490
....*....|....*...
gi 933767453 434 LADQGKTLLVITHD-PEL 450
Cdd:NF040905 450 LAAEGKGVIVISSElPEL 467
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
285-468 |
1.08e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTL---------DWKARLKHCYMVMQDTS---HQLFTE 351
Cdd:PRK14246 30 TIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSKIKVDGKVLyfgkdifqiDAIKLRKEVGMVFQQPNpfpHLSIYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 352 SVADEvLLSMDNKDETVVDKI----LKQFDLL-EYKDR--HPLS-LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKH 423
Cdd:PRK14246 110 NIAYP-LKSHGIKEKREIKKIveecLRKVGLWkEVYDRlnSPASqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 933767453 424 MREVARSLKSLADQgKTLLVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:PRK14246 189 SQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-221 |
1.25e-09 |
|
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: 58.31 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKsvsDTPLydLAAMVGsvFQNPKSQFFNV 99
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP-----PDSGTVTVRGR---VSSL--LGLGGG--FNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 100 dtdselAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEpssnldMAAID 179
Cdd:cd03220 106 ------YLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE------VLAVG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 933767453 180 DLR------QVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIE 221
Cdd:cd03220 174 DAAfqekcqRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-226 |
1.27e-09 |
|
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: 61.18 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 13 EESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDtplyDLAAMVGSVFQNP 92
Cdd:TIGR01257 939 EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP-----PTSGTVLVGGKDIET----NLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 93 KSQ--FFNVDTDSELAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPS 170
Cdd:TIGR01257 1010 QHNilFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 171 SNLDMAAIDDLRQVLsLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTP 226
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLL-LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-220 |
1.51e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLvPHYyeGKLEGDVLLDGKSVSD-TPlyDLAAMVGS--VFQNP---- 92
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAY--KILEGDILFKGESILDlEP--EERAHLGIflAFQYPieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 93 ---KSQFFNVDTDSELAFacenLGYPQEDILKRIDRTVSDYHIEDL----MGRSVF-ALSGGEKQKIACASSSVLLPGIM 164
Cdd:CHL00131 98 gvsNADFLRLAYNSKRKF----QGLPELDPLEFLEIINEKLKLVGMdpsfLSRNVNeGFSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 165 VLDEPSSNLDmaaIDDLRQV---LSLWKKQGKTILIAEH--RLY-YLhdLADRVLYVKDGEI 220
Cdd:CHL00131 174 ILDETDSGLD---IDALKIIaegINKLMTSENSIILITHyqRLLdYI--KPDYVHVMQNGKI 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-213 |
1.54e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 59.33 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 23 VNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSV---SDTPLYDLAAMVGSVFQNPKSQFFNV 99
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVK-----ATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 100 DTDSELAFACENLGYPQ---EDILKRIDRTVSDYHI-EDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDM 175
Cdd:PRK15079 115 MTIGEIIAEPLRTYHPKlsrQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 933767453 176 ---AAIDDLRQvlSLWKKQGKT-ILIAehrlyylHDLA------DRVL 213
Cdd:PRK15079 195 siqAQVVNLLQ--QLQREMGLSlIFIA-------HDLAvvkhisDRVL 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
271-446 |
1.67e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.11 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 271 FAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCIC-GLEKKCGFLQVEGKTL------DWKARLKhcymVMQD 343
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrHFDVSEGDIRFHDIPLtklqldSWRSRLA----VVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 344 TSHqLFTESVADEVLLSMDNKDE----------TVVDKILK--QFDLLEYKDRHPLsLSGGQKQRVAIASAIVSNREIIV 411
Cdd:PRK10789 397 TPF-LFSDTVANNIALGRPDATQqeiehvarlaSVHDDILRlpQGYDTEVGERGVM-LSGGQKQRISIARALLLNAEILI 474
|
170 180 190
....*....|....*....|....*....|....*
gi 933767453 412 FDEPTSGLDLKHMREVARSLKSLAdQGKTLLVITH 446
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAH 508
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
388-461 |
2.21e-09 |
|
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: 58.01 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 388 SLSGGQKQRVAIASAI---VSNREIIVFDEPTSGL---DLKHMREVarsLKSLADQGKTLLVITHDPElVMAGCSYVVHM 461
Cdd:cd03271 169 TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLhfhDVKKLLEV---LQRLVDKGNTVVVIEHNLD-VIKCADWIIDL 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
291-464 |
2.25e-09 |
|
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: 60.41 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTLdwkarLKHCYMVMQDTSHQLFTESVaDEVLLSMDN------ 363
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGdTTVTSGDATVAGKSI-----LTNISDVHQNMGYCPQFDAI-DDLLTGREHlylyar 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 -------KDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAD 436
Cdd:TIGR01257 2039 lrgvpaeEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR 2118
|
170 180
....*....|....*....|....*...
gi 933767453 437 QGKTLLVITHDPELVMAGCSYVVHMEKG 464
Cdd:TIGR01257 2119 EGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
291-448 |
2.84e-09 |
|
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: 56.48 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGlEKKCGFlqVEGktldwkarlkhcymvmqdtshqlftesvadEVLLSMDNKDETVVD 370
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAG-RKTAGV--ITG------------------------------EILINGRPLDKNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 371 KI--LKQFDLLE--YKDRHPL-------SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGK 439
Cdd:cd03232 80 STgyVEQQDVHSpnLTVREALrfsallrGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ 159
|
....*....
gi 933767453 440 TLLVITHDP 448
Cdd:cd03232 160 AILCTIHQP 168
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-220 |
2.99e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYgeesSGGGI--RNVNLTINTGEFVLLTGESGCGKTTITRLVNGlvphyyegklegdvlldgksvsdtpl 78
Cdd:PLN03073 508 IISFSDASFGY----PGGPLlfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG-------------------------- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 79 yDLAAMVGSVFQNPKSQF--FNVDTDSELAFACENL--------GYPQEdilkRIDRTVSDYHIE-DLMGRSVFALSGGE 147
Cdd:PLN03073 558 -ELQPSSGTVFRSAKVRMavFSQHHVDGLDLSSNPLlymmrcfpGVPEQ----KLRAHLGSFGVTgNLALQPMYTLSGGQ 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 148 KQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWkkQGKtILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PLN03073 633 KSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF--QGG-VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
2.99e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.35 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSY--GEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTitrLVNGLvphyyeGKLE----GDVLLDGKSVS 74
Cdd:PRK10535 4 LLELKDIRRSYpsGEEQVEV-LKGISLDIYAGEMVAIVGASGSGKST---LMNIL------GCLDkptsGTYRVAGQDVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 75 DTPLYDLAAM----VGSVFQNPK-----SQFFNVDTDSELAfacenlGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSG 145
Cdd:PRK10535 74 TLDADALAQLrrehFGFIFQRYHllshlTAAQNVEVPAVYA------GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 146 GEKQKIACASSsvLLPG--IMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYyLHDLADRVLYVKDGEI 220
Cdd:PRK10535 148 GQQQRVSIARA--LMNGgqVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEI 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
273-420 |
3.49e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 57.35 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 273 YKKREP---ESLHIPSAElpvgetiaIIGL---NGAGKSTLARCICGLEKkcgflQVEGK-TLD---------WK-ARLK 335
Cdd:COG1137 13 YGKRTVvkdVSLEVNQGE--------IVGLlgpNGAGKTTTFYMIVGLVK-----PDSGRiFLDgedithlpmHKrARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 336 HCYMVmQDTShqLFTE-SVADEVL----LSMDNKDE--TVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNRE 408
Cdd:COG1137 80 IGYLP-QEAS--IFRKlTVEDNILavleLRKLSKKEreERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170
....*....|..
gi 933767453 409 IIVFDEPTSGLD 420
Cdd:COG1137 157 FILLDEPFAGVD 168
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-213 |
3.56e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.05 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 23 VNLTINTGEFVLLTGESGCGKTTITRLVNGLvphyyEGKLEGDVLLDGKSVSDTP---LYDLAAMVGSVFQNPksqffnv 99
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMI-----ETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 100 dtdselaFACENlgyPQEDI-------------LKRIDRTVSdyhIEDLM----------GRSVFALSGGEKQKIACASS 156
Cdd:PRK11308 102 -------YGSLN---PRKKVgqileepllintsLSAAERREK---ALAMMakvglrpehyDRYPHMFSGGQRQRIAIARA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAaiddLR-QVLSLWKKqgktiLIAEHRLYYL---HDL------ADRVL 213
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVS----VQaQVLNLMMD-----LQQELGLSYVfisHDLsvvehiADEVM 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-230 |
3.81e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 15 SSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVS-DTPLYDLAAMVG------- 86
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAD-----SGEIRLDGKPVRiRSPRDAIRAGIAyvpedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 87 --------SVFQN------PK-SQFFNVDTDSELAFAcenlgypqEDILKRID-RTVSdyhIEDLMGrsvfALSGGEKQK 150
Cdd:COG1129 338 geglvldlSIRENitlaslDRlSRGGLLDRRRERALA--------EEYIKRLRiKTPS---PEQPVG----NLSGGNQQK 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 151 iacasssVLL-------PGIMVLDEPSSNLDMAA-------IDDLRqvlslwkKQGKTILIA-----EhrlyyLHDLADR 211
Cdd:COG1129 403 -------VVLakwlatdPKVLILDEPTRGIDVGAkaeiyrlIRELA-------AEGKAVIVIsselpE-----LLGLSDR 463
|
250
....*....|....*....
gi 933767453 212 VLYVKDGEIEREYTPAEFD 230
Cdd:COG1129 464 ILVMREGRIVGELDREEAT 482
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
359-478 |
3.82e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.21 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 LSMDNKDETV-VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ 437
Cdd:NF000106 114 LDLSRKDARArADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 933767453 438 GKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDESGSK 478
Cdd:NF000106 194 GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
291-482 |
5.14e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLE-KKCGFLQVEGKTLdwkARLK----H---CYMVMQDtSHQLFTESVADEVLLSM- 361
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVpPDSGTLEIGGNPC---ARLTpakaHqlgIYLVPQE-PLLFPNLSVKENILFGLp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 362 -DNKDETVVDKILK----QFDLleykDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAD 436
Cdd:PRK15439 113 kRQASMQKMKQLLAalgcQLDL----DSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 933767453 437 QGKTLLVITHD-PElVMAGCSYVVHMEKGQVKESYPLDESGSKKVLD 482
Cdd:PRK15439 189 QGVGIVFISHKlPE-IRQLADRISVMRDGTIALSGKTADLSTDDIIQ 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
287-474 |
6.33e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGlekkcGFLQVEGKTLDWKARLKHCYMVmqdtsHQLFTESVADEVLLSMD---N 363
Cdd:PLN03130 639 DVPVGSLVAIVGSTGEGKTSLISAMLG-----ELPPRSDASVVIRGTVAYVPQV-----SWIFNATVRDNILFGSPfdpE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 KDETVVD--------KILKQFDLLEYKDRHpLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLA 435
Cdd:PLN03130 709 RYERAIDvtalqhdlDLLPGGDLTEIGERG-VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDE 787
|
170 180 190
....*....|....*....|....*....|....*....
gi 933767453 436 DQGKTLLVITHDPELvMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:PLN03130 788 LRGKTRVLVTNQLHF-LSQVDRIILVHEGMIKEEGTYEE 825
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
295-463 |
6.39e-09 |
|
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: 55.69 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 295 AIIGLNGAGKSTLARCI---------------CGLEKKCGFLQVEGK-TLDWKARLKHCYMVMQDTShqlftesVADEVL 358
Cdd:cd03240 26 LIVGQNGAGKTTIIEALkyaltgelppnskggAHDPKLIREGEVRAQvKLAFENANGKKYTITRSLA-------ILENVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 lsmdnkdetvvdkILKQFDLLEYKDRHPLSLSGGQKQ------RVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLK 432
Cdd:cd03240 99 -------------FCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEII 165
|
170 180 190
....*....|....*....|....*....|...
gi 933767453 433 SLADQGKT--LLVITHDPELVMAgCSYVVHMEK 463
Cdd:cd03240 166 EERKSQKNfqLIVITHDEELVDA-ADHIYRVEK 197
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
359-461 |
6.81e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 58.50 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 LSMDNKDETVVDKILK------QFdL----LEYK--DRHPLSLSGGQKQRVAIASAI------VsnreIIVFDEPTSGLd 420
Cdd:COG0178 445 LELTEREAEIAERILKeirsrlGF-LvdvgLDYLtlDRSAGTLSGGEAQRIRLATQIgsglvgV----LYVLDEPSIGL- 518
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 933767453 421 lkHMREVAR---SLKSLADQGKTLLVITHDPElVMAGCSYVVHM 461
Cdd:COG0178 519 --HQRDNDRlieTLKRLRDLGNTVIVVEHDED-TIRAADYIIDI 559
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-209 |
7.17e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 21 RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVS---DTPLYDLaAMVG---------SV 88
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPD-----AGEVLWQGEPIRrqrDEYHQDL-LYLGhqpgiktelTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 89 FQNpksqffnvdtdseLAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSvfaLSGGEKQKIACASSSVLLPGIMVLDE 168
Cdd:PRK13538 92 LEN-------------LRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933767453 169 PSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHrlyylHDLA 209
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQGGMVILTTH-----QDLP 191
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
281-465 |
8.48e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.89 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGLekkcgflqvegktldWKA---RLkhcymVMQDTSHQLF-------- 349
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL---------------WPYgsgRI-----ARPAGARVLFlpqrpylp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 350 -------------TESVADEVLLsmdnkdetvvdKILKQFDLLEYKDRhpLS--------LSGGQKQRVAIASAIVSNRE 408
Cdd:COG4178 439 lgtlreallypatAEAFSDAELR-----------EALEAVGLGHLAER--LDeeadwdqvLSLGEQQRLAFARLLLHKPD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 409 IIVFDEPTSGLDLKHMREVARSLKSlADQGKTLLVITHDPELvMAGCSYVVHMEKGQ 465
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTL-AAFHDRVLELTGDG 560
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
280-479 |
9.20e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 56.25 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSaelpvGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTL----DWKaRLKHCYMVMQD----TSHQLft 350
Cdd:COG1101 26 NLTIEE-----GDFVTVIGSNGAGKSTLLNAIAGsLPPDSGSILIDGKDVtklpEYK-RAKYIGRVFQDpmmgTAPSM-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 351 eSVADEVLL------------SMDNKDETVVDKILKQFDL-LEYKDRHPL-SLSGGQKQRVAIASAIVSNREIIVFDEPT 416
Cdd:COG1101 98 -TIEENLALayrrgkrrglrrGLTKKRRELFRELLATLGLgLENRLDTKVgLLSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 417 SGLDLKHMREVARSLKSLADQGK-TLLVITHDPE--------LVMagcsyvvhMEKGQVKesypLDESGSKK 479
Cdd:COG1101 177 AALDPKTAALVLELTEKIVEENNlTTLMVTHNMEqaldygnrLIM--------MHEGRII----LDVSGEEK 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
291-450 |
9.38e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGleKKCGFLQVEGK------TLDWKA-------RLKHCYMVMQDTSHQLFTESVADEV 357
Cdd:PRK13547 27 GRVTALLGRNGAGKSTLLKALAG--DLTGGGAPRGArvtgdvTLNGEPlaaidapRLARLRAVLPQAAQPAFAFSAREIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 358 LL----------SMDNKDETVVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAI---------VSNREIIVFDEPTSG 418
Cdd:PRK13547 105 LLgrypharragALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAA 184
|
170 180 190
....*....|....*....|....*....|...
gi 933767453 419 LDLKHMREVARSLKSLA-DQGKTLLVITHDPEL 450
Cdd:PRK13547 185 LDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNL 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-235 |
1.03e-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: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYgEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyegklEGDVLLDGKSVSDTPLYDL 81
Cdd:cd03288 20 IKIHDLCVRY-ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLHTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNP----KSQFFNVD-----TDSELAFACE--NLGYPQEDILKRIDRTVSDyhiedlmGRSVFalSGGEKQK 150
Cdd:cd03288 94 RSRLSIILQDPilfsGSIRFNLDpeckcTDDRLWEALEiaQLKNMVKSLPGGLDAVVTE-------GGENF--SVGQRQL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 151 IACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLsLWKKQGKTILIAEHRLYYLHDlADRVLYVKDGEIEREYTPAEFD 230
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
....*
gi 933767453 231 SLSDG 235
Cdd:cd03288 243 AQEDG 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-228 |
1.06e-08 |
|
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: 57.50 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYyEGKLE---GDVLLDGKSVSDTPLYDLAAMVGSVFQN----PKS 94
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT-SGEVNvrvGDEWVDMTKPGPDGRGRAKRYIGILHQEydlyPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 95 QFFNVDTDSElafaceNLGYPQEDILKRIDRTVSDYHIEDLMGRSVF-----ALSGGEKQKIACASSSVLLPGIMVLDEP 169
Cdd:TIGR03269 381 TVLDNLTEAI------GLELPDELARMKAVITLKMVGFDEEKAEEILdkypdELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 170 SSNLD-MAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:TIGR03269 455 TGTMDpITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
285-468 |
1.21e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEkkcgfLQVEGkTLDWKARLKhCYMVMQDTSHQLF-TESVADEVLLSMDN 363
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVT-----MPNKG-TVDIKGSAA-LIAISSGLNGQLTgIENIELKGLMMGLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 KDET--VVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTL 441
Cdd:PRK13545 117 KEKIkeIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTI 196
|
170 180
....*....|....*....|....*..
gi 933767453 442 LVITHDPELVMAGCSYVVHMEKGQVKE 468
Cdd:PRK13545 197 FFISHSLSQVKSFCTKALWLHYGQVKE 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-213 |
1.37e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.51 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyEGKLEGDVLLdgksvsdtply 79
Cdd:PRK09544 4 LVSLENVSVSFGQRRV---LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPD--EGVIKRNGKL----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 dlaaMVGSVFQNpksqfFNVDTDSELA---FACENLGYPQEDILKRIDRTVSDYHIEDLMGRsvfaLSGGEKQKIACASS 156
Cdd:PRK09544 68 ----RIGYVPQK-----LYLDTTLPLTvnrFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK----LSGGETQRVLLARA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAA-------IDDLRQVLslwkkqGKTILIAEHRLYYLHDLADRVL 213
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGqvalydlIDQLRREL------DCAVLMVSHDLHLVMAKTDEVL 192
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
364-451 |
1.46e-08 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 56.24 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 KDETVVDKILKQFDLLEYKDRHPL---SLSGGQKQRVAIASAIVSNRE---IIVFDEPTSGLDLKHMREVARSLKSLADQ 437
Cdd:pfam13304 209 SLLVDDRLRERGLILLENGGGGELpafELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRN 288
|
90
....*....|....
gi 933767453 438 GKTLLVITHDPELV 451
Cdd:pfam13304 289 GAQLILTTHSPLLL 302
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-220 |
1.50e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.42 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHYYEGKLEGDVLLDgkSVSDTPLYDLAAMVGSVFQnpksqffnvd 100
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTrPQKGRIVLNGRVLFD--AEKGICLPPEKRRIGYVFQ---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 101 tDSELaF----ACENLGYPQEDILK-RIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDM 175
Cdd:PRK11144 84 -DARL-FphykVRGNLRYGMAKSMVaQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 933767453 176 AAIDDLRQVLSLWKKQGKT-ILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK11144 162 PRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-451 |
1.58e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhYYEGKL--EGDVLldgksVS----DTPlydlAAMVGSVFqnpksq 95
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVL-LDDGRIiyEQDLI-----VArlqqDPP----RNVEGTVY------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 96 ffnvDTDSE-LAFACENL-GY----------PQEDILKRIDR--TVSDYH--------IEDLMGR-------SVFALSGG 146
Cdd:PRK11147 85 ----DFVAEgIEEQAEYLkRYhdishlvetdPSEKNLNELAKlqEQLDHHnlwqlenrINEVLAQlgldpdaALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 147 EKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWkkQGKTILIAEHRlYYLHDLADRV-------------- 212
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QGSIIFISHDR-SFIRNMATRIvdldrgklvsypgn 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 213 --LYVkDGEIE----REYTPAEFDS--------LSDG-----TRKEIGLRpfslsKLKPANQYQAHTAKQMEFQNFCFAY 273
Cdd:PRK11147 238 ydQYL-LEKEEalrvEELQNAEFDRklaqeevwIRQGikarrTRNEGRVR-----ALKALRRERSERREVMGTAKMQVEE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 274 KKR------EPESLH--IP--------SAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVeGKTLDwkarlkh 336
Cdd:PRK11147 312 ASRsgkivfEMENVNyqIDgkqlvkdfSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQADSGRIHC-GTKLE------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 337 cymvmqdtshqlftesVA--DEVLLSMDnKDETVVDKIL--KQFDLLEYKDRHPLS------------------LSGGQK 394
Cdd:PRK11147 384 ----------------VAyfDQHRAELD-PEKTVMDNLAegKQEVMVNGRPRHVLGylqdflfhpkramtpvkaLSGGER 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 395 QRVAIASAIVSNREIIVFDEPTSGLDLkhmrEVARSLKSLAD--QGkTLLVITHDPELV 451
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDsyQG-TVLLVSHDRQFV 500
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-220 |
1.69e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.98 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTitrLVNGLVpHYYEGKLE--GDVLLDGKSVSdtpLYDLAAMVGSVFQNpkSQFF 97
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTT---LMNALA-FRSPKGVKgsGSVLLNGMPID---AKEMRAISAYVQQD--DLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 98 NVDTDSE-LAFACEnLGYPqEDILKRIDRTVSDYHIEDLMGRS-----------VFALSGGEKQKIACASSSVLLPGIMV 165
Cdd:TIGR00955 112 PTLTVREhLMFQAH-LRMP-RRVTKKEKRERVDEVLQALGLRKcantrigvpgrVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 166 LDEPSSNLD--MAAiddlrQVLSLWKK---QGKTILIAEHR-LYYLHDLADRVLYVKDGEI 220
Cdd:TIGR00955 190 CDEPTSGLDsfMAY-----SVVQVLKGlaqKGKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
285-447 |
1.72e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.49 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGKTL-------DWKARL---KHCYMVMQDTSHqlFTESVA 354
Cdd:PRK14271 41 SMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrsifNYRDVLefrRRVGMLFQRPNP--FPMSIM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEVL-------LSMDNKDETVVDKILKQFDLLE-YKDR---HPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKH 423
Cdd:PRK14271 119 DNVLagvrahkLVPRKEFRGVAQARLTEVGLWDaVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTT 198
|
170 180
....*....|....*....|....
gi 933767453 424 MREVARSLKSLADQgKTLLVITHD 447
Cdd:PRK14271 199 TEKIEEFIRSLADR-LTVIIVTHN 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
291-457 |
1.87e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLekkcgfLQVEGKTLDWKAR-LKHCymvmQDTSHQ--LF--------TESVADEVL- 358
Cdd:PRK13538 27 GELVQIEGPNGAGKTSLLRILAGL------ARPDAGEVLWQGEpIRRQ----RDEYHQdlLYlghqpgikTELTALENLr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 ----LSMDNKDETVVDkILKQFDLLEYKD---RHplsLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSL 431
Cdd:PRK13538 97 fyqrLHGPGDDEALWE-ALAQVGLAGFEDvpvRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170 180
....*....|....*....|....*.
gi 933767453 432 KSLADQGKTLLVITHDPeLVMAGCSY 457
Cdd:PRK13538 173 AQHAEQGGMVILTTHQD-LPVASDKV 197
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-231 |
2.68e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.02 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 23 VNLTINTGEFVLLTGESGCGKTTITRLVNGLV-----PHYYEGKLEGDVLLDGKSVSDtpLYDLAAMVGSVFQnpksQFF 97
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksAGSHIELLGRTVQREGRLARD--IRKSRANTGYIFQ----QFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 98 NVDTDSEL------AFACEN-----LGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVL 166
Cdd:PRK09984 97 LVNRLSVLenvligALGSTPfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 167 DEPSSNLD-------MAAIDDLRQvlslwkKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAEFDS 231
Cdd:PRK09984 177 DEPIASLDpesarivMDTLRDINQ------NDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
291-447 |
2.87e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEK------------KCGFLQVE-----------------GKTLDWKARLKHCYMvm 341
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKefegearpapgiKVGYLPQEpqldpektvrenveegvAEVKAALDRFNEIYA-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 342 qdtshqLFTESVAD-EVLLS--------MDNKDETVVDKILKQ-FDLLeykdRHP------LSLSGGQKQRVAIASAIVS 405
Cdd:PRK11819 111 ------AYAEPDADfDALAAeqgelqeiIDAADAWDLDSQLEIaMDAL----RCPpwdakvTKLSGGERRRVALCRLLLE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 933767453 406 NREIIVFDEPTSGLDlkhmrevARSL----KSLADQGKTLLVITHD 447
Cdd:PRK11819 181 KPDMLLLDEPTNHLD-------AESVawleQFLHDYPGTVVAVTHD 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
291-445 |
3.51e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.81 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKkcGFLQVEG----KTLDWKARLKHCY----MVMQDTSHQLfTESVADEVLLSMD 362
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALANRTE--GNVSVEGdihyNGIPYKEFAEKYPgeiiYVSEEDVHFP-TLTVRETLDFALR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 363 NKDETVVDKIlkqfdlleykdrhplslSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLL 442
Cdd:cd03233 110 CKGNEFVRGI-----------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTT 172
|
...
gi 933767453 443 VIT 445
Cdd:cd03233 173 FVS 175
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
281-447 |
3.54e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.95 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 281 LHIPSAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGK---TLDWKARLKHCYMVMQDTShqLFTESVADE 356
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLiSPTSGTLLFEGEdisTLKPEIYRQQVSYCAQTPT--LFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 357 VL----LSMDNKDETVVDKILKQFDLLEYKDRHPLS-LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSL 431
Cdd:PRK10247 101 LIfpwqIRNQQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEII 180
|
170
....*....|....*..
gi 933767453 432 KSLA-DQGKTLLVITHD 447
Cdd:PRK10247 181 HRYVrEQNIAVLWVTHD 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
355-446 |
4.09e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 355 DEVLLSMDNKDETVVDKILKqfdlleykdrhplSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSL 434
Cdd:PTZ00265 1338 DEFIESLPNKYDTNVGPYGK-------------SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
90
....*....|...
gi 933767453 435 ADQG-KTLLVITH 446
Cdd:PTZ00265 1405 KDKAdKTIITIAH 1417
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
369-446 |
4.15e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 369 VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDlkhmrEVAR-----SLKSLA-DQGKTLL 442
Cdd:NF033858 378 VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD-----PVARdmfwrLLIELSrEDGVTIF 452
|
....
gi 933767453 443 VITH 446
Cdd:NF033858 453 ISTH 456
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-258 |
4.20e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.39 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSV---SDTP 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCI---FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIA-----PDHGEILFDGENIpamSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAMVGSVFQNpkSQFFnvdTDSELAfacENLGYP---QEDILKRIDRTVSDYHIE--------DLMGRSvfaLSGG 146
Cdd:PRK11831 79 LYTVRKRMSMLFQS--GALF---TDMNVF---DNVAYPlreHTQLPAPLLHSTVMMKLEavglrgaaKLMPSE---LSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 147 EKQKIACASSSVLLPGIMVLDEPSSNLD-------MAAIDDLRQVLslwkkqGKTILIAEHRLYYLHDLADRVLYVKDGE 219
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDpitmgvlVKLISELNSAL------GVTCVVVSHDVPEVLSIADHAYIVADKK 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 933767453 220 IEREYTPAEFDSLSDGTRKEI------GLRPFSLsklkPANQYQA 258
Cdd:PRK11831 222 IVAHGSAQALQANPDPRVRQFldgiadGPVPFRY----PAGDYHA 262
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-220 |
5.15e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLvnglvphyyegkLEGDVLLDGKSV--SDtplydlA 82
Cdd:PRK15064 323 ENLTKGFDNGPL---FKNLNLLLEAGERLAIIGENGVGKTTLLRT------------LVGELEPDSGTVkwSE------N 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 83 AMVGSVFQNPKSQFfnvDTDSELAFACENLGYPQED------ILKRIDRTvsdyhiEDLMGRSVFALSGGEKQKIACASS 156
Cdd:PRK15064 382 ANIGYYAQDHAYDF---ENDLTLFDWMSQWRQEGDDeqavrgTLGRLLFS------QDDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAAIDDLRqvLSLWKKQGkTILIAEHRLYYLHDLADRVLYVKDGEI 220
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESLN--MALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
285-450 |
5.17e-08 |
|
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: 52.54 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQvegktldwKARLKHCYMVMQdtsHQLFTESVADEVLLsmdn 363
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSGRIG--------MPEGEDLLFLPQ---RPYLPLGTLREQLI---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 364 kdetvvdkilkqfdlleykdrHPLS--LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLkhmrEVARSLKSLA-DQGKT 440
Cdd:cd03223 86 ---------------------YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLYQLLkELGIT 140
|
170
....*....|
gi 933767453 441 LLVITHDPEL 450
Cdd:cd03223 141 VISVGHRPSL 150
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
389-467 |
5.95e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 389 LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDlKHMRE-VARSLKSLADQGKTLLVITHDPELVmAGCSYVVHMEKGQVK 467
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALD-AHVGErVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDGRVE 860
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-220 |
6.00e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.04 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 6 NVSFSYGEESSGGGI-RNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYegKLEGDVLLDGKSVSDTPLYDLAAm 84
Cdd:cd03233 8 NISFTTGKGRSKIPIlKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNV--SVEGDIHYNGIPYKEFAEKYPGE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 85 vgSVFQNPKSQFFNVDTDSE-LAFACENLGypqedilkridrtvsdyhiedlmGRSVFALSGGEKQKIACASSSVLLPGI 163
Cdd:cd03233 85 --IIYVSEEDVHFPTLTVREtLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 164 MVLDEPSSNLD-MAAIDDLRQVLSLWKKQGKTILI----AEHRLYylhDLADRVLYVKDGEI 220
Cdd:cd03233 140 LCWDNSTRGLDsSTALEILKCIRTMADVLKTTTFVslyqASDEIY---DLFDKVLVLYEGRQ 198
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-240 |
6.24e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAMVGSVFQNPKS----- 94
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-----PTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTslnpr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 95 QFFNVDTDSELAFaceNLGYPQEDILKRIDRTVSDYHI-EDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNL 173
Cdd:PRK15112 104 QRISQILDFPLRL---NTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 174 DMAAIDDL-RQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEI-EREYTPAEFDS-LSDGTRKEI 240
Cdd:PRK15112 181 DMSMRSQLiNLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVvERGSTADVLASpLHELTKRLI 250
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-307 |
6.67e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 55.61 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 136 MGRSVFALSGGEKQ--KIACA-SSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLhDLADRV 212
Cdd:PRK00635 803 LGRPLSSLSGGEIQrlKLAYElLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYV 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 213 LYV------KDGEIEREYTPAEFDSLSDGTRKeiGLRPF-----SLSKLKPANQyQAHTAKQMEFQNfcfAYKKREPesl 281
Cdd:PRK00635 882 LELgpeggnLGGYLLASCSPEELIHLHTPTAK--ALRPYlsspqELPYLPDPSP-KPPVPADITIKN---AYQHNLK--- 952
|
170 180
....*....|....*....|....*.
gi 933767453 282 HIPSAeLPVGETIAIIGLNGAGKSTL 307
Cdd:PRK00635 953 HIDLS-LPRNALTAVTGPSASGKHSL 977
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
389-470 |
8.37e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 55.03 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 389 LSGGQKQRVAIASAIV---SNREIIVFDEPTSGLdlkHMREVAR---SLKSLADQGKTLLVITHDPElVMAGCSYVVHM- 461
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGL---HFHDIRKlleVLHRLVDKGNTVVVIEHNLD-VIKTADWIIDLg 902
|
90 100
....*....|....*....|....*.
gi 933767453 462 ----EKG-------------QVKESY 470
Cdd:COG0178 903 peggDGGgeivaegtpeevaKVKASY 928
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
280-465 |
9.19e-08 |
|
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: 54.45 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 280 SLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKkCGflQVEGKTLDWKARLKHCYMvmQDTS-------HQLFT-- 350
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYP-HG--TWDGEIYWSGSPLKASNI--RDTEragiviiHQELTlv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 351 --ESVADEVLLSMD--------NKDETV--VDKILKQFDLLEYKDRHPLS-LSGGQKQRVAIASAIVSNREIIVFDEPTS 417
Cdd:TIGR02633 91 peLSVAENIFLGNEitlpggrmAYNAMYlrAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 933767453 418 GLDLKHMREVARSLKSLADQGKTLLVITHDPELVMAGCSYVVHMEKGQ 465
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
389-446 |
9.36e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 9.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 389 LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSL-ADQGKTLLVITH 446
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAH 638
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-207 |
1.01e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.50 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 27 INTGEFVLLTGESGCGKTTitrLVNGLVPHYYEGKLEGDVLLDGKSVSDTPLydlaAMVGSVFQNpkSQFFNVDTDSELA 106
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKST---LLNALAGRIQGNNFTGTILANNRKPTKQIL----KRTGFVTQD--DILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 107 FACENLGYPQEdiLKRIDRT-VSDYHIEDL---------MGRS-VFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDM 175
Cdd:PLN03211 162 VFCSLLRLPKS--LTKQEKIlVAESVISELgltkcentiIGNSfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190
....*....|....*....|....*....|....*.
gi 933767453 176 AAIDDLRQVLSLWKKQGKTILIAEH----RLYYLHD 207
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMFD 275
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-233 |
1.03e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegklegdvlldgkSVSDTPlydl 81
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP----------------PRSDAS---- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 AAMVGSVFQNPK-SQFFNVDTDSELAFACEnlgYPQEDILKRIDRTVSDYHIEDLMG--------RSVfALSGGEKQKIA 152
Cdd:PLN03130 675 VVIRGTVAYVPQvSWIFNATVRDNILFGSP---FDPERYERAIDVTALQHDLDLLPGgdlteigeRGV-NISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 153 CASSSVLLPGIMVLDEPSSNLDmAAIDdlRQVLSLWKK---QGKTILIAEHRLYYLHDLaDRVLYVKDGEIEREYTpaeF 229
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALD-AHVG--RQVFDKCIKdelRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGT---Y 823
|
....
gi 933767453 230 DSLS 233
Cdd:PLN03130 824 EELS 827
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
285-446 |
1.03e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLDwKARLKH----CYMVMQDTSHQLFT--ESVADEV 357
Cdd:PRK13540 21 SFHLPAGGLLHLKGSNGAGKTTLLKLIAGLlNPEKGEILFERQSIK-KDLCTYqkqlCFVGHRSGINPYLTlrENCLYDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 358 LLSMDNKDetvVDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQ 437
Cdd:PRK13540 100 HFSPGAVG---ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAK 176
|
....*....
gi 933767453 438 GKTLLVITH 446
Cdd:PRK13540 177 GGAVLLTSH 185
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-224 |
1.16e-07 |
|
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: 52.93 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTI----TRLVNglvphyyegkLEGDVLLDGKSVSDTPLYDLAAMVGSVfqnPKSQ 95
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN----------TEGDIQIDGVSWNSVPLQKWRKAFGVI---PQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 96 FF-------NVD-----TDSELAFACENLGypqediLKRIdrtvsdyhIEDLMGRSVF-------ALSGGEKQKIACASS 156
Cdd:cd03289 87 FIfsgtfrkNLDpygkwSDEEIWKVAEEVG------LKSV--------IEQFPGQLDFvlvdggcVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 157 SVLLPGIMVLDEPSSNLDMAAIDDLRQVLslwkKQ---GKTILIAEHRLYYLHDlADRVLYVKDGEIeREY 224
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTL----KQafaDCTVILSEHRIEAMLE-CQRFLVIEENKV-RQY 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-212 |
2.12e-07 |
|
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: 51.98 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 30 GEFVLLTGESGCGKTTITRLVNG-LVPHYyeGKLEgdvlldgksvsDTPLYD--LAAMVGSVFQNpksqFFNVDTDSELA 106
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPNL--GKFD-----------DPPDWDeiLDEFRGSELQN----YFTKLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 107 FACEnlgyPQ-------------EDILKRIDRT------VSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLD 167
Cdd:cd03236 89 VIVK----PQyvdlipkavkgkvGELLKKKDERgkldelVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 933767453 168 EPSSNLdmaaidDLRQVLSLWK------KQGKTILIAEHRLYYLHDLADRV 212
Cdd:cd03236 165 EPSSYL------DIKQRLNAARlirelaEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
292-446 |
2.40e-07 |
|
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: 53.86 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 292 ETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLDWKARLKHCYMVMQDTSHQLFTE-SVADEVLLSMDNKDETVV 369
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLlPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 370 DKILKQFDLLE------YKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLAdQGKTLLV 443
Cdd:TIGR01257 1037 EAQLEMEAMLEdtglhhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIM 1115
|
...
gi 933767453 444 ITH 446
Cdd:TIGR01257 1116 STH 1118
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
263-468 |
2.50e-07 |
|
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: 53.41 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 263 QMEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTL------DWKARLK 335
Cdd:TIGR00957 1284 RVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRiNESAEGEIIIDGLNIakiglhDLRFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 336 hcyMVMQDTShqLFTESVAdevlLSMDNKDETVVDKILKQFDLLEYKD---------RHPLS-----LSGGQKQRVAIAS 401
Cdd:TIGR00957 1364 ---IIPQDPV--LFSGSLR----MNLDPFSQYSDEEVWWALELAHLKTfvsalpdklDHECAeggenLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 402 AIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGkTLLVITHDPELVMaGCSYVVHMEKGQVKE 468
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC-TVLTIAHRLNTIM-DYTRVIVLDKGEVAE 1499
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
359-453 |
2.79e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 53.15 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 LSMDNKDETVVDKILK------QFDL---LEY--KDRHPLSLSGGQKQRVAIASAIVSNRE--IIVFDEPTSGLdlkHMR 425
Cdd:PRK00349 449 LKLSEQEAKIAEPILKeirerlKFLVdvgLDYltLSRSAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGL---HQR 525
|
90 100 110
....*....|....*....|....*....|.
gi 933767453 426 EVAR---SLKSLADQGKTLLVITHDPELVMA 453
Cdd:PRK00349 526 DNDRlieTLKHLRDLGNTLIVVEHDEDTIRA 556
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
291-471 |
3.31e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICG----------LEK--KCGFLQ------VEGKTLDWKAR-LKHCYMVM---QDTSHQL 348
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGevllddgriiYEQdlIVARLQqdpprnVEGTVYDFVAEgIEEQAEYLkryHDISHLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 349 FTESvADEVLlsmdNKDETVVDKI----LKQFD--------LLEYKDRHPLS-LSGGQKQRVAIASAIVSNREIIVFDEP 415
Cdd:PRK11147 109 ETDP-SEKNL----NELAKLQEQLdhhnLWQLEnrinevlaQLGLDPDAALSsLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 416 TSGLDLKHMREVARSLKSLadQGkTLLVITHDPELVMAGCSYVVHMEKGQVKeSYP 471
Cdd:PRK11147 184 TNHLDIETIEWLEGFLKTF--QG-SIIFISHDRSFIRNMATRIVDLDRGKLV-SYP 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-220 |
4.57e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.08 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 5 QNVSFSYGeesSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNG-LVPHyyegklEGDVLLDGKsvsDTPLYDLAA 83
Cdd:PRK11701 10 RGLTKLYG---PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPD------AGEVHYRMR---DGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 84 MV------------GSVFQNPK-------SQFFNVdtdSELAFACENLGYpqedilKRIDRTVSDY---------HIEDL 135
Cdd:PRK11701 78 LSeaerrrllrtewGFVHQHPRdglrmqvSAGGNI---GERLMAVGARHY------GDIRATAGDWlerveidaaRIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 136 MGrsvfALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAA----IDDLRqvlSLWKKQGKTILIAEHRLYYLHDLADR 211
Cdd:PRK11701 149 PT----TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVqarlLDLLR---GLVRELGLAVVIVTHDLAVARLLAHR 221
|
....*....
gi 933767453 212 VLYVKDGEI 220
Cdd:PRK11701 222 LLVMKQGRV 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
134-451 |
4.94e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 134 DLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKqgkTILIAEHRLYYLHDLADRVL 213
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK---TFIVVSHAREFLNTVVTDIL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 214 YVKDGEI----------ER----------------EYTPAEFDSLSDGTRKEIGLRPFSLSKLKpANQYQAHTAKQMEFQ 267
Cdd:PLN03073 413 HLHGQKLvtykgdydtfERtreeqlknqqkafesnERSRSHMQAFIDKFRYNAKRASLVQSRIK-ALDRLGHVDAVVNDP 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 268 NFCFAYKKREPE------SLHIPSAELPVGET--------------IAIIGLNGAGKSTLARCICGLekkcgfLQVEGKT 327
Cdd:PLN03073 492 DYKFEFPTPDDRpgppiiSFSDASFGYPGGPLlfknlnfgidldsrIAMVGPNGIGKSTILKLISGE------LQPSSGT 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 328 LDWKARLKHCYMvmqdTSHQLFTESVADEVLLSMDNKDETVVDKILK----QFDLLEYKDRHPL-SLSGGQKQRVAIASA 402
Cdd:PLN03073 566 VFRSAKVRMAVF----SQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRahlgSFGVTGNLALQPMyTLSGGQKSRVAFAKI 641
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 933767453 403 IVSNREIIVFDEPTSGLDLKHMREVARSLksLADQGKTLLViTHDPELV 451
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMV-SHDEHLI 687
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
287-446 |
5.01e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 287 ELPVGETIAIIGLNGAGKSTLARCICGLEKkcgfLQVEGKTLDWKARL-----------KHCYMVMQ------DTSHQLF 349
Cdd:PRK09580 23 EVRPGEVHAIMGPNGSGKSTLSATLAGRED----YEVTGGTVEFKGKDllelspedragEGIFMAFQypveipGVSNQFF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 350 TESVADEVllsMDNKDETVVDKILKQfDLLEYKDR---HPLSL---------SGGQKQRVAIASAIVSNREIIVFDEPTS 417
Cdd:PRK09580 99 LQTALNAV---RSYRGQEPLDRFDFQ-DLMEEKIAllkMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDS 174
|
170 180
....*....|....*....|....*....
gi 933767453 418 GLDLKHMREVARSLKSLADQGKTLLVITH 446
Cdd:PRK09580 175 GLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-228 |
5.40e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 23 VNLTINTGEFVLLTGESGCGKTTITRLVNglvphYYEGKLEGDVLLDGKSVSDTPLYDLAAMVGSVFQN-PKSQFFNVdt 101
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLG-----RHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTV-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 102 dSELAfaceNLG-YPQEDILKRI---DRTVSDYHIeDLMG------RSVFALSGGEKQKIACA-----SSSVLLpgimvL 166
Cdd:PRK10575 103 -RELV----AIGrYPWHGALGRFgaaDREKVEEAI-SLVGlkplahRLVDSLSGGERQRAWIAmlvaqDSRCLL-----L 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 167 DEPSSNLDMA-AIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTPAE 228
Cdd:PRK10575 172 DEPTSALDIAhQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
285-474 |
6.39e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.34 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICGLEK--------KCGFLQVEGKTLDWKARLK----HCYMVMQDTSHQLF-TE 351
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrvtadRMRFDDIDLLRLSPRERRKlvghNVSMIFQEPQSCLDpSE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 352 SVADEVLLSMD------------NKDETVVDKILKQFDLLEYKD---RHPLSLSGGQKQRVAIASAIVSNREIIVFDEPT 416
Cdd:PRK15093 107 RVGRQLMQNIPgwtykgrwwqrfGWRKRRAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIADEPT 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 933767453 417 SGLDLKHMREVARSLKSL-ADQGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:PRK15093 187 NAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-200 |
7.12e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGE-FVLLtGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTplyDLAAM--VGSVfqnpkSQFFN 98
Cdd:NF033858 284 HVSFRIRRGEiFGFL-GSNGCGKSTTMKMLTGLLP-----ASEGEAWLFGQPVDAG---DIATRrrVGYM-----SQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 VDtdSELAFAcENL-------GYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSS 171
Cdd:NF033858 350 LY--GELTVR-QNLelharlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190
....*....|....*....|....*....|
gi 933767453 172 NLDMAAIDDL-RQVLSLWKKQGKTILIAEH 200
Cdd:NF033858 427 GVDPVARDMFwRLLIELSREDGVTIFISTH 456
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
291-474 |
9.84e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 50.67 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGLEKKCgfLQVEGKTLDW----------KARLK----HCYMVMQDTSHQLF-TESVAD 355
Cdd:COG4170 33 GEIRGLVGESGSGKSLIAKAICGITKDN--WHVTADRFRWngidllklspRERRKiigrEIAMIFQEPSSCLDpSAKIGD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 356 EVLLSMDNKD------------ETVVDKILKQFDLLEYKD---RHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLD 420
Cdd:COG4170 111 QLIEAIPSWTfkgkwwqrfkwrKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAME 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 421 LKHMREVARSLKSLAD-QGKTLLVITHDPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:COG4170 191 STTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-218 |
1.08e-06 |
|
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: 51.55 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 15 SSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVphyyeGKLEGDVLLDGKSVSdTPLYDLAAMVGSVfqnpkS 94
Cdd:TIGR01257 1950 TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDT-----TVTSGDATVAGKSIL-TNISDVHQNMGYC-----P 2018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 95 QFFNVD---TDSELAFACENL-GYPQEDILKridrtVSDYHIEDLmGRSVFA------LSGGEKQKIACASSSVLLPGIM 164
Cdd:TIGR01257 2019 QFDAIDdllTGREHLYLYARLrGVPAEEIEK-----VANWSIQSL-GLSLYAdrlagtYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933767453 165 VLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDG 218
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-202 |
1.16e-06 |
|
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: 51.17 E-value: 1.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 136 MGRSVFALSGGEKQKIACA---SSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRL 202
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAkelSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
264-488 |
1.83e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 264 MEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARC---ICGLEKkcGFLQVEGKTLDwKARLKHCYMV 340
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNAlfrIVELEK--GRIMIDDCDVA-KFGLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 341 MQ--DTSHQLFTESVADEVLLSMDNKDETVVdKILKQFDLLEYKDRHPLSL-----------SGGQKQRVAIASAIVSNR 407
Cdd:PLN03232 1312 LSiiPQSPVLFSGTVRFNIDPFSEHNDADLW-EALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 408 EIIVFDEPTSGLDLKHMREVARSLKSlADQGKTLLVITHDPELVMaGCSYVVHMEKGQVKESYPLDESGSKKVLDFFRIR 487
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTII-DCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
.
gi 933767453 488 Q 488
Cdd:PLN03232 1469 H 1469
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-240 |
2.03e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 18 GGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVS-DTPLYDLAAMVGSVFQNPKSQ- 95
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISpRSPLDAVKKGMAYITESRRDNg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 96 FF-NVDTDSELAFA--CENLGYPQEDIL--KRIDRTVSDYHIEDL------MGRSVFALSGGEKQKIACASSSVLLPGIM 164
Cdd:PRK09700 352 FFpNFSIAQNMAISrsLKDGGYKGAMGLfhEVDEQRTAENQRELLalkchsVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 165 VLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEreytpAEFDSLSDGTRKEI 240
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT-----QILTNRDDMSEEEI 502
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
383-447 |
2.59e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.77 E-value: 2.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 383 DRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLkhmrEV-ARSLKSL----ADQGKTLLVITHD 447
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVqARLLDLLrglvRELGLAVVIVTHD 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-202 |
4.11e-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: 49.52 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKTTIT----RLVNglvphyyegkLEGDVLLDGKSVSDTP 77
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAV-LQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLS----------TEGEIQIDGVSWNSVT 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAAMVGSVfqnPKSQFF-------NVD-----TDSELAFACENLGYpQEDILKRIDRTvsDYHIEDlmgrSVFALSG 145
Cdd:TIGR01271 1287 LQTWRKAFGVI---PQKVFIfsgtfrkNLDpyeqwSDEEIWKVAEEVGL-KSVIEQFPDKL--DFVLVD----GGYVLSN 1356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 146 GEKQkIACASSSVLLPG-IMVLDEPSSNLDMAAIDDLRQVLslwkKQG---KTILIAEHRL 202
Cdd:TIGR01271 1357 GHKQ-LMCLARSILSKAkILLLDEPSAHLDPVTLQIIRKTL----KQSfsnCTVILSEHRV 1412
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
291-446 |
4.39e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICGL-EKKCGFLQVEGKTLD------WKARLKHCYMVMQDTS-----HqlFTESVADEVL 358
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLlHVESGQIQIDGKTATrgdrsrFMAYLGHLPGLKADLStlenlH--FLCGLHGRRA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 359 LSMDNKDETVVDkilkqfdLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQG 438
Cdd:PRK13543 115 KQMPGSALAIVG-------LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGG 187
|
....*...
gi 933767453 439 KTLLVITH 446
Cdd:PRK13543 188 GAALVTTH 195
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
263-468 |
5.12e-06 |
|
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: 47.93 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 263 QMEFQNFCFAYKKREPESLHIPSAELPVGETIAIIGLNGAGKSTLARCICGLEKKCGFLQVEGktLDW-KARLKHCYMVM 341
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDG--VSWnSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 342 QDTSHQLFTES--------------------VADEVLLsmdnkdETVVDKILKQFDL-LEYKDrhpLSLSGGQKQRVAIA 400
Cdd:cd03289 80 GVIPQKVFIFSgtfrknldpygkwsdeeiwkVAEEVGL------KSVIEQFPGQLDFvLVDGG---CVLSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 401 SAIVSNREIIVFDEPTSGLDLKHMREVARSLKSlADQGKTLLVITHDPElVMAGCSYVVHMEKGQVKE 468
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIE-AMLECQRFLVIEENKVRQ 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-201 |
8.10e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLV-PHyyegklEGDVLLDGKSVSDtply 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPL---LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPE------KGEILFERQSIKK---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 80 DLAAMVGSV-FQNPKSQFFNVDTDSE-----LAFACENLGypqedilkrIDRTVSDYHIEDLMGRSVFALSGGEKQKIAC 153
Cdd:PRK13540 68 DLCTYQKQLcFVGHRSGINPYLTLREnclydIHFSPGAVG---------ITELCRLFSLEHLIDYPCGLLSSGQKRQVAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 933767453 154 ASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHR 201
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
261-473 |
2.28e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 261 AKQMEFQNFCFAYKKREpeSLHIPSAELPVGETIAIIGLNGAGKSTLAR-----CICGLEKKCGFLQVEGKTLDWKARLK 335
Cdd:PLN03073 175 IKDIHMENFSISVGGRD--LIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIPKNCQILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 336 HCYM--------VMQDTSHQL-------FTESVADEVLLSMDNKDETVVDK----ILKQFDLL----------------- 379
Cdd:PLN03073 253 QCVLntdiertqLLEEEAQLVaqqreleFETETGKGKGANKDGVDKDAVSQrleeIYKRLELIdaytaearaasilagls 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 380 ---EYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLkhmREVARSLKSLADQGKTLLVITHDPELVMAGCS 456
Cdd:PLN03073 333 ftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKWPKTFIVVSHAREFLNTVVT 409
|
250
....*....|....*..
gi 933767453 457 YVVHMEkGQVKESYPLD 473
Cdd:PLN03073 410 DILHLH-GQKLVTYKGD 425
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
325-445 |
2.35e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 325 GKTLDWKARLKHCYMVMQDTSHQLFTESVADEVL--LSMDNKDETVVDKilkqfDLLEykdrhplSLSGGQKQRVAIASA 402
Cdd:TIGR00956 156 GETLDFAARCKTPQNRPDGVSREEYAKHIADVYMatYGLSHTRNTKVGN-----DFVR-------GVSGGERKRVSIAEA 223
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 933767453 403 IVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVIT 445
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-242 |
2.39e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVSDTPLYDLAAMVgsvfqnPKSQffnv 99
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVR-----LASGKISILGQPTRQALQKNLVAYV------PQSE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 100 DTDSELAFACEN------------LGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLD 167
Cdd:PRK15056 88 EVDWSFPVLVEDvvmmgryghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 168 EPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVK-----DGEIEREYTPAEFDSLSDGTRKEIGL 242
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKgtvlaSGPTETTFTAENLELAFSGVLRHVAL 247
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
112-221 |
2.47e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 112 LGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQ 191
Cdd:NF000106 114 LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
90 100 110
....*....|....*....|....*....|....*.
gi 933767453 192 GKTILIAEHRLYYLHDLA------DRVLYVKDGEIE 221
Cdd:NF000106 194 GATVLLTTQYMEEAEQLAheltviDRGRVIADGKVD 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-242 |
2.60e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.56 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHyyegkLEGDVLLDGKSVSDT----------------------- 76
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP-----ASGSIRLDGEDITGLsprerrrlgvayipedrlgrglv 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLYDLA--AMVGSVFQNPKSQFFNVDTDSELAFAcenlgypqEDILKRID-RTVSdyhIEDLMGrsvfALSGGEKQKiac 153
Cdd:COG3845 349 PDMSVAenLILGRYRRPPFSRGGFLDRKAIRAFA--------EELIEEFDvRTPG---PDTPAR----SLSGGNQQK--- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 154 asssVLL-------PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTP 226
Cdd:COG3845 411 ----VILarelsrdPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPA 486
|
250
....*....|....*.
gi 933767453 227 AEFdslsdgTRKEIGL 242
Cdd:COG3845 487 AEA------TREEIGL 496
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
143-219 |
3.30e-05 |
|
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: 44.49 E-value: 3.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933767453 143 LSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAA-IDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVlYVKDGE 219
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQrLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI-HVFEGE 148
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
136-202 |
3.42e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.30 E-value: 3.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933767453 136 MGRSVFALSGGEKQKIACASSsvLL-----PGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRL 202
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKE--LSkrstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
285-449 |
4.03e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 285 SAELPVGETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGktldwkaRLKHCYMVmqdtsHQLFTESVADEVL--LSM 361
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKIKHSG-------RISFSPQT-----SWIMPGTIKDNIIfgLSY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 362 DNKDETVVDK---ILKQFDLLEYKDRHPL-----SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKS 433
Cdd:TIGR01271 514 DEYRYTSVIKacqLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLC 593
|
170
....*....|....*.
gi 933767453 434 LADQGKTLLVITHDPE 449
Cdd:TIGR01271 594 KLMSNKTRILVTSKLE 609
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
389-446 |
4.39e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.22 E-value: 4.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 389 LSGGQKQRVAIASAIvSNRE----IIVFDEPTSGLdlkHMREVARSLK---SLADQGKTLLVITH 446
Cdd:PRK00349 831 LSGGEAQRVKLAKEL-SKRStgktLYILDEPTTGL---HFEDIRKLLEvlhRLVDKGNTVVVIEH 891
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
263-450 |
5.21e-05 |
|
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: 44.57 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 263 QMEFQNFcFAYKKREPeslhIPSAELPVGETIAIIGLNGAGKSTLARCICglekkcgfLQVEGKTldwkARLKHCYMVMQ 342
Cdd:cd03279 5 KLELKNF-GPFREEQV----IDFTGLDNNGLFLICGPTGAGKSTILDAIT--------YALYGKT----PRYGRQENLRS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 343 DTSHQLFTESVADEVLLS-----------MDNKDETVVdKILKQFDLLEYKDRHPLSLSGGQKQRVAIA-----SAIVSN 406
Cdd:cd03279 68 VFAPGEDTAEVSFTFQLGgkkyrversrgLDYDQFTRI-VLLPQGEFDRFLARPVSTLSGGETFLASLSlalalSEVLQN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 933767453 407 R-----EIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPEL 450
Cdd:cd03279 147 RggarlEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEEL 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-230 |
7.40e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.29 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 16 SGGGIRN-VNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKSVS-DTPLYDLAA---------- 83
Cdd:PRK11288 264 KGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATR-----RTAGQVYLDGKPIDiRSPRDAIRAgimlcpedrk 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 84 -----MVGSVFQNpksqffnvdtdseLAFACENLGYPQEDIL-KRIDRTVSDYHIEDLMGRS------VFALSGGEKQKI 151
Cdd:PRK11288 339 aegiiPVHSVADN-------------INISARRHHLRAGCLInNRWEAENADRFIRSLNIKTpsreqlIMNLSGGNQQKA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 152 ACA-----SSSVLLpgimvLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEREYTP 226
Cdd:PRK11288 406 ILGrwlseDMKVIL-----LDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAR 480
|
....
gi 933767453 227 AEFD 230
Cdd:PRK11288 481 EQAT 484
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-234 |
7.76e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 44.90 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 14 ESSGGGIR---NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPHYYegKLEGDVL-LDGKSVSDTPLYDLAAMVGS-- 87
Cdd:COG4170 14 DTPQGRVKavdRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW--HVTADRFrWNGIDLLKLSPRERRKIIGRei 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 88 --VFQNPKSqffNVDTdSELAFA--CENLgyPQEDiLK---------RIDRTVSDYH---I---EDLMGRSVFALSGGEK 148
Cdd:COG4170 92 amIFQEPSS---CLDP-SAKIGDqlIEAI--PSWT-FKgkwwqrfkwRKKRAIELLHrvgIkdhKDIMNSYPHELTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 149 QKIACASSSVLLPGIMVLDEPSSNLD---MAAIddLRQVLSLWKKQGKTILIAEHRLYYLHDLADR--VLY----VKDGE 219
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMEsttQAQI--FRLLARLNQLQGTSILLISHDLESISQWADTitVLYcgqtVESGP 242
|
250 260
....*....|....*....|..
gi 933767453 220 IER-------EYTPAEFDSLSD 234
Cdd:COG4170 243 TEQilksphhPYTKALLRSMPD 264
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-228 |
8.22e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEESSGGgIRNVNLTINTGEFVLLTGESGCGKT----TITRLVnglvphyyegKLE-GDVLLDGKSVSDT 76
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPV-LHGLSFEISPSEKVGIVGRTGAGKSsmlnALFRIV----------ELErGRILIDGCDISKF 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 77 PLYDLAAMVGSVFQNP----KSQFFNVDTDSElafacenlgYPQEDILKRIDRTvsdyHIEDLMGRSVFAL--------- 143
Cdd:PLN03130 1307 GLMDLRKVLGIIPQAPvlfsGTVRFNLDPFNE---------HNDADLWESLERA----HLKDVIRRNSLGLdaevseage 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 144 --SGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAiDDLRQvlslwkkqgKTI---------LIAEHRLYYLHDlADRV 212
Cdd:PLN03130 1374 nfSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT-DALIQ---------KTIreefksctmLIIAHRLNTIID-CDRI 1442
|
250
....*....|....*.
gi 933767453 213 LYVKDGEIEREYTPAE 228
Cdd:PLN03130 1443 LVLDAGRVVEFDTPEN 1458
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
6-245 |
9.09e-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: 44.46 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 6 NVSFSYGEESSGGGIRNVNLTINTGEFVLLTGESGCGKTTITRLVNG-LVPHyyegklEGDVLLDGKsVSDTPLYDLaAM 84
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPS------EGKIKHSGR-ISFSSQFSW-IM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 85 VGSVFQNPksqFFNVDTDS----ELAFACEnlgyPQEDILK--RIDRTVsdyhiedlMGRSVFALSGGEKQKIACASSSV 158
Cdd:cd03291 111 PGTIKENI---IFGVSYDEyrykSVVKACQ----LEEDITKfpEKDNTV--------LGEGGITLSGGQRARISLARAVY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 159 LLPGIMVLDEPSSNLDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHdLADRVLYVKDGEIEREYTPAEFDSLS-DGTR 237
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLK-KADKILILHEGSSYFYGTFSELQSLRpDFSS 254
|
....*...
gi 933767453 238 KEIGLRPF 245
Cdd:cd03291 255 KLMGYDTF 262
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-184 |
1.41e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYGEESSgggIRNVNLTINTGEFVLLTGESGCGKTTITRLVNGlvPHYYEgKLEGDVLLDGKSVSDTPLYD 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAI---LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYE-VTGGTVEFKGKDLLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 81 LAAM-VGSVFQNP------KSQFFnvdtdseLAFACENL-GYPQEDILKRIDrtVSDYHIE---------DLMGRSV-FA 142
Cdd:PRK09580 75 RAGEgIFMAFQYPveipgvSNQFF-------LQTALNAVrSYRGQEPLDRFD--FQDLMEEkiallkmpeDLLTRSVnVG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933767453 143 LSGGEKQKIACASSSVLLPGIMVLDEPSSNLDmaaIDDLRQV 184
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLD---IDALKIV 184
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
385-468 |
1.80e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 385 HPLS-LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADqgkTLLVITHDPELVMAGCSYVVHMEK 463
Cdd:PRK10636 145 RPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIEQ 221
|
....*
gi 933767453 464 GQVKE 468
Cdd:PRK10636 222 QSLFE 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
383-451 |
2.82e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 2.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933767453 383 DRHPLSLSGGQKQRVAIASAIVSNREII--VFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPELV 451
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI 541
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
291-449 |
3.07e-04 |
|
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: 42.54 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGktldwkaRLKHCYMVmqdtsHQLFTESVADEVL--LSMDN-KDE 366
Cdd:cd03291 63 GEMLAITGSTGSGKTSLLMLILGeLEPSEGKIKHSG-------RISFSSQF-----SWIMPGTIKENIIfgVSYDEyRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 367 TVVDKILKQFDLLEY--KDRHPL-----SLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGK 439
Cdd:cd03291 131 SVVKACQLEEDITKFpeKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANK 210
|
170
....*....|
gi 933767453 440 TLLVITHDPE 449
Cdd:cd03291 211 TRILVTSKME 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-219 |
3.47e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 29 TGEFVLLTGESGCGKTTITRLVnglvpHYYEGKLEGDVLLdgksvsdtplydlaamvgsvfqnpksqffnVDTDselafa 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL-----ARELGPPGGGVIY------------------------------IDGE------ 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 109 cenlgypqedilkRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMA------AIDDLR 182
Cdd:smart00382 40 -------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqealllLLEELR 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933767453 183 QVLSLWKKQGKTILIAEHRLYYLHDLA-----DRVLYVKDGE 219
Cdd:smart00382 107 LLLLLKSEKNLTVILTTNDEKDLGPALlrrrfDRRIVLLLIL 148
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-234 |
3.91e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.11 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNGLVPhyyegKLEGDVLLDGKsVSdtplydlaamVGSVFQNPKSQFFNV 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS-----PTVGKVDRNGE-VS----------VIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 100 DTdseLAFACENLGYPQEDILKRIDRTVSDYHIEDLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAID 179
Cdd:PRK13546 104 EN---IEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933767453 180 DLRQVLSLWKKQGKTILIAEHRLYYLHDLADRVLYVKDGEIEreytpaEFDSLSD 234
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK------DYGELDD 229
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
291-474 |
4.09e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.11 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 291 GETIAIIGLNGAGKSTLARCICG-LEKKCGFLQVEGKTldwkarlkHCYMVMQDTSHQLFTESVADEVLLSMDNKDETV- 368
Cdd:PRK13546 50 GDVIGLVGINGSGKSTLSNIIGGsLSPTVGKVDRNGEV--------SVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIk 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 369 --VDKILKQFDLLEYKDRHPLSLSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITH 446
Cdd:PRK13546 122 amTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSH 201
|
170 180
....*....|....*....|....*...
gi 933767453 447 DPELVMAGCSYVVHMEKGQVKESYPLDE 474
Cdd:PRK13546 202 NLGQVRQFCTKIAWIEGGKLKDYGELDD 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
288-447 |
5.24e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 288 LPVGETIAIIGLNGAGKSTLARCICGLEK-KCGFLQVeGKTldwkarLKHCYMvmqDTSHQlftesvadevllSMDNkDE 366
Cdd:PRK11819 347 LPPGGIVGIIGPNGAGKSTLFKMITGQEQpDSGTIKI-GET------VKLAYV---DQSRD------------ALDP-NK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 367 TVVDKILKQFDLLEYKDRHPLS--------------------LSGGQKQRVAIASAIVSNREIIVFDEPTSGLDLkhmrE 426
Cdd:PRK11819 404 TVWEEISGGLDIIKVGNREIPSrayvgrfnfkggdqqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV----E 479
|
170 180
....*....|....*....|..
gi 933767453 427 VARSLKS-LADQGKTLLVITHD 447
Cdd:PRK11819 480 TLRALEEaLLEFPGCAVVISHD 501
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-214 |
5.50e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.10 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 1 MIDFQNVSFSYgeESSGGGIR---NVNLTINTGEFVLLTGESGCGKTTITRLVNGLVphyyegKLEGDVLLDGKSVSDTP 77
Cdd:PRK15093 3 LLDIRNLTIEF--KTSDGWVKavdRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVT------KDNWRVTADRMRFDDID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 78 LYDLAA-----MVGS----VFQNPKSqffnvdtdselafaCENlgyPQEDILKRIDRTVSDY----------------HI 132
Cdd:PRK15093 75 LLRLSPrerrkLVGHnvsmIFQEPQS--------------CLD---PSERVGRQLMQNIPGWtykgrwwqrfgwrkrrAI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 133 E-----------DLMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSNLDMAAIDDLRQVLS-LWKKQGKTILIAEH 200
Cdd:PRK15093 138 EllhrvgikdhkDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTrLNQNNNTTILLISH 217
|
250
....*....|....*.
gi 933767453 201 RLYYLHDLADR--VLY 214
Cdd:PRK15093 218 DLQMLSQWADKinVLY 233
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
388-449 |
7.04e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 42.03 E-value: 7.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 388 SLSGGQKQRVAIA--------SAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKTLLVITHDPE 449
Cdd:COG4694 491 TLSEGEKTAIALAyflaelegDENDLKKKIVVIDDPVSSLDSNHRFAVASLLKELSKKAKQVIVLTHNLY 560
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
295-467 |
1.40e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 39.60 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 295 AIIGLNGAGKSTLARCICglekkcgflqvegktldwkarlkhcyMVMQDTSHQLFTESVADEV---LLSMDNKD--ETVV 369
Cdd:cd03239 26 AIVGPNGSGKSNIVDAIC--------------------------FVLGGKAAKLRRGSLLFLAgggVKAGINSAsvEITF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 370 DK---ILKQFDLLEYkdrhplsLSGGQKQRVAIAsAIVSNREI-----IVFDEPTSGLDLKHMREVARSLKSLADQGKTL 441
Cdd:cd03239 80 DKsyfLVLQGKVEQI-------LSGGEKSLSALA-LIFALQEIkpspfYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQF 151
|
170 180
....*....|....*....|....*..
gi 933767453 442 LVITHDPELVMAGCSYV-VHMEKGQVK 467
Cdd:cd03239 152 IVITLKKEMFENADKLIgVLFVHGVST 178
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
27-57 |
2.24e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 39.77 E-value: 2.24e-03
10 20 30
....*....|....*....|....*....|...
gi 933767453 27 INTGE-FVLLTGESGCGKTTITR-LVNGLVPHY 57
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRrLLERLPDDV 71
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
138-190 |
2.38e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.21 E-value: 2.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 138 RSVFALSGGEKQKIA----CASSSVLL---------PGIMVLDEPSSNLDMAAIddlRQVLSLWKK 190
Cdd:pfam13558 28 RRSGGLSGGEKQLLAylplAAALAAQYgsaegrppaPRLVFLDEAFAKLDEENI---RTALELLRA 90
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
389-451 |
2.64e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 39.55 E-value: 2.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933767453 389 LSGGQKQRVAIAS--AI--VSNREIIVFDEPTSGLDLKHMREVARSLKSLADQGKtLLVITHDPELV 451
Cdd:cd03272 159 LSGGQKSLVALALifAIqkCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQ-FITTTFRPELL 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-220 |
2.72e-03 |
|
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: 40.70 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 2 IDFQNVSFSYGEeSSGGGIRNVNLTINTGEFVLLTGESGCGKTTitrLVNGLVPHYyeGKLEGDVlldgksvsdtplydl 81
Cdd:TIGR00957 637 ITVHNATFTWAR-DLPPTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALLAEM--DKVEGHV--------------- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 82 aAMVGSVFQNPKSQFFNVDTDSE-LAFACE-NLGY-----------PQEDILKRIDRTVsdyhiedlMGRSVFALSGGEK 148
Cdd:TIGR00957 696 -HMKGSVAYVPQQAWIQNDSLREnILFGKAlNEKYyqqvleacallPDLEILPSGDRTE--------IGEKGVNLSGGQK 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933767453 149 QKIACASSSVLLPGIMVLDEPSSNLDMAA----IDDLRQVLSLWKkqGKTILIAEHRLYYLHDLaDRVLYVKDGEI 220
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHVgkhiFEHVIGPEGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-174 |
3.08e-03 |
|
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: 38.76 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 22 NVNLTINTGEFVLLTGESGCGKTTitrLVNGLVPHYYEGKLEGDVLLDGKsvsdtplydlaamvgsvfqnPKSQFFNVDT 101
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKTAGVITGEILINGR--------------------PLDKNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 102 dselafacenlGY-PQEDIlkridrtvsdyHIEDLMGRSVF-------ALSGGEKQKIACASSSVLLPGIMVLDEPSSNL 173
Cdd:cd03232 82 -----------GYvEQQDV-----------HSPNLTVREALrfsallrGLSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
.
gi 933767453 174 D 174
Cdd:cd03232 140 D 140
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
378-451 |
4.25e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 378 LLEYKDR---HPLS---LSGGQKQRVAIASAIVSNRE--IIVFDEPTSGLDLKHMREVARSLKSLADQGkTLLVITHDPE 449
Cdd:COG4637 242 LLEFREKgldRPFPareLSDGTLRFLALLAALLSPRPppLLCIEEPENGLHPDLLPALAELLREASERT-QVIVTTHSPA 320
|
..
gi 933767453 450 LV 451
Cdd:COG4637 321 LL 322
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
392-461 |
4.27e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 4.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 392 GQKQRVAIASAIVSNREIIVFDEPTSGLDLKHMR---EVARSLKSladqgkTLLVITHDPELVMAGCSyvvHM 461
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRwleDVLNERNS------TMIIISHDRHFLNSVCT---HM 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-218 |
4.56e-03 |
|
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: 39.89 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 20 IRNVNLTINTGEFVLLTGESGCGKTTITRLVNG-LVPHyyegklEGDVLLDGKsVSDTPLYDLaAMVGSVFQNpksQFFN 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPS------EGKIKHSGR-ISFSPQTSW-IMPGTIKDN---IIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933767453 99 VDTD----SELAFACEnlgyPQEDI--LKRIDRTVsdyhiedlMGRSVFALSGGEKQKIACASSSVLLPGIMVLDEPSSN 172
Cdd:TIGR01271 511 LSYDeyryTSVIKACQ----LEEDIalFPEKDKTV--------LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 933767453 173 LDMAAIDDLRQVLSLWKKQGKTILIAEHRLYYLHDlADRVLYVKDG 218
Cdd:TIGR01271 579 LDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
390-451 |
5.67e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 5.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933767453 390 SGGQKQ------RVAIASAIVSNREIIVFDEPTSGLDLKHMREVARSLKSLA---DQGKT--LLVITHDPELV 451
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIksrSQQRNfqLLVITHDEDFV 1273
|
|
| |
