|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-307 |
8.75e-145 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 410.28 E-value: 8.75e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI------ 74
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 75 --RSGSQ-----RIMQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:COG4608 83 tgLSGRElrplrRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEA 227
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 228 QQVLTAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPGNRTLPQGCFFRERCPLATSGC-EVRQSLTTRADGREIRCWR 306
Cdd:COG4608 243 DELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCaTEEPPLREVGPGHQVACHL 322
|
.
gi 15831341 307 A 307
Cdd:COG4608 323 A 323
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-307 |
1.47e-140 |
|
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: 399.43 E-value: 1.47e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS---------HGQYIR 75
Cdd:COG0444 1 LLEVRNLKVYFPTRRGV-------VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitsgeilfDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 76 SGSQRIM--------QMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRP--EYLDRLPHAFSG 145
Cdd:COG0444 74 KLSEKELrkirgreiQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 146 GQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 226 EAQQVLTAPAHPYTRLLLDSLPAIDKPLEEEWALrKTDLPGNRTLPQGCFFRERCPLATSGC-EVRQSLTTRADGREIRC 304
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDPDGRRLIPI-PGEPPSLLNPPSGCRFHPRCPYAMDRCrEEEPPLREVGPGHRVAC 312
|
...
gi 15831341 305 WRA 307
Cdd:COG0444 313 HLY 315
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-250 |
2.17e-121 |
|
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: 358.23 E-value: 2.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 3 DTLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmLQPSHGQyIRSGSQRI- 81
Cdd:COG4172 273 PPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGE-IRFDGQDLd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 82 -------------MQMMFQDPLSSLNPRLPVWRIITEPLWI-AKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:COG4172 351 glsrralrplrrrMQVVFQDPFGSLSPRMTVGQIIAEGLRVhGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEA 227
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPT 510
|
250 260
....*....|....*....|...
gi 15831341 228 QQVLTAPAHPYTRLLLDSLPAID 250
Cdd:COG4172 511 EQVFDAPQHPYTRALLAAAPLLE 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-250 |
3.22e-121 |
|
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: 357.29 E-value: 3.22e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFPARKnwlgktTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI------ 74
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRG------KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 75 --RSGSQ-----RIMQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:COG1123 330 tkLSRRSlrelrRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEA 227
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
250 260
....*....|....*....|...
gi 15831341 228 QQVLTAPAHPYTRLLLDSLPAID 250
Cdd:COG1123 490 EEVFANPQHPYTRALLAAVPSLD 512
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-307 |
7.17e-113 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 329.23 E-value: 7.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFPARKNwLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-- 78
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRG-LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 79 -----------QRIMQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:PRK11308 80 lkadpeaqkllRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEA 227
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 228 QQVLTAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPGNRTLPQGCFFRERCPLATSGCEVRQSLTTRADGREIRCWRA 307
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVACFAV 319
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-225 |
1.85e-106 |
|
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: 309.44 E-value: 1.85e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------S 78
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-------VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 79 QRI-------MQMMFQDPLSSLNPRLPVWRIITEPLWIA-KHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQR 150
Cdd:cd03257 74 RRLrkirrkeIQMVFQDPMSSLNPRMTIGEQIAEPLRIHgKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-252 |
2.87e-103 |
|
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: 302.11 E-value: 2.87e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPARKnwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ---------YIR 75
Cdd:COG1124 1 MLEVRNLSVSYGQGG-------RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEvtfdgrpvtRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 76 SGSQ-RIMQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRralAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIA 154
Cdd:COG1124 74 RKAFrRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREER---IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 155 RALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
250
....*....|....*...
gi 15831341 235 AHPYTRLLLDSLPAIDKP 252
Cdd:COG1124 231 KHPYTRELLAASLAFERA 248
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-307 |
3.10e-99 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 295.08 E-value: 3.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRD--VHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYIRS 76
Cdd:PRK15079 8 LLEVADlkVHFDIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGevawlgKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 77 GSQRIM-------QMMFQDPLSSLNPRLPVWRIITEPLWIAK-HSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQR 148
Cdd:PRK15079 88 MKDDEWravrsdiQMIFQDPLASLNPRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 149 QRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQ 228
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 229 QVLTAPAHPYTRLLLDSLPAIDKPLE--EEWALRKTDLPGNRTLPQGCFFRERCPLATSGCEVRQSLTTRADGREIRCWR 306
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVPIPDPDLErnKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFRHAVSCLK 327
|
.
gi 15831341 307 A 307
Cdd:PRK15079 328 V 328
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-245 |
2.62e-86 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 259.38 E-value: 2.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 4 TLLTLRDVHINFPARKNWLGKttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------ 77
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRR--QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleyg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 -----SQRImQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIA 152
Cdd:COG4167 81 dykyrCKHI-RMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 153 IARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLT 232
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239
|
250
....*....|...
gi 15831341 233 APAHPYTRLLLDS 245
Cdd:COG4167 240 NPQHEVTKRLIES 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-252 |
6.43e-85 |
|
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: 264.62 E-value: 6.43e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFparknwlGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS----------H 70
Cdd:COG4172 2 MSMPLLSVEDLSVAF-------GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpsgsilfD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 71 GQYIRSGSQRIMQ--------MMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIR-PEY-LDRLP 140
Cdd:COG4172 75 GQDLLGLSERELRrirgnriaMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdPERrLDAYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 141 HAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250 260 270
....*....|....*....|....*....|..
gi 15831341 221 IVELGEAQQVLTAPAHPYTRLLLDSLPAIDKP 252
Cdd:COG4172 235 IVEQGPTAELFAAPQHPYTRKLLAAEPRGDPR 266
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-307 |
2.66e-75 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 233.85 E-value: 2.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFparknwlgKTTE-HVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQpSHGqyIRSGSQ 79
Cdd:PRK09473 8 QADALLDVKDLRVTF--------STPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANG--RIGGSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 80 RI--------------------MQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQrrALAEEL----AVQVgirPEY 135
Cdd:PRK09473 77 TFngreilnlpekelnklraeqISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAE--AFEESVrmldAVKM---PEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 136 LDRL---PHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDR 212
Cdd:PRK09473 152 RKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 213 VAVMYLGQIVELGEAQQVLTAPAHPYTRLLLDSLPAIDkplEEEWALrkTDLPGNR----TLPQGCFFRERCPLATSGCE 288
Cdd:PRK09473 232 VLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLD---AEGESL--LTIPGNPpnllRLPKGCPFQPRCPHAMEICS 306
|
330
....*....|....*....
gi 15831341 289 VRQSLTTRADGREIRCWRA 307
Cdd:PRK09473 307 SAPPLEEFGPGRLRACFKP 325
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-243 |
4.04e-72 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 231.52 E-value: 4.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 4 TLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLqPSHGQYIRSGS----- 78
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQplhnl 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 79 --------QRIMQMMFQDPLSSLNPRLPVWRIITEPLWI-AKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQ 149
Cdd:PRK15134 353 nrrqllpvRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQ 229
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512
|
250
....*....|....
gi 15831341 230 VLTAPAHPYTRLLL 243
Cdd:PRK15134 513 VFAAPQQEYTRQLL 526
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-265 |
5.06e-69 |
|
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: 222.86 E-value: 5.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 3 DTLLTLRDVHINFPARKnwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS---------HGQY 73
Cdd:COG1123 2 TPLLEVRDLSVRYPGGD---------VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgrisgevllDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 74 IRSGSQRIMQ----MMFQDPLSSLNPrLPVWRIITEPLWIAKHSSEQqRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQ 149
Cdd:COG1123 73 LLELSEALRGrrigMVFQDPMTQLNP-VTVGDQIAEALENLGLSRAE-ARARVLELLEAVGL-ERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQ 229
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 15831341 230 VLTAPAhpytrlLLDSLPAIDKPLEEEWALRKTDLP 265
Cdd:COG1123 230 ILAAPQ------ALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-267 |
5.55e-68 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 222.81 E-value: 5.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 2 SDTLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRI 81
Cdd:PRK10261 310 GEPILQVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG-QRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 82 --------------MQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQ 147
Cdd:PRK10261 389 dtlspgklqalrrdIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQ 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEA 227
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15831341 228 QQVLTAPAHPYTRLLLDSLPAIDKPLEE-EWALRKTDLPGN 267
Cdd:PRK10261 549 RAVFENPQHPYTRKLMAAVPVADPSRQRpQRVLLSDDLPSN 589
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-245 |
1.27e-62 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 199.25 E-value: 1.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 3 DTLLTLRDVHINFPARKNWLGKttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG----- 77
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 ------SQRImQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRI 151
Cdd:PRK15112 80 gdysyrSQRI-RMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
250
....*....|....
gi 15831341 232 TAPAHPYTRLLLDS 245
Cdd:PRK15112 239 ASPLHELTKRLIAG 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
31-304 |
1.48e-61 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 198.43 E-value: 1.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQ-PS---------HGQYIRSGSQRIMQ--------MMFQDPLSS 92
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGrvmaeklefNGQDLQRISEKERRnlvgaevaMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 93 LNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGI-RPEY-LDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpDPASrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 171 SALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYTRLLLDSLPaid 250
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALP--- 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 251 kpleeEWALRKTDL-------PGNRTLPQGCFFRERCPLATSGCEVRQSLTTRADGREIRC 304
Cdd:PRK11022 259 -----EFAQDKARLaslpgvvPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAGRQSKC 314
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-248 |
5.84e-61 |
|
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: 195.02 E-value: 5.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 4 TLLTLRDVHINFpaRKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS----- 78
Cdd:TIGR02769 1 SLLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyql 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 79 --------QRIMQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQR 150
Cdd:TIGR02769 79 drkqrrafRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQV 230
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
250
....*....|....*....
gi 15831341 231 LTApAHPYTRLLLDS-LPA 248
Cdd:TIGR02769 239 LSF-KHPAGRNLQSAvLPE 256
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
32-248 |
1.46e-60 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 193.75 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------------QRIMQMMFQDPLSSLNPRLP 98
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklnraqrkafRRDIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 99 VWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831341 179 AQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE---LGEAQQVltapAHPYTRLLLDS-LPA 248
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDKLTF----SSPAGRVLQNAvLPA 257
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-304 |
3.45e-59 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 192.43 E-value: 3.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS----------HGQYI--RSGSQR--IM----QMMFQDPL 90
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLlkLSPRERrkIIgreiAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 91 SSLNPRLPVWRIITE--PLWIAKHS---SEQQRRALAEELAVQVGIR--PEYLDRLPHAFSGGQRQRIAIARALSSQPDV 163
Cdd:COG4170 100 SCLDPSAKIGDQLIEaiPSWTFKGKwwqRFKWRKKRAIELLHRVGIKdhKDIMNSYPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 164 IVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYTRLLL 243
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALL 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 244 DSLPAIDKPLEEEWALrkTDLPGN----RTLPQGCFFRERCPLATSGCeVRQSLTTRADGREIRC 304
Cdd:COG4170 260 RSMPDFRQPLPHKSRL--NTLPGSipplQHLPIGCRLGPRCPYAQKKC-VETPRLRKIKGHEFAC 321
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-266 |
5.23e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 181.81 E-value: 5.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-- 83
Cdd:COG1135 2 IELENLSKTFPTKGG-------PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGS-VLVDGVDLTAls 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 84 ------------MMFQDP--LSSLNprlpVWRIITEPLWIAKHSSEQqRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQ 149
Cdd:COG1135 74 erelraarrkigMIFQHFnlLSSRT----VAENVALPLEIAGVPKAE-IRKRVAELLELVGLS-DKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQ 229
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLD 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 15831341 230 VLTAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPG 266
Cdd:COG1135 228 VFANPQSELTRRFLPTVLNDELPEELLARLREAAGGG 264
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-240 |
7.25e-54 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 175.55 E-value: 7.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFPARknwlgktteHVHaiNGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYI 74
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDR---------VVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDsgeilvDGQDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 75 RSGSQRIMQ-------MMFQDP--LSSLNprlpVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSG 145
Cdd:COG1127 70 TGLSEKELYelrrrigMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 146 GQRQRIAIARALSSQPDVIVLDEPTSALD-ISVqAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVEL 224
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|....*.
gi 15831341 225 GEAQQVLTAPaHPYTR 240
Cdd:COG1127 224 GTPEELLASD-DPWVR 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-256 |
2.18e-53 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 182.21 E-value: 2.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFpaRKnwlGKTTEHVhaINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLqPS----------- 69
Cdd:PRK15134 1 MTQPLLAIENLSVAF--RQ---QQTVRTV--VNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypsgdir 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 70 -HGQYIRSGSQRI--------MQMMFQDPLSSLNPRLPVWRIITEPLwiAKHSSEQQRRALAEELAV--QVGIR--PEYL 136
Cdd:PRK15134 73 fHGESLLHASEQTlrgvrgnkIAMIFQEPMVSLNPLHTLEKQLYEVL--SLHRGMRREAARGEILNCldRVGIRqaAKRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 137 DRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:PRK15134 151 TDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15831341 217 YLGQIVELGEAQQVLTAPAHPYTRLLLDSLPAIDK-PLEEE 256
Cdd:PRK15134 231 QNGRCVEQNRAATLFSAPTHPYTQKLLNSEPSGDPvPLPEP 271
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-234 |
1.37e-52 |
|
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: 172.38 E-value: 1.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPARKNwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS------ 78
Cdd:cd03258 1 MIELKNVSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltlls 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 79 -------QRIMQMMFQ--DPLSSLNprlpVWRIITEPLWIAkHSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQ 149
Cdd:cd03258 74 gkelrkaRRRIGMIFQhfNLLSSRT----VFENVALPLEIA-GVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQ 229
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
....*
gi 15831341 230 VLTAP 234
Cdd:cd03258 228 VFANP 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
22-225 |
2.10e-52 |
|
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: 171.16 E-value: 2.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ---------MMFQDPlsS 92
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE-ILIDGRDVTGvpperrnigMVFQDY--A 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 93 LNPRLPVWRIITEPLWIAKhSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15831341 173 LDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-238 |
5.21e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 174.52 E-value: 5.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFparknwlGKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQR 80
Cdd:COG3842 1 MAMPALELENVSKRY-------GDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGR-ILLDGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 81 I---------MQMMFQDPlsSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAvQVGIrPEYLDRLPHAFSGGQRQRI 151
Cdd:COG3842 69 VtglppekrnVGMVFQDY--ALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLE-LVGL-EGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHN----VSvirhMSDRVAVMYLGQIVELGEA 227
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVGTP 220
|
250
....*....|.
gi 15831341 228 QQVLTAPAHPY 238
Cdd:COG3842 221 EEIYERPATRF 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-265 |
1.38e-51 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 179.28 E-value: 1.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ------YIRSGSQRI------------------MQM 84
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmLLRRRSRQVielseqsaaqmrhvrgadMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 MFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIrPE---YLDRLPHAFSGGQRQRIAIARALSSQP 161
Cdd:PRK10261 109 IFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEaqtILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 162 DVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYTRL 241
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRA 267
|
250 260
....*....|....*....|....
gi 15831341 242 LLDSLPAIDkpleeewALRKTDLP 265
Cdd:PRK10261 268 LLAAVPQLG-------AMKGLDYP 284
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-223 |
5.31e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 167.91 E-value: 5.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 3 DTLLTLRDVHINFPARKNwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRIM 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDG-QDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 83 QM---------------MFQDPlsSLNPRLPVWRIITEPLWIAKhSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQ 147
Cdd:COG1136 74 SLserelarlrrrhigfVFQFF--NLLPELTALENVALPLLLAG-VSRKERRERARELLERVGL-GDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVE 223
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARA-DRVIRLRDGRIVS 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
6.17e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 168.73 E-value: 6.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFPARKNwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYI 74
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTsgevlvDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 75 RSGSQRIMqMMFQDPlsSLNPRLPVWRIITEPLWIAKHSSEQqRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIA 154
Cdd:COG1116 76 TGPGPDRG-VVFQEP--ALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 155 RALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVS-VIRhMSDRVAVM 216
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVL 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-234 |
2.14e-50 |
|
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: 166.35 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFParknwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY-----------I 74
Cdd:COG1122 1 IELENLSFSYP----------GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkditkknL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 75 RSGSQRImQMMFQDP--------------LSSLNPRLPvwriiteplwiakhssEQQRRALAEELAVQVGIRpEYLDRLP 140
Cdd:COG1122 71 RELRRKV-GLVFQNPddqlfaptveedvaFGPENLGLP----------------REEIRERVEEALELVGLE-HLADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 141 HAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
250
....*....|....
gi 15831341 221 IVELGEAQQVLTAP 234
Cdd:COG1122 212 IVADGTPREVFSDY 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-216 |
1.54e-49 |
|
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: 163.80 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRIMQ-- 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGA-------VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-EPVTGpg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 84 ----MMFQDPlsSLNPRLPVWRIITEPLWIAKHSsEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSS 159
Cdd:cd03293 73 pdrgYVFQQD--ALLPWLTVLDNVALGLELQGVP-KAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 160 QPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-246 |
2.54e-49 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 164.01 E-value: 2.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFparknwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGS 78
Cdd:COG1126 1 MIEIENLHKSF-----------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDsgtitvDGEDLTDSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 79 QRIMQ------MMFQdplsSLN--PRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQR 150
Cdd:COG1126 70 KDINKlrrkvgMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQV 230
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
250
....*....|....*.
gi 15831341 231 LTAPAHPYTRLLLDSL 246
Cdd:COG1126 224 FENPQHERTRAFLSKV 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-240 |
3.84e-49 |
|
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: 163.44 E-value: 3.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 8 LRDVHINFPARknwlgktteHVHaiNGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGSQ-- 79
Cdd:cd03261 3 LRGLTKSFGGR---------TVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsgevliDGEDISGLSEae 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 80 -----RIMQMMFQDP--LSSLNPRLPVwriitePLWIAKHS--SEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQR 150
Cdd:cd03261 72 lyrlrRRMGMLFQSGalFDSLTVFENV------AFPLREHTrlSEEEIREIVLEKLEAVGLRG-AEDLYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQV 230
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
250
....*....|
gi 15831341 231 LTAPaHPYTR 240
Cdd:cd03261 225 RASD-DPLVR 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-248 |
6.39e-49 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 163.56 E-value: 6.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDvhinfparknwLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI---RSG 77
Cdd:PRK11701 2 MDQPLLSVRG-----------LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 SQRIMQMM----------------FQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPH 141
Cdd:PRK11701 71 QLRDLYALseaerrrllrtewgfvHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 142 AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250 260
....*....|....*....|....*...
gi 15831341 222 VELGEAQQVLTAPAHPYTRLLLDS-LPA 248
Cdd:PRK11701 231 VESGLTDQVLDDPQHPYTQLLVSSvLQV 258
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-270 |
1.36e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 162.66 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 7 TLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------- 77
Cdd:PRK11153 3 ELKNISKVFPQGGRT-------IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalsek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 ----SQRIMQMMFQ--DPLSSLNprlpVWRIITEPLWIAKHSSEQQRRALAEELAVqVGIRpEYLDRLPHAFSGGQRQRI 151
Cdd:PRK11153 76 elrkARRQIGMIFQhfNLLSSRT----VFDNVALPLELAGTPKAEIKARVTELLEL-VGLS-DKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVF 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 15831341 232 TAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPGNRTL 270
Cdd:PRK11153 230 SHPKHPLTREFIQSTLHLDLPEDYLARLQAEPTTGSGPL 268
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-231 |
5.31e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.92 E-value: 5.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY------IRSGSQRIMQM---MFQDPlsS 92
Cdd:COG1131 6 LTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedVARDPAEVRRRigyVPQEP--A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 93 LNPRLPVWRIITeplWIAK--HSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:COG1131 84 LYPDLTVRENLR---FFARlyGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 171 SALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:COG1131 160 SGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-221 |
1.11e-46 |
|
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: 156.50 E-value: 1.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 18 RKNWlGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM------------- 84
Cdd:cd03255 7 SKTY-GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE-VRVDGTDISKLsekelaafrrrhi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 --MFQDPlsSLNPRLPVWRIITEPLWIAKHSSEQqRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPD 162
Cdd:cd03255 85 gfVFQSF--NLLPDLTALENVELPLLLAGVPKKE-RRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 163 VIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQI 221
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-235 |
2.47e-45 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 153.55 E-value: 2.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------QRIMQMMFQDplSSLNP 95
Cdd:cd03300 8 KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphKRPVNTVFQN--YALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 96 RLPVWRIITEPLWIAKHSSEQQRRALAEELA-VQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:cd03300 86 HLTVFENIAFGLRLKKLPKAEIKERVAEALDlVQLE---GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 175 ISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPA 235
Cdd:cd03300 163 LKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
31-220 |
5.56e-45 |
|
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: 151.85 E-value: 5.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG----SQRIMQ------MMFQDPLSSL-NPRlpv 99
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltKLSLKElrrkvgLVFQNPDDQFfGPT--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 wrIITEplwIA-----KHSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:cd03225 93 --VEEE---VAfglenLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15831341 175 ISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:cd03225 167 PAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-220 |
1.96e-44 |
|
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: 149.26 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ------------YIRSGSQRIMQMMFQDPls 91
Cdd:cd03229 8 KRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdleDELPPLRRRIGMVFQDF-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 92 SLNPRLPVWRIITEPLwiakhsseqqrralaeelavqvgirpeyldrlphafSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:cd03229 86 ALFPHLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15831341 172 ALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-287 |
3.74e-44 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 153.42 E-value: 3.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPARKNWlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMG-------------------M 65
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGW-------VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadrmrfddidL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 66 LQPSHGQYiRSGSQRIMQMMFQDPLSSLNPRLPVWRIITE--PLWIAKHSSEQ-----QRRALaeELAVQVGIRPEY--L 136
Cdd:PRK15093 76 LRLSPRER-RKLVGHNVSMIFQEPQSCLDPSERVGRQLMQniPGWTYKGRWWQrfgwrKRRAI--ELLHRVGIKDHKdaM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 137 DRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 217 YLGQIVELGEAQQVLTAPAHPYTRLLLDSLPAIDKPLEEEwaLRKTDLPGN----RTLPQGCFFRERCPLATSGC 287
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHK--SRLNTLPGAipllEHLPIGCRLGPRCPYAQREC 305
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-240 |
8.62e-44 |
|
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: 150.49 E-value: 8.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 17 ARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YI-------------RSGSQRIM 82
Cdd:cd03294 25 KSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKvLIdgqdiaamsrkelRELRRKKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 83 QMMFQDplSSLNPRLPVWRIITEPLWIAkHSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPD 162
Cdd:cd03294 105 SMVFQS--FALLPHRTVLENVAFGLEVQ-GVPRAEREERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 163 VIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYTR 240
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVR 258
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
30-230 |
4.32e-43 |
|
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: 147.71 E-value: 4.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGML-----QPSHGQYIRSGS------------QRIMQMMFQDPlss 92
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdiydldvdvlelRRRVGMVFQKP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 93 lNP-RLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRL-PHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:cd03260 91 -NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 171 SALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQV 230
Cdd:cd03260 170 SALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-232 |
1.30e-42 |
|
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: 147.60 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ--------------MMFQDP 89
Cdd:TIGR04521 13 GTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGT-VTIDGRDITAkkkkklkdlrkkvgLVFQFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 90 LSSL-----------NPR-LPVwriiteplwiakhsSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARAL 157
Cdd:TIGR04521 92 EHQLfeetvykdiafGPKnLGL--------------SEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 158 SSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLT 232
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
2.37e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.00 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFparknwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYI 74
Cdd:COG1121 2 MMMPAIELENLTVSY-----------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtvrlfgKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 75 RSGSQRI---MQMMFQDP----------LSSLNPRLPVWRIITeplwiakhsseQQRRALAEELAVQVGIRpEYLDRLPH 141
Cdd:COG1121 71 RRARRRIgyvPQRAEVDWdfpitvrdvvLMGRYGRRGLFRRPS-----------RADREAVDEALERVGLE-DLADRPIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 142 AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMyLGQI 221
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL-NRGL 216
|
250
....*....|....
gi 15831341 222 VELGEAQQVLTAPA 235
Cdd:COG1121 217 VAHGPPEEVLTPEN 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
24-245 |
7.80e-42 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 144.75 E-value: 7.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVH-AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQmmfQDPLS----------- 91
Cdd:cd03295 8 KRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGE-IFIDGEDIRE---QDPVElrrkigyviqq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 92 -SLNPRLPVWRIITEPLWIAKHSsEQQRRALAEELAVQVGIRP-EYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEP 169
Cdd:cd03295 84 iGLFPHMTVEENIALVPKLLKWP-KEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 170 TSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYTRLLLDS 245
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-239 |
9.79e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 147.60 E-value: 9.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSdtlLTLRDVHINFPARknwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-------- 72
Cdd:COG1118 1 MS---IEVRNISKRFGSF-----------TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRivlngrdl 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 73 YIRSGSQ-RIMQMMFQDPLssLNPRLPVWRIITEPLWIAKHsSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRI 151
Cdd:COG1118 67 FTNLPPReRRVGFVFQHYA--LFPHMTVAENIAFGLRVRPP-SKAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
....*...
gi 15831341 232 TAPAHPYT 239
Cdd:COG1118 223 DRPATPFV 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-233 |
1.79e-41 |
|
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: 144.03 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPARknwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM 84
Cdd:COG1120 1 MLEAENLSVGYGGR-----------PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGE-VLLDGRDLASL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 -----------MFQDPLSSLN------------PRLPVWRiiteplwiakHSSEQQRRALAEELAvQVGIRpEYLDRLPH 141
Cdd:COG1120 69 srrelarriayVPQEPPAPFGltvrelvalgryPHLGLFG----------RPSAEDREAVEEALE-RTGLE-HLADRPVD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 142 AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
250
....*....|..
gi 15831341 222 VELGEAQQVLTA 233
Cdd:COG1120 217 VAQGPPEEVLTP 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
30-221 |
5.57e-41 |
|
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: 141.51 E-value: 5.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGSQRIMQ------MMFQDplSSLNPRL 97
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsgtiiiDGLKLTDDKKNINElrqkvgMVFQQ--FNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 98 PVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:cd03262 92 TVLENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15831341 178 QAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:cd03262 171 VGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
35-243 |
6.05e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.20 E-value: 6.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMMFQDplSSLNPRLPVWRIITep 106
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppAERPVSMLFQE--NNLFPHLTVAQNIG-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 107 LWIA---KHSSEQQRRAlaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILN 183
Cdd:COG3840 94 LGLRpglKLTAEQRAQV--EQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 184 LLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYTRLLL 243
Cdd:COG3840 171 LVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-221 |
1.23e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.72 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNWlgkttehvhaiNGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyirsgsqrimqMM 85
Cdd:COG4619 1 LELEGLSFRVGGKPIL-----------SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGE-----------IY 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 FQD-PLSSLNPrlPVWR-----IITEPLWIA-----------KHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQR 148
Cdd:COG4619 59 LDGkPLSAMPP--PEWRrqvayVPQEPALWGgtvrdnlpfpfQLRERKFDRERALELLERLGLPPDILDKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 149 QRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-236 |
1.59e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.45 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDtlLTLRDVHINFparknwlGKttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQR 80
Cdd:COG3839 1 MAS--LELENVSKSY-------GG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGE-ILIGGRD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 81 I---------MQMMFQDPlsSLNPRLPVWRIITEPLWIAKHSsEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRI 151
Cdd:COG3839 67 VtdlppkdrnIAMVFQSY--ALYPHMTVYENIAFPLKLRKVP-KAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHN----VSvirhMSDRVAVMYLGQIVELGEA 227
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRIAVMNDGRIQQVGTP 218
|
....*....
gi 15831341 228 QQVLTAPAH 236
Cdd:COG3839 219 EELYDRPAN 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-220 |
1.91e-40 |
|
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: 138.67 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNWlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMm 85
Cdd:cd03228 1 IEFKNVSFSYPGRPKP---------VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE-ILIDGVDLRDL- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 fqdPLSSLnprlpvwriiteplwiakhsseqqRRALAeelavqvgirpeYLDRLPHAF---------SGGQRQRIAIARA 156
Cdd:cd03228 70 ---DLESL------------------------RKNIA------------YVPQDPFLFsgtirenilSGGQRQRIAIARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831341 157 LSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVMYLGQ 220
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-241 |
4.60e-40 |
|
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: 148.44 E-value: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNWlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMm 85
Cdd:COG2274 474 IELENVSFRYPGDSPP---------VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR-ILIDGIDLRQI- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 fqdPLSSL---------NPRL---PVWRIITepLWIAKHSSEQQRRALAeelavQVGIRpEYLDRLPH-----------A 142
Cdd:COG2274 543 ---DPASLrrqigvvlqDVFLfsgTIRENIT--LGDPDATDEEIIEAAR-----LAGLH-DFIEALPMgydtvvgeggsN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 143 FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLvtLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIV 222
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIV 688
|
250
....*....|....*....
gi 15831341 223 ELGEAQQVLTAPAHpYTRL 241
Cdd:COG2274 689 EDGTHEELLARKGL-YAEL 706
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-240 |
9.01e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 139.79 E-value: 9.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 2 SDTLLTLRDVHInfparknWLGKTtehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGM--LQPS---------H 70
Cdd:COG1117 8 LEPKIEVRNLNV-------YYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvegeillD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 71 GQYIRSGS-------QRIMqMMFQDPlsslNPrLP--VWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRL-- 139
Cdd:COG1117 77 GEDIYDPDvdvvelrRRVG-MVFQKP----NP-FPksIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLkk 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 140 -PHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD-ISVqAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVMY 217
Cdd:COG1117 151 sALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFY 227
|
250 260
....*....|....*....|...
gi 15831341 218 LGQIVELGEAQQVLTAPAHPYTR 240
Cdd:COG1117 228 LGELVEFGPTEQIFTNPKDKRTE 250
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
32-244 |
1.15e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.50 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI-------------------MQMMFQDplSS 92
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGT-IRVGDITIdtarslsqqkglirqlrqhVGFVFQN--FN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 93 LNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYlDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:PRK11264 96 LFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831341 173 LDISVQAQILNLLVTLQENHgLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYTRLLLD 244
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-231 |
1.28e-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: 145.67 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMM 85
Cdd:COG4988 337 IELEDVSFSYPGGRP----------ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS-ILINGVDLSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 FQDPLSSL-----NPRLPVWRIItEPLWIAKH--SSEQQRRALAeelavQVGIRpEYLDRLPH-----------AFSGGQ 147
Cdd:COG4988 406 PASWRRQIawvpqNPYLFAGTIR-ENLRLGRPdaSDEELEAALE-----AAGLD-EFVAALPDgldtplgeggrGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 148 RQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVMYLGQIVELGEA 227
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQA-DRILVLDDGRIVEQGTH 555
|
....
gi 15831341 228 QQVL 231
Cdd:COG4988 556 EELL 559
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
30-221 |
1.32e-39 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 136.76 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGSQRIMQM---MFQDPlsSLNPRLPVW 100
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDsgeikvLGKDIKKEPEEVKRRigyLPEEP--SLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 riiteplwiakhsseqqrralaeelavqvgirpEYLDrlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:cd03230 92 ---------------------------------ENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15831341 181 ILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:cd03230 134 FWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-222 |
2.74e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 138.27 E-value: 2.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 4 TLLTLRDVHINFPARKnwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ 83
Cdd:COG3638 1 PMLELRNLSKRYPGGT----------PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGE-ILVDGQDVTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 84 --------------MMFQDPlsSLNPRLPV--------------WRiitepLWIAKHSSEQQRRALaEELAvQVGIrPEY 135
Cdd:COG3638 70 lrgralrrlrrrigMIFQQF--NLVPRLSVltnvlagrlgrtstWR-----SLLGLFPPEDRERAL-EALE-RVGL-ADK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 136 LDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAV 215
Cdd:COG3638 140 AYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIG 219
|
....*..
gi 15831341 216 MYLGQIV 222
Cdd:COG3638 220 LRDGRVV 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
22-231 |
3.98e-39 |
|
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: 137.68 E-value: 3.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ------YIRSGSQRIMQ---MMFQDPlsS 92
Cdd:COG4555 7 LSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilidgeDVRKEPREARRqigVLPDER--G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 93 LNPRLPVWRII--TEPLWiakHSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:COG4555 85 LYDRLTVRENIryFAELY---GLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 171 SALDISVQAQILNLLVTLQeNHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:COG4555 161 NGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-220 |
6.21e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 134.68 E-value: 6.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrimqmmfqdplsslnprlpvwr 101
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD---------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 102 iiteplwIAKHSSEQQRRalaeelavQVGIRPEyldrlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:cd00267 63 -------IAKLPLEELRR--------RIGYVPQ--------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 15831341 182 LNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:cd00267 120 LELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-222 |
1.28e-38 |
|
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: 133.71 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmm 85
Cdd:cd03216 1 LELRGITKRFGG-----------VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE-ILVDGK------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 fqdPLSSLNPRLpvwriiteplwiakhsseqqrralaeelAVQVGIRpeyldrLPHAFSGGQRQRIAIARALSSQPDVIV 165
Cdd:cd03216 63 ---EVSFASPRD----------------------------ARRAGIA------MVYQLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 166 LDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-235 |
1.96e-38 |
|
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: 135.64 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFparknwlGKttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMM 85
Cdd:cd03219 1 LEVRGLTKRF-------GG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS-VLFDGEDITGLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 ------------FQDP--LSSL----NPRLPVWRIITEPLWIAKHS-SEQQRRALAEELAVQVGIRpEYLDRLPHAFSGG 146
Cdd:cd03219 69 pheiarlgigrtFQIPrlFPELtvleNVMVAAQARTGSGLLLARARrEEREARERAEELLERVGLA-DLADRPAGELSYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 147 QRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGE 226
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
....*....
gi 15831341 227 AQQVLTAPA 235
Cdd:cd03219 227 PDEVRNNPR 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-241 |
4.65e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 138.43 E-value: 4.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------QRIMQMMFQDplSSL 93
Cdd:PRK11607 25 LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyQRPINMMFQS--YAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 94 NPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVqVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK11607 103 FPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGL-VHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 174 DISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLtapAHPYTRL 241
Cdd:PRK11607 181 DKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---EHPTTRY 245
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-235 |
4.80e-38 |
|
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: 135.17 E-value: 4.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 2 SDTLLTLRDVHINFparknwlGKttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI 81
Cdd:COG0411 1 SDPLLEVRGLTKRF-------GG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGR-ILFDGRDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 82 MQMM------------FQDP-----LSSL-NPRLPVWRIITEPLWIAK------HSSEQQRRALAEELAVQVGIRpEYLD 137
Cdd:COG0411 69 TGLPphriarlgiartFQNPrlfpeLTVLeNVLVAAHARLGRGLLAALlrlpraRREEREARERAEELLERVGLA-DRAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 138 RLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMY 217
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLD 227
|
250
....*....|....*...
gi 15831341 218 LGQIVELGEAQQVLTAPA 235
Cdd:COG0411 228 FGRVIAEGTPAEVRADPR 245
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
24-225 |
5.30e-38 |
|
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: 133.92 E-value: 5.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMMFQDplSSLNP 95
Cdd:cd03301 8 KRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppKDRDIAMVFQN--YALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 96 RLPVWRIITEPLWIAKHSSE---QQRRALAEELAVQvgirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:cd03301 86 HMTVYDNIAFGLKLRKVPKDeidERVREVAELLQIE-----HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15831341 173 LDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
36-232 |
5.70e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 134.32 E-value: 5.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 36 DLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMMFQDplSSLNPRLPVWRIITEPL 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppSRRPVSMLFQE--NNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 108 WIAKHSSEQQRRALaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVT 187
Cdd:PRK10771 97 NPGLKLNAAQREKL-HAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15831341 188 LQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLT 232
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
47-238 |
1.16e-37 |
|
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: 136.08 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 47 IVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ--------RIMQMMFQDplSSLNPRLPVWRIITEPLWIAKHSSEQQR 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDvtnvpphlRHINMVFQS--YALFPHMTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 119 RALAEELA-VQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYV 197
Cdd:TIGR01187 79 PRVLEALRlVQLE---EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15831341 198 LISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPY 238
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-242 |
1.50e-37 |
|
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: 140.29 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNWlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmm 85
Cdd:COG4987 334 LELEDVSFRYPGAGRP---------VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS-ITLGGV------ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 fqdPLSSLNPRLpVWRIIT--------------EPLWIAKH--SSEQQRRALAeelavQVGIRPeYLDRLPH-------- 141
Cdd:COG4987 398 ---DLRDLDEDD-LRRRIAvvpqrphlfdttlrENLRLARPdaTDEELWAALE-----RVGLGD-WLAALPDgldtwlge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 142 ---AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLtyVLISHNVSVIRHMsDRVAVMYL 218
Cdd:COG4987 468 ggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVLED 544
|
250 260
....*....|....*....|....
gi 15831341 219 GQIVELGEAQQVLTAPAHpYTRLL 242
Cdd:COG4987 545 GRIVEQGTHEELLAQNGR-YRQLY 567
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
32-225 |
1.97e-37 |
|
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: 131.40 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyirsgsqrIMqmMFQDPLSSLNPRlpvwriiteplWIAK 111
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE--------IL--LDGKDLASLSPK-----------ELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 112 HsseqqrRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEN 191
Cdd:cd03214 74 K------IAYVPQALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARE 146
|
170 180 190
....*....|....*....|....*....|....
gi 15831341 192 HGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03214 147 RGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
29-227 |
5.72e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.33 E-value: 5.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-----------------YIRsgsqRIMQMMFQDplS 91
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdlsrlkrreipYLR----RRIGVVFQD--F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 92 SLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:COG2884 89 RLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLD-LVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 172 ALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEA 227
Cdd:COG2884 167 NLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
29-230 |
1.26e-36 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 131.27 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-------------SQRIMQMMFQD-----PL 90
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrkLRRRIGMIFQHynlieRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 91 SS----LNPRL---PVWRIITEPLwiakhSSEQQRRALaeELAVQVGIRPEYLDRLpHAFSGGQRQRIAIARALSSQPDV 163
Cdd:TIGR02315 95 TVlenvLHGRLgykPTWRSLLGRF-----SEEDKERAL--SALERVGLADKAYQRA-DQLSGGQQQRVAIARALAQQPDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 164 IVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQV 230
Cdd:TIGR02315 167 ILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
32-245 |
1.34e-36 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 131.36 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQP----SHGQYIRSGSQ--------RIMQMMFQDPLSSLNPRLPV 99
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPvapcalrgRKIATIMQNPRSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 WRIITEPLW-IAKHSSEQQRRALAEelAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK10418 99 HTHARETCLaLGKPADDATLTAALE--AVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 179 AQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYTRLLLDS 245
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
32-171 |
2.21e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 127.76 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ----------YIRSGSQRIMQMMFQDPlsSLNPRLPVWR 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltdDERKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 102 IITEPLWI---AKHSSEQQRRALAEELAvQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:pfam00005 79 NLRLGLLLkglSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
32-224 |
3.07e-36 |
|
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: 129.89 E-value: 3.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ-------RIMqmMFQDplSSLNPrlpvWRIIT 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQitepgpdRMV--VFQN--YSLLP----WLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 EPLWIA-----KHSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:TIGR01184 73 ENIALAvdrvlPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15831341 180 QILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVM------YLGQIVEL 224
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEV 202
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-239 |
3.59e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.53 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVhinfpaRKNWLGKTtehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--- 77
Cdd:PRK09452 10 SLSPLVELRGI------SKSFDGKE-----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 -----SQRIMQMMFQDplSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELA-VQVgirPEYLDRLPHAFSGGQRQRI 151
Cdd:PRK09452 79 thvpaENRHVNTVFQS--YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRmVQL---EEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 233
|
....*...
gi 15831341 232 TAPAHPYT 239
Cdd:PRK09452 234 EEPKNLFV 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
31-235 |
4.63e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 130.91 E-value: 4.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI---------------MQMMFQDPLSSLNP 95
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT-VTIGERVItagkknkklkplrkkVGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 96 RLPVWRIITEPLWIAkhSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:PRK13634 101 ETVEKDICFGPMNFG--VSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 176 SVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPA 235
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
34-234 |
5.26e-36 |
|
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: 129.38 E-value: 5.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------QRIMQMMFQDplSSLNPRLPVWRIITE 105
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppeKRDISYVPQN--YALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 106 PLWIAKHS-SEQQRRALaeELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNL 184
Cdd:cd03299 95 GLKKRKVDkKEIERKVL--EIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831341 185 LVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:cd03299 172 LKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
32-223 |
8.34e-36 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 128.24 E-value: 8.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqRIMQMMFQDPLSSLNPR-----------LPVW 100
Cdd:TIGR02211 21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNG--QSLSKLSSNERAKLRNKklgfiyqfhhlLPDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 RI---ITEPLWIAKHS-SEQQRRALAEELAVQVGIRpeyLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:TIGR02211 99 TAlenVAMPLLIGKKSvKEAKERAYEMLEKVGLEHR---INHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15831341 177 VQAQILNLLVTLQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVE 223
Cdd:TIGR02211 176 NAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-228 |
1.78e-35 |
|
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: 127.94 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFPARknwlgktTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQR 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTG-------AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGT-VRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 81 IMQM---------------MFQDplSSLNPRLPVWRIITEPLWIAKHSSEQQRralAEELAVQVGIRpEYLDRLPHAFSG 145
Cdd:COG4181 76 LFALdedararlrarhvgfVFQS--FQLLPTLTALENVMLPLELAGRRDARAR---ARALLERVGLG-HRLDHYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 146 GQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELG 225
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
...
gi 15831341 226 EAQ 228
Cdd:COG4181 229 AAT 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
31-238 |
1.88e-35 |
|
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: 127.84 E-value: 1.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------QRIMQMMFQDplSSLNPRLPVWRI 102
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqERNVGFVFQH--YALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 103 ITEPLWIAKHS---SEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:cd03296 95 VAFGLRVKPRSerpPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 180 QILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPY 238
Cdd:cd03296 174 ELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
1.97e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 129.20 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFParknwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--- 77
Cdd:PRK13636 1 MEDYILKVEELNYNYS----------DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 ---SQRIMQ------MMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRAlaEELAVQVGIRPeYLDRLPHAFSGGQR 148
Cdd:PRK13636 71 dysRKGLMKlresvgMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRV--DNALKRTGIEH-LKDKPTHCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 149 QRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQ 228
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
...
gi 15831341 229 QVL 231
Cdd:PRK13636 228 EVF 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
31-227 |
5.34e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 127.05 E-value: 5.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------------RIMQMMFQDplSSLN 94
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkpsekairllrQKVGMVFQQ--YNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 95 PRLPVWRIITE-PLWIAKHSsEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:COG4161 95 PHLTVMENLIEaPCKVLGLS-KEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831341 174 DISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEA 227
Cdd:COG4161 173 DPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
36-225 |
7.95e-35 |
|
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: 125.68 E-value: 7.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 36 DLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMMFQDplSSLNPRLPVWRIITEPL 107
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappADRPVSMLFQE--NNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 108 WIAKHSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVT 187
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALA-RVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 15831341 188 LQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-221 |
1.44e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 126.33 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 20 NWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGS------QRIMQMMFQDPlssl 93
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTaplaeaREDTRLMFQDA---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 94 npRLPVWRIITE--PLWIAKHSSEQQRRALAEelavqVGIRPEYLDrLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:PRK11247 91 --RLLPWKKVIDnvGLGLKGQWRDAALQALAA-----VGLADRANE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831341 172 ALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-225 |
1.45e-34 |
|
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: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 27 EHVH--------AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-----------MMFQ 87
Cdd:COG1132 343 ENVSfsypgdrpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR-ILIDGVDIRDltleslrrqigVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 88 DPL---SSL--NprlpvwriITepLWIAKHSSEQQRRALAeelAVQVGirpEYLDRLPH-----------AFSGGQRQRI 151
Cdd:COG1132 422 DTFlfsGTIreN--------IR--YGRPDATDEEVEEAAK---AAQAH---EFIEALPDgydtvvgergvNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831341 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVMYLGQIVELG 225
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRNA-DRILVLDDGRIVEQG 556
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
22-222 |
2.17e-34 |
|
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: 125.37 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEH-VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ-------------RIMQMMFQ 87
Cdd:cd03256 6 LSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrRQIGMIFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 88 DP------------LSSLNPRLPVWRIITEPLwiakhSSEQQRRALaeELAVQVGIRPEYLDRLpHAFSGGQRQRIAIAR 155
Cdd:cd03256 86 QFnlierlsvlenvLSGRLGRRSTWRSLFGLF-----PKEEKQRAL--AALERVGLLDKAYQRA-DQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 156 ALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTyVLIS-HNVSVIRHMSDRVAVMYLGQIV 222
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGIT-VIVSlHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-225 |
2.48e-34 |
|
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: 124.33 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRrGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------------QRIMQMMFQDplSSLNPRLPVW 100
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqQRKIGLVFQQ--YALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 RIITeplWIAKHSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:cd03297 94 ENLA---FGLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15831341 181 ILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-223 |
4.66e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 124.97 E-value: 4.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 4 TLLTLRDVHINFPARKnwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGG-------QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGE-ITLDGVPVTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 84 ------MMFQDplSSLNPRLPVWRIITEPLWIAKhSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARAL 157
Cdd:COG4525 74 pgadrgVVFQK--DALLPWLNVLDNVAFGLRLRG-VPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 158 SSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVM--YLGQIVE 223
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-231 |
2.26e-33 |
|
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: 128.00 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIRSG----------------SQRIMQMMFQDplS 91
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvNVRVGdewvdmtkpgpdgrgrAKRYIGILHQE--Y 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 92 SLNPRLPVWRIITEPLWIAKHSSEQQRRALAeeLAVQVGIRPEY----LDRLPHAFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGLELPDELARMKAVI--TLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831341 168 EPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
29-229 |
2.27e-33 |
|
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: 121.84 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ------YIRSGSQRIMQMM---FQDplSSLNPRLPV 99
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTayingySIRTDRKAARQSLgycPQF--DALFDELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 WriitEPLWI---AKHSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:cd03263 93 R----EHLRFyarLKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15831341 177 VQAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQ 229
Cdd:cd03263 168 SRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
28-216 |
4.29e-33 |
|
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: 121.10 E-value: 4.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 28 HVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----SQRIMQMMFQdpLSSLNPRLP--VW 100
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekERKRIGYVPQ--RRSIDRDFPisVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 RIITEPLW----IAKHSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:cd03235 89 DVVLMGLYghkgLFRRLSKADKAKVDEALE-RVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15831341 177 VQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:cd03235 167 TQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
35-228 |
5.53e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 121.66 E-value: 5.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------------RIMQMMFQDplSSLNPRLP 98
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdkairelrRNVGMVFQQ--YNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 99 VWRIITE-PLWIAKhSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:PRK11124 99 VQQNLIEaPCRVLG-LSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15831341 178 QAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQ 228
Cdd:PRK11124 177 TAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-231 |
1.32e-32 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 120.34 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 7 TLRDVHINFPARKNwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqrimqmmf 86
Cdd:cd03249 2 EFKNVSFRYPSRPD--------VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 87 qDPLSSLNPRLpvWR-----IITEPLWIA-------KHSSEQQRRALAEELAVQVGIRpEYLDRLPHAF----------- 143
Cdd:cd03249 65 -VDIRDLNLRW--LRsqiglVSQEPVLFDgtiaeniRYGKPDATDEEVEEAAKKANIH-DFIMSLPDGYdtlvgergsql 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 144 SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnhGLTYVLISHNVSVIRHmSDRVAVMYLGQIVE 223
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVE 217
|
....*...
gi 15831341 224 LGEAQQVL 231
Cdd:cd03249 218 QGTHDELM 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
35-268 |
4.79e-32 |
|
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: 121.75 E-value: 4.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGqYIRSGS---------------QRIMQMMFQDPlsSLNPRLPV 99
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSG-RIRLGGevlqdsargiflpphRRRIGYVFQEA--RLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 WRIItepLWIAKHSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:COG4148 95 RGNL---LYGRKRAPRAERRISFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 180 QILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHpyTRLLLDS-----LPAIDKPLE 254
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDL--LPLAGGEeagsvLEATVAAHD 248
|
250
....*....|....
gi 15831341 255 EEWALRKTDLPGNR 268
Cdd:COG4148 249 PDYGLTRLALGGGR 262
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
36-225 |
6.36e-32 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 118.04 E-value: 6.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 36 DLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------SQRIMQMMFQDplSSLNPRLPVWRIITEPL 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqshtglapYQRPVSMLFQE--NNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 108 WIA-KHSSEQQRRAlaEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLV 186
Cdd:TIGR01277 96 HPGlKLNAEQQEKV--VDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 15831341 187 TLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-238 |
8.58e-32 |
|
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: 121.37 E-value: 8.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS--------------QRIMQMMFQDplSSLNPRLPVW 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppeKRRIGYVFQE--ARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 RIITEPLWIAKHSseqQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:TIGR02142 94 GNLRYGMKRARPS---ERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 181 ILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPY 238
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
27-231 |
8.72e-32 |
|
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: 118.10 E-value: 8.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 27 EHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMmfqdPLSSLNPRLPVwrIITEP 106
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQ-ILIDGIDIRDI----SRKSLRSMIGV--VLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 107 LWIA-------KHSSEQQRRALAEELAVQVGIRpEYLDRLPHA-----------FSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:cd03254 87 FLFSgtimeniRLGRPNATDEEVIEAAKEAGAH-DFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 169 PTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVL 231
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-230 |
1.03e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.42 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 23 GKTTEHVhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ--------RIMQ---MMFQDPLS 91
Cdd:PRK13633 18 EESTEKL-ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwDIRNkagMVFQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 92 SLnprlpVWRIITE-----PLWIAKHSSEQQRRAlaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVL 166
Cdd:PRK13633 97 QI-----VATIVEEdvafgPENLGIPPEEIRERV--DESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 167 DEPTSALDISVQAQILNLLVTLQENHGLTYVLISHnvsvirHM-----SDRVAVMYLGQIVELGEAQQV 230
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKYGITIILITH------YMeeaveADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
31-225 |
1.84e-31 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 117.09 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS---------QRIMQMMFQDPlsSLNPRLPVWR 101
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdvvreprevRRRIGIVFQDL--SVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 102 IItepLWIAK--HSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:cd03265 93 NL---YIHARlyGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15831341 180 QILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03265 169 HVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
32-222 |
1.86e-31 |
|
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: 116.59 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------QRIMQMMFQDPLSSLNpRLPVWRIIT 104
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerRKSIGYVMQDVDYQLF-TDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 EPLWIAKHSSEQQRRALAE-ELAvqvgirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILN 183
Cdd:cd03226 95 LGLKELDAGNEQAETVLKDlDLY-------ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 15831341 184 LLVTLQeNHGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:cd03226 168 LIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-230 |
4.70e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.28 E-value: 4.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 2 SDTLLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG---- 77
Cdd:COG1129 1 AEPLLEMRGISKSFGG-----------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 ------SQR--ImQMMFQDPlsSLNPRLPVW------RIITEPLWIakhsSEQQRRALAEELAVQVG--IRPeylDRLPH 141
Cdd:COG1129 70 frsprdAQAagI-AIIHQEL--NLVPNLSVAeniflgREPRRGGLI----DWRAMRRRARELLARLGldIDP---DTPVG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 142 AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
....*....
gi 15831341 222 VELGEAQQV 230
Cdd:COG1129 219 VGTGPVAEL 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-234 |
5.29e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.10 E-value: 5.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFParknwlgKTTEhvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS------ 78
Cdd:PRK13639 1 ILETRDLKYSYP-------DGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydk 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 79 ------QRIMQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRAlaEELAVQVGIRpEYLDRLPHAFSGGQRQRIA 152
Cdd:PRK13639 71 ksllevRKTVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRV--KEALKAVGME-GFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 153 IARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLT 232
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
..
gi 15831341 233 AP 234
Cdd:PRK13639 227 DI 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-221 |
7.17e-31 |
|
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: 113.85 E-value: 7.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNWLgkttehvhaINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmm 85
Cdd:cd03246 1 LEVENVSFRYPGAEPPV---------LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGR-VRLDGA------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 fqdPLSSLNPrlpvwriiteplwiakhsseqqrralaEELAVQVGIRPEYLDRLP-----HAFSGGQRQRIAIARALSSQ 160
Cdd:cd03246 65 ---DISQWDP---------------------------NELGDHVGYLPQDDELFSgsiaeNILSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 161 PDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRhMSDRVAVMYLGQI 221
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-225 |
1.07e-30 |
|
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: 113.56 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNWlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrimQMM 85
Cdd:cd03247 1 LSINNVSFSYPEQEQQ---------VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP---VSD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 FQDPLSSLNPRLPvwriiteplwiakhsseQQRRALAEELAVQVGIRpeyldrlphaFSGGQRQRIAIARALSSQPDVIV 165
Cdd:cd03247 69 LEKALSSLISVLN-----------------QRPYLFDTTLRNNLGRR----------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 166 LDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVMYLGQIVELG 225
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-223 |
1.17e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.80 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 23 GKTTEHVhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG---------------QYIRSGSQRImQMMFQ 87
Cdd:PRK13646 15 GTPYEHQ-AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvdditithktkdKYIRPVRKRI-GMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 88 DPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALaeELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK13646 93 FPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAH--RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 168 EPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
31-230 |
1.54e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.30 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG----SQRI--------MQMMFQDPLSSLNPRLP 98
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditDKKVklsdirkkVGLVFQYPEYQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 99 VWRIITEPLWIAKHSSEQQRRAL-AEELavqVGIRPE-YLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKrAMNI---VGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831341 177 VQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQV 230
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-241 |
2.08e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.80 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 13 INFPARKNWLGKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI---------RSGSQRIMQ 83
Cdd:PRK09493 2 IEFKNVSKHFGPTQ----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvndpKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 84 ---MMFQDplSSLNPRLPVWR-IITEPLWIaKHSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSS 159
Cdd:PRK09493 78 eagMVFQQ--FYLFPHLTALEnVMFGPLRV-RGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 160 QPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPahPYT 239
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP--PSQ 230
|
..
gi 15831341 240 RL 241
Cdd:PRK09493 231 RL 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
31-282 |
3.58e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 115.08 E-value: 3.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-----------QRIMQMMFQDPLSSLnprlpV 99
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgiRKLVGIVFQNPETQF-----V 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 WRIITEPLWIAKHS--------SEQQRRALAEelavqVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:PRK13644 92 GRTVEEDLAFGPENlclppieiRKRVDRALAE-----IGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 172 ALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIrHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYTRLLLDSLpaIDk 251
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSL--IE- 240
|
250 260 270
....*....|....*....|....*....|.
gi 15831341 252 pLEEEWALRKTDLPGNRTLPQGCFFRERCPL 282
Cdd:PRK13644 241 -LAENLKMHGVVIPWENTSSPSSFAEEICRL 270
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
29-231 |
4.01e-30 |
|
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: 113.30 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRImqmmfqdplsslnPRLPVWRIITepLW 108
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGS-IRFDGRDI-------------TGLPPHERAR--AG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 109 IAkhSSEQQRRALAE-------ELAVQVGIRPEYLDRLPHAF-----------------SGGQRQRIAIARALSSQPDVI 164
Cdd:cd03224 77 IG--YVPEGRRIFPEltveenlLLGAYARRRAKRKARLERVYelfprlkerrkqlagtlSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 165 VLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
25-232 |
6.10e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.32 E-value: 6.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 25 TTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ--------------YIRSGsqriMQMMFQDPL 90
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEikidgitiskenlkEIRKK----IGIIFQNPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 91 SSL--------------NPRLP---VWRIIteplwiakhsseqqrralaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAI 153
Cdd:PRK13632 94 NQFigatveddiafgleNKKVPpkkMKDII-------------------DDLAKKVGME-DYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 154 ARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVS-VIrhMSDRVAVMYLGQIVELGEAQQVLT 232
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDeAI--LADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-233 |
2.51e-29 |
|
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: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 3 DTLLTLRDVHINFPARKnwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI-----RSG 77
Cdd:COG1119 1 DPLLELRNVTVRRGGKT-----------ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgeRRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 S-------QRI------MQMMFQdplsslnPRLPVWRII------TEPLWiaKHSSEQQRRaLAEELAVQVGIRpEYLDR 138
Cdd:COG1119 70 GedvwelrKRIglvspaLQLRFP-------RDETVLDVVlsgffdSIGLY--REPTDEQRE-RARELLELLGLA-HLADR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 139 LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYL 218
Cdd:COG1119 139 PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKD 218
|
250
....*....|....*
gi 15831341 219 GQIVELGEAQQVLTA 233
Cdd:COG1119 219 GRVVAAGPKEEVLTS 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-229 |
2.65e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.03 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHInfparknwlgkTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS---------HGQYIRS 76
Cdd:COG4136 2 LSLENLTI-----------TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsasgevllNGRRLTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 77 GS--QRIMQMMFQDPLssLNPRLPVWRIItePLWIAKHSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIA 154
Cdd:COG4136 71 LPaeQRRIGILFQDDL--LFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 155 RALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVsvirhmSDRVAVmylGQIVELGEAQQ 229
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDE------EDAPAA---GRVLDLGNWQH 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-235 |
3.34e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.05 E-value: 3.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFparknwlGKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YI----- 74
Cdd:PRK11432 2 TQKNFVVLKNITKRF-------GSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQiFIdgedv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 75 --RSGSQRIMQMMFQDplSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAV--QVGIRPEYLDRLphafSGGQRQR 150
Cdd:PRK11432 71 thRSIQQRDICMVFQS--YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELvdLAGFEDRYVDQI----SGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQV 230
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
....*
gi 15831341 231 LTAPA 235
Cdd:PRK11432 225 YRQPA 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
37-240 |
3.48e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.13 E-value: 3.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 37 LQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG--------------SQRIMQMMFQDplSSLNPRLPVWRI 102
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevRRKKIAMVFQS--FALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 103 ITEPLWIAKHSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL 182
Cdd:PRK10070 127 TAFGMELAGINAEERREKALDALR-QVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 183 NLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYTR 240
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-237 |
5.35e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.60 E-value: 5.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFparknwlgktTEHvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYI 74
Cdd:PRK10619 1 MSENKLNVIDLHKRY----------GEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGsivvngQTI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 75 RSGSQRIMQMMFQDP--LSSLNPRLP-------VWRIIT-------EPLWIAKhSSEQQRRALAEELAVQVGIRPEYLDR 138
Cdd:PRK10619 70 NLVRDKDGQLKVADKnqLRLLRTRLTmvfqhfnLWSHMTvlenvmeAPIQVLG-LSKQEARERAVKYLAKVGIDERAQGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 139 LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYL 218
Cdd:PRK10619 149 YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQ 227
|
250
....*....|....*....
gi 15831341 219 GQIVELGEAQQVLTAPAHP 237
Cdd:PRK10619 228 GKIEEEGAPEQLFGNPQSP 246
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
32-233 |
5.63e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRsgsqrimqmMFQDPLSSLNPR--------LP----- 98
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGE-VR---------LNGRPLADWSPAelarrravLPqhssl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 99 --------VWRIITEPLwiakHSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARAL------SSQPDVI 164
Cdd:PRK13548 88 sfpftveeVVAMGRAPH----GLSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 165 VLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTA 233
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-256 |
8.21e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.43 E-value: 8.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------RIMQMMFQDPLSSLNPRLP 98
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPitkenirevrKFVGLVFQNPDDQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 99 VWRIITEPLWIAKHSSEQQRRAlaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK13652 97 EQDIAFGPINLGLDEETVAHRV--SSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 179 AQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAP-AHPYTRLLLDSLPAIDKPLEEE 256
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPdLLARVHLDLPSLPKLIRSLQAQ 252
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-239 |
9.50e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.64 E-value: 9.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFPARKnwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLL--MGMLQPS--------- 69
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKK-----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtitgsivy 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 70 HGQYIRSGSQRIMQ------MMFQDPlsslNP-RLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLpH- 141
Cdd:PRK14239 70 NGHNIYSPRTDTVDlrkeigMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRL-Hd 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 142 ---AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVMYL 218
Cdd:PRK14239 145 salGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLD 222
|
250 260
....*....|....*....|.
gi 15831341 219 GQIVELGEAQQVLTAPAHPYT 239
Cdd:PRK14239 223 GDLIEYNDTKQMFMNPKHKET 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
29-221 |
1.03e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 109.42 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------------QRIMQMMFQDplSSLNP 95
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraipylRRKIGVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 96 RLPVWRIITEPLWIAKHSSEQQRRALAEELAvQVGIRPEYlDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKRVPAALE-LVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15831341 176 SVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:cd03292 170 DTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-230 |
1.16e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 111.26 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQ-----------RIMQMMFQDPLSSL------ 93
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGT-ITVGGMvlseetvwdvrRQVGMVFQNPDNQFvgatvq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 94 --------NPRLPvwriiteplwiakhSSEQQRRAlaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIV 165
Cdd:PRK13635 101 ddvafgleNIGVP--------------REEMVERV--DQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 166 LDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQV 230
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
6-241 |
1.20e-28 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 115.18 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNWLgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMM 85
Cdd:TIGR02204 338 IEFEQVNFAYPARPDQP--------ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGR-ILLDGVDLRQLD 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 FQD-----PLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEelAVQVGirpEYLDRLPHAF-----------SGGQRQ 149
Cdd:TIGR02204 409 PAElrarmALVPQDPVLFAASVMENIRYGRPDATDEEVEAAAR--AAHAH---EFISALPEGYdtylgergvtlSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnhGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGeAQQ 229
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQG-THA 559
|
250
....*....|..
gi 15831341 230 VLTAPAHPYTRL 241
Cdd:TIGR02204 560 ELIAKGGLYARL 571
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-231 |
1.23e-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: 110.01 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS----------QRIMQMMFQDP-LSSLNprlpv 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslRRQIGLVSQDVfLFNDT----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 wriITEPLWIAKH--SSEQQRRALAEELAVqvgirpEYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVL 166
Cdd:cd03251 92 ---VAENIAYGRPgaTREEVEEAARAANAH------EFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 167 DEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVL 231
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
34-201 |
1.49e-28 |
|
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: 108.72 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIRSGSQRIM------QMMFQDPLSSLNPRLPVWRIITep 106
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvLWNGEPIRDAredyrrRLAYLGHADGLKPELTVRENLR-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 107 lWIAKHSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLV 186
Cdd:COG4133 98 -FWAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
170
....*....|....*
gi 15831341 187 TLQENHGLTyVLISH 201
Cdd:COG4133 176 AHLARGGAV-LLTTH 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
27-231 |
1.69e-28 |
|
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: 109.63 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 27 EHVH--------AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMMfqdpLSSLNPRLP 98
Cdd:cd03253 4 ENVTfaydpgrpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGS-ILIDGQDIREVT----LDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 99 VWRIITePLW-------IA----KHSSEQQRRA------------LAEELAVQVGIRPEYLdrlphafSGGQRQRIAIAR 155
Cdd:cd03253 79 VVPQDT-VLFndtigynIRygrpDATDEEVIEAakaaqihdkimrFPDGYDTIVGERGLKL-------SGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 156 ALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVL 231
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-233 |
2.43e-28 |
|
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: 109.11 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ--------------YIRSGSQRIMQ--MMF----QDPL 90
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlvdghdlaladpaWLRRQVGVVLQenVLFnrsiRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 91 SSLNPRLPVWRIIteplwiakhssEQQRRALAEELAVQVgirPEYLDRL----PHAFSGGQRQRIAIARALSSQPDVIVL 166
Cdd:cd03252 97 ALADPGMSMERVI-----------EAAKLAGAHDFISEL---PEGYDTIvgeqGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 167 DEPTSALDISVQAQILNLLVTLQEnhGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVLTA 233
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-222 |
2.98e-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: 108.45 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMM 85
Cdd:cd03245 3 IEFRNVSFSYPNQEI---------PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGS-VLLDGTDIRQLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 FQDPLSSL-----NPRLpVWRIITEPLWIAKHSSEQQRRALAEELAvqvGIRpEYLDRLPHAF-----------SGGQRQ 149
Cdd:cd03245 73 PADLRRNIgyvpqDVTL-FYGTLRDNITLGAPLADDERILRAAELA---GVT-DFVNKHPNGLdlqigergrglSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnhGLTYVLISHNVSVIRhMSDRVAVMYLGQIV 222
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
31-230 |
4.76e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.46 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-----------MMFQDPLSSLnprlpV 99
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE-IFYNNQAITDdnfeklrkhigIVFQNPDNQF-----V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 WRIITE--PLWIAKHS--SEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:PRK13648 98 GSIVKYdvAFGLENHAvpYDEMHRRVSEALK-QVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 176 SVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQV 230
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
31-230 |
1.40e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 108.29 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYIRSGSQR--IMQ------MMFQDPLSSLNPR 96
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvddTLITSTSKNkdIKQirkkvgLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 97 LPVWRIITEPLWIAkhSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:PRK13649 102 TVLKDVAFGPQNFG--VSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831341 177 VQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQV 230
Cdd:PRK13649 180 GRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-239 |
1.48e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 107.83 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQ------PSHGQYIRSGS----------QRIMQMMFQDPlsSLNP 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKdifqidaiklRKEVGMVFQQP--NPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 96 RLPVWRIITEPLwiAKHSSEQQR--RALAEELAVQVGIRPEYLDRL---PHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:PRK14246 104 HLSIYDNIAYPL--KSHGIKEKReiKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 171 SALDIsVQAQILNLLVTLQENHgLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYT 239
Cdd:PRK14246 182 SMIDI-VNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-223 |
1.56e-27 |
|
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: 106.15 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPShgqyirSGSQRIMQMMFQDPLSSLNpRLPVwr 101
Cdd:cd03268 6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD------SGEITFDGKSYQKNIEALR-RIGA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 102 IITEPLWIAKHSSEQQRRALA----------EELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLArllgirkkriDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831341 172 ALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
32-231 |
1.72e-27 |
|
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: 112.14 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqriMQMMFQDPLS-------SLNPRLPVWRIIT 104
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDG----VDLAIADPAWlrrqmgvVLQENVLFSRSIR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 EPLWIAKHSSEQQRRALAEELAVQVgirpEYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:TIGR01846 549 DNIALCNPGAPFEHVIHAAKLAGAH----DFISELPQGYntevgekganlSGGQRQRIAIARALVGNPRILIFDEATSAL 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 174 DISVQAQILNLLVTLQEnhGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVL 231
Cdd:TIGR01846 625 DYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELL 679
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-233 |
1.81e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.09 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDtLLTLRDVHINFPAR-------KNWL----GKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS 69
Cdd:COG1134 1 MSS-MIEVENVSKSYRLYhepsrslKELLlrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 70 HGQYIRSGsqRImqmmfqdplSSL-------NPRLPVW-------RIIteplwiaKHSSEQQRRALAE--ELAvQVGirp 133
Cdd:COG1134 80 SGRVEVNG--RV---------SALlelgagfHPELTGReniylngRLL-------GLSRKEIDEKFDEivEFA-ELG--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 134 EYLDrLP-HAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGlTYVLISHNVSVIRHMSDR 212
Cdd:COG1134 138 DFID-QPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDR 215
|
250 260
....*....|....*....|.
gi 15831341 213 VAVMYLGQIVELGEAQQVLTA 233
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
28-225 |
3.53e-27 |
|
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: 105.53 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 28 HVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-------SQRIMQMMFQDPLSSLNPRLPVW 100
Cdd:cd03266 17 TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepAEARRRLGFVSDSTGLYDRLTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 RIItepLWIAKHSSEQQRRALA--EELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:cd03266 97 ENL---EYFAGLYGLKGDELTArlEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15831341 179 AQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03266 173 RALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
32-234 |
4.32e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 106.35 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRsgsqrimqmMFQDPLSSLNPR--------------- 96
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGE-VR---------LNGRPLAAWSPWelarrravlpqhssl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 97 ---LPVWRIITEPLwIAKHSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARAL-------SSQPDVIVL 166
Cdd:COG4559 87 afpFTVEEVVALGR-APHGSSAAQDRQIVREALALVGLAH-LAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 167 DEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:COG4559 165 DEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
31-231 |
4.53e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 107.13 E-value: 4.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGS---------------QRIMQMMFQDPLSSLNP 95
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGK-VTVGDivvsstskqkeikpvRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 96 RLPVWRIITEP--LWIAKHSSEQqrraLAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK13643 100 ETVLKDVAFGPqnFGIPKEKAEK----IAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 174 DISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:PRK13643 176 DPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-239 |
4.81e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.08 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSH-----------GQYIRSGS------QRIMQMMFQDPlsS 92
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegevrlfGRNIYSPDvdpievRREVGMVFQYP--N 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 93 LNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQ-VGIRPEYLDRL---PHAFSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKkAALWDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 169 PTSALDISVQAQILNLLVTLQENhgLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYT 239
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-235 |
5.13e-27 |
|
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: 105.45 E-value: 5.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 3 DTLLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIM 82
Cdd:COG0410 1 MPMLEVENLHAGYGG-----------IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGS-IRFDGEDIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 83 qmmfqdplsslnpRLPVWRI-------------------ITEPLWIA---KHSSEQQRRALAE------ELAvqvgirpE 134
Cdd:COG0410 69 -------------GLPPHRIarlgigyvpegrrifpsltVEENLLLGayaRRDRAEVRADLERvyelfpRLK-------E 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 135 YLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVA 214
Cdd:COG0410 129 RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAY 207
|
250 260
....*....|....*....|.
gi 15831341 215 VMYLGQIVELGEAQQVLTAPA 235
Cdd:COG0410 208 VLERGRIVLEGTAAELLADPE 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-202 |
6.19e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 110.14 E-value: 6.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSqrimqmm 85
Cdd:TIGR02868 335 LELRDLSAGYPGAPP----------VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 fqdPLSSLNPRLPVWRI-------------ITEPLWIAKH--SSEQQRRALAeelAVQVGirpEYLDRLPH--------- 141
Cdd:TIGR02868 398 ---PVSSLDQDEVRRRVsvcaqdahlfdttVRENLRLARPdaTDEELWAALE---RVGLA---DWLRALPDgldtvlgeg 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 142 --AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLvtLQENHGLTYVLISHN 202
Cdd:TIGR02868 469 gaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-224 |
6.63e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 6.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 8 LRDVHINFPARKnwLgkttehvhaINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRI---MQM 84
Cdd:COG0488 1 LENLSKSFGGRP--L---------LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIgylPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 MFQDP--------LSSLNPRLPVWRIITEPLWIAKHSSEQQRR-----------------ALAEELAVQVGIRPEYLDRL 139
Cdd:COG0488 70 PPLDDdltvldtvLDGDAELRALEAELEELEAKLAEPDEDLERlaelqeefealggweaeARAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 140 PHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI-SVQ--AQILNllvtlqeNHGLTYVLISHNvsviRHMSDRVAvm 216
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEwlEEFLK-------NYPGTVLVVSHD----RYFLDRVA-- 216
|
....*...
gi 15831341 217 ylGQIVEL 224
Cdd:COG0488 217 --TRILEL 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
22-225 |
6.64e-27 |
|
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: 104.58 E-value: 6.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGeTLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-SQRIMQMMFQDPLSSL------N 94
Cdd:cd03264 6 LTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqDVLKQPQKLRRRIGYLpqefgvY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 95 PRLPVWRIITEPLWIAKHSSEQQRRALAEEL-AVQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:cd03264 85 PNFTVREFLDYIAWLKGIPSKEVKARVDEVLeLVNLG---DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831341 174 DISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03264 162 DPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-235 |
1.08e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.86 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG-----------------QYIRSGSQRI----- 81
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnheLITNPYSKKIknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 82 ----MQMMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQqrRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARAL 157
Cdd:PRK13631 114 lrrrVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEA--KKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 158 SSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPA 235
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-222 |
1.32e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.96 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIRSGSQ 79
Cdd:COG3845 1 MMPPALELRGITKRFGG-----------VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEiLIDGKPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 80 RIMQ----------MMFQDPlsSLNPRLPVWR-II--TEPLWIAKHSSEQQRRALaEELAVQVG--IRPeylDRLPHAFS 144
Cdd:COG3845 70 RIRSprdaialgigMVHQHF--MLVPNLTVAEnIVlgLEPTKGGRLDRKAARARI-RELSERYGldVDP---DAKVEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 145 GGQRQRIAIARALSSQPDVIVLDEPTSALdisVQAQILNLLVTLQE--NHGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-241 |
2.02e-26 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 109.04 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPARKnwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------- 77
Cdd:TIGR02203 330 DVEFRNVTFRYPGRD---------RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladyt 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 -----------SQRIMqmMFQDPLSSlNprlpvwriiteplwIAKHSSEQQRRALAEElAVQVGIRPEYLDRLPHAF--- 143
Cdd:TIGR02203 401 laslrrqvalvSQDVV--LFNDTIAN-N--------------IAYGRTEQADRAEIER-ALAAAYAQDFVDKLPLGLdtp 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 144 --------SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAV 215
Cdd:TIGR02203 463 igengvllSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVV 539
|
250 260
....*....|....*....|....*.
gi 15831341 216 MYLGQIVELGEAQQVLTAPAHpYTRL 241
Cdd:TIGR02203 540 MDDGRIVERGTHNELLARNGL-YAQL 564
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-239 |
2.86e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.22 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGM--LQPS---HGQYIRSGS----------QRIMQMMFQDPlsSL 93
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQdifkmdvielRRRVQMVFQIP--NP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 94 NPRLPVWRIITEPL---WIAKHSSE-QQRRALAEELAvqvGIRPEYLDRL--PHA-FSGGQRQRIAIARALSSQPDVIVL 166
Cdd:PRK14247 94 IPNLSIFENVALGLklnRLVKSKKElQERVRWALEKA---QLWDEVKDRLdaPAGkLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 167 DEPTSALDISVQAQILNLLVTLQENhgLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYT 239
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-221 |
3.24e-26 |
|
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: 102.13 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSqrimqmmfqdPLSSLNPRLpvwriiteplWIA 110
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK----------PVTRRSPRD----------AIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 111 KH----SSEQQRRALAEELAVQVGIRpeyldrLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLV 186
Cdd:cd03215 75 AGiayvPEDRKREGLVLDLSVAENIA------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR 148
|
170 180 190
....*....|....*....|....*....|....*
gi 15831341 187 TLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:cd03215 149 ELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
31-231 |
3.53e-26 |
|
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: 108.29 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMMFQDPLSSLN--PRLPVW---RIITE 105
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE-ILLNGFSLKDIDRHTLRQFINylPQEPYIfsgSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 106 PLWIAKHSSEQQRRALAEELAvqvGIRPEyLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:TIGR01193 568 LLLGAKENVSQDEIWAACEIA---EIKDD-IENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 175 ISVQAQILNLLVTLQENhglTYVLISHNVSVIRhMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-225 |
3.72e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 106.27 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 7 TLRDVhinfparknwlGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIrsGSQRI---- 81
Cdd:PRK11000 5 TLRNV-----------TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDlFI--GEKRMndvp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 82 -----MQMMFQDplSSLNPRLPVWRIITEPLWIAKHS-SEQQRR--ALAEELavQVGirpEYLDRLPHAFSGGQRQRIAI 153
Cdd:PRK11000 72 paergVGMVFQS--YALYPHLSVAENMSFGLKLAGAKkEEINQRvnQVAEVL--QLA---HLLDRKPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831341 154 ARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-235 |
4.46e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 105.70 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVhinfpaRKNWLGKTtehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-- 83
Cdd:PRK11650 4 LKLQAV------RKSYDGKT----QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-IWIGGRVVNEle 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 84 -------MMFQDplSSLNPRLPVWRIITEPLWIAKhSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARA 156
Cdd:PRK11650 73 padrdiaMVFQN--YALYPHMSVRENMAYGLKIRG-MPKAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 157 LSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPA 235
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPA 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
8-233 |
4.89e-26 |
|
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: 108.03 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 8 LRDVHINFPARKNwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG----------QYIRSG 77
Cdd:TIGR03375 466 FRNVSFAYPGQET---------PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGsvlldgvdirQIDPAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 SQRIMQMMFQDPlsslnpRLpVWRIITEPLWIAKHSSEQQRRALAEELAvqvGIRpEYLDRLPHAF-----------SGG 146
Cdd:TIGR03375 537 LRRNIGYVPQDP------RL-FYGTLRDNIALGAPYADDEEILRAAELA---GVT-EFVRRHPDGLdmqigergrslSGG 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 147 QRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVtlQENHGLTYVLISHNVSVIRhMSDRVAVMYLGQIVELGE 226
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLK--RWLAGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGP 682
|
....*..
gi 15831341 227 AQQVLTA 233
Cdd:TIGR03375 683 KDQVLEA 689
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
32-261 |
9.75e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 103.27 E-value: 9.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------RIMQMMFQDPLSSL-------- 93
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirHKIGMVFQNPDNQFvgatvedd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 94 ------NPRLPvwriiteplwiakHSSEQQRRALAEELavqVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK13650 103 vafgleNKGIP-------------HEEMKERVNEALEL---VGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 168 EPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRhMSDRVAVMYLGQIVELGEAQQVLTAPAH--------PYT 239
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDllqlgldiPFT 244
|
250 260
....*....|....*....|..
gi 15831341 240 RLLLDSLPAIDKPLEEEWALRK 261
Cdd:PRK13650 245 TSLVQSLRQNGYDLPEGYLTEK 266
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
34-234 |
1.04e-25 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 102.57 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 34 GIDLQIRRGETLGIVGESGCGKSTLAQLlMGML-QPSHGQYI-----------RSGS---------QRI---MQMMFQdp 89
Cdd:COG4598 26 GVSLTARKGDVISIIGSSGSGKSTFLRC-INLLeTPDSGEIRvggeeirlkpdRDGElvpadrrqlQRIrtrLGMVFQ-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 90 lsSLN--PRLPVWRIITE-PLWIAKhSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVL 166
Cdd:COG4598 103 --SFNlwSHMTVLENVIEaPVHVLG-RPKAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 167 DEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDLAE-EGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-222 |
2.28e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 9 RDVHINFPARKNWLGKT---TEHV---HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ--------YI 74
Cdd:COG1129 239 RELEDLFPKRAAAPGEVvleVEGLsvgGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEirldgkpvRI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 75 RSGSQRIMQ-MMFqdpLS------SLNPRLPVWRIITEPlWIAKHS-----SEQQRRALAEELAVQVGIRPEYLDRLPHA 142
Cdd:COG1129 319 RSPRDAIRAgIAY---VPedrkgeGLVLDLSIRENITLA-SLDRLSrggllDRRRERALAEEYIKRLRIKTPSPEQPVGN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 143 FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
32-231 |
6.73e-25 |
|
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: 104.44 E-value: 6.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmmfqdPLSSLNPR--------LPvwrii 103
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS-VRLDGA---------DLSQWDREelgrhigyLP----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 104 teplwiakhsseqQRRAL-----AE--------------ELAVQVGIRpEYLDRLP-----------HAFSGGQRQRIAI 153
Cdd:COG4618 413 -------------QDVELfdgtiAEniarfgdadpekvvAAAKLAGVH-EMILRLPdgydtrigeggARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 154 ARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVELGEAQQVL 231
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGPRDEVL 554
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-232 |
7.44e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 101.24 E-value: 7.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI------RSGSQRIMQ---------MMFQD 88
Cdd:PRK13645 19 KTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdyaiPANLKKIKEvkrlrkeigLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 89 PLSSLNPRLPVWRIITEPLWIAKHSSEQQRRAlaEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:PRK13645 99 PEYQLFQETIEKDIAFGPVNLGENKQEAYKKV--PELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831341 169 PTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLT 232
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-222 |
8.39e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.95 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 3 DTLLTLRDVHInfparknwlgKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI-------- 74
Cdd:COG3845 255 EVVLEVENLSV----------RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRldgeditg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 75 RSGSQRIMQMMF---QDPLSS-LNPRLPVW------RIITEPL----WIakhsSEQQRRALAEELAVQVGIRPEYLDRLP 140
Cdd:COG3845 325 LSPRERRRLGVAyipEDRLGRgLVPDMSVAenlilgRYRRPPFsrggFL----DRKAIRAFAEELIEEFDVRTPGPDTPA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 141 HAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGR 479
|
..
gi 15831341 221 IV 222
Cdd:COG3845 480 IV 481
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
32-233 |
8.82e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 103.97 E-value: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMMFQDplssLNPR---LPvWRIITEPLW 108
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGS-VRLDGADLKQWDRET----FGKHigyLP-QDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 109 IAKHSSEQQRRALAE---ELAVQVGIRpEYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:TIGR01842 408 VAENIARFGENADPEkiiEAAKLAGVH-ELILRLPDGYdtvigpggatlSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 175 ISVQAQILNLLVTLQEnHGLTYVLISHNVSVIrHMSDRVAVMYLGQIVELGEAQQVLTA 233
Cdd:TIGR01842 487 EEGEQALANAIKALKA-RGITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-214 |
9.81e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 9.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 9 RDVHINFPARKNwLGK---TTEHVHA-------INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS 78
Cdd:COG0488 299 KTVEIRFPPPER-LGKkvlELEGLSKsygdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 79 QRI---MQMmfqdpLSSLNPRLPVWRIITEplwIAKHSSEQQRRALAEELavqvGIRPEYLDRLPHAFSGGQRQRIAIAR 155
Cdd:COG0488 378 VKIgyfDQH-----QEELDPDKTVLDELRD---GAPGGTEQEVRGYLGRF----LFSGDDAFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 156 ALSSQPDVIVLDEPTSALDI-SVQAqilnLLVTLQENHGlTYVLISHNvsviRHMSDRVA 214
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHD----RYFLDRVA 496
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-203 |
1.15e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 99.08 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 27 EHVHAI-NGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRIMQM---------------MFQDPL 90
Cdd:PRK10584 20 EHELSIlTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVG-QPLHQMdeearaklrakhvgfVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 91 ssLNPRLPVWRIITEPLwIAKHSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:PRK10584 99 --LIPTLNALENVELPA-LLRGESSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190
....*....|....*....|....*....|...
gi 15831341 171 SALDISVQAQILNLLVTLQENHGLTYVLISHNV 203
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREHGTTLILVTHDL 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
31-225 |
1.27e-24 |
|
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: 98.72 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMmfqdPLSSLNPRLPVwrIITEPLWIA 110
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGS-ILIDGVDISKI----GLHDLRSRISI--IPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 111 -----------KHSSEQQRRALAeelavQVGIRpEYLDRLPHA-----------FSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:cd03244 92 gtirsnldpfgEYSDEELWQALE-----RVGLK-EFVESLPGGldtvveeggenLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 169 PTSALDISVQAQILNllvTLQEN-HGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELG 225
Cdd:cd03244 166 ATASVDPETDALIQK---TIREAfKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-231 |
1.28e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.93 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ---YIRSGSQRIMQMMFQDPLSSLNPRLPVW 100
Cdd:PRK13651 15 KLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKEKVLEKLVIQKTRF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 R-------------------------------IITEPlwIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQ 149
Cdd:PRK13651 95 KkikkikeirrrvgvvfqfaeyqlfeqtiekdIIFGP--VSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQ 229
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
..
gi 15831341 230 VL 231
Cdd:PRK13651 252 IL 253
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
32-225 |
1.76e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.99 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmlqpsHGQY-IRSGS-----QRIMQM------------MFQDPlssl 93
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-----HPKYeVTSGSilldgEDILELspderaragiflAFQYP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 94 nPRLP------VWRIITEplwiAKHSSEQQRRA---LAEELAVQVGIRPEYLDR-LPHAFSGGQRQRIAIARALSSQPDV 163
Cdd:COG0396 87 -VEIPgvsvsnFLRTALN----ARRGEELSAREflkLLKEKMKELGLDEDFLDRyVNEGFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 164 IVLDEPTSALDI-SVQ--AQILNLLvtLQENHGLtyVLISHNVSVIRHMS-DRVAVMYLGQIVELG 225
Cdd:COG0396 162 AILDETDSGLDIdALRivAEGVNKL--RSPDRGI--LIITHYQRILDYIKpDFVHVLVDGRIVKSG 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
33-234 |
2.63e-24 |
|
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: 103.11 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 33 NGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqrimqmmfQDpLSSLNPR---------LPVWRII 103
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDG---------QD-LAGLDVQavrrqlgvvLQNGRLM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 104 TEPLW--IAKHSSEQQRRALaeELAVQVGIRpEYLDRLP---H--------AFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:TIGR03797 540 SGSIFenIAGGAPLTLDEAW--EAARMAGLA-EDIRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDEAT 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831341 171 SALDISVQAQILNLLVTLQenhgLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:TIGR03797 617 SALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-222 |
2.79e-24 |
|
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: 98.17 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 26 TEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY----IRSGSQR------IMQMMFQDplSSLNP 95
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRkkflrrIGVVFGQK--TQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 96 RLPV---WRIITEPLWIAKHSSEQQRRALAEELAVQvgirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:cd03267 109 DLPVidsFYLLAAIYDLPPARFKKRLDELSELLDLE-----ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831341 173 LDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
32-242 |
3.23e-24 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 102.71 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------------------SQRIMqmMFQ----DP 89
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGipreeiprevlansvamvDQDIF--LFEgtvrDN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 90 LSslnprlpvwriitepLWIAKHSSEQQRRALAE-ELAVQVGIRP-EYLDRLPHA---FSGGQRQRIAIARALSSQPDVI 164
Cdd:TIGR03796 573 LT---------------LWDPTIPDADLVRACKDaAIHDVITSRPgGYDAELAEGganLSGGQRQRLEIARALVRNPSIL 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 165 VLDEPTSALDISVQAQIL-NLlvtlqENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVLTAPAhPYTRLL 242
Cdd:TIGR03796 638 ILDEATSALDPETEKIIDdNL-----RRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVGG-AYARLI 709
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-232 |
3.39e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.21 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPARknwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIM-- 82
Cdd:PRK11160 338 SLTLNNVSFTYPDQ---------PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE-ILLNGQPIAdy 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 83 ------QMMfqdplSSLNPRLPVWR-IITEPLWIAKHSSEQQRraLAEELAvQVGIR-----PEYLD-------RlphAF 143
Cdd:PRK11160 408 seaalrQAI-----SVVSQRVHLFSaTLRDNLLLAAPNASDEA--LIEVLQ-QVGLEklledDKGLNawlgeggR---QL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 144 SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVMYLGQIVE 223
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQIIE 553
|
....*....
gi 15831341 224 LGEAQQVLT 232
Cdd:PRK11160 554 QGTHQELLA 562
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
31-225 |
4.36e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.96 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI----------RSGSQRIMQMMFQDPLSsLNprlpvw 100
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtvtRASLRRNIAVVFQDAGL-FN------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 RIITEPLWIAKH--SSEQQRRALAEELAVqvgirpEYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK13657 423 RSIEDNIRVGRPdaTDEEMRAAAERAQAH------DFIERKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 168 EPTSALDISVQAQILNLLVTLQenHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELG 225
Cdd:PRK13657 497 EATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-216 |
4.45e-24 |
|
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: 101.98 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmmfqdPLSSLNPRlpVWRiiTEPLWIA 110
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS-IAVNGV---------PLADADAD--SWR--DQIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 111 KH-------------------SSEQQRRAL-AEELAVQVGIRPEYLDRL----PHAFSGGQRQRIAIARALSSQPDVIVL 166
Cdd:TIGR02857 403 QHpflfagtiaenirlarpdaSDAEIREALeRAGLDEFVAALPQGLDTPigegGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831341 167 DEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVM 216
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAALA-DRIVVL 529
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-234 |
5.90e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.72 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFPARKnwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQP---SHGQYIRSG 77
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSK---------KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 SQRIMQMM----------FQDPLSSL--------------N---PRLPVWRIIteplwiakhsseqqRRALAeelavQVG 130
Cdd:PRK13640 72 ITLTAKTVwdirekvgivFQNPDNQFvgatvgddvafgleNravPRPEMIKIV--------------RDVLA-----DVG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 131 IRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIrHMS 210
Cdd:PRK13640 133 ML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMA 210
|
250 260
....*....|....*....|....
gi 15831341 211 DRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:PRK13640 211 DQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
30-225 |
8.21e-24 |
|
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: 96.83 E-value: 8.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIM------------------QMMFqdpls 91
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGS-IRLDGEDITklppheraragiayvpqgREIF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 92 slnPRLPVWriitEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:TIGR03410 88 ---PRLTVE----ENLLTGLAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831341 172 ALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-208 |
1.21e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.65 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 3 DTLLTLRDVHINFPArknwlGKTTehvhaINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIM 82
Cdd:COG4178 360 DGALALEDLTLRTPD-----GRPL-----LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 83 qMMFQD---PLSSLnpRlpvwRIITEPLWIAKHSSEQQRRALAeelavQVGIrPEYLDRL------PHAFSGGQRQRIAI 153
Cdd:COG4178 430 -FLPQRpylPLGTL--R----EALLYPATAEAFSDAELREALE-----AVGL-GHLAERLdeeadwDQVLSLGEQQRLAF 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 154 ARALSSQPDVIVLDEPTSALDISVQAQILNLLvtLQENHGLTYVLISHNVSVIRH 208
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAF 549
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-216 |
1.82e-23 |
|
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: 95.96 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 4 TLLTLRDVHINFparknwlgktTEH------VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIRS 76
Cdd:COG4778 3 TLLEVENLSKTF----------TLHlqggkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSiLVRH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 77 GSQRI-------MQMM------------FqdpLSSLnPRLPVWRIITEPLwIAKHSSEQQRRALAEELAVQVGIrPEYLD 137
Cdd:COG4778 73 DGGWVdlaqaspREILalrrrtigyvsqF---LRVI-PRVSALDVVAEPL-LERGVDREEARARARELLARLNL-PERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 138 RLPHA-FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:COG4778 147 DLPPAtFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
35-234 |
3.45e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.44 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ--------------RIMQMMFQDPLSSLNPRLPVW 100
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetgnknlkklrKKVSLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 RIITEPLWIAkhSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:PRK13641 106 DVEFGPKNFG--FSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831341 181 ILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:PRK13641 184 MMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-234 |
4.17e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.99 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFparknwlGKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqrimqmm 85
Cdd:PRK09536 4 IDVSDLSVEF-------GDTT----VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 fqDPLSSLNPRLPVWRIITEPLWIA----------------KHSS------EQQRRALAEELAvQVGIrPEYLDRLPHAF 143
Cdd:PRK09536 65 --DDVEALSARAASRRVASVPQDTSlsfefdvrqvvemgrtPHRSrfdtwtETDRAAVERAME-RTGV-AQFADRPVTSL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 144 SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
250
....*....|.
gi 15831341 224 LGEAQQVLTAP 234
Cdd:PRK09536 220 AGPPADVLTAD 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-225 |
4.45e-23 |
|
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: 94.91 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 27 EHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqRIMQMMfqDPLSSLNPRLPVWRIITEP 106
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--RVSSLL--GLGGGFNPELTGRENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 107 LWIAKHSSEQQRRALAE-----ELavqvgirPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:cd03220 109 GRLLGLSRKEIDEKIDEiiefsEL-------GDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15831341 182 LNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03220 182 QRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-234 |
4.77e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.41 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPARKNwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqrimqm 84
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPD--------VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG------- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 mfqDPLSSLNPRL---PVWRIITEPLWIAKHSSEQ----QRRALAEEL--AVQVGIRPEYLDRLPHAF-----------S 144
Cdd:TIGR00958 543 ---VPLVQYDHHYlhrQVALVGQEPVLFSGSVRENiaygLTDTPDEEImaAAKAANAHDFIMEFPNGYdtevgekgsqlS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 145 GGQRQRIAIARALSSQPDVIVLDEPTSALDisvqAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVEL 224
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEM 694
|
250
....*....|
gi 15831341 225 GEAQQVLTAP 234
Cdd:TIGR00958 695 GTHKQLMEDQ 704
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-213 |
5.41e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.88 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 28 HVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ------------RIMQMMFQDPLSSLNP 95
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssaakaelRNQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 96 RLPVWRIITEPLWIA-KHSSEQQRRALaeELAVQVGIRPEYLDRlPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:PRK11629 101 DFTALENVAMPLLIGkKKPAEINSRAL--EMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 15831341 175 ISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRV 213
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
31-203 |
6.42e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ------MMFQDplSSLNPRLPVWRIIT 104
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS-ITLDGKPVEGpgaergVVFQN--EGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 EPLWIAKHSSEQqRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNL 184
Cdd:PRK11248 93 FGLQLAGVEKMQ-RLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
|
170
....*....|....*....
gi 15831341 185 LVTLQENHGLTYVLISHNV 203
Cdd:PRK11248 171 LLKLWQETGKQVLLITHDI 189
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-216 |
7.86e-23 |
|
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: 93.69 E-value: 7.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 21 WLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----SQR--IMQMMFQDplssl 93
Cdd:cd03250 10 WDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsiayvSQEpwIQNGTIRE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 94 NprlpvwriiteplwIAKHSSEQQRR--------ALAEELAV-------QVGIRPEYLdrlphafSGGQRQRIAIARALS 158
Cdd:cd03250 85 N--------------ILFGKPFDEERyekvikacALEPDLEIlpdgdltEIGEKGINL-------SGGQKQRISLARAVY 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 159 SQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVM 216
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVL 200
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
31-207 |
1.04e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.07 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMMFQdplSSLNPRLP--VWRIITEPLW 108
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR---SEVPDSLPltVRDLVAMGRW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 109 ----IAKHSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNL 184
Cdd:NF040873 84 arrgLWRRLTRDDRAAVDDALE-RVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161
|
170 180
....*....|....*....|...
gi 15831341 185 LVTLQENhGLTYVLISHNVSVIR 207
Cdd:NF040873 162 LAEEHAR-GATVVVVTHDLELVR 183
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-222 |
1.21e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.79 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------------QRIMQMMFQDplSSLNPR 96
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlknrevpflRRQIGMIFQD--HHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 97 LPVWRIITEPLWIAKHSSEQQRRALAEELAvQVGIrpeyLDR---LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALD-KVGL----LDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15831341 174 DISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:PRK10908 169 DDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
32-214 |
1.51e-22 |
|
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: 90.97 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqrimqmmfqdplsslnprlpvwriiteplwiak 111
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 112 hsseqqrralaeelavqvGIRPEYLDRLphafSGGQRQRIAIARALSSQPDVIVLDEPTSALDI-SVQAqilnLLVTLQE 190
Cdd:cd03221 62 ------------------TVKIGYFEQL----SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSIEA----LEEALKE 115
|
170 180
....*....|....*....|....
gi 15831341 191 NHGlTYVLISHNvsviRHMSDRVA 214
Cdd:cd03221 116 YPG-TVILVSHD----RYFLDQVA 134
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
222-287 |
3.69e-22 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 87.84 E-value: 3.69e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 222 VELGEAQQVLTAPAHPYTRLLLDSLPAIDKPLeEEWALRKTDLPGNRTLPQGCFFRERCPLATSGC 287
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPK-RPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-246 |
5.51e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.38 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 20 NWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGqYIRSGSQRIMQM---------MFQDpl 90
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG-HIRFHGTDVSRLhardrkvgfVFQH-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 91 SSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELA-----VQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIV 165
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTqllemVQLA---HLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 166 LDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAhpyTRLLLDS 245
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA---TRFVLEF 236
|
.
gi 15831341 246 L 246
Cdd:PRK10851 237 M 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
30-235 |
1.29e-21 |
|
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: 91.07 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM-MF-----------QDPlsSLNPRL 97
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGK-ILLDGQDITKLpMHkrarlgigylpQEA--SIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 98 PVWRIITEPLWIAKHSSEQQRR---ALAEELAVQvgirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:cd03218 91 TVEENILAVLEIRGLSKKEREEkleELLEEFHIT-----HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 175 -ISVQaQILNLLVTLQENhGLTyVLIS-HNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPA 235
Cdd:cd03218 166 pIAVQ-DIQKIIKILKDR-GIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-222 |
1.52e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.79 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPARKnwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYiRSGSQRIMQM 84
Cdd:PRK10535 4 LLELKDIRRSYPSGE-------EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTY-RVAGQDVATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 MfQDPLSSLN--------------PRLPVWRIITEPLWIAKhSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQR 150
Cdd:PRK10535 76 D-ADALAQLRrehfgfifqryhllSHLTAAQNVEVPAVYAG-LERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831341 151 IAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHmSDRVAVMYLGQIV 222
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-230 |
1.86e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----------SQRIMQMMFQDpL 90
Cdd:PRK09700 11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaAQLGIGIIYQE-L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 91 SSLNpRLPVwriiTEPLWIAKHSSEQ----------QRRALAEELAVQVGIRPEyLDRLPHAFSGGQRQRIAIARALSSQ 160
Cdd:PRK09700 90 SVID-ELTV----LENLYIGRHLTKKvcgvniidwrEMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831341 161 PDVIVLDEPTSALdisVQAQILNLLVTLQE--NHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQV 230
Cdd:PRK09700 164 AKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
29-225 |
1.96e-21 |
|
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: 90.03 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQriMQMMFQDPLSSLnPR----LPVWRIIT 104
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP--LDIAARNRIGYL-PEerglYPKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 EPLWIA--KHSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL 182
Cdd:cd03269 90 QLVYLAqlKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15831341 183 NLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03269 169 DVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
31-231 |
2.54e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.93 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG------------------SQRIMqmMFQDPLSS 92
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnqvalvSQNVH--LFNDTIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 93 lNprlpvwriiteplwIAKHSSEQQRRALAEElAVQVGIRPEYLDRLPHAF-----------SGGQRQRIAIARALSSQP 161
Cdd:PRK11176 436 -N--------------IAYARTEQYSREQIEE-AARMAYAMDFINKMDNGLdtvigengvllSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 162 DVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVL 231
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-225 |
3.37e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 91.69 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 19 KNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGS-----------QRIMQMMFQ 87
Cdd:COG4586 25 KGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE-VRVLGyvpfkrrkefaRRIGVVFGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 88 DplSSLNPRLPVWriitEPLWIAKHS---SEQQRRALAEELAVQVGIRpEYLDR----LphafSGGQRQRIAIARALSSQ 160
Cdd:COG4586 104 R--SQLWWDLPAI----DSFRLLKAIyriPDAEYKKRLDELVELLDLG-ELLDTpvrqL----SLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 161 PDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-239 |
3.61e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.93 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 47 IVGESGCGKSTLAQLLMGMLQPSHGqYIRSGS-----------------QRIMQMMFQDPlsslNP-RLPVWRIITEPLW 108
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDvllggrsifnyrdvlefRRRVGMLFQRP----NPfPMSIMDNVLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 109 IAKHSSEQQRRALAEELAVQVGIRPEYLDRL---PHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:PRK14271 127 AHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831341 186 VTLQENhgLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPAHPYT 239
Cdd:PRK14271 207 RSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
29-223 |
3.64e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.92 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQ----------RIMQMMFQDPLSSLnprlp 98
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnlrRKIGMVFQNPDNQF----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 99 VWRIITEPLWIAKHSS-----EQQRRALAEELAVQVgirPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK13642 95 VGATVEDDVAFGMENQgipreEMIKRVDEALLAVNM---LDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831341 174 DISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVE 223
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
38-215 |
5.63e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.95 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 38 QIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------------QYIRSGSqrimQMMFQDPLSSLNPRL---PVWRI 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpelkisykpQYIKPDY----DGTVEDLLRSITDDLgssYYKSE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 103 ITEPLWIakhsseqqrralaEELavqvgirpeyLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL 182
Cdd:PRK13409 437 IIKPLQL-------------ERL----------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
|
170 180 190
....*....|....*....|....*....|...
gi 15831341 183 NLLVTLQENHGLTYVLISHNVSVIRHMSDRVAV 215
Cdd:PRK13409 494 KAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
35-249 |
5.74e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQpshgqYirSGSQRIMQMmfqdPLSSLNPrlPVWR------------- 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-----Y--QGSLKINGI----ELRELDP--ESWRkhlswvgqnpqlp 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 102 --IITEPLWIAKHS-SEQQRRALAEELAVQvgirpEYLDRLPH-----------AFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK11174 436 hgTLRDNVLLGNPDaSDEQLQQALENAWVS-----EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 168 EPTSALDISVQAQILNLLvtLQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVELGEAQQVLTAPAhPYTRLLLDSLP 247
Cdd:PRK11174 511 EPTASLDAHSEQLVMQAL--NAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGG-LFATLLAHRQE 586
|
..
gi 15831341 248 AI 249
Cdd:PRK11174 587 EI 588
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
22-213 |
9.49e-21 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 88.60 E-value: 9.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKT-TEHVH------AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ-YIRSG---------SQRIMQM 84
Cdd:TIGR02324 7 LSKTfTLHQQggvrlpVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRiLVRHEgawvdlaqaSPREVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 MFQDPLSSLN------PRLPVWRIITEPLwIAKHSSEQQRRALAEELAVQVGIrPEYLDRLPHA-FSGGQRQRIAIARAL 157
Cdd:TIGR02324 87 VRRKTIGYVSqflrviPRVSALEVVAEPL-LERGVPREAARARARELLARLNI-PERLWHLPPAtFSGGEQQRVNIARGF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 158 SSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRV 213
Cdd:TIGR02324 165 IADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRV 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-222 |
1.08e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.37 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPArknwlGKTTEhVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM- 84
Cdd:COG1101 2 LELKNLSKTFNP-----GTVNE-KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGS-ILIDGKDVTKLp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 ----------MFQDPLSSLNPRLpvwrIITEPLWIAKH---------SSEQQRRALAEELAVQVGIRPEylDRLPH---A 142
Cdd:COG1101 75 eykrakyigrVFQDPMMGTAPSM----TIEENLALAYRrgkrrglrrGLTKKRRELFRELLATLGLGLE--NRLDTkvgL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 143 FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNvsvIRH---MSDRVAVMYLG 219
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN---MEQaldYGNRLIMMHEG 225
|
...
gi 15831341 220 QIV 222
Cdd:COG1101 226 RII 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-220 |
1.33e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.53 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGML-------------Q 67
Cdd:PRK13549 1 MMEYLLEMKNITKTFGG-----------VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgtyegeiifegE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 68 PSHGQYIRSGSQRIMQMMFQDplSSLNPRLPVWRII---TEPL------WIAKHSSEQqrRALAEelaVQVGIRPEyldr 138
Cdd:PRK13549 70 ELQASNIRDTERAGIAIIHQE--LALVKELSVLENIflgNEITpggimdYDAMYLRAQ--KLLAQ---LKLDINPA---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 139 LP-HAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQeNHGLTYVLISHNVSVIRHMSDRVAVMY 217
Cdd:PRK13549 139 TPvGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIR 217
|
...
gi 15831341 218 LGQ 220
Cdd:PRK13549 218 DGR 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-229 |
1.78e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.53 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQ-----PSHGQYIRSGSQRIMQM------------ 84
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksaGSHIELLGRTVQREGRLardirksrantg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 -MFQDplSSLNPRLPVWRII------TEPLW---IAKHSSEQQRRALaeELAVQVGIRPEYLDRLPhAFSGGQRQRIAIA 154
Cdd:PRK09984 90 yIFQQ--FNLVNRLSVLENVligalgSTPFWrtcFSWFTREQKQRAL--QALTRVGMVHFAHQRVS-TLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 155 RALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQ 229
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
30-247 |
1.99e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.64 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQ-----------MMFQDP----LSSln 94
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGR-VKVMGREVNAenekwvrskvgLVFQDPddqvFSS-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 95 prlPVWRIIT-EPLWIAKHSSEQQRRAlaEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:PRK13647 96 ---TVWDDVAfGPVNMGLDKDEVERRV--EEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 174 DISVQAQILNLLVTLQeNHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGE----------AQQVLTAPA-----HPY 238
Cdd:PRK13647 170 DPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDkslltdedivEQAGLRLPLvaqifEDL 248
|
....*....
gi 15831341 239 TRLLLDSLP 247
Cdd:PRK13647 249 PELGQSKLP 257
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-240 |
2.22e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.56 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLL--MGMLQPS---------HGQYIRSGS------QRIMQMMFQDPlsSLN 94
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEvrvegrvefFNQNIYERRvnlnrlRRQVSMVHPKP--NLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 95 PrLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHA---FSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:PRK14258 101 P-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSaldLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831341 172 ALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMY-----LGQIVELGEAQQVLTAPAHPYTR 240
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-221 |
2.68e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.88 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI--------RSGSQRIMQMMFQDP----LSSLNPRLPV-WR 101
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMlngkeinaLSTAQRLARGLVYLPedrqSSGLYLDAPLaWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 102 II-----TEPLWIakhsSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:PRK15439 362 VCalthnRRGFWI----KPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15831341 177 VQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:PRK15439 438 ARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
32-233 |
5.44e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyirsgsqrimqMMFQD-PLSSLNPR--------LPVWRI 102
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGT-----------VFLGDkPISMLSSRqlarrlalLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 103 ITE----------------PLWiAKHSSEQQRRAlaeELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVL 166
Cdd:PRK11231 87 TPEgitvrelvaygrspwlSLW-GRLSAEDNARV---NQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 167 DEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTA 233
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
27-225 |
6.21e-20 |
|
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: 89.88 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 27 EHVH--------AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS------HGQYIRSGSQ----RIMQMMFQD 88
Cdd:COG5265 361 ENVSfgydperpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTsgriliDGQDIRDVTQaslrAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 89 PL---SSL--NprlpvwriiteplwIA---KHSSEQQRRALAEelAVQVGirpEYLDRLPHAF-----------SGGQRQ 149
Cdd:COG5265 441 TVlfnDTIayN--------------IAygrPDASEEEVEAAAR--AAQIH---DFIESLPDGYdtrvgerglklSGGEKQ 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELG 225
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
32-231 |
6.25e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 86.62 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM-MF-----------QDPlsSLNPRLPV 99
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGR-IFLDGEDITHLpMHkrarlgigylpQEA--SIFRKLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 W---RIITEPLwiakHSSEQQRRALAEELAVQVGIrpEYL-DRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD- 174
Cdd:COG1137 96 EdniLAVLELR----KLSKKEREERLEELLEEFGI--THLrKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDp 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831341 175 ISVqAQILNLLVTLQEnHGLTyVLIS-HNV----SVIrhmsDRVAVMYLGQIVELGEAQQVL 231
Cdd:COG1137 170 IAV-ADIQKIIRHLKE-RGIG-VLITdHNVretlGIC----DRAYIISEGKVLAEGTPEEIL 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-215 |
7.17e-20 |
|
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: 86.69 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 39 IRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG-------------QYIRSGSqrimQMMFQDPLSSLNPRL---PVWRI 102
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdieieldtvsykpQYIKADY----EGTVRDLLSSITKDFythPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 103 -ITEPLWIakhsseqqrralaEELavqvgirpeyLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:cd03237 98 eIAKPLQI-------------EQI----------LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190
....*....|....*....|....*....|....
gi 15831341 182 LNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAV 215
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-225 |
7.80e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.17 E-value: 7.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPS---HGQYIRSGSQRIMQMM-----FQDPLSSLNPRLPVWRII 103
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFqkcvaYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 104 T--EPLWIAKHSSEQQRRALAEelavQVGIRPEYLDRLPHAF----SGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:cd03234 103 TytAILRLPRKSSDAIRKKRVE----DVLLRDLALTRIGGNLvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15831341 178 QAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
31-234 |
1.00e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.58 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-------SQRIMQM----MFQdplsslNPRLPV 99
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGqhieglpGHQIARMgvvrTFQ------HVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 WRIITEPLWIAKHSSEQQ------------RRALAEELAV------QVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQP 161
Cdd:PRK11300 94 EMTVIENLLVAQHQQLKTglfsgllktpafRRAESEALDRaatwleRVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 162 DVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-222 |
1.04e-19 |
|
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: 89.11 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGML-------------QPSHGQYIRSGSQRIMQMMFQDpl 90
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgeiywsgSPLKASNIRDTERAGIVIIHQE-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 91 SSLNPRLPVWRII------TEPLWIAkHSSEQQRRAlaEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVI 164
Cdd:TIGR02633 87 LTLVPELSVAENIflgneiTLPGGRM-AYNAMYLRA--KNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 165 VLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-215 |
7.99e-19 |
|
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: 86.76 E-value: 7.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 38 QIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------------QYIRSGSQrimqMMFQDPLSSLNPRlpvwrIITE 105
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlkisykpQYISPDYD----GTVEEFLRSANTD-----DFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 106 PLWIakhsseqqrralaEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:COG1245 433 SYYK-------------TEIIKPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170 180 190
....*....|....*....|....*....|
gi 15831341 186 VTLQENHGLTYVLISHNVSVIRHMSDRVAV 215
Cdd:COG1245 499 RRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-270 |
1.02e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.39 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRsgsqrimqmMFQDPLSS--------------LN 94
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE-VL---------WDGEPLDPedrrrigylpeergLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 95 PRLPVWRIItepLWIA--KHSSEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:COG4152 84 PKMKVGEQL---VYLArlKGLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 173 LD-ISVQAqILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTapAHPYTRLLLDSLPAIDK 251
Cdd:COG4152 160 LDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR--QFGRNTLRLEADGDAGW 235
|
250
....*....|....*....
gi 15831341 252 pLEEEWALRKTDLPGNRTL 270
Cdd:COG4152 236 -LRALPGVTVVEEDGDGAE 253
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-221 |
1.17e-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: 82.90 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 9 RDVHINFPARKnwlgktteHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS---------- 78
Cdd:cd03248 15 QNVTFAYPTRP--------DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkyl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 79 QRIMQMMFQDP-LSSlnprlpvwRIITEPLWIAKHSSEQQRralAEELAVQVGIRpEYLDRLPHAF-----------SGG 146
Cdd:cd03248 87 HSKVSLVGQEPvLFA--------RSLQDNIAYGLQSCSFEC---VKEAAQKAHAH-SFISELASGYdtevgekgsqlSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 147 QRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQI 221
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
32-225 |
1.61e-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: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGM--LQPSHGQyIRSGSQRIMQ------------MMFQDPlsslnPRL 97
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGE-ILFKGEDITDlppeerarlgifLAFQYP-----PEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 98 PvwriiteplwiakhsseqqrralaeelavqvGIR-PEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDIS 176
Cdd:cd03217 90 P-------------------------------GVKnADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831341 177 VQAQILNLLVTLQENhGLTYVLISHNVSVIRHM-SDRVAVMYLGQIVELG 225
Cdd:cd03217 139 ALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-238 |
2.74e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.77 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQI-RRGETlGIVGESGCGKSTLAQLLMGMLQPSHGqYIRSGS---------------QRIMQMMFQDPlsslnpRL- 97
Cdd:PRK11144 17 VNLTLpAQGIT-AIFGRSGAGKTSLINAISGLTRPQKG-RIVLNGrvlfdaekgiclppeKRRIGYVFQDA------RLf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 98 PVWRIITEPLWIAKHSSEQQRRALAEELavqvGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:PRK11144 89 PHYKVRGNLRYGMAKSMVAQFDKIVALL----GIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831341 178 QAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAPA-HPY 238
Cdd:PRK11144 164 KRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPW 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
22-231 |
3.12e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.86 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYI-----------RSGSQRIMQMMFQDPl 90
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplHARARRGIGYLPQEA- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 91 sSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIrpEYL-DRLPHAFSGGQRQRIAIARALSSQPDVIVLDEP 169
Cdd:PRK10895 88 -SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI--EHLrDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 170 TSALD-ISVqAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:PRK10895 165 FAGVDpISV-IDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-234 |
3.86e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 2 SDTLLTLRDVHINFParknwlGKTTEHvhainGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRI 81
Cdd:PRK10575 8 SDTTFALRNVSFRVP------GRTLLH-----PLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA-QPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 82 MQM---MFQDPLSSLNPRLPVWRIIT--EPLWIAKHSSE-------QQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQ 149
Cdd:PRK10575 76 ESWsskAFARKVAYLPQQLPAAEGMTvrELVAIGRYPWHgalgrfgAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 150 RIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQ 229
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
....*
gi 15831341 230 VLTAP 234
Cdd:PRK10575 235 LMRGE 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-231 |
4.21e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.36 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----SQRIM-------QMMFQDPlsslNPRLPV 99
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpldySKRGLlalrqqvATVFQDP----EQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 WRIITEPLWIAKH---SSEQQRRALAEELAV--QVGIRPEYLDRLPHafsgGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:PRK13638 93 TDIDSDIAFSLRNlgvPEAEITRRVDEALTLvdAQHFRHQPIQCLSH----GQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 175 ISVQAQILNLL--VTLQENHgltYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:PRK13638 169 PAGRTQMIAIIrrIVAQGNH---VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
31-240 |
4.39e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.14 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLL--MGMLQPS---------HGQYIRSGS------QRIMQMMFQDPlssl 93
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvegkvtfHGKNLYAPDvdpvevRRRIGMVFQKP---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 94 NPrLP--VWRIITEPLWIAKHSSEQQRraLAEELAVQVGIRPEYLDRLPH---AFSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:PRK14243 101 NP-FPksIYDNIAYGARINGYKGDMDE--LVERSLRQAALWDEVKDKLKQsglSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 169 PTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMSDRVAVM---------YLGQIVELGEAQQVLTAPAHPYT 239
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQAT 255
|
.
gi 15831341 240 R 240
Cdd:PRK14243 256 R 256
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
32-216 |
5.70e-18 |
|
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: 80.84 E-value: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMMFQDPLSSlnpRLPVWRIITEPlWIAK 111
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN---RYSVAYAAQKP-WLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 112 HSSE-----------QQRRALAEELAVQVGIrpeylDRLPHA-----------FSGGQRQRIAIARALSSQPDVIVLDEP 169
Cdd:cd03290 93 ATVEenitfgspfnkQRYKAVTDACSLQPDI-----DLLPFGdqteigerginLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15831341 170 TSALDISVQAQILN--LLVTLQENHgLTYVLISHNVSVIRHmSDRVAVM 216
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLPH-ADWIIAM 214
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-223 |
6.88e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 83.69 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmLQPsHGQY---------------IRSGSQR----IMQM 84
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYP-HGSYegeilfdgevcrfkdIRDSEALgiviIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 MFQDPLSSlnprlpvwriITEPLWIakhSSEQQRRAL---------AEELAVQVGirpeyLDRLPHAFSG----GQRQRI 151
Cdd:NF040905 87 LALIPYLS----------IAENIFL---GNERAKRGVidwnetnrrARELLAKVG-----LDESPDTLVTdigvGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831341 152 AIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
34-233 |
8.59e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 8.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLqPSHGQYIRSGsqrimqmmfqDPLSSLNPR----------------- 96
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNG----------RPLSDWSAAelarhraylsqqqsppf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 97 -LPVWRIITepLWIAKHSSEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARAL-------SSQPDVIVLDE 168
Cdd:COG4138 83 aMPVFQYLA--LHQPAGASSEAVEQLLAQLAEALGLED-KLSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 169 PTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTA 233
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTP 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-231 |
1.47e-17 |
|
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: 83.46 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIM--QMMFQDplSSLNPRLPVWRIITEPlwi 109
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVpqQAWIQN--DSLRENILFGKALNEK--- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 110 aKHSSEQQRRALAEELAV-QVGIRPEYLDRLPHaFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL-NLLVT 187
Cdd:TIGR00957 729 -YYQQVLEACALLPDLEIlPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGP 806
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15831341 188 LQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVELGEAQQVL 231
Cdd:TIGR00957 807 EGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
35-201 |
1.76e-17 |
|
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: 77.96 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMmfqdplsslnPRLPVWRIITeplwiakhss 114
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFL----------PQRPYLPLGT---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 115 eqqrraLAEELavqvgIRPEYldrlpHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLvtlqENHGL 194
Cdd:cd03223 80 ------LREQL-----IYPWD-----DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGI 139
|
....*..
gi 15831341 195 TYVLISH 201
Cdd:cd03223 140 TVISVGH 146
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
220-305 |
1.87e-17 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 75.86 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 220 QIVELGEAQQVLTAPAHPYTRLLLDSLPAIDKPLEeewalRKTDLPGN----RTLPQGCFFRERCPLATSGCEVRQSLTT 295
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDR-----KLISIPGEvpslINLPSGCRFYPRCPYAQDECRKEPPALV 75
|
90
....*....|.
gi 15831341 296 R-ADGREIRCW 305
Cdd:TIGR01727 76 EiAEGHRVACH 86
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
35-244 |
1.96e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-------------SQRIMQMMFQDplSSLNPRLPVWR 101
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrsrlytVRKRMSMLFQS--GALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 102 IITEPLWIAKHSSEQQRRALAEELAVQVGIRPEyLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:PRK11831 104 NVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 182 LNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQvLTAPAHPYTRLLLD 244
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA-LQANPDPRVRQFLD 244
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
6-241 |
2.65e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 79.61 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINfparknwlgktTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmlqpsHGQY------IRSGSQ 79
Cdd:TIGR01978 1 LKIKDLHVS-----------VEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG-----HPSYevtsgtILFKGQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 80 RIMQMM------------FQDPL------------SSLNPRlpvwriiTEPLWIAKHSSEQQRRALAEELAVqVGIRPEY 135
Cdd:TIGR01978 65 DLLELEpderaraglflaFQYPEeipgvsnleflrSALNAR-------RSARGEEPLDLLDFEKLLKEKLAL-LDMDEEF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 136 LDR-LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGlTYVLISHNVSVIRHMS-DRV 213
Cdd:TIGR01978 137 LNRsVNEGFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDR-SFLIITHYQRLLNYIKpDYV 215
|
250 260
....*....|....*....|....*...
gi 15831341 214 AVMYLGQIVELGEAQQVLTAPAHPYTRL 241
Cdd:TIGR01978 216 HVLLDGRIVKSGDVELAKELEAKGYDWV 243
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
37-233 |
7.00e-17 |
|
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: 77.97 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 37 LQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSqrimqmmfqdplsslnPRLPVWRIIT------EPLWIA 110
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA----------------SPGKGWRHIGyvpqrhEFAWDF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 111 KHSSEQ-------------QRRALAEELAVQVGIR----PEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:TIGR03771 65 PISVAHtvmsgrtghigwlRRPCVADFAAVRDALRrvglTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 174 DISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVaVMYLGQIVELGEAQQVLTA 233
Cdd:TIGR03771 145 DMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDP 202
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
31-225 |
7.27e-17 |
|
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: 77.45 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMMFQDPLSSLN--PRLPVW--RIITEP 106
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGK-IEIDGIDISTIPLEDLRSSLTiiPQDPTLfsGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 107 LWIAKHSSEQQrraLAEELAVQVGirpeyldrlPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNllV 186
Cdd:cd03369 102 LDPFDEYSDEE---IYGALRVSEG---------GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK--T 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 15831341 187 TLQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVELG 225
Cdd:cd03369 168 IREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
36-231 |
7.39e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 80.44 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 36 DLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYiRSGSQRI-------MQMMFQDPLSSLNPRL----------P 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER-QSQFSHItrlsfeqLQKLVSDEWQRNNTDMlspgeddtgrT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 99 VWRIITEplwiakhssEQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK10938 102 TAEIIQD---------EVKDPARCEQLAQQFGITA-LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15831341 179 AQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:PRK10938 172 QQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-213 |
7.58e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 4 TLLTLRDVHINFPARKnwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRI-- 81
Cdd:PRK09544 3 SLVSLENVSVSFGQRR-----------VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIgy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 82 -MQMMFQDPlsslnprlpvwriiTEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLP-HAFSGGQRQRIAIARALSS 159
Cdd:PRK09544 72 vPQKLYLDT--------------TLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPmQKLSGGETQRVLLARALLN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831341 160 QPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRV 213
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-230 |
8.19e-17 |
|
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: 80.62 E-value: 8.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGM--LQPSHGQYI----------------RSGSQ---- 79
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPcpvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 80 --------------------RIMQ---MMFQDPLSSLNPRLPVWRIITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYL 136
Cdd:TIGR03269 86 ggtlepeevdfwnlsdklrrRIRKriaIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 137 DRlphAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:TIGR03269 166 AR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWL 242
|
250
....*....|....
gi 15831341 217 YLGQIVELGEAQQV 230
Cdd:TIGR03269 243 ENGEIKEEGTPDEV 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-235 |
1.04e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.05 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ----------------------YI---RSGSQRIMQMMF 86
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYvtldghevvtrspqdglangivYIsedRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 87 QDPLSslnprLPVWRIITEPLWIAKHSSEQQrraLAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVL 166
Cdd:PRK10762 348 KENMS-----LTALRYFSRAGGSLKHADEQQ---AVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 167 DEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVelGE------AQQVLTAPA 235
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIS--GEftreqaTQEKLMAAA 491
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-211 |
1.13e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.45 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 2 SDTLLTLRDVHINFPARKnwlgkttehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqri 81
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAK-----------ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 82 mqmmfqDPLSSLNP-----------RLP------VWRIITEPLWIAKHSSEQQrrALAEELAvQVGIRPEYLDRLPHAFS 144
Cdd:PRK10247 69 ------EDISTLKPeiyrqqvsycaQTPtlfgdtVYDNLIFPWQIRNQQPDPA--IFLDDLE-RFALPDTILTKNIAELS 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 145 GGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSD 211
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADK 206
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
35-233 |
1.85e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.76 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIR-------SGSQRIMQ----MMFQDPL---SSLNPRLPVW 100
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE-IRldgrplsSLSHSVLRqgvaMVQQDPVvlaDTFLANVTLG 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 RIITEP-LWIAKHSSE--QQRRALAEELAVQVGirpEYLDRLphafSGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:PRK10790 439 RDISEEqVWQALETVQlaELARSLPDGLYTPLG---EQGNNL----SVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 178 QAQILNLLVTLQENhgLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVLTA 233
Cdd:PRK10790 512 EQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
35-233 |
2.15e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrIMQMMFQD-----PLSSLNPRLPvwRIITEPLWI 109
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH-IQHYASKEvarriGLLAQNATTP--GDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 110 AKHSSEQQ----RRALAEELAVQVGIRPEYLDRLPH----AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:PRK10253 103 ARGRYPHQplftRWRKEDEEAVTKAMQATGITHLADqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831341 182 LNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTA 233
Cdd:PRK10253 183 LELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
41-219 |
2.20e-16 |
|
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: 74.72 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 41 RGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRsgsqrimqmmfqdplsslnprlpvwriiteplwiakHSSEQQRRA 120
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------------IDGEDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 121 LAEELavqvgiRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVT-----LQENHGLT 195
Cdd:smart00382 45 VLDQL------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSEKNLT 118
|
170 180
....*....|....*....|....*....
gi 15831341 196 YVLISHNVSV-----IRHMSDRVAVMYLG 219
Cdd:smart00382 119 VILTTNDEKDlgpalLRRRFDRRIVLLLI 147
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-217 |
3.03e-16 |
|
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: 76.64 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQ----IRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyirsgsqrimqmmFQDPlsslnprl 97
Cdd:cd03236 2 LEDEPVHRYGPNSFKLHrlpvPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-------------FDDP-------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 98 PVWRIITEplwiAKHSSEQQR--RALAEElAVQVGIRPEYLDRLPHAF-------------------------------- 143
Cdd:cd03236 61 PDWDEILD----EFRGSELQNyfTKLLEG-DVKVIVKPQYVDLIPKAVkgkvgellkkkdergkldelvdqlelrhvldr 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 144 -----SGGQRQRIAIARALSSQPDVIVLDEPTSALDISvqaQILNLLVTLQE--NHGLTYVLISHNVSVIRHMSDRVAVM 216
Cdd:cd03236 136 nidqlSGGELQRVAIAAALARDADFYFFDEPSSYLDIK---QRLNAARLIRElaEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
.
gi 15831341 217 Y 217
Cdd:cd03236 213 Y 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
34-185 |
4.02e-16 |
|
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: 75.09 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------QRIMQMMFQDPLSSLNPRLPVWRIITep 106
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdEPHENILYLGHLPGLKPELSALENLH-- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 107 LWIAKHSSEQqrRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:TIGR01189 96 FWAAIHGGAQ--RTIEDALA-AVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-223 |
5.17e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 23 GKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimQMMFQDPLSSLN-------- 94
Cdd:PRK11288 11 GKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS-ILIDGQ---EMRFASTTAALAagvaiiyq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 95 -----PRLPVwriiTEPLWIAK--------HSSEQQRRALAEELAVQVGIRPEY-LDRLphafSGGQRQRIAIARALSSQ 160
Cdd:PRK11288 87 elhlvPEMTV----AENLYLGQlphkggivNRRLLNYEAREQLEHLGVDIDPDTpLKYL----SIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831341 161 PDVIVLDEPTSALDISVQAQILNLLVTL-QENHGLTYVliSHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELrAEGRVILYV--SHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-225 |
2.09e-15 |
|
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: 72.97 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 12 HINFPARKNWLGKTTEHVHAINGIdlqIRRGETLGIVGESGCGKSTLAQLLMGMLQPSH--GQYIRSGSQ-------RIM 82
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKNVSGK---AKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPldkrsfrKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 83 QMMFQDplSSLNPRLPVWriitEPLWIAKHSSeqqrralaeelavqvGIrpeyldrlphafSGGQRQRIAIARALSSQPD 162
Cdd:cd03213 85 GYVPQD--DILHPTLTVR----ETLMFAAKLR---------------GL------------SGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831341 163 VIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVS-VIRHMSDRVAVMYLGQIVELG 225
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
32-234 |
5.26e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.19 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQ-----------RIMQMMFQDPlsSLNPRLPV- 99
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGE-VLVDGLdvattpsrelaKRLAILRQEN--HINSRLTVr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 -------------------WRIITEplwiakhsseqqrrALAE-ELAvqvGIRPEYLDRLphafSGGQRQRIAIARALSS 159
Cdd:COG4604 94 elvafgrfpyskgrltaedREIIDE--------------AIAYlDLE---DLADRYLDEL----SGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 160 QPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
31-233 |
9.00e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQMMFQDPLSSLNPRLPV-WR--IITEPL 107
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGK-ISILGQPTRQALQKNLVAYVPQSEEVdWSfpVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 108 ----------WIAKHSSEQqrRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:PRK15056 101 vmmgryghmgWLRRAKKRD--RQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 178 QAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDrVAVMYLGQIVELGEAQQVLTA 233
Cdd:PRK15056 178 EARIISLLRELRD-EGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTA 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-231 |
1.04e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 24 KTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSH--GQYIRSGSQRIMQMM------FQDPLssLNP 95
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILkrtgfvTQDDI--LYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 96 RLPVWR--IITEPLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHAF----SGGQRQRIAIARALSSQPDVIVLDEP 169
Cdd:PLN03211 154 HLTVREtlVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 170 TSALDISVQAQILNLLVTLQeNHGLTYVLISHNVSV-IRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
29-222 |
1.13e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.83 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsQRIMQMmfqdplsslnprlPVWRIITEPLW 108
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG-KDITDW-------------QTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 109 IAKHSSEQQRRALAEELAVQVGI---RPEYLDRLPHAF-----------------SGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFfaeRDQFQERIKWVYelfprlherriqragtmSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831341 169 PTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
31-234 |
1.36e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.98 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRsgsqrimqmmFQD-PLSSLnpRLPVWR-------- 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD-IR----------FHDiPLTKL--QLDSWRsrlavvsq 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 102 -------IITEPLWIAKHSSEQQRralAEELAVQVGIRPEYLdRLPHAF-----------SGGQRQRIAIARALSSQPDV 163
Cdd:PRK10789 397 tpflfsdTVANNIALGRPDATQQE---IEHVARLASVHDDIL-RLPQGYdtevgergvmlSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 164 IVLDEPTSALDISVQAQILNLLVtlQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
34-185 |
2.78e-14 |
|
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: 70.21 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQ-------MMFQDPLSSLNPRLPVWRIITep 106
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrdsiargLLYLGHAPGIKTTLSVLENLR-- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 107 LWIAKHSSEQQRRALAeelavQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:cd03231 96 FWHADHSDEQVEEALA-----RVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-221 |
2.94e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.94 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 25 TTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMG---------MLQPSHGQYIRSGSQRIMQ---MMFQD-PLS 91
Cdd:TIGR02633 269 INPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnVFINGKPVDIRNPAQAIRAgiaMVPEDrKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 92 SLNPRLPVWRIITEPLwIAKHSSEQQRRALAEELAVQVGIRPEYLdRLPHAF------SGGQRQRIAIARALSSQPDVIV 165
Cdd:TIGR02633 349 GIVPILGVGKNITLSV-LKSFCFKMRIDAAAELQIIGSAIQRLKV-KTASPFlpigrlSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 166 LDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-268 |
1.12e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 5 LLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSqrimqm 84
Cdd:PRK15439 11 LLCARSISKQYSG-----------VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 mfqdPLSSLNP----RLPVWRIITEPLW-------------IAKHSSEQQR-RALAEELAVQVGirpeyLDRLPHAFSGG 146
Cdd:PRK15439 74 ----PCARLTPakahQLGIYLVPQEPLLfpnlsvkenilfgLPKRQASMQKmKQLLAALGCQLD-----LDSSAGSLEVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 147 QRQRIAIARALSSQPDVIVLDEPTSALdisVQAQILNLLVTLQE--NHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVEL 224
Cdd:PRK15439 145 DRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALS 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15831341 225 GEAQQVLTApahpytrlllDSLPAIdKPLEEEWALRKT-----DLPGNR 268
Cdd:PRK15439 222 GKTADLSTD----------DIIQAI-TPAAREKSLSASqklwlELPGNR 259
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-223 |
1.42e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 4 TLLTLRDVHINFPArknwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRImq 83
Cdd:PRK10762 3 ALLQLKGIDKAFPG-----------VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 84 mmFQDPLSS-----------LN--PRLPV------WRIITEPL----WiakhsseQQRRALAEELAVQVGIRPEYlDRLP 140
Cdd:PRK10762 70 --FNGPKSSqeagigiihqeLNliPQLTIaeniflGREFVNRFgridW-------KKMYAEADKLLARLNLRFSS-DKLV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 141 HAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQ-ENHGLTYvlISHNVSVIRHMSDRVAVMYLG 219
Cdd:PRK10762 140 GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKsQGRGIVY--ISHRLKEIFEICDDVTVFRDG 217
|
....*
gi 15831341 220 Q-IVE 223
Cdd:PRK10762 218 QfIAE 222
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-227 |
1.43e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 1 MSDTLLTLRDVHINFparknwlgKTTEhvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmlqpsHGQY-IRSG-- 77
Cdd:CHL00131 3 KNKPILEIKNLHASV--------NENE---ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-----HPAYkILEGdi 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 ---------------SQRIMQMMFQDP------------------------LSSLNPrLPVWRIITEPLWIakhsseqqr 118
Cdd:CHL00131 67 lfkgesildlepeerAHLGIFLAFQYPieipgvsnadflrlaynskrkfqgLPELDP-LEFLEIINEKLKL--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 119 ralaeelavqVGIRPEYLDR-LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI---LNLLVTLQEnhgl 194
Cdd:CHL00131 137 ----------VGMDPSFLSRnVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIaegINKLMTSEN---- 202
|
250 260 270
....*....|....*....|....*....|....
gi 15831341 195 TYVLISHNVSVIRHMS-DRVAVMYLGQIVELGEA 227
Cdd:CHL00131 203 SIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDA 236
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-232 |
1.48e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 70.69 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 21 WLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMMfqdplSSLNPRLPVW 100
Cdd:PRK13545 29 FRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS-----SGLNGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 RIITEPLWIAKHSSEQQRRALAE--ELAvQVGirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PRK13545 104 ENIELKGLMMGLTKEKIKEIIPEiiEFA-DIG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831341 179 AQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLT 232
Cdd:PRK13545 180 KKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
29-213 |
1.61e-13 |
|
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: 67.35 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQllmgmlqpshgqyirSGSQRIMQMMFQDPLSsLNPRLPVWRIiteplw 108
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------EGLYASGKARLISFLP-KFSRNKLIFI------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 109 iakhsseQQRRALaeelaVQVGIRPEYLDRLPHAFSGGQRQRIAIARAL--SSQPDVIVLDEPTSALDISVQAQILNLLV 186
Cdd:cd03238 66 -------DQLQFL-----IDVGLGYLTLGQKLSTLSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDINQLLEVIK 133
|
170 180
....*....|....*....|....*..
gi 15831341 187 TLQENhGLTYVLISHNVSVIRHmSDRV 213
Cdd:cd03238 134 GLIDL-GNTVILIEHNLDVLSS-ADWI 158
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
13-217 |
1.67e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 13 INFPARknwLGKTTEHVHAINGIDL----QIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY---------IR--SG 77
Cdd:PRK13409 69 VNLPEE---LEEEPVHRYGVNGFKLyglpIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevLKrfRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 SQriMQMMFQDpLSSLNPR----------LP------VWRIIteplwiaKHSSEqqrRALAEELAVQVGIRPeYLDRLPH 141
Cdd:PRK13409 146 TE--LQNYFKK-LYNGEIKvvhkpqyvdlIPkvfkgkVRELL-------KKVDE---RGKLDEVVERLGLEN-ILDRDIS 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 142 AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHgltYVL-ISHNVSVIRHMSDRVAVMY 217
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK---YVLvVEHDLAVLDYLADNVHIAY 285
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
34-185 |
1.99e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRIMQM---MFQDPL-----SSLNPRLPVWriitE 105
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE-VLWQGEPIRRQrdeYHQDLLylghqPGIKTELTAL----E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 106 PL-WIAKHSSEQQRRALAEELAvQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNL 184
Cdd:PRK13538 94 NLrFYQRLHGPGDDEALWEALA-QVGLA-GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
.
gi 15831341 185 L 185
Cdd:PRK13538 172 L 172
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
38-234 |
2.57e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 38 QIRRGETLGIVGESGCGKSTLAQLLMGMLqPSHGQyIRSGSQRIMQMmfqdPLSSLNPR-------------LPVWRIIT 104
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGS-IQFAGQPLEAW----SAAELARHraylsqqqtppfaMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 epLWIAKHSSEQQRRALAEELAVQVGIRPEyLDRLPHAFSGG--QRQRIA-----IARALSSQPDVIVLDEPTSALDISV 177
Cdd:PRK03695 92 --LHQPDKTRTEAVASALNEVAEALGLDDK-LGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 178 QAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTAP 234
Cdd:PRK03695 169 QAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
32-233 |
3.20e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.68 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-------QRIMQMMFQDPLSSLNPRLPVwriiT 104
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarHARQRVGVVPQFDNLDPDFTV----R 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 EPLWIAKHS---SEQQRRALAEELaVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQI 181
Cdd:PRK13537 99 ENLLVFGRYfglSAAAARALVPPL-LEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831341 182 LNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLTA 233
Cdd:PRK13537 178 WERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-217 |
4.02e-13 |
|
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: 69.43 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 13 INFPARknwLGKTTEHVHAINGIDL----QIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIR-----------SG 77
Cdd:COG1245 69 VNLPEE---LEEDPVHRYGENGFRLyglpVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEepswdevlkrfRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 78 SQrimqmmFQDPLSSL-NPRLpvwRIITEPLW---IAKHSSEQQR--------RALAEELAVQVGIRPeYLDRLPHAFSG 145
Cdd:COG1245 146 TE------LQDYFKKLaNGEI---KVAHKPQYvdlIPKVFKGTVRellekvdeRGKLDELAEKLGLEN-ILDRDISELSG 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 146 GQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHglTYVL-ISHNVSVIRHMSDRVAVMY 217
Cdd:COG1245 216 GELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEG--KYVLvVEHDLAILDYLADYVHILY 286
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
39-217 |
4.48e-13 |
|
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: 66.44 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 39 IRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGqyirsgsqrimqmmfqdplsslNPRLPVWRIIteplwiakhsseqqr 118
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD----------------------NDEWDGITPV--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 119 ralaeelavqvgIRPEYLDrlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVL 198
Cdd:cd03222 65 ------------YKPQYID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALV 127
|
170
....*....|....*....
gi 15831341 199 ISHNVSVIRHMSDRVAVMY 217
Cdd:cd03222 128 VEHDLAVLDYLSDRIHVFE 146
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-221 |
5.25e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 28 HVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQpshGQY------------IRSGSQRIMQ---MMFQD-PLS 91
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP---GRWegeifidgkpvkIRNPQQAIAQgiaMVPEDrKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 92 SLNPRLPVWRIITepLWIAKHSSEQQRRALAEELAVqvgIRpEYLDRL----PHAF------SGGQRQRIAIARALSSQP 161
Cdd:PRK13549 351 GIVPVMGVGKNIT--LAALDRFTGGSRIDDAAELKT---IL-ESIQRLkvktASPElaiarlSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 162 DVIVLDEPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
35-233 |
5.37e-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: 69.59 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrIMQMMFQDPLSSLN--PRLPVW-----RIITEPL 107
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN-IAKIGLHDLRFKITiiPQDPVLfsgslRMNLDPF 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 108 wiAKHSSEQQRRALaeELAVQVGIRPEYLDRLPHA-------FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQ 180
Cdd:TIGR00957 1384 --SQYSDEEVWWAL--ELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 1459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15831341 181 ILNLLVTLQENhgLTYVLISHNVSVIRHMSdRVAVMYLGQIVELGEAQQVLTA 233
Cdd:TIGR00957 1460 IQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
35-228 |
5.79e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY--------IRSGSQRIMQ-MMF--QD-------PLSSLNPR 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVyldgkpidIRSPRDAIRAgIMLcpEDrkaegiiPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 97 LPV--------WRIITEPLWIAKhSSEQQRRALAeelavqvgIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDE 168
Cdd:PRK11288 352 INIsarrhhlrAGCLINNRWEAE-NADRFIRSLN--------IKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 169 PTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIV-ELGEAQ 228
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAgELAREQ 482
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
35-182 |
6.41e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 69.17 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqRImqmmfqdplsSLNPRLPvWRI---ITEPLWIAK 111
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RI----------SFSPQTS-WIMpgtIKDNIIFGL 511
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831341 112 HSSEQQRRAL--AEELAVQVGIRPEYlDRLPH-----AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL 182
Cdd:TIGR01271 512 SYDEYRYTSVikACQLEEDIALFPEK-DKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-201 |
6.73e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 38 QIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQrimqmmfqdplsslnprlpvwriitepLWIAKHssEQQ 117
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-IHCGTK---------------------------LEVAYF--DQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 118 RRALAEE------LA-----VQVGIRPE----YL-DRLPH---------AFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:PRK11147 391 RAELDPEktvmdnLAegkqeVMVNGRPRhvlgYLqDFLFHpkramtpvkALSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180
....*....|....*....|....*....
gi 15831341 173 LDIsvqaQILNLLVTLQENHGLTYVLISH 201
Cdd:PRK11147 471 LDV----ETLELLEELLDSYQGTVLLVSH 495
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
35-220 |
9.67e-13 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.19 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGsqrimQMMFQDPLSSLNPrlpvwRIITEPLWIAKHSS 114
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----RISFSSQFSWIMP-----GTIKENIIFGVSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 115 EQQRRALAEELAVQVGIR--PEYlDRLPHA-----FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLV- 186
Cdd:cd03291 126 EYRYKSVVKACQLEEDITkfPEK-DNTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVc 204
|
170 180 190
....*....|....*....|....*....|....
gi 15831341 187 TLQENHglTYVLISHNVSVIRhMSDRVAVMYLGQ 220
Cdd:cd03291 205 KLMANK--TRILVTSKMEHLK-KADKILILHEGS 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-186 |
1.02e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 68.35 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 34 GIDLQIRrgetLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRiMQMMFQ---DPLS-SLNPRLPVWRIITEPLwi 109
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR-MAVFSQhhvDGLDlSSNPLLYMMRCFPGVP-- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 110 akhssEQQRRALAEELAV--QVGIRPEYldrlphAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI-SVQAQILNLLV 186
Cdd:PLN03073 604 -----EQKLRAHLGSFGVtgNLALQPMY------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLVL 672
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-208 |
1.31e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNwlgkttehVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRI---- 81
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD--------VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLkdin 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 82 -------MQMMFQDPL-----------------------------------SSLNPRLPVWRIITEPLWIAKHSSE---- 115
Cdd:PTZ00265 455 lkwwrskIGVVSQDPLlfsnsiknnikyslyslkdlealsnyynedgndsqENKNKRNSCRAKCAGDLNDMSNTTDsnel 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 116 ----QQRRALAEELAVQVGIR---PEYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLDEPTSALDISV 177
Cdd:PTZ00265 535 iemrKNYQTIKDSEVVDVSKKvliHDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270
....*....|....*....|....*....|.
gi 15831341 178 QAQILNLLVTLQENHGLTYVLISHNVSVIRH 208
Cdd:PTZ00265 615 EYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-235 |
2.10e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKnwlgkttehvHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSqrimqmm 85
Cdd:PRK10522 323 LELRNVTFAYQDNG----------FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 86 fqdPLSSLNPRlpVWR-----IITEpLWIAKHSSEQQRRALAEELAVQVGIRPEYLDRLPHA--------FSGGQRQRIA 152
Cdd:PRK10522 386 ---PVTAEQPE--DYRklfsaVFTD-FHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELEdgrisnlkLSKGQKKRLA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 153 IARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIrHMSDRVAVMYLGQIVEL-GEAQQVL 231
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSELtGEERDAA 538
|
....
gi 15831341 232 TAPA 235
Cdd:PRK10522 539 SRDA 542
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-248 |
2.22e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrIMQMMFQDPLSSLN--PRLPVW-----RIIT 104
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD-VAKFGLTDLRRVLSiiPQSPVLfsgtvRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 EPLwiAKHSSEQQRRALaEELAVQVGIR--PEYLD----RLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQ 178
Cdd:PLN03232 1331 DPF--SEHNDADLWEAL-ERAHIKDVIDrnPFGLDaevsEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 179 AQILNLLvtLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVLTAPAHPYTRLLLDSLPA 248
Cdd:PLN03232 1408 SLIQRTI--REEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPA 1474
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
6-229 |
2.92e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.99 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNWLGKTTEHVhaINGIDLQIRRGETLGIVGESGCGKSTL----AQLLMGMLQ----------PSHG 71
Cdd:TIGR00955 17 DGSWKQLVSRLRGCFCRERPRKHL--LKNVSGVAKPGELLAVMGSSGAGKTTLmnalAFRSPKGVKgsgsvllngmPIDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 72 QYIRSGSQRIMQ-------------MMFQDPLsslnpRLPvwriiteplwiaKHSSEQQRRALAEELAVQVGIR------ 132
Cdd:TIGR00955 95 KEMRAISAYVQQddlfiptltvrehLMFQAHL-----RMP------------RRVTKKEKRERVDEVLQALGLRkcantr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 133 ---PEYLDRLphafSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQeNHGLTYVLISHNVSV-IRH 208
Cdd:TIGR00955 158 igvPGRVKGL----SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPSSeLFE 232
|
250 260
....*....|....*....|.
gi 15831341 209 MSDRVAVMYLGQIVELGEAQQ 229
Cdd:TIGR00955 233 LFDKIILMAEGRVAYLGSPDQ 253
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-174 |
4.51e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG------QYIRSGS----QRI--MQMMFqdplsSLNPRLP 98
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgQPVDAGDiatrRRVgyMSQAF-----SLYGELT 355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 99 VwRiitEPLWI-AK--HSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:NF033858 356 V-R---QNLELhARlfHLPAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-225 |
5.67e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 20 NWLGKTTEHvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQ--YIRSGSQRIMQM--MFQDPLSSlnp 95
Cdd:PLN03232 623 SWDSKTSKP--TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsvVIRGSVAYVPQVswIFNATVRE--- 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 96 rlpvwriitEPLWIAKHSSEQQRRALaEELAVQvgirpEYLDRLPHA-----------FSGGQRQRIAIARALSSQPDVI 164
Cdd:PLN03232 698 ---------NILFGSDFESERYWRAI-DVTALQ-----HDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 165 VLDEPTSALDISVQAQILNLLVTlQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVELG 225
Cdd:PLN03232 763 IFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-185 |
6.41e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 34 GIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----SQRIMQMMFQDPLSSLNPRLPV------WRI 102
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddPDVAEACHYLGHRNAMKPALTVaenlefWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 103 I--TEPLWIAkhsseqqrRALAeelavQVGIRPeyLDRLPHAF-SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:PRK13539 100 FlgGEELDIA--------AALE-----AVGLAP--LAHLPFGYlSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
....*.
gi 15831341 180 QILNLL 185
Cdd:PRK13539 165 LFAELI 170
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
46-211 |
7.28e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 46 GIVGESGCGKSTLAQLLMGMLQPSHGQY-----IRSGSQRIMQMMFQDplsslnprlpvWRIIT------EPLWIAKhsS 114
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVsldpnERLGKLRQDQFAFEE-----------FTVLDtvimghTELWEVK--Q 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 115 EQQR-RALAE-----------------------------ELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVI 164
Cdd:PRK15064 98 ERDRiYALPEmseedgmkvadlevkfaemdgytaearagELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDIL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 165 VLDEPTSALDISV---QAQILNllvtlqeNHGLTYVLISH-----NvSVIRHMSD 211
Cdd:PRK15064 178 LLDEPTNNLDINTirwLEDVLN-------ERNSTMIIISHdrhflN-SVCTHMAD 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-232 |
7.65e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 4 TLLTLRDVHINFPARK----NWLGKTTEHVHAI--------NGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHG 71
Cdd:PRK09700 239 RLMVGRELQNRFNAMKenvsNLAHETVFEVRNVtsrdrkkvRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGG 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 72 QYIRSGSQrimqMMFQDPLSSL-------------NPRLPVWRI-----ITEPLWIAK--------HSSEQQRraLAEEL 125
Cdd:PRK09700 319 EIRLNGKD----ISPRSPLDAVkkgmayitesrrdNGFFPNFSIaqnmaISRSLKDGGykgamglfHEVDEQR--TAENQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 126 AVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSV 205
Cdd:PRK09700 393 RELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPE 471
|
250 260
....*....|....*....|....*..
gi 15831341 206 IRHMSDRVAVMYLGQIVELGEAQQVLT 232
Cdd:PRK09700 472 IITVCDRIAVFCEGRLTQILTNRDDMS 498
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
36-222 |
7.88e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 36 DLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMMfQDPlsslnPRL---PVWRIITEPL----- 107
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQ-QDP-----PRNvegTVYDFVAEGIeeqae 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 108 ----------WIAKHSSEQQRRALAE------------------ELAVQVGIRPeylDRLPHAFSGGQRQRIAIARALSS 159
Cdd:PRK11147 97 ylkryhdishLVETDPSEKNLNELAKlqeqldhhnlwqlenrinEVLAQLGLDP---DAALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 160 QPDVIVLDEPTSALDISVQAQILNLLVTLQEnhglTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-215 |
7.99e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 134 EYLDRLPHAF-----------SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHN 202
Cdd:PTZ00265 1339 EFIESLPNKYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1418
|
90
....*....|...
gi 15831341 203 VSVIRHmSDRVAV 215
Cdd:PTZ00265 1419 IASIKR-SDKIVV 1430
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-230 |
9.33e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.81 E-value: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQmmfqdpLSSLNPRL---PVWRIITEPL 107
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------ISDVHQNMgycPQFDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 108 WIAKHSS--EQQRRALAEEL------AVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQA 179
Cdd:TIGR01257 2028 TGREHLYlyARLRGVPAEEIekvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15831341 180 QILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQV 230
Cdd:TIGR01257 2108 MLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-214 |
1.01e-11 |
|
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: 65.34 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQriMQMMFQDPL-SSLNPRLPVWRII---TEPL 107
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEIGET--VKLAYVDQSrDALDPNKTVWEEIsggLDII 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 108 WIAKHS--------------SEQQRRalaeelavqVGIrpeyldrlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:TIGR03719 415 KLGKREipsrayvgrfnfkgSDQQKK---------VGQ-----------LSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15831341 174 DIsvqaqilNLLVTLQE---NHGLTYVLISHNvsviRHMSDRVA 214
Cdd:TIGR03719 475 DV-------ETLRALEEallNFAGCAVVISHD----RWFLDRIA 507
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
8-231 |
1.16e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.68 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 8 LRDVHInfPARKNwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMMfq 87
Cdd:PRK13546 24 MKDALI--PKHKN------KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAIS-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 88 dplSSLNPRLPVWRIItEPLWIAKHSSEQQRRALAEELaVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK13546 94 ---AGLSGQLTGIENI-EFKMLCMGFKRKEIKAMTPKI-IEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831341 168 EPTSALDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVL 231
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
30-201 |
1.88e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLqpshgqyirsgSQRIMQMMFQDPLSSLNPRLPvwriITEPLWI 109
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-----------KGTPVAGCVDVPDNQFGREAS----LIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 110 AKHSSEqqrralAEELAVQVGIRPEYL-DRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDiSVQAQILNLLV-T 187
Cdd:COG2401 109 KGDFKD------AVELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD-RQTAKRVARNLqK 181
|
170
....*....|....
gi 15831341 188 LQENHGLTYVLISH 201
Cdd:COG2401 182 LARRAGITLVVATH 195
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-232 |
4.17e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrIMQMMFQDPLSSLN--PRLPVW-----RIIT 104
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCD-ISKFGLMDLRKVLGiiPQAPVLfsgtvRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 EP--------LWIA---KHSSEQQRR-ALAEELAVQVGirpeyldrlPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:PLN03130 1334 DPfnehndadLWESlerAHLKDVIRRnSLGLDAEVSEA---------GENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 173 LDISVQAQILNllvTLQEN-HGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVLT 232
Cdd:PLN03130 1405 VDVRTDALIQK---TIREEfKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-168 |
4.28e-11 |
|
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: 63.28 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 6 LTLRDVHINFPARKNwlgkttEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI---- 81
Cdd:COG4615 328 LELRGVTYRYPGEDG------DEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE-ILLDGQPVtadn 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 82 ----MQMM---------FQDPLSSLNPRLPvwriiteplwiakhssEQQRRALAE-ELAVQVGIRPEYLDRLphAFSGGQ 147
Cdd:COG4615 401 reayRQLFsavfsdfhlFDRLLGLDGEADP----------------ARARELLERlELDHKVSVEDGRFSTT--DLSQGQ 462
|
170 180
....*....|....*....|.
gi 15831341 148 RQRIAIARALSSQPDVIVLDE 168
Cdd:COG4615 463 RKRLALLVALLEDRPILVFDE 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
30-224 |
6.75e-11 |
|
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: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 30 HAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRImQMMFQDPlsSLNPRLPVWRIITEPLWI 109
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKV-GYLPQEP--QLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 110 AKHSseQQR---------------RALAEE---------------LAVQVGIRPEYLdRLP------HAFSGGQRQRIAI 153
Cdd:TIGR03719 96 IKDA--LDRfneisakyaepdadfDKLAAEqaelqeiidaadawdLDSQLEIAMDAL-RCPpwdadvTKLSGGERRRVAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 154 ARALSSQPDVIVLDEPTSALDISVQAQILNLlvtLQENHGlTYVLISHNvsviRHMSDRVAvmylGQIVEL 224
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERH---LQEYPG-TVVAVTHD----RYFLDNVA----GWILEL 231
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-242 |
8.51e-11 |
|
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: 61.08 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 20 NWLGKTTEHVHAIngidlqIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrIMQMmfqdPLSSLNPRLPV 99
Cdd:cd03288 31 NNLKPVLKHVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID-ISKL----PLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 wrIITEPLWIA-----------KHSSEQQRRALA-EELAVQVGIRPEYLDRL----PHAFSGGQRQRIAIARALSSQPDV 163
Cdd:cd03288 100 --ILQDPILFSgsirfnldpecKCTDDRLWEALEiAQLKNMVKSLPGGLDAVvtegGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 164 IVLDEPTSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHmSDRVAVMYLGQIVELGEAQQVLTAPAHPYTRLL 242
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
32-223 |
1.01e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.77 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY----------IRSGSQRIMQMMFQDplsSLNPRLPVwr 101
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvparARLARARIGVVPQFD---NLDLEFTV-- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 102 iiTEPLWIAKHSSEQQRRALAEelavqvgIRPEYLD--RLPHA-------FSGGQRQRIAIARALSSQPDVIVLDEPTSA 172
Cdd:PRK13536 132 --RENLLVFGRYFGMSTREIEA-------VIPSLLEfaRLESKadarvsdLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831341 173 LDISVQAQILNLLVTLQEnHGLTYVLISHNVSVIRHMSDRVAVMYLG-QIVE 223
Cdd:PRK13536 203 LDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
32-236 |
1.32e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPShgqyIRSGSQRIMQMMFQD--PLSSLN-PRLPVWRIITeplw 108
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGG----GAPRGARVTGDVTLNgePLAAIDaPRLARLRAVL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 109 iakhsSEQQRRAL---AEELAVqvgirpeyLDRLPHA---------------------------------FSGGQRQRIA 152
Cdd:PRK13547 89 -----PQAAQPAFafsAREIVL--------LGRYPHArragalthrdgeiawqalalagatalvgrdvttLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 153 IARALS---------SQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVE 223
Cdd:PRK13547 156 FARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
250
....*....|...
gi 15831341 224 LGEAQQVLTaPAH 236
Cdd:PRK13547 236 HGAPADVLT-PAH 247
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-208 |
2.83e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.92 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLmGMLQPSHGQYIRSGSQRIMQMMFQDPLSSLnprlpvwRIITEPLWIAK 111
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRLTKPAKGKLFYVPQRPYMTL-------GTLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 112 HSSEQQRRALAEELAVQvgirpeYLD--RLPH----------------AFSGGQRQRIAIARALSSQPDVIVLDEPTSAL 173
Cdd:TIGR00954 540 SSEDMKRRGLSDKDLEQ------ILDnvQLTHilereggwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180 190
....*....|....*....|....*....|....*
gi 15831341 174 DISVQAQILNLLvtlqENHGLTYVLISHNVSVIRH 208
Cdd:TIGR00954 614 SVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-222 |
3.11e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-------SQRIMQ----MMFQDplssLNprL 97
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidfksSKEALEngisMVHQE----LN--L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 98 PVWRIITEPLWIAKHSSE----------QQRRALAEELAVQVGIRPEYLDrlphaFSGGQRQRIAIARALSSQPDVIVLD 167
Cdd:PRK10982 85 VLQRSVMDNMWLGRYPTKgmfvdqdkmyRDTKAIFDELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15831341 168 EPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-232 |
3.42e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.57 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQY-----IRSGSQRIMQMMF----QDPLSSLNPrlpvwri 102
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgIKLGYFAQHQLEFlradESPLQHLAR------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 103 iteplwIAKHSSEQQRRALAEELAVQVGIRPEYLDRlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQIL 182
Cdd:PRK10636 401 ------LAPQELEQKLRDYLGGFGFQGDKVTEETRR----FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831341 183 NLLVTLQEnhglTYVLISHNVSVIRHMSDRVAVMYLGQIV----ELGEAQQVLT 232
Cdd:PRK10636 471 EALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKVEpfdgDLEDYQQWLS 520
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-221 |
4.84e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 31 AINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQrimqmmFQDPLSSLNPRL---PVWRIITEPL 107
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD------IETNLDAVRQSLgmcPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 108 WIAKH-------------SSEQQRRALAEELAVQVGIRPEYLDrlphaFSGGQRQRIAIARALSSQPDVIVLDEPTSALD 174
Cdd:TIGR01257 1019 TVAEHilfyaqlkgrsweEAQLEMEAMLEDTGLHHKRNEEAQD-----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15831341 175 ISVQAQILNLLvtLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQI 221
Cdd:TIGR01257 1094 PYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
37-202 |
7.94e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 37 LQIRRG---------------ETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRiMQMMFQDplsslNPRLPV-- 99
Cdd:PRK10636 7 LQIRRGvrvlldnatatinpgQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQ-LAWVNQE-----TPALPQpa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 100 ----------WRIITEPLWIAKHSSEQQR----------------RALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAI 153
Cdd:PRK10636 81 leyvidgdreYRQLEAQLHDANERNDGHAiatihgkldaidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831341 154 ARALSSQPDVIVLDEPTSALDisvqaqiLNLLVTLQ---ENHGLTYVLISHN 202
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLD-------LDAVIWLEkwlKSYQGTLILISHD 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-225 |
2.33e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS----------QRIMQMMFQDP-LSSLNPRLPVw 100
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReigayglrelRRQFSMIPQDPvLFDGTVRQNV- 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 101 riitEPLWIAkhSSEQQRRALaeELavqVGIR------PEYLD-RLPHA---FSGGQRQRIAIARALSSQ-PDVIVLDEP 169
Cdd:PTZ00243 1405 ----DPFLEA--SSAEVWAAL--EL---VGLRervaseSEGIDsRVLEGgsnYSVGQRQLMCMARALLKKgSGFILMDEA 1473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 170 TSALDISVQAQILNLLVTLQENHglTYVLISHNVSVIRHMsDRVAVMYLGQIVELG 225
Cdd:PTZ00243 1474 TANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMG 1526
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
22-201 |
2.48e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 22 LGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRImQMMFQDPLSSLNPRLPVWR 101
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANI-GYYAQDHAYDFENDLTLFD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 102 iiteplWIAKHSSEQQrralaEELAVQvGIrpeyLDRL----------PHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:PRK15064 404 ------WMSQWRQEGD-----DEQAVR-GT----LGRLlfsqddikksVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTN 467
|
170 180 190
....*....|....*....|....*....|.
gi 15831341 172 ALDI-SVQAqiLNLLVtlqENHGLTYVLISH 201
Cdd:PRK15064 468 HMDMeSIES--LNMAL---EKYEGTLIFVSH 493
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
144-225 |
3.91e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 144 SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTlQENHGLTYVLISHNVSVIRHMsDRVAVMYLGQIVE 223
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
..
gi 15831341 224 LG 225
Cdd:PLN03130 820 EG 821
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
142-229 |
7.48e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 142 AFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTL-QENHGLtyVLISHNVSVIRHMSDRVAVMYLGQ 220
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGL 468
|
90
....*....|..
gi 15831341 221 ---IVELGEAQQ 229
Cdd:PRK10982 469 vagIVDTKTTTQ 480
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
29-213 |
1.39e-08 |
|
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: 54.19 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGCGKSTLAqllMGMLQpSHGQ--YIRSGS----QRIMQMmfQDP-------LS---- 91
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLA---FDTIY-AEGQrrYVESLSayarQFLGQM--DKPdvdsiegLSpaia 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 92 ------SLNPRLPVwRIITEP------LWiakhsseqQRRALAEELAVQVGIRPEYL--DRLPHAFSGGQRQRIAIARAL 157
Cdd:cd03270 82 idqkttSRNPRSTV-GTVTEIydylrlLF--------ARVGIRERLGFLVDVGLGYLtlSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 158 SSQ-PDVI-VLDEPTSALDisvQAQILNLLVTLQE--NHGLTYVLISHNVSVIRHmSDRV 213
Cdd:cd03270 153 GSGlTGVLyVLDEPSIGLH---PRDNDRLIETLKRlrDLGNTVLVVEHDEDTIRA-ADHV 208
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
35-226 |
1.45e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGS-----QR--IMQMMFQDPLSSLNPRLPvwriitEPL 107
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSiayvpQQawIMNATVRGNILFFDEEDA------ARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 108 WIAKHSS--EQQRRALAEELAVQVGIRPEYLdrlphafSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLL 185
Cdd:PTZ00243 753 ADAVRVSqlEADLAQLGGGLETEIGEKGVNL-------SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC 825
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15831341 186 VtLQENHGLTYVLISHNVSVIRHmSDRVAVMYLGQIVELGE 226
Cdd:PTZ00243 826 F-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGS 864
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
29-232 |
1.61e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 29 VHAINGIDLQIRRGETLGIVGESGcgkstlAQLLMGMLqPSHGQYIRSGSQRIMQMMFQDPLSSLNPRLPVWRIIT---- 104
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*G------AA**RGAL-PAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*grr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 ------EPLWIAKHS---SEQQRRALAEELAVQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:NF000106 99 esfsgrENLYMIGR*ldlSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 176 SVQAQILNLLVTLQENhGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGEAQQVLT 232
Cdd:NF000106 178 RTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
133-219 |
1.72e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 133 PEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQEnhglTYVLISHN-------VSV 205
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHAreflntvVTD 410
|
90
....*....|....
gi 15831341 206 IRHMSDRVAVMYLG 219
Cdd:PLN03073 411 ILHLHGQKLVTYKG 424
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
32-201 |
2.37e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQyIRSGSQRI--------MQMMFQDPLSSLNPRLpvwrII 103
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE-ILFERQSIkkdlctyqKQLCFVGHRSGINPYL----TL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 104 TEPLWIAKHSSEQqrrALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDisvQAQILN 183
Cdd:PRK13540 92 RENCLYDIHFSPG---AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLLT 165
|
170 180
....*....|....*....|
gi 15831341 184 LLVTLQEN--HGLTYVLISH 201
Cdd:PRK13540 166 IITKIQEHraKGGAVLLTSH 185
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
32-226 |
4.44e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.87 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGM--LQPSHGQYIRSGSQRI-----------MQMMFQDPLSSlnPRLP 98
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLelspedragegIFMAFQYPVEI--PGVS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 99 VWRIITEPLWIAKHSSEQQR------RALAEELAVQVGIRPEYLDR-LPHAFSGGQRQRIAIARALSSQPDVIVLDEPTS 171
Cdd:PRK09580 95 NQFFLQTALNAVRSYRGQEPldrfdfQDLMEEKIALLKMPEDLLTRsVNVGFSGGEKKRNDILQMAVLEPELCILDESDS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831341 172 ALDISVQAQILNLLVTLQeNHGLTYVLISHNVSVIRHMS-DRVAVMYLGQIVELGE 226
Cdd:PRK09580 175 GLDIDALKIVADGVNSLR-DGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-214 |
6.83e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPShgqyirSGSQRI---MQMMFQDPL-SSLNPRLPVWRIIT--- 104
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPD------SGTIKIgetVKLAYVDQSrDALDPNKTVWEEISggl 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 105 EPLWIAKHS--------------SEQQRRalaeelavqVGIrpeyldrlphaFSGGQRQRIAIARALSSQPDVIVLDEPT 170
Cdd:PRK11819 414 DIIKVGNREipsrayvgrfnfkgGDQQKK---------VGV-----------LSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831341 171 SALDISvqaqilnllvTLQ--ENHGLTY----VLISHNvsviRHMSDRVA 214
Cdd:PRK11819 474 NDLDVE----------TLRalEEALLEFpgcaVVISHD----RWFLDRIA 509
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
46-224 |
8.10e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 46 GIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRImQMMFQDPLssLNPRLPVWRIITEPLwiaKHSSEQQRR------ 119
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKV-GYLPQEPQ--LDPEKTVRENVEEGV---AEVKAALDRfneiya 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 120 ----------ALAEELA-VQvgirpEYLD------------------RLPHA------FSGGQRQRIAIARALSSQPDVI 164
Cdd:PRK11819 111 ayaepdadfdALAAEQGeLQ-----EIIDaadawdldsqleiamdalRCPPWdakvtkLSGGERRRVALCRLLLEKPDML 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831341 165 VLDEPTSALDI-SVQAqilnLLVTLQENHGlTYVLISHNvsviRHMSDRVAvmylGQIVEL 224
Cdd:PRK11819 186 LLDEPTNHLDAeSVAW----LEQFLHDYPG-TVVAVTHD----RYFLDNVA----GWILEL 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-229 |
9.86e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 9 RDVHINFPAR-----------KNWlgkTTEH-VHA----INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMlqpSHGQ 72
Cdd:NF040905 240 RDLEDRYPERtpkigevvfevKNW---TVYHpLHPerkvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SYGR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 73 YIrSGSQR---------------------------------IMQMMFQDPLSSLNPrlpvwriiteplwIAKHS--SEQQ 117
Cdd:NF040905 314 NI-SGTVFkdgkevdvstvsdaidaglayvtedrkgyglnlIDDIKRNITLANLGK-------------VSRRGviDENE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 118 RRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDisVQA-----QILNLLVtlqeNH 192
Cdd:NF040905 380 EIKVAEEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID--VGAkyeiyTIINELA----AE 453
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15831341 193 GLTYVLISHNVSVIRHMSDRVAVMYLGQIV-EL--GEAQQ 229
Cdd:NF040905 454 GKGVIVISSELPELLGMCDRIYVMNEGRITgELprEEASQ 493
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
143-222 |
1.65e-07 |
|
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: 50.72 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 143 FSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSV-IRHMSDRVAVMYLGQI 221
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQ 198
|
.
gi 15831341 222 V 222
Cdd:cd03233 199 I 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-175 |
1.48e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 35 IDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSG-----SQRIMQMMFQDPLSSLNPRLPVwriiTEPL-W 108
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktatrGDRSRFMAYLGHLPGLKADLST----LENLhF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 109 IAKHSSEQQRRALAEELAVqVGIrPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDI 175
Cdd:PRK13543 106 LCGLHGRRAKQMPGSALAI-VGL-AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
47-207 |
1.52e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 47 IVGESGCGKSTLAQLLMGMLQPSHGQ-YIRSGSQRIMQMMFQDPLS-SLNPRLPVWRIITEPLWIAKHSSEQQRRALAEE 124
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNiYYKNCNINNIAKPYCTYIGhNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 125 LAVQvgirpEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDiSVQAQILNLLVTLQENHGLTYVLISHNVS 204
Cdd:PRK13541 111 FKLH-----DLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS-KENRDLLNNLIVMKANSGGIVLLSSHLES 184
|
...
gi 15831341 205 VIR 207
Cdd:PRK13541 185 SIK 187
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-207 |
1.71e-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: 49.24 E-value: 1.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 144 SGGQRQRIAIARALSSQ---PDVIVLDEPTSAL---DIsvqAQILNLLVTLQENhGLTYVLISHNVSVIR 207
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDK-GNTVVVIEHNLDVIK 896
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
144-207 |
2.70e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.61 E-value: 2.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831341 144 SGGQRQRIAIARALSSQ---PDVIVLDEPTSALDISVQAQILNLLVTLQENhGLTYVLISHNVSVIR 207
Cdd:cd03271 171 SGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLDVIK 236
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
32-219 |
4.53e-06 |
|
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: 46.47 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLmgmlqpshgqyirsgSQR-IMQMMFQDPLSSLNPRLPVWRIITeplwia 110
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVL---------------AGRkTAGVITGEILINGRPLDKNFQRST------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 111 khSSEQQRRALAEELAVQVGIRPEYLDRlphAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQe 190
Cdd:cd03232 82 --GYVEQQDVHSPNLTVREALRFSALLR---GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA- 155
|
170 180 190
....*....|....*....|....*....|
gi 15831341 191 NHGLTYVLISHNVS-VIRHMSDRVAVMYLG 219
Cdd:cd03232 156 DSGQAILCTIHQPSaSIFEKFDRLLLLKRG 185
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
144-207 |
1.11e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 1.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 144 SGGQRQRIAIARALS---SQPDVIVLDEPTSAL---DISVQAQILNLLVtlqeNHGLTYVLISHNVSVIR 207
Cdd:COG0178 828 SGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDIRKLLEVLHRLV----DKGNTVVVIEHNLDVIK 893
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
144-232 |
1.87e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 144 SGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTL-QENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIV 222
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSaNILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQI 290
|
90
....*....|
gi 15831341 223 ELGEAQQVLT 232
Cdd:TIGR00956 291 YFGPADKAKQ 300
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
144-207 |
2.71e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 2.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 144 SGGQRQRIAIARALSSQPD---VIVLDEPTSAL---DISVQAQILNLLVtlqeNHGLTYVLISHNVSVIR 207
Cdd:PRK00349 832 SGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDIRKLLEVLHRLV----DKGNTVVVIEHNLDVIK 897
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
10-225 |
3.26e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 10 DVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMlqpSHGQYIrSGSQRI-----MQM 84
Cdd:PLN03140 874 NYFVDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR---KTGGYI-EGDIRIsgfpkKQE 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 85 MF--------QDPLSSlnPRLPVWR--IITEPLWIAKHSSEQQRRALAEELAVQVgirpeYLDRLPHAFSG--------- 145
Cdd:PLN03140 950 TFarisgyceQNDIHS--PQVTVREslIYSAFLRLPKEVSKEEKMMFVDEVMELV-----ELDNLKDAIVGlpgvtglst 1022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 146 GQRQRIAIARALSSQPDVIVLDEPTSALDiSVQAQILNLLVTLQENHGLTYVLISHNVSV-IRHMSDRVAVMYL-GQIVE 223
Cdd:PLN03140 1023 EQRKRLTIAVELVANPSIIFMDEPTSGLD-ARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIY 1101
|
..
gi 15831341 224 LG 225
Cdd:PLN03140 1102 SG 1103
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-225 |
4.06e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 136 LDRLP-----HAFSGGQRQRIAIARAL---SSQPDVIVLDEPTSALDI-SVQAQILNLLVTLQENHglTYVLISHNVSVI 206
Cdd:PRK00635 798 LDYLPlgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHThDIKALIYVLQSLTHQGH--TVVIIEHNMHVV 875
|
90
....*....|....*....
gi 15831341 207 RhMSDRVavmylgqiVELG 225
Cdd:PRK00635 876 K-VADYV--------LELG 885
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
133-211 |
5.85e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 133 PEYLDRLphafSGGQRQ------RIAIARALSSQPDVIVLDEPTSALDI-SVQAQILNLLVTLQENHGLTYVLISHNVSV 205
Cdd:cd03240 110 LDMRGRC----SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEEL 185
|
....*.
gi 15831341 206 IRHMSD 211
Cdd:cd03240 186 VDAADH 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-206 |
1.86e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 26 TEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLL-----MGMLQP----SHGQYIRSGSQRIMQMMFQDPLSSlnPR 96
Cdd:TIGR00956 773 KEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVITGgdrlVNGRPLDSSFQRSIGYVQQQDLHL--PT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 97 LPVWR--IITEPLWIAKHSSEQQRRALAEELAVQVGIRpEYLDRLPHAFSGG----QRQRIAIARALSSQPDVIV-LDEP 169
Cdd:TIGR00956 851 STVREslRFSAYLRQPKSVSKSEKMEYVEEVIKLLEME-SYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190
....*....|....*....|....*....|....*..
gi 15831341 170 TSALDISVQAQILNLLVTLQeNHGLTYVLISHNVSVI 206
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSAI 965
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-174 |
2.20e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 32 INGIDLQIRRGETLGIVGESGCGKSTLAQLLMGmlqpSHGQ-YI--------RSGS--------QRI------MQMMFQD 88
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQgYSndltlfgrRRGSgetiwdikKHIgyvsssLHLDYRV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 89 PLSSLNPrlpvwrIIT---EPLWIAKHSSEQQRRaLAEELAVQVGIRPEYLDRLPHAFSGGQrQRIA-IARALSSQPDVI 164
Cdd:PRK10938 352 STSVRNV------ILSgffDSIGIYQAVSDRQQK-LAQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLL 423
|
170
....*....|
gi 15831341 165 VLDEPTSALD 174
Cdd:PRK10938 424 ILDEPLQGLD 433
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
41-199 |
3.90e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.56 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 41 RGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMmfqDPLSSLNPRLPVWRIITEPLwiAKHSSEQQRRA 120
Cdd:pfam13191 23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPY---SPLLEALTREGLLRQLLDEL--ESSLLEAWRAA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831341 121 LAEELAVQVGIRPEYLDRLPHAFsggqrQRIAIARALSSQPDVIVLDEptsaLDISVQAQiLNLLVTLQENHGLTYVLI 199
Cdd:pfam13191 98 LLEALAPVPELPGDLAERLLDLL-----LRLLDLLARGERPLVLVLDD----LQWADEAS-LQLLAALLRLLESLPLLV 166
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
127-234 |
3.97e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 127 VQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQ-PDVI-VLDEPTSALDISVQAQILNLLVTLQeNHGLTYVLISHNVS 204
Cdd:TIGR00630 473 IDVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLR-DLGNTLIVVEHDED 551
|
90 100 110
....*....|....*....|....*....|....*.
gi 15831341 205 VIRHmSDRV------AVMYLGQIVELGEAQQVLTAP 234
Cdd:TIGR00630 552 TIRA-ADYVidigpgAGEHGGEVVASGTPEEILANP 586
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
16-201 |
7.34e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 40.06 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 16 PARKNWLgkttehvhaINGIdlqIRRGETLGIVGESGCGKSTLA-QLLMGMLQ--PSHGQYIRSGSQRIMQMMFQDPLSS 92
Cdd:pfam13481 19 PPPRRWL---------IKGL---LPAGGLGLLAGAPGTGKTTLAlDLAAAVATgkPWLGGPRVPEQGKVLYVSAEGPADE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 93 LNPRLpvwriitepLWIAKHSSEQQRRALaeeLAVQVGIRPEYLDRLPHAFSGGQRQRIAIARAlSSQPDVIVLDEPTSA 172
Cdd:pfam13481 87 LRRRL---------RAAGADLDLPARLLF---LSLVESLPLFFLDRGGPLLDADVDALEAALEE-VEDPDLVVIDPLARA 153
|
170 180 190
....*....|....*....|....*....|....
gi 15831341 173 LDISVQA-----QILNLLVTLQENHGLTYVLISH 201
Cdd:pfam13481 154 LGGDENSnsdvgRLVKALDRLARRTGATVLLVHH 187
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-202 |
8.09e-04 |
|
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: 39.27 E-value: 8.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831341 144 SGGQRQRIAIARALSSQP----DVIVLDEPTSALDISVQAQILNLLVtLQENHGLTYVLISHN 202
Cdd:cd03227 79 SGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAIL-EHLVKGAQVIVITHL 140
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-174 |
1.16e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 23 GKTTehvhAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMG---------------MLQPSHGqyiRSGSQRIMQMmfq 87
Cdd:NF033858 12 GKTV----ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkiqqgrvevlggdMADARHR---RAVCPRIAYM--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831341 88 dP--L-SSLNPRLPVwriiTEPL-WIAK---HSSeQQRRALAEELAVQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSQ 160
Cdd:NF033858 82 -PqgLgKNLYPTLSV----FENLdFFGRlfgQDA-AERRRRIDELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHD 154
|
170
....*....|....
gi 15831341 161 PDVIVLDEPTSALD 174
Cdd:NF033858 155 PDLLILDEPTTGVD 168
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
29-66 |
1.23e-03 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 40.01 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|....*...
gi 15831341 29 VHAINGIdLQIRRGETLGIVGESGCGKSTlaqlLMGML 66
Cdd:COG1157 145 VRAIDGL-LTVGRGQRIGIFAGSGVGKST----LLGMI 177
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
29-66 |
5.88e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 37.54 E-value: 5.88e-03
10 20 30
....*....|....*....|....*....|....*...
gi 15831341 29 VHAINGIdLQIRRGETLGIVGESGCGKSTlaqlLMGML 66
Cdd:cd01136 55 VRAIDGL-LTCGEGQRIGIFAGSGVGKST----LLGMI 87
|
|
|