|
Name |
Accession |
Description |
Interval |
E-value |
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-249 |
3.06e-112 |
|
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: 322.52 E-value: 3.06e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKK--KV 78
Cdd:COG1124 1 MLEVRNLSVSYGQ----GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRrrKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 RRHQIGAVFQDYTSSLHPFQTVREILFEVMCQCDgqpKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAI 158
Cdd:COG1124 77 FRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHG---LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 159 CINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKS-DNA 237
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGpKHP 233
|
250
....*....|..
gi 446513169 238 YTRELIEKQLSF 249
Cdd:COG1124 234 YTRELLAASLAF 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-244 |
1.60e-90 |
|
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: 276.40 E-value: 1.60e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYqsaHVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR- 79
Cdd:COG1123 260 LLEVRNLSKRY---PVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRs 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 ----RHQIGAVFQDYTSSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIA 155
Cdd:COG1123 337 lrelRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 156 RAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSA-LHKS 234
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEvFANP 496
|
250
....*....|
gi 446513169 235 DNAYTRELIE 244
Cdd:COG1123 497 QHPYTRALLA 506
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-225 |
1.96e-84 |
|
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: 251.27 E-value: 1.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK----- 75
Cdd:cd03257 1 LLEVKNLSVSFPT----GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 KKVRRHQIGAVFQDYTSSLHPFQTVREILFEVM-CQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAI 154
Cdd:cd03257 77 RKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLrIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 155 ARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQ 225
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-244 |
4.25e-73 |
|
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: 231.88 E-value: 4.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSY-QSAHVFKRRRTPI--VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEkPDKGCVTLNDQPMHKKKV 78
Cdd:COG4172 276 LEARDLKVWFpIKRGLFRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 R-----RHQIGAVFQDYTSSLHPFQTVREILFEVM-CQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRV 152
Cdd:COG4172 355 RalrplRRRMQVVFQDPFGSLSPRMTVGQIIAEGLrVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 153 AIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSA-L 231
Cdd:COG4172 435 AIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQvF 514
|
250
....*....|...
gi 446513169 232 HKSDNAYTRELIE 244
Cdd:COG4172 515 DAPQHPYTRALLA 527
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-244 |
3.30e-72 |
|
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: 223.01 E-value: 3.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKP---DKGCVTLNDQPMHK-- 75
Cdd:COG0444 1 LLEVRNLKVYFPT----RRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 ----KKVRRHQIGAVFQDYTSSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKA--YMDKYPNMLSGGEA 149
Cdd:COG0444 77 ekelRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPerRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 150 QRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTS 229
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
250 260
....*....|....*....|
gi 446513169 230 AL-----HksdnAYTRELIE 244
Cdd:COG0444 237 ELfenprH----PYTRALLS 252
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-243 |
1.02e-68 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 214.60 E-value: 1.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQ-SAHVFKRRRTPI--VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK--- 75
Cdd:COG4608 8 LEVRDLKKHFPvRGGLFGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlsg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 ---KKVRRH-QIgaVFQDYTSSLHPFQTVREILFEVM-CQCDGQPKDVMEvQAITLLEEVGLSKAYMDKYPNMLSGGEAQ 150
Cdd:COG4608 88 relRPLRRRmQM--VFQDPYASLNPRMTVGDIIAEPLrIHGLASKAERRE-RVAELLELVGLRPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 151 RVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSA 230
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDE 244
|
250
....*....|....*.
gi 446513169 231 LHksDNA---YTRELI 243
Cdd:COG4608 245 LY--ARPlhpYTQALL 258
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-248 |
1.04e-65 |
|
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: 205.04 E-value: 1.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVF-KRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---- 75
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 --KKVRRhQIGAVFQDYTSSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVA 153
Cdd:TIGR02769 82 qrRAFRR-DVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHK 233
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
250
....*....|....*
gi 446513169 234 SDNAYTRELIEKQLS 248
Cdd:TIGR02769 241 FKHPAGRNLQSAVLP 255
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-246 |
1.60e-63 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 199.29 E-value: 1.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQS-AHVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKK--KV 78
Cdd:COG4167 5 LEVRNLSKTFKYrTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGdyKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 RRHQIGAVFQDYTSSLHPFQTVREILFEVM---CQCDGQPKdvmEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIA 155
Cdd:COG4167 85 RCKHIRMIFQDPNTSLNPRLNIGQILEEPLrlnTDLTAEER---EERIFATLRLVGLLPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 156 RAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSA-LHKS 234
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEvFANP 241
|
250
....*....|..
gi 446513169 235 DNAYTRELIEKQ 246
Cdd:COG4167 242 QHEVTKRLIESH 253
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-227 |
1.12e-62 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 195.65 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKK---- 76
Cdd:COG1136 4 LLELRNLTKSYGTGEG----EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLsere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 --KVRRHQIGAVFQDYTssLHPFQTVRE-IlfEVMCQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVA 153
Cdd:COG1136 80 laRLRRRHIGFVFQFFN--LLPELTALEnV--ALPLLLAGVSRKERRERARELLERVGLGD-RLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYlCDQLIIFKNGKIEEQIP 227
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSDER 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-231 |
2.99e-61 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 193.36 E-value: 2.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVF-KRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---- 75
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 -KKVRRHQIGAVFQDYTSSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAI 154
Cdd:PRK10419 83 qRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446513169 155 ARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-227 |
1.70e-60 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 191.07 E-value: 1.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKkvrR 80
Cdd:COG1116 7 ALELRGVSKRFPT----GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQDYTssLHPFQTVRE-ILF--EVMcqcdGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARA 157
Cdd:COG1116 80 PDRGVVFQEPA--LLPWLTVLDnVALglELR----GVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 158 ICINPKYILFDEAISSLDmsIQT--QILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKN--GKIEEQIP 227
Cdd:COG1116 153 LANDPEVLLMDEPFGALD--ALTreRLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEID 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-222 |
4.30e-59 |
|
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: 186.16 E-value: 4.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKK----- 76
Cdd:cd03255 1 IELKNLSKTYGGGGE----KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 -KVRRHQIGAVFQDYTssLHPFQTVREilfEVM--CQCDGQPKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVA 153
Cdd:cd03255 77 aAFRRRHIGFVFQSFN--LLPDLTALE---NVElpLLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYlCDQLIIFKNGKI 222
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-227 |
6.68e-57 |
|
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: 180.75 E-value: 6.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKkkvRRH 81
Cdd:cd03293 1 LEVRNVSKTYGG----GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---PGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYtsSLHPFQTVRE-ILFEVMCQcdGQPKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVAIARAICI 160
Cdd:cd03293 74 DRGYVFQQD--ALLPWLTVLDnVALGLELQ--GVPKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 161 NPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKN--GKIEEQIP 227
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVE 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-243 |
2.21e-56 |
|
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: 180.18 E-value: 2.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVFKrrrtpivkGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK----- 75
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLD--------GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlseke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 -KKVRRhQIGAVFQDYT--SSLhpfqTVRE-ILFeVMCQCDGQPKDVMEVQAITLLEEVGLSKAYmDKYPNMLSGGEAQR 151
Cdd:COG1127 77 lYELRR-RIGMLFQGGAlfDSL----TVFEnVAF-PLREHTDLSEAEIRELVLEKLELVGLPGAA-DKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 152 VAIARAICINPKYILFDEAISSLD--MSiqTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTS 229
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDpiTS--AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
250
....*....|....
gi 446513169 230 ALHKSDNAYTRELI 243
Cdd:COG1127 228 ELLASDDPWVRQFL 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-224 |
1.44e-55 |
|
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: 176.94 E-value: 1.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRH 81
Cdd:cd03259 1 LELKGLSKTYGS--------VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYtsSLHPFQTVRE-ILF--EVMcqcdGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAI 158
Cdd:cd03259 73 NIGMVFQDY--ALFPHLTVAEnIAFglKLR----GVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 159 CINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEE 224
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-225 |
3.17e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 174.41 E-value: 3.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVFKrrrtpivkGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR- 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLK--------GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDi 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 ---RHQIGAVFQDYtsSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIAR 156
Cdd:COG1126 73 nklRRKVGMVFQQF--NLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 157 AICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQ 225
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAK-EGMTMVVVTHEMGFAREVADRVVFMDGGRIVEE 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-231 |
1.25e-53 |
|
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: 172.77 E-value: 1.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ---PMHKKK 77
Cdd:cd03258 1 MIELKNVSKVFGDTG----GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VR--RHQIGAVFQDYT--SSlhpfQTVRE-ILFEVmcQCDGQPKDVMEVQAITLLEEVGLS-KAymDKYPNMLSGGEAQR 151
Cdd:cd03258 77 LRkaRRRIGMIFQHFNllSS----RTVFEnVALPL--EIAGVPKAEIEERVLELLELVGLEdKA--DAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 152 VAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-231 |
1.96e-53 |
|
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: 180.10 E-value: 1.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPD---KGCVTLNDQPM--HK 75
Cdd:COG1123 4 LLEVRDLSVRYPG------GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLleLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 KKVRRHQIGAVFQDYTSSLHPfQTVREILFEVMcQCDGQPKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVAIA 155
Cdd:COG1123 78 EALRGRRIGMVFQDPMTQLNP-VTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 156 RAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-222 |
1.29e-52 |
|
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: 170.21 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAhvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-- 79
Cdd:COG1122 1 IELENLSFSYPGG-------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDYTSSLHpFQTVRE-ILF--EVMcqcdGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIAR 156
Cdd:COG1122 74 RRKVGLVFQNPDDQLF-APTVEEdVAFgpENL----GLPREEIRERVEEALELVGLEH-LADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 157 AICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-243 |
1.82e-52 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 172.84 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 5 KDVEKSYQ-SAHVFKRRRTpiVK---GVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ-----PMHK 75
Cdd:PRK11308 9 IDLKKHYPvKRGLFKPERL--VKaldGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllkaDPEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 KKVRRHQIGAVFQDYTSSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIA 155
Cdd:PRK11308 87 QKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 156 RAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSA----- 230
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQifnnp 246
|
250
....*....|...
gi 446513169 231 LHksdnAYTRELI 243
Cdd:PRK11308 247 RH----PYTQALL 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-244 |
4.42e-52 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 176.82 E-value: 4.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 16 VFKRRRTP--IVKGVSFECPIGATIAIIGESGSGKST----LSRMIlgiekPDKGCVTLNDQPMHKKKVR-----RHQIG 84
Cdd:PRK15134 291 ILKRTVDHnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRqllpvRHRIQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 85 AVFQDYTSSLHPFQTVREILFEvmcqcdG----QP---KDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARA 157
Cdd:PRK15134 366 VVFQDPNSSLNPRLNVLQIIEE------GlrvhQPtlsAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 158 ICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKS-DN 236
Cdd:PRK15134 440 LILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAApQQ 519
|
....*...
gi 446513169 237 AYTRELIE 244
Cdd:PRK15134 520 EYTRQLLA 527
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-226 |
6.93e-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: 171.82 E-value: 6.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR 80
Cdd:COG3842 5 ALELENVSKRYGD--------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQDYtsSLHPFQTVRE-ILFEVMCQcdGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAIC 159
Cdd:COG3842 77 RNVGMVFQDY--ALFPHLTVAEnVAFGLRMR--GVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIeEQI 226
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRI-EQV 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-241 |
1.31e-50 |
|
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: 164.98 E-value: 1.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVFKrrrtpivkGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK------ 75
Cdd:cd03261 1 IELRGLTKSFGGRTVLK--------GVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseael 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 KKVRRhQIGAVFQDYT--SSLHPFQTVREILFEvMCQCdgqPKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVA 153
Cdd:cd03261 73 YRLRR-RMGMLFQSGAlfDSLTVFENVAFPLRE-HTRL---SEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHK 233
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*...
gi 446513169 234 SDNAYTRE 241
Cdd:cd03261 227 SDDPLVRQ 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-243 |
3.68e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 167.18 E-value: 3.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KK 77
Cdd:COG1135 1 MIELENLSKTFPT----KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlseRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VR--RHQIGAVFQDYT--SSlhpfQTVRE-ILF--EVMcqcdGQPKDVMEVQAITLLEEVGLS-KAymDKYPNMLSGGEA 149
Cdd:COG1135 77 LRaaRRKIGMIFQHFNllSS----RTVAEnVALplEIA----GVPKAEIRKRVAELLELVGLSdKA--DAYPSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 150 QRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTS 229
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
250
....*....|....*
gi 446513169 230 AL-HKSDNAYTRELI 243
Cdd:COG1135 227 DVfANPQSELTRRFL 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-231 |
9.55e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.93 E-value: 9.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYqsahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK--KKVR 79
Cdd:COG1131 1 IEVRGLTKRY--------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARdpAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHqIGAVFQDytSSLHPFQTVREILfEVMCQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAIC 159
Cdd:COG1131 73 RR-IGYVPQE--PALYPDLTVRENL-RFFARLYGLPRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-222 |
4.46e-49 |
|
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: 161.75 E-value: 4.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYqsahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KK 77
Cdd:COG1120 1 MLEAENLSVGY--------GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsrRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRRhQIGAVFQDYTSSLhPFqTVREI----------LFevmcqcdGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGG 147
Cdd:COG1120 73 LAR-RIAYVPQEPPAPF-GL-TVRELvalgryphlgLF-------GRPSAEDREAVEEALERTGLE-HLADRPVDELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 148 EAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDI-QAATYlCDQLIIFKNGKI 222
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLnLAARY-ADRLVLLKDGRI 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-243 |
6.25e-49 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 161.88 E-value: 6.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQ-SAHVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH--KKK 77
Cdd:PRK15112 4 LLEVRNLSKTFRyRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRRHQIGAVFQDYTSSLHPFQTVREIL-FEVMCQCDGQPKDvMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIAR 156
Cdd:PRK15112 84 YRSQRIRMIFQDPSTSLNPRQRISQILdFPLRLNTDLEPEQ-REKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 157 AICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPT-----SAL 231
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTadvlaSPL 242
|
250
....*....|..
gi 446513169 232 HKsdnaYTRELI 243
Cdd:PRK15112 243 HE----LTKRLI 250
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-222 |
7.03e-49 |
|
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: 160.00 E-value: 7.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVFKrrrtpivkGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM--HKKKVR 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLK--------GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 --RHQIGAVFQDYTssLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLS-KAymDKYPNMLSGGEAQRVAIAR 156
Cdd:cd03262 73 elRQKVGMVFQQFN--LFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAdKA--DAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 157 AICINPKYILFDEAISSLDMSIQTQILDLLIHLRETrQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-228 |
2.22e-48 |
|
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: 159.43 E-value: 2.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAhvfkrrrtPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRH 81
Cdd:cd03296 3 IEVRNVSKRFGDF--------VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYtsSLHPFQTVRE-ILF--EVMCQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAI 158
Cdd:cd03296 75 NVGFVFQHY--ALFRHMTVFDnVAFglRVKPRSERPPEAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 159 CINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIeEQIPT 228
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI-EQVGT 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-231 |
1.10e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.08 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYqsahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH-KKKVRR 80
Cdd:COG1118 3 IEVRNISKRF--------GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQDYtsSLHPFQTVRE-ILF--EVMcqcdGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARA 157
Cdd:COG1118 75 RRVGFVFQHY--ALFPHMTVAEnIAFglRVR----PPSKAEIRARVEELLELVQLEG-LADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 158 ICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-221 |
2.45e-47 |
|
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: 156.09 E-value: 2.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 3 KIKDVEKSYQsahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--R 80
Cdd:cd03225 1 ELKNLSFSYP------DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQDytsslhPFQ-----TVREilfEVM--CQCDGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVA 153
Cdd:cd03225 75 RKVGLVFQN------PDDqffgpTVEE---EVAfgLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-222 |
2.75e-46 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 154.44 E-value: 2.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KK 77
Cdd:COG3638 2 MLELRNLSKRYPG-------GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrgRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VR--RHQIGAVFQDYtsSLHPFQTVREilfEVMCQCDGQ------------PKDVMevQAITLLEEVGLS-KAYmdKYPN 142
Cdd:COG3638 75 LRrlRRRIGMIFQQF--NLVPRLSVLT---NVLAGRLGRtstwrsllglfpPEDRE--RALEALERVGLAdKAY--QRAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 143 MLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-221 |
3.24e-46 |
|
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: 151.96 E-value: 3.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKK----K 77
Cdd:cd03229 1 LELKNVSKRYGQKTV--------LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRRHQIGAVFQDYTssLHPFQTVREIlfevmcqcdgqpkdvmevqaITLLeevglskaymdkypnmLSGGEAQRVAIARA 157
Cdd:cd03229 73 PLRRRIGMVFQDFA--LFPHLTVLEN--------------------IALG----------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 158 ICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-244 |
3.87e-46 |
|
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: 154.72 E-value: 3.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 3 KIKDVEKSYQSAHVFKRR-RTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK------ 75
Cdd:cd03294 17 AFKLLAKGKSKEEILKKTgQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 KKVRRHQIGAVFQDYtsSLHPFQTVRE-ILFEVMCQcdGQPKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVAI 154
Cdd:cd03294 97 RELRRKKISMVFQSF--ALLPHRTVLEnVAFGLEVQ--GVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 155 ARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIeEQI--PTSALH 232
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL-VQVgtPEEILT 250
|
250
....*....|..
gi 446513169 233 KSDNAYTRELIE 244
Cdd:cd03294 251 NPANDYVREFFR 262
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-244 |
3.05e-45 |
|
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: 158.69 E-value: 3.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 20 RRTPIVKGVSFECPIGATIAIIGESGSGKS--TLSRMIL---GIEKPDkGCVTLNDQPMHKK------KVRRHQIGAVFQ 88
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtALSILRLlpdPAAHPS-GSILFDGQDLLGLserelrRIRGNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 89 DYTSSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGL--SKAYMDKYPNMLSGGEAQRVAIARAICINPKYIL 166
Cdd:COG4172 100 EPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIpdPERRLDAYPHQLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 167 FDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL-----HksdnAYTRE 241
Cdd:COG4172 180 ADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELfaapqH----PYTRK 255
|
...
gi 446513169 242 LIE 244
Cdd:COG4172 256 LLA 258
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-226 |
2.00e-44 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.53 E-value: 2.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR 80
Cdd:COG3839 3 SLELENVSKSYGG--------VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQDYtsSLHPFQTVRE-ILF--EVMcqcdGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARA 157
Cdd:COG3839 75 RNIAMVFQSY--ALYPHMTVYEnIAFplKLR----KVPKAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 158 ICINPKYILFDEAISSLD----MSIQTQILDLLihlretRQLSYIFI--THD-IQAATyLCDQLIIFKNGKIeEQI 226
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrVEMRAEIKRLH------RRLGTTTIyvTHDqVEAMT-LADRIAVMNDGRI-QQV 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-231 |
2.55e-44 |
|
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: 149.24 E-value: 2.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR- 79
Cdd:COG4555 1 MIEVENLSKKYGK--------VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREa 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytSSLHPFQTVREILfEVMCQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAIC 159
Cdd:COG4555 73 RRQIGVLPDE--RGLYDRLTVRENI-RYFAELYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-231 |
3.46e-44 |
|
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: 152.18 E-value: 3.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 28 VSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ-----------PMHKkkvRRhqIGAVFQDytSSLHP 96
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflPPHR---RR--IGYVFQE--ARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 97 FQTVREILFEVMCQCDGQPKDVMEVQAITLLeevGLSkAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDM 176
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIG-HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 177 SIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
6.69e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.51 E-value: 6.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHvfkrrrtPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KK 77
Cdd:COG2884 1 MIRFENVSKRYPGGR-------EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 V---RRhQIGAVFQDYtsSLHPFQTVRE-ILF--EVMcqcdGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQR 151
Cdd:COG2884 74 IpylRR-RIGVVFQDF--RLLPDRTVYEnVALplRVT----GKSRKEIRRRVREVLDLVGLSD-KAKALPHELSGGEQQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 152 VAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRE---TrqlsyIFI-THDIQaatyLCDQL----IIFKNGKIE 223
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrgtT-----VLIaTHDLE----LVDRMpkrvLELEDGRLV 216
|
.
gi 446513169 224 E 224
Cdd:COG2884 217 R 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-228 |
8.52e-44 |
|
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: 147.77 E-value: 8.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRH 81
Cdd:cd03300 1 IELENVSKFYGGFVA--------LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYtsSLHPFQTVRE-ILFEVMCQcdGQPKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVAIARAICI 160
Cdd:cd03300 73 PVNTVFQNY--ALFPHLTVFEnIAFGLRLK--KLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 161 NPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIeEQIPT 228
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI-QQIGT 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-230 |
9.36e-44 |
|
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: 147.58 E-value: 9.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAhvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK----- 75
Cdd:COG4181 8 IIELRGLTKTVGTG----AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 -KKVRRHQIGAVFQDYTssLHPFQTVREilfEVM--CQCDGQPkDVMEvQAITLLEEVGLSkAYMDKYPNMLSGGEAQRV 152
Cdd:COG4181 84 rARLRARHVGFVFQSFQ--LLPTLTALE---NVMlpLELAGRR-DARA-RARALLERVGLG-HRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 153 AIARAICINPKyILF-DEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATyLCDQLIIFKNGKIEEQIPTSA 230
Cdd:COG4181 156 ALARAFATEPA-ILFaDEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-225 |
1.27e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 147.47 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLND------QPMHK 75
Cdd:COG4161 3 IQLKNINCFYGS--------HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 KKVR--RHQIGAVFQDYtsSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVA 153
Cdd:COG4161 75 KAIRllRQKVGMVFQQY--NLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTD-KADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETrQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQ 225
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-229 |
1.74e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 149.95 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KK 77
Cdd:PRK11153 1 MIELKNISKVFPQ----GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlseKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VR--RHQIGAVFQDYT--SSLHPFQTVR---EIlfevmcqcDGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQ 150
Cdd:PRK11153 77 LRkaRRQIGMIFQHFNllSSRTVFDNVAlplEL--------AGTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 151 RVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTS 229
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVS 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
2.57e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.77 E-value: 2.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYqsahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKkvrR 80
Cdd:COG1121 6 AIELENLTVSY--------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQDYTSSLH-PFqTVREIlfeVMCQCDGQ--------PKDVMEVQAItlLEEVGLSkAYMDKYPNMLSGGEAQR 151
Cdd:COG1121 75 RRIGYVPQRAEVDWDfPI-TVRDV---VLMGRYGRrglfrrpsRADREAVDEA--LERVGLE-DLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 152 VAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKIeeqiptsAL 231
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRGLV-------AH 219
|
250
....*....|....
gi 446513169 232 HKSDNAYTRELIEK 245
Cdd:COG1121 220 GPPEEVLTPENLSR 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-170 |
2.59e-43 |
|
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: 143.56 E-value: 2.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKK--KVRRHQIGAVFQDytSSLHPFQTVRE 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRKEIGYVFQD--PQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 103 ILFEVMCqCDGQPKDVMEVQAITLLEEVGLS---KAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEA 170
Cdd:pfam00005 79 NLRLGLL-LKGLSKREKDARAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-222 |
4.17e-43 |
|
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: 146.17 E-value: 4.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAhvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KKV 78
Cdd:cd03256 1 IEVENLSKTYPNG-------KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 R--RHQIGAVFQDYtsSLHPFQTVREilfEVMCQCDGQ------------PKDVmeVQAITLLEEVGLS-KAYmdKYPNM 143
Cdd:cd03256 74 RqlRRQIGMIFQQF--NLIERLSVLE---NVLSGRLGRrstwrslfglfpKEEK--QRALAALERVGLLdKAY--QRADQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 144 LSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-225 |
1.03e-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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 145.65 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ----PMHKKK 77
Cdd:TIGR04520 1 IEVENVSFSYPESEK------PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLdtldEENLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRRHqIGAVFQDytsslhP---F--QTVRE-ILF--EVMcqcdGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEA 149
Cdd:TIGR04520 75 IRKK-VGMVFQN------PdnqFvgATVEDdVAFglENL----GVPREEMRKRVDEALKLVGMED-FRDREPHLLSGGQK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 150 QRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATyLCDQLIIFKNGKIEEQ 225
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAE 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-247 |
2.91e-42 |
|
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: 152.30 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQsahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK--KKVR 79
Cdd:COG2274 474 IELENVSFRYP------GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQidPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytssLHPFQ-TVRE-ILFevmcqcdGQPkDVMEVQAITLLEEVGLSkAYMDKYPN-----------MLSG 146
Cdd:COG2274 548 RRQIGVVLQD----VFLFSgTIREnITL-------GDP-DATDEEIIEAARLAGLH-DFIEALPMgydtvvgeggsNLSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 147 GEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLsyIFITHDIQAATyLCDQLIIFKNGKIEEQI 226
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
250 260
....*....|....*....|.
gi 446513169 227 PTSALHKSDNAYtRELIEKQL 247
Cdd:COG2274 692 THEELLARKGLY-AELVQQQL 711
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-222 |
6.63e-42 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 141.03 E-value: 6.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH--KKKVRRHQIGAVFQdytssl 94
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAslSPKELARKIAYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 95 hpfqtvreilfevmcqcdgqpkdvmevqaitLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSL 174
Cdd:cd03214 81 -------------------------------ALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446513169 175 DMSIQTQILDLLIHLRETRQLSYIFITHDI-QAATYlCDQLIIFKNGKI 222
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLnLAARY-ADRVILLKDGRI 176
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-225 |
1.43e-41 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 142.05 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHvfkrrrtPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKK---KV 78
Cdd:cd03295 1 IEFENVTKRYGGGK-------KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 RRHqIGAVFQDYtsSLHPFQTVREILFEVMcQCDGQPKDVMEVQAITLLEEVGL-SKAYMDKYPNMLSGGEAQRVAIARA 157
Cdd:cd03295 74 RRK-IGYVIQQI--GLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 158 ICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQ 225
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
17-222 |
2.87e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.34 E-value: 2.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--RHQIGAVFQDytssl 94
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewRRQVAYVPQE----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 95 hPF---QTVREILFEVMcQCDGQPKDVMEVQAitLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAI 171
Cdd:COG4619 83 -PAlwgGTVRDNLPFPF-QLRERKFDRERALE--LLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446513169 172 SSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-243 |
4.63e-41 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 143.31 E-value: 4.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQP---MHKKKVR--RHQIGAVFQDYTSSLHPFQT 99
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllgMKDDEWRavRSDIQMIFQDPLASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 100 VREILFEVMCQCdgQPK----DVME-VQAITLleEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSL 174
Cdd:PRK15079 117 IGEIIAEPLRTY--HPKlsrqEVKDrVKAMML--KVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 175 DMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL-HKSDNAYTRELI 243
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVyHNPLHPYTKALM 262
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-221 |
6.11e-41 |
|
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: 138.28 E-value: 6.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK--KKVR 79
Cdd:cd03228 1 IEFKNVSFSYPG------RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDldLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytsslhPF---QTVREilfevmcqcdgqpkdvmevqaitlleevglskaymdkypNMLSGGEAQRVAIAR 156
Cdd:cd03228 75 RKNIAYVPQD------PFlfsGTIRE---------------------------------------NILSGGQRQRIAIAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 157 AICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLsyIFITHDIQAATyLCDQLIIFKNGK 221
Cdd:cd03228 110 ALLRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-223 |
9.67e-41 |
|
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: 139.35 E-value: 9.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 28 VSFECPiGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH--KKKV----RRHQIGAVFQDYTssLHPFQTVR 101
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsRKKInlppQQRKIGLVFQQYA--LFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 102 EILFEVMCQCDgqpKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQ 181
Cdd:cd03297 94 ENLAFGLKRKR---NREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446513169 182 ILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIE 223
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-248 |
2.44e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.11 E-value: 2.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLND------QPMH 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTV--------LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtaRSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 75 KKK--VR--RHQIGAVFQDYtsSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQ 150
Cdd:PRK11264 75 QQKglIRqlRQHVGFVFQNF--NLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLA-GKETSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 151 RVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSA 230
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
250
....*....|....*....
gi 446513169 231 LHKS-DNAYTRELIEKQLS 248
Cdd:PRK11264 231 LFADpQQPRTRQFLEKFLL 249
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-222 |
2.50e-40 |
|
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: 2.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYqsahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-R 80
Cdd:cd03230 1 IEVRNLSKRY--------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQDytSSLHPFQTVREILfevmcqcdgqpkdvmevqaitlleevglskaymdkypnMLSGGEAQRVAIARAICI 160
Cdd:cd03230 73 RRIGYLPEE--PSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446513169 161 NPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
17-222 |
5.28e-40 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 137.28 E-value: 5.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKkvrRHQIGAVFQ----DYTS 92
Cdd:cd03235 7 VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---RKRIGYVPQrrsiDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 93 SLhpfqTVREI----LFEVMCQCDGQPKDVMEVqAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAICINPKYILFD 168
Cdd:cd03235 84 PI----SVRDVvlmgLYGHKGLFRRLSKADKAK-VDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446513169 169 EAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-226 |
3.22e-39 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 135.07 E-value: 3.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRH 81
Cdd:cd03301 1 VELENVTKRFGNVTA--------LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYtsSLHPFQTVRE-ILFEVmcQCDGQPKD-----VMEVQAITLLEEvglskaYMDKYPNMLSGGEAQRVAIA 155
Cdd:cd03301 73 DIAMVFQNY--ALYPHMTVYDnIAFGL--KLRKVPKDeiderVREVAELLQIEH------LLDRKPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 156 RAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIeEQI 226
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI-QQI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-231 |
5.08e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 136.25 E-value: 5.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH-------------KKKVR--RHQIGAVFQ 88
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRllRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 89 DYtsSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFD 168
Cdd:PRK10619 100 HF--NLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446513169 169 EAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-236 |
5.20e-39 |
|
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: 138.71 E-value: 5.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 28 VSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ-----------PMHKKKvrrhqIGAVFQDytSSLHP 96
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflPPEKRR-----IGYVFQE--ARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 97 FQTVREILFEVMCQCDGQPKDVMEVQAITLLeevGLSKaYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDM 176
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISFERVIELL---GIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 177 SIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKSDN 236
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-236 |
8.49e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.50 E-value: 8.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHV-FkrrrtpivkgvSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR 79
Cdd:COG3840 1 MLRLDDLTYRYGDFPLrF-----------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDYTssLHPFQTVRE-ILFEVmcQCDGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAI 158
Cdd:COG3840 70 ERPVSMLFQENN--LFPHLTVAQnIGLGL--RPGLKLTAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 159 CINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKSDN 236
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-224 |
1.40e-38 |
|
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: 134.39 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvFKrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRH 81
Cdd:cd03299 1 LKVENLSKDWKE---FK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYtsSLHPFQTVRE-ILFEVMCQCDGQPKDVMEVQAITllEEVGLSKaYMDKYPNMLSGGEAQRVAIARAICI 160
Cdd:cd03299 72 DISYVPQNY--ALFPHMTVYKnIAYGLKKRKVDKKEIERKVLEIA--EMLGIDH-LLNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 161 NPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEE 224
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-225 |
4.04e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.22 E-value: 4.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLND------QPMHK 75
Cdd:PRK11124 3 IQLNGINCFYGA--------HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 KKVR--RHQIGAVFQDYtsSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVA 153
Cdd:PRK11124 75 KAIRelRRNVGMVFQQY--NLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETrQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQ 225
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-231 |
6.84e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 132.52 E-value: 6.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR 80
Cdd:PRK09493 1 MIEFKNVSKHFGP--------TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQI----GAVFQDYtsSLHPFQTVREilfEVM---CQCDGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVA 153
Cdd:PRK09493 73 RLIrqeaGMVFQQF--YLFPHLTALE---NVMfgpLRVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
1.94e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.42 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR- 79
Cdd:PRK13632 7 MIKVENVSFSYPNSE------NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 -RHQIGAVFQDYTSSLHPFQTVREILFEVMCQCdgQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAI 158
Cdd:PRK13632 81 iRKKIGIIFQNPDNQFIGATVEDDIAFGLENKK--VPPKKMKDIIDDLAKKVGMED-YLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 159 CINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATyLCDQLIIFKNGKI 222
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
3.36e-37 |
|
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: 137.20 E-value: 3.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH--KKKVR 79
Cdd:COG4988 337 IELEDVSFSYPG-------GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdlDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQdytsslHP--FQ-TVRE-ILFevmcqcdGQPkDVMEVQAITLLEEVGLSkAYMDKYPN-----------ML 144
Cdd:COG4988 410 RRQIAWVPQ------NPylFAgTIREnLRL-------GRP-DASDEELEAALEAAGLD-EFVAALPDgldtplgeggrGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 145 SGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLsyIFITHDIQAATyLCDQLIIFKNGKIEE 224
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV--ILITHRLALLA-QADRILVLDDGRIVE 551
|
.
gi 446513169 225 Q 225
Cdd:COG4988 552 Q 552
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-222 |
5.28e-37 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 129.55 E-value: 5.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKsyqsahVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM--HKKKVR 79
Cdd:cd03263 1 LQIRNLTK------TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHqIGAVFQDytSSLHPFQTVREILfEVMCQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAIC 159
Cdd:cd03263 75 QS-LGYCPQF--DALFDELTVREHL-RFYARLKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLRETRqlSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-243 |
7.02e-37 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 136.91 E-value: 7.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 20 RRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ-----PMHKKKVRRHQIGAVFQDYTSSL 94
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlSPGKLQALRRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 95 HPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSL 174
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 175 DMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKS-DNAYTRELI 243
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENpQHPYTRKLM 564
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-221 |
8.09e-37 |
|
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: 127.36 E-value: 8.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 3 KIKDVEKSYQSAHVFKrrrtpivkGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--R 80
Cdd:cd00267 1 EIENLSFRYGGRTALD--------NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQdytsslhpfqtvreilfevmcqcdgqpkdvmevqaitlleevglskaymdkypnmLSGGEAQRVAIARAICI 160
Cdd:cd00267 73 RRIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 161 NPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
8.24e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 130.64 E-value: 8.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVFKrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM---HKKK 77
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFT------LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRRHqIGAVFQDYTSslhpfQTVREIL-FEVMCQCDGQ--PKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAI 154
Cdd:PRK13648 81 LRKH-IGIVFQNPDN-----QFVGSIVkYDVAFGLENHavPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 155 ARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYlCDQLIIFKNGKIEEQ 225
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKE 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-243 |
9.24e-37 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 135.60 E-value: 9.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKS--TLSRMILGIEKP---DKGCVTLNDQPMHK------KKVRRHQIGAVFQDYT 91
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtALSILRLLPSPPvvyPSGDIRFHGESLLHaseqtlRGVRGNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 92 SSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKA--YMDKYPNMLSGGEAQRVAIARAICINPKYILFDE 169
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAakRLTDYPHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 170 AISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL-HKSDNAYTRELI 243
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLfSAPTHPYTQKLL 257
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-228 |
2.18e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.99 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRH 81
Cdd:PRK09452 15 VELRGISKSFDG--------KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYtsSLHPFQTVRE-ILFEVMCQcdGQPKD-----VMEVQAITLLEEVGlskaymDKYPNMLSGGEAQRVAIA 155
Cdd:PRK09452 87 HVNTVFQSY--ALFPHMTVFEnVAFGLRMQ--KTPAAeitprVMEALRMVQLEEFA------QRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 156 RAICINPKYILFDEAISSLDMSIQTQILDLLIHLRetRQL--SYIFITHDIQAATYLCDQLIIFKNGKIeEQIPT 228
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQ--RKLgiTFVFVTHDQEEALTMSDRIVVMRDGRI-EQDGT 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-246 |
1.14e-35 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 126.58 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KKVRRHqIGAVFQDytsslhpfqT 99
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtlDSLRRA-IGVVPQD---------T 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 100 V---REILFEVmcqCDGQPkDVMEVQAITLLEEVGLSKAYM---DKYPN-------MLSGGEAQRVAIARAICINPKYIL 166
Cdd:cd03253 85 VlfnDTIGYNI---RYGRP-DATDEEVIEAAKAAQIHDKIMrfpDGYDTivgerglKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 167 FDEAISSLDMSIQTQILDLLIHLRETRQLsyIFITHDIQAATYlCDQLIIFKNGKIEEQIPTSALHKSDNAYtRELIEKQ 246
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTT--IVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGGLY-AEMWKAQ 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-231 |
1.93e-35 |
|
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: 125.76 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMI-----LGIEKPDKGCVTLNDQPMHKK 76
Cdd:cd03260 1 IELRDLNVYYGDKHA--------LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 KVR----RHQIGAVFQDYTsslhPFQ-TVRE-ILFEVMCQcDGQPKDVMEVQAITLLEEVGLSKAYMDK-YPNMLSGGEA 149
Cdd:cd03260 73 DVDvlelRRRVGMVFQKPN----PFPgSIYDnVAYGLRLH-GIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 150 QRVAIARAICINPKYILFDEAISSLDmSIQTQILDLLIH-LRetRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPT 228
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALD-PISTAKIEELIAeLK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
...
gi 446513169 229 SAL 231
Cdd:cd03260 225 EQI 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-220 |
2.68e-35 |
|
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: 125.66 E-value: 2.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRHqigAVFQDYtsSLHPFQTVRE-I 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNY--SLLPWLTVREnI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 104 LFEVMCQCDGQPKDvmEVQAIT--LLEEVGLSKAyMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQ 181
Cdd:TIGR01184 76 ALAVDRVLPDLSKS--ERRAIVeeHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 446513169 182 ILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNG 220
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-222 |
1.38e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 123.14 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 4 IKDVEKSYqsahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKvRRHQI 83
Cdd:cd03226 2 IENISFSY-------KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 84 GAVFQDYTSSLHpFQTVREilfEVMCQCDGQPKDVMEVQaiTLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAICINPK 163
Cdd:cd03226 74 GYVMQDVDYQLF-TDSVRE---ELLLGLKELDAGNEQAE--TVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 164 YILFDEAISSLDMSIQTQILDLLIHLRETRQLSyIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAV-IVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-228 |
3.02e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 125.97 E-value: 3.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQsahvfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRH 81
Cdd:PRK10851 3 IEIANIKKSFG--------RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYTSSLHpfQTVRE-ILF--EVMCQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAI 158
Cdd:PRK10851 75 KVGFVFQHYALFRH--MTVFDnIAFglTVLPRRERPNAAAIKAKVTQLLEMVQLAH-LADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 159 CINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIeEQIPT 228
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI-EQAGT 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-225 |
3.05e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.36 E-value: 3.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAhvfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-- 79
Cdd:PRK13635 6 IRVEHISFRYPDA------ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytsslhP---F--QTVRE-ILFEVMCQcdGQPKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVA 153
Cdd:PRK13635 80 RRQVGMVFQN------PdnqFvgATVQDdVAFGLENI--GVPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYlCDQLIIFKNGKIEEQ 225
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-227 |
3.43e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 123.43 E-value: 3.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR 80
Cdd:COG4525 3 MLTVRHVSVRYPG----GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 hqiGAVFQDYTssLHPFQTVRE-ILFEVmcQCDGQPKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVAIARAIC 159
Cdd:COG4525 79 ---GVVFQKDA--LLPWLNVLDnVAFGL--RLRGVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 160 INPKYILFDEAISSLDM----SIQTQILDLlihLRETRQlSYIFITHDIQAATYLCDQLIIFKN--GKIEEQIP 227
Cdd:COG4525 151 ADPRFLLMDEPFGALDAltreQMQELLLDV---WQRTGK-GVFLITHSVEEALFLATRLVVMSPgpGRIVERLE 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-244 |
5.09e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 128.35 E-value: 5.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAhvfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK--KKVR 79
Cdd:COG4987 334 LELEDVSFRYPGA------GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDldEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDYtsslHPF-QTVRE-ILFevmcqcdGQPkDVMEVQAITLLEEVGLSKaYMDKYPN-----------MLSG 146
Cdd:COG4987 408 RRRIAVVPQRP----HLFdTTLREnLRL-------ARP-DATDEELWAALERVGLGD-WLAALPDgldtwlgeggrRLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 147 GEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLsyIFITHDIQAATyLCDQLIIFKNGKIEEQI 226
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLE-RMDRILVLEDGRIVEQG 551
|
250
....*....|....*...
gi 446513169 227 PTSALHKSDNAYtRELIE 244
Cdd:COG4987 552 THEELLAQNGRY-RQLYQ 568
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-225 |
1.02e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 121.42 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK------KKVRRHQIGAVFQDY--TSSLH 95
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearAKLRAKHVGFVFQSFmlIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 96 PFQTVrEILFEVMCQCDGQPKDvmevQAITLLEEVGLSKAyMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLD 175
Cdd:PRK10584 105 ALENV-ELPALLRGESSRQSRN----GAKALLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446513169 176 MSIQTQILDLLIHLRETRQLSYIFITHDIQAATYlCDQLIIFKNGKIEEQ 225
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-225 |
2.49e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.83 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPD---KGCVTLNDQPMHKKKVR--RHQIGAVFQDYT 91
Cdd:PRK13640 15 YPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWdiREKVGIVFQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 92 SSLHPFQTVREILFEVmcQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAI 171
Cdd:PRK13640 95 NQFVGATVGDDVAFGL--ENRAVPRPEMIKIVRDVLADVGMLD-YIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446513169 172 SSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATyLCDQLIIFKNGKIEEQ 225
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQ 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
13-243 |
3.44e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 122.54 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 13 SAHvFKRRRTPI--VKGVSFECPIGATIAIIGESGSGKSTLSRMILG-IEKPDK---GCVTLNDQPMHK--KKVRRHQIG 84
Cdd:PRK11022 10 SVH-FGDESAPFraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDYPGRvmaEKLEFNGQDLQRisEKERRNLVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 85 A----VFQDYTSSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLS--KAYMDKYPNMLSGGEAQRVAIARAI 158
Cdd:PRK11022 89 AevamIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 159 CINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKSD-NA 237
Cdd:PRK11022 169 ACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPrHP 248
|
....*.
gi 446513169 238 YTRELI 243
Cdd:PRK11022 249 YTQALL 254
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-248 |
4.46e-33 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 120.57 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPD----KGCVTLNDQPMHKKKVRRHQIGAVFQDYTSSLHPFQ 98
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALRGRKIATIMQNPRSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 TVREILFEVmCQCDGQPKDvmEVQAITLLEEVGLS--KAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDM 176
Cdd:PRK10418 97 TMHTHARET-CLALGKPAD--DATLTAALEAVGLEnaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446513169 177 SIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL-HKSDNAYTRELIEKQLS 248
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLfNAPKHAVTRSLVSAHLA 246
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-225 |
6.72e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 125.28 E-value: 6.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHvfkrrrtPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH--KKKVR 79
Cdd:COG1132 340 IEFENVSFSYPGDR-------PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdlTLESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytSSLhpFQ-TVRE-ILFevmcqcdGQPK----DVME----VQA---I--------TLLEEVGlskaymd 138
Cdd:COG1132 413 RRQIGVVPQD--TFL--FSgTIREnIRY-------GRPDatdeEVEEaakaAQAhefIealpdgydTVVGERG------- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 139 kypNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLsyIFITHD---IQAAtylcDQLI 215
Cdd:COG1132 475 ---VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTT--IVIAHRlstIRNA----DRIL 545
|
250
....*....|
gi 446513169 216 IFKNGKIEEQ 225
Cdd:COG1132 546 VLDDGRIVEQ 555
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-248 |
8.78e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.51 E-value: 8.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVFKRRRtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM--HKK--- 76
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRA---LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItaGKKnkk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 -KVRRHQIGAVFQDYTSSLhpF-QTV-REILFEVMCQcdGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVA 153
Cdd:PRK13634 80 lKPLRKKVGIVFQFPEHQL--FeETVeKDICFGPMNF--GVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQ-IPTSALH 232
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQgTPREIFA 235
|
250
....*....|....*.
gi 446513169 233 KSDnaytrELIEKQLS 248
Cdd:PRK13634 236 DPD-----ELEAIGLD 246
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-203 |
1.75e-32 |
|
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: 117.89 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAhvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQP---MHKKKV 78
Cdd:cd03292 1 IEFINVTKTYPNG-------TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 ---RRHqIGAVFQDytSSLHPFQTVRE-ILFEVmcQCDGQPKDVMEVQAITLLEEVGLSKAYmDKYPNMLSGGEAQRVAI 154
Cdd:cd03292 74 pylRRK-IGVVFQD--FRLLPDRNVYEnVAFAL--EVTGVPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446513169 155 ARAICINPKYILFDEAISSLDMSIQTQILDLL--IHLRETrqlSYIFITHD 203
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLkkINKAGT---TVVVATHA 195
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
39-249 |
2.02e-32 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 120.78 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 39 AIIGESGSGKSTLSRMILGIEKpDKGCVT-----LNDQ------PMHKKKVRRHQIGAVFQDYTSSLHPFQTVREILFEV 107
Cdd:COG4170 37 GLVGESGSGKSLIAKAICGITK-DNWHVTadrfrWNGIdllklsPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 108 McqcdgqPKDVMEV-----------QAITLLEEVGL--SKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSL 174
Cdd:COG4170 116 I------PSWTFKGkwwqrfkwrkkRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAM 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 175 DMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGK-IE----EQIPTSALHksdnAYTRELIEKQLSF 249
Cdd:COG4170 190 ESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQtVEsgptEQILKSPHH----PYTKALLRSMPDF 265
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-246 |
2.85e-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: 118.03 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-- 79
Cdd:cd03249 1 IEFKNVSFRYPS-----RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytsslhP--FQ-TVRE-ILFevmcqCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNM-------LSGGE 148
Cdd:cd03249 76 RSQIGLVSQE------PvlFDgTIAEnIRY-----GKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLvgergsqLSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 149 AQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRqlSYIFITH---DIQAAtylcDQLIIFKNGKIEEQ 225
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHrlsTIRNA----DLIAVLQNGQVVEQ 218
|
250 260
....*....|....*....|.
gi 446513169 226 IPTSALHKSDNAYtRELIEKQ 246
Cdd:cd03249 219 GTHDELMAQKGVY-AKLVKAQ 238
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-222 |
3.44e-32 |
|
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: 115.78 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 21 RTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK--KKVRRHQIGAVFQDytsslhpfq 98
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwdPNELGDHVGYLPQD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 tvrEILFevmcqcDGqpkdvmevqaiTLLEevglskaymdkypNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSI 178
Cdd:cd03246 85 ---DELF------SG-----------SIAE-------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446513169 179 QTQILDLLIHLREtRQLSYIFITHDIQAATyLCDQLIIFKNGKI 222
Cdd:cd03246 132 ERALNQAIAALKA-AGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-224 |
1.92e-31 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 117.90 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPD---KGCVTLNDQ-----PMHK-KKVRRHQIGAVFQDYTSSLH 95
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGReilnlPEKElNKLRAEQISMIFQDPMTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 96 PFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKAY--MDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISS 173
Cdd:PRK09473 112 PYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446513169 174 LDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEE 224
Cdd:PRK09473 192 LDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-240 |
2.80e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 118.98 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK------KKVRRHQIGAVFQDYtsSLHPFQ 98
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelREVRRKKIAMVFQSF--ALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 TVREILFEVMcQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSI 178
Cdd:PRK10070 122 TVLDNTAFGM-ELAGINAEERREKALDALRQVGLEN-YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446513169 179 QTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGK-IEEQIPTSALHKSDNAYTR 240
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvVQVGTPDEILNNPANDYVR 262
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-222 |
5.85e-31 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 119.52 E-value: 5.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKG--CVTLNDQ------- 71
Cdd:TIGR03269 279 IIKVRNVSKRYIS---VDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEwvdmtkp 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 72 -PMHKKKVRRHqIGAVFQDYTssLHPFQTVREILFEVMCQcdGQPKDVMEVQAITLLEEVGLSKAY----MDKYPNMLSG 146
Cdd:TIGR03269 356 gPDGRGRAKRY-IGILHQEYD--LYPHRTVLDNLTEAIGL--ELPDELARMKAVITLKMVGFDEEKaeeiLDKYPDELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 147 GEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-223 |
1.12e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.83 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKV-- 78
Cdd:PRK13650 4 IIEVKNLTFKYKE-----DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 RRHQIGAVFQDYTSSLHPFQTVREILFEVMCQcdGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAI 158
Cdd:PRK13650 79 IRHKIGMVFQNPDNQFVGATVEDDVAFGLENK--GIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 159 CINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATyLCDQLIIFKNGKIE 223
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVE 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-214 |
1.15e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 113.76 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 9 KSYQSAHVfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH------KKKVRRHQ 82
Cdd:PRK11629 13 KRYQEGSV----QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaaKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 83 IGAVFQdYTSSLHPFQTVREILFEVMCqcDGQPKDVMEVQAITLLEEVGLSKAYMDKyPNMLSGGEAQRVAIARAICINP 162
Cdd:PRK11629 89 LGFIYQ-FHHLLPDFTALENVAMPLLI--GKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446513169 163 KYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQL 214
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-228 |
1.71e-30 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 116.10 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR 80
Cdd:PRK11650 3 GLKLQAVRKSYDG-------KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQDYtsSLHPFQTVREILfEVMCQCDGQPKD-----VMEVQAITLLEEvglskaYMDKYPNMLSGGEAQRVAIA 155
Cdd:PRK11650 76 RDIAMVFQNY--ALYPHMSVRENM-AYGLKIRGMPKAeieerVAEAARILELEP------LLDRKPRELSGGQRQRVAMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 156 RAICINPKYILFDEAISSLDMSiqtqildLLIHLR-ETRQL------SYIFITHD-IQAATyLCDQLIIFKNGKIeEQIP 227
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAK-------LRVQMRlEIQRLhrrlktTSLYVTHDqVEAMT-LADRVVVMNGGVA-EQIG 217
|
.
gi 446513169 228 T 228
Cdd:PRK11650 218 T 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-222 |
1.75e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.71 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK-KKVRRHQIGAVFQDYTSSLH 95
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAVLPQHSSLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 96 PFqTVREIlfeV----MCQCDGQPKDVMEVQAItlLEEVGLSkAYMDK-YPNmLSGGEAQRVAIARAIC------INPKY 164
Cdd:PRK13548 90 PF-TVEEV---VamgrAPHGLSRAEDDALVAAA--LAQVDLA-HLAGRdYPQ-LSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 165 ILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDI-QAATYlCDQLIIFKNGKI 222
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLnLAARY-ADRIVLLHQGRL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-222 |
3.73e-30 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 111.69 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKK--V 78
Cdd:cd03266 1 MITADALTKRFRD----VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaeA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 RRhQIGAVFQdyTSSLHPFQTVREILfEVMCQCDGQPKDVMEvQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAI 158
Cdd:cd03266 77 RR-RLGFVSD--STGLYDRLTARENL-EYFAGLYGLKGDELT-ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 159 CINPKYILFDEAISSLDMSIQTQILDLLIHLRETrQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-222 |
8.28e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 110.75 E-value: 8.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYqsahvfkrRRTPIVKGVSFECPIGATiAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM--HKKKVR 79
Cdd:cd03264 1 LQLENLTKRY--------GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlkQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHqIGAVFQDYTssLHPFQTVREILfEVMCQCDGQPKDVMEVQAITLLEEVGLSKAYmDKYPNMLSGGEAQRVAIARAIC 159
Cdd:cd03264 72 RR-IGYLPQEFG--VYPNFTVREFL-DYIAWLKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLRETRqlSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-203 |
9.28e-30 |
|
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: 110.26 E-value: 9.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSyqsahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR- 79
Cdd:COG4133 2 MLEAENLSCR--------RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDy 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytSSLHPFQTVREILfEVMCQCDGQPKDVMEVQAitLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAIC 159
Cdd:COG4133 74 RRRLAYLGHA--DGLKPELTVRENL-RFWAALYGLRADREAIDE--ALEAVGLA-GLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHD 203
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLTTHQ 190
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-243 |
9.79e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.88 E-value: 9.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 18 KRRRTPIVKGVSFECPIGATIAIIGESGSGKS----TLSRMI-----------LGIEKPDKGCVTLNDQPMHK-KKVRRH 81
Cdd:PRK10261 25 EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqagglvqcdkMLLRRRSRQVIELSEQSAAQmRHVRGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYTSSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGL--SKAYMDKYPNMLSGGEAQRVAIARAIC 159
Cdd:PRK10261 105 DMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeAQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGK-IEEQIPTSALHKSDNAY 238
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEaVETGSVEQIFHAPQHPY 264
|
....*
gi 446513169 239 TRELI 243
Cdd:PRK10261 265 TRALL 269
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-222 |
1.01e-29 |
|
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: 110.66 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 30 FECPI--GATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRHQIGAVFQDytSSLHPFQTVRE-ILFE 106
Cdd:cd03298 17 FDLTFaqGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE--NNLFAHLTVEQnVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 107 VMCQCDGQPKDVMEVQAItlLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLL 186
Cdd:cd03298 95 LSPGLKLTAEDRQAIEVA--LARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 446513169 187 IHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-225 |
4.47e-29 |
|
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: 107.78 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYqsahvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK-KKVRR 80
Cdd:cd03247 1 LSINNVSFSY------PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDlEKALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQdytsSLHPFQTvreilfevmcqcdgqpkdvmevqaiTLLEEVGLSkaymdkypnmLSGGEAQRVAIARAICI 160
Cdd:cd03247 75 SLISVLNQ----RPYLFDT-------------------------TLRNNLGRR----------FSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 161 NPKYILFDEAISSLDMSIQTQILDLLihLRETRQLSYIFITHDIQAATYLcDQLIIFKNGKIEEQ 225
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-225 |
5.64e-29 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 109.24 E-value: 5.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHvfkrrrtPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH--KKKVR 79
Cdd:cd03254 3 IEFENVNFSYDEKK-------PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdiSRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytsslhPF---QTVRE-ILFevmcqcdGQPKDVMEVQAItLLEEVGLSKaYMDKYPN-----------ML 144
Cdd:cd03254 76 RSMIGVVLQD------TFlfsGTIMEnIRL-------GRPNATDEEVIE-AAKEAGAHD-FIMKLPNgydtvlgenggNL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 145 SGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRqlSYIFITH---DIQAAtylcDQLIIFKNGK 221
Cdd:cd03254 141 SQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHrlsTIKNA----DKILVLDDGK 214
|
....
gi 446513169 222 IEEQ 225
Cdd:cd03254 215 IIEE 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
6.02e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.58 E-value: 6.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR 80
Cdd:COG4152 1 MLELKGLTKRFGDKTA--------VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 hqIGavfqdY---TSSLHPFQTVRE-ILFevMCQCDGQPKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVAIAR 156
Cdd:COG4152 73 --IG-----YlpeERGLYPKMKVGEqLVY--LARLKGLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446513169 157 AICINPKYILFDEAISSLDmSIQTQIL-DLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:COG4152 143 ALLHDPELLILDEPFSGLD-PVNVELLkDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-222 |
9.68e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 108.58 E-value: 9.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYqsahvfKRRRtpIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ-----PMHK 75
Cdd:COG1137 3 TLEAENLVKSY------GKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPMHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 kkvR-RHQIGAVFQDytSSLhpFQ--TVRE----ILfEVMcqcdGQPKDVMEVQAITLLEEVGL-----SKAYMdkypnm 143
Cdd:COG1137 75 ---RaRLGIGYLPQE--ASI--FRklTVEDnilaVL-ELR----KLSKKEREERLEELLEEFGIthlrkSKAYS------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 144 LSGGEAQRVAIARAICINPKYILFDEAISSLD-MSIQtQILDLLIHLREtRQLSyIFIT-HDIQAATYLCDQLIIFKNGK 221
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAVA-DIQKIIRHLKE-RGIG-VLITdHNVRETLGICDRAYIISEGK 213
|
.
gi 446513169 222 I 222
Cdd:COG1137 214 V 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-236 |
1.26e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVFKRRrtpIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLND-QPMHKKKVR- 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQ---AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 ----RHQIGAVFQDYTSSLHPFQTVREILFevmcqcdgQPK----DVMEVQ--AITLLEEVGLSKAYMDKYPNMLSGGEA 149
Cdd:PRK13646 80 irpvRKRIGMVFQFPESQLFEDTVEREIIF--------GPKnfkmNLDEVKnyAHRLLMDLGFSRDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 150 QRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTS 229
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPK 231
|
....*..
gi 446513169 230 ALHKSDN 236
Cdd:PRK13646 232 ELFKDKK 238
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-222 |
4.06e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.51 E-value: 4.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVekSYQsahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK-KKVR 79
Cdd:COG4559 1 MLEAENL--SVR------LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVF-QDytSSLH-PFqTVREIlfeVM------CQCDGQPKDVMEvQAitlLEEVGLSkAYMDKYPNMLSGGEAQR 151
Cdd:COG4559 73 LARRRAVLpQH--SSLAfPF-TVEEV---VAlgraphGSSAAQDRQIVR-EA---LALVGLA-HLAGRSYQTLSGGEQQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 152 VAIARAIC-------INPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQ-AATYlCDQLIIFKNGKI 222
Cdd:COG4559 142 VQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNlAAQY-ADRILLLHQGRL 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-225 |
5.94e-28 |
|
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: 111.45 E-value: 5.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHvfkrrrtPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPmhkkkVR-- 79
Cdd:COG5265 358 VRFENVSFGYDPER-------PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD-----IRdv 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 -----RHQIGAVFQDytsslhpfqTVreiLFEvmcqcD--------GQPKDVME--VQAI-----------------TLL 127
Cdd:COG5265 426 tqaslRAAIGIVPQD---------TV---LFN-----DtiayniayGRPDASEEevEAAAraaqihdfieslpdgydTRV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 128 EEVGLskaymdkypnMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRqlSYIFITH---DI 204
Cdd:COG5265 489 GERGL----------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHrlsTI 556
|
250 260
....*....|....*....|.
gi 446513169 205 QAAtylcDQLIIFKNGKIEEQ 225
Cdd:COG5265 557 VDA----DEILVLEAGRIVER 573
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-227 |
8.70e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 106.71 E-value: 8.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRhqiGAVFQDytSSLHPFQTVRE 102
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQN--EGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 103 -ILFEVmcQCDGQPKDVMEVQAITLLEEVGLSKAYmDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQ 181
Cdd:PRK11248 90 nVAFGL--QLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446513169 182 ILDLLIHL-RETRQlSYIFITHDIQAATYLCDQLIIFK--NGKIEEQIP 227
Cdd:PRK11248 167 MQTLLLKLwQETGK-QVLLITHDIEEAVFMATELVLLSpgPGRVVERLP 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-222 |
9.81e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 108.42 E-value: 9.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 39 AIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ-----------PMHKKKvrrhqIGAVFQDytSSLHPFQTVREILFEV 107
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclPPEKRR-----IGYVFQD--ARLFPHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 108 McqcdgqpKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLI 187
Cdd:PRK11144 101 M-------AKSMVAQFDKIVALLGI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190
....*....|....*....|....*....|....*
gi 446513169 188 HLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK11144 173 RLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-207 |
1.89e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.49 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 19 RRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPD---KGCVTLNDQPMHKKKVRRHQIGAVFQDytSSLH 95
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILFQD--DLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 96 PFQTVRE-ILFevmcqcdGQPKDV----MEVQAITLLEEVGLSKAYmDKYPNMLSGGEAQRVAIARAICINPKYILFDEA 170
Cdd:COG4136 89 PHLSVGEnLAF-------ALPPTIgraqRRARVEQALEEAGLAGFA-DRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 446513169 171 ISSLDMSIQTQILDLLI-HLREtRQLSYIFITHDIQAA 207
Cdd:COG4136 161 FSKLDAALRAQFREFVFeQIRQ-RGIPALLVTHDEEDA 197
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
2.13e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.55 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR 80
Cdd:COG4604 1 MIEIKNVSKRYGG--------KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 --HQIGAVFQD--YTSSLhpfqTVREIL-F-------EVMCQCDgqpKDVMEvQAITLLEEVGLSKAYMDKypnmLSGGE 148
Cdd:COG4604 73 laKRLAILRQEnhINSRL----TVRELVaFgrfpyskGRLTAED---REIID-EAIAYLDLEDLADRYLDE----LSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 149 AQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDI-QAATYlCDQLIIFKNGKIEEQIP 227
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDInFASCY-ADHIVAMKDGRVVAQGT 219
|
.
gi 446513169 228 T 228
Cdd:COG4604 220 P 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-222 |
2.15e-27 |
|
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: 105.21 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ-----PMHkk 76
Cdd:cd03219 1 LEVRGLTKRFGGLVA--------LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglPPH-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 KVRRHQIGAVFQdyTSSLHPFQTVREILfEVMCQCDG----------QPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSG 146
Cdd:cd03219 71 EIARLGIGRTFQ--IPRLFPELTVLENV-MVAAQARTgsglllararREEREARERAEELLERVGLA-DLADRPAGELSY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 147 GEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-226 |
3.22e-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: 103.84 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRH 81
Cdd:cd03268 1 LKTNDLTKTYGKKRV--------LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFqDYtSSLHPFQTVREILFEVMCQCDGQPKDVMEVqaitlLEEVGLsKAYMDKYPNMLSGGEAQRVAIARAICIN 161
Cdd:cd03268 73 RIGALI-EA-PGFYPNLTARENLRLLARLLGIRKKRIDEV-----LDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 162 PKYILFDEAISSLDMSIQTQILDLLIHLRETrQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQI 226
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-237 |
4.40e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 106.73 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 4 IKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRHQI 83
Cdd:PRK11432 9 LKNITKRFGSNTV--------IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 84 GAVFQDYtsSLHPFQTVRE-ILFEVMCQcdGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAICINP 162
Cdd:PRK11432 81 CMVFQSY--ALFPHMSLGEnVGYGLKML--GVPKEERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 163 KYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKSDNA 237
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-222 |
8.17e-27 |
|
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: 101.35 E-value: 8.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH---KKKV 78
Cdd:cd03216 1 LELRGITKRFGGVKA--------LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfasPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 RRHQIGAVFQdytsslhpfqtvreilfevmcqcdgqpkdvmevqaitlleevglskaymdkypnmLSGGEAQRVAIARAI 158
Cdd:cd03216 73 RRAGIAMVYQ-------------------------------------------------------LSVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 159 CINPKYILFDEAISSLDmsiQTQILDLLIHLRETRQ--LSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03216 98 ARNARLLILDEPTAALT---PAEVERLFKVIRRLRAqgVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-215 |
9.63e-27 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 107.76 E-value: 9.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 21 RTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH--KKKVRRHQIGAVFQdytsslHPFQ 98
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRDQIAWVPQ------HPFL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 TVREILFEVMCQCDGQPKDVME--VQAITLLEEV-GLSKAY---MDKYPNMLSGGEAQRVAIARAICINPKYILFDEAIS 172
Cdd:TIGR02857 408 FAGTIAENIRLARPDASDAEIReaLERAGLDEFVaALPQGLdtpIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446513169 173 SLDMSIQTQILDLLIHLRETRQLsyIFITHDIqAATYLCDQLI 215
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQGRTV--LLVTHRL-ALAALADRIV 527
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-222 |
9.97e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 103.99 E-value: 9.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 4 IKDVEKSYQSahvfkrrRTpIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKkvrRHQI 83
Cdd:PRK11247 15 LNAVSKRYGE-------RT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA---REDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 84 GAVFQDytSSLHPFQTVREilfEVMCQCDGQPKDvmevQAITLLEEVGLSKAYMDkYPNMLSGGEAQRVAIARAICINPK 163
Cdd:PRK11247 84 RLMFQD--ARLLPWKKVID---NVGLGLKGQWRD----AALQALAAVGLADRANE-WPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 164 YILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-222 |
1.08e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 102.24 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 21 RTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILG--IEKPDKGCVTLNDQPMHKKKVRRhQIGAVFQDytSSLHPFQ 98
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRK-IIGYVPQD--DILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 TVREIL-FEVMCQCdgqpkdvmevqaitlleevglskaymdkypnmLSGGEAQRVAIARAICINPKYILFDEAISSLDMS 177
Cdd:cd03213 98 TVRETLmFAAKLRG--------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446513169 178 IQTQILDLLIHLRETrQLSYIFITHDIQAATY-LCDQLIIFKNGKI 222
Cdd:cd03213 146 SALQVMSLLRRLADT-GRTIICSIHQPSSEIFeLFDKLLLLSQGRV 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-220 |
2.67e-26 |
|
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: 102.13 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQsAHVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ--------- 71
Cdd:COG4778 4 LLEVENLSKTFT-LHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 72 -PMHKKKVRRHQIGAVFQdytsSLH--PFQTVREILFEVMCQcDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGE 148
Cdd:COG4778 83 sPREILALRRRTIGYVSQ----FLRviPRVSALDVVAEPLLE-RGVDREEARARARELLARLNLPERLWDLPPATFSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446513169 149 AQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNG 220
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-222 |
7.03e-26 |
|
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: 101.08 E-value: 7.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYqsahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ-----PMHKK 76
Cdd:cd03218 1 LRAENLSKRY--------GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklPMHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 kvRRHQIGAVFQDytSSLHPFQTVREILFEVMcQCDGQPKDVMEVQAITLLEEVGLSKAyMDKYPNMLSGGEAQRVAIAR 156
Cdd:cd03218 73 --ARLGIGYLPQE--ASIFRKLTVEENILAVL-EIRGLSKKEREEKLEELLEEFHITHL-RKSKASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 157 AICINPKYILFDEAISSLD-MSIQtQILDLLIHLREtRQLSyIFIT-HDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKILKD-RGIG-VLITdHNVRETLSITDRAYIIYEGKV 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-222 |
1.05e-25 |
|
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: 100.36 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 22 TPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLND---QPMHKKKVRRHqIGAVFQDytSSLHpFQ 98
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADLRRN-IGYVPQD--VTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 TVREILfevmcqCDGQP--KDVMEVQAITLLeevGLSKaYMDKYPN-----------MLSGGEAQRVAIARAICINPKYI 165
Cdd:cd03245 93 TLRDNI------TLGAPlaDDERILRAAELA---GVTD-FVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446513169 166 LFDEAISSLDMSIQTQILDLLIHLRETRQLsyIFITHDiQAATYLCDQLIIFKNGKI 222
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHR-PSLLDLVDRIIVMDSGRI 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
27-225 |
1.24e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.16 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 27 GVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVT--LNDQPMH---------KKKVRRHQIGAVFQdytsslH 95
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRdlyalseaeRRRLLRTEWGFVHQ------H 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 96 PFQTVR----------EILFEVMCQCDGQPKDvmevQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYI 165
Cdd:PRK11701 98 PRDGLRmqvsaggnigERLMAVGARHYGDIRA----TAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 166 LFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQ 225
Cdd:PRK11701 174 FMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
25-222 |
1.91e-25 |
|
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: 100.50 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR---RHQIGAVFQdyTSSLHPFQTVR 101
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriaRLGIARTFQ--NPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 102 E------------ILFEVMCQCDGQPKDVMEV--QAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAICINPKYILF 167
Cdd:COG0411 98 EnvlvaaharlgrGLLAALLRLPRARREEREAreRAEELLERVGLA-DRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 168 DEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
2.02e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAhvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR- 79
Cdd:PRK13639 1 ILETRDLKYSYPDG-------TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 ---RHQIGAVFQDYTSSLHPFQTVREILFEVMCQcdGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIAR 156
Cdd:PRK13639 74 levRKTVGIVFQNPDDQLFAPTVEEDVAFGPLNL--GLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 157 AICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
25-222 |
3.46e-25 |
|
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: 98.98 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLN--DQPMHKKKVRRhQIGAVFQDytSSLHPFQTVRE 102
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghDVVREPREVRR-RIGIVFQD--LSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 103 ILfEVMCQCDGQPKDVMEVQAITLLEEVGLSKAyMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQI 182
Cdd:cd03265 93 NL-YIHARLYGVPGAERRERIDELLDFVGLLEA-ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446513169 183 LDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03265 171 WEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-222 |
4.02e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 98.51 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYqsahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKvrRH 81
Cdd:cd03269 1 LEVENVTKRF--------GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDytSSLHPFQTVREILFeVMCQCDGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAICIN 161
Cdd:cd03269 71 RIGYLPEE--RGLYPKMKVIDQLV-YLAQLKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 162 PKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
4.23e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.55 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQsahvfkrRRTPI----VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCV----------- 66
Cdd:PRK13651 3 IKVKNIVKIFN-------KKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 67 ----------TLNDQPMHKKKVR-----RHQIGAVFQDYTSSLHPFQTVREILFEVMCQcdGQPKDVMEVQAITLLEEVG 131
Cdd:PRK13651 76 ktkekekvleKLVIQKTRFKKIKkikeiRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSM--GVSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 132 LSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQAATYLC 211
Cdd:PRK13651 154 LDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWT 232
|
250
....*....|.
gi 446513169 212 DQLIIFKNGKI 222
Cdd:PRK13651 233 KRTIFFKDGKI 243
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-224 |
5.27e-25 |
|
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: 98.37 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSY--------------QSAHVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVT 67
Cdd:cd03220 1 IELENVSKSYptykggssslkklgILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 68 lndqpmhkkkvRRHQIGAVFqDYTSSLHPFQTVRE-ILFevMCQCDGQPKDVM-----EVQAITLLEEvglskaYMDKYP 141
Cdd:cd03220 81 -----------VRGRVSSLL-GLGGGFNPELTGREnIYL--NGRLLGLSRKEIdekidEIIEFSELGD------FIDLPV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 142 NMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGK 219
|
...
gi 446513169 222 IEE 224
Cdd:cd03220 220 IRF 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-222 |
9.19e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.42 E-value: 9.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVFKRRrtpIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLND----QPMHKK 76
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASR---ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 KVR--RHQIGAVFQDYTSSLHPFQTVREILFEVmcQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAI 154
Cdd:PRK13643 78 EIKpvRKKVGVVFQFPESQLFEETVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 155 ARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-221 |
9.51e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.68 E-value: 9.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHA--------VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQDYtsSLHPFQTVRE-ILFEVmcQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAIC 159
Cdd:PRK11607 91 RPINMMFQSY--ALFPHMTVEQnIAFGL--KQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 160 INPKYILFDEAISSLDMSI----QTQILDLLihlrETRQLSYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-236 |
1.32e-24 |
|
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: 97.85 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVeksyqsahVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGC-VTLNDQPMHKKKVR 79
Cdd:COG1119 3 LLELRNV--------TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 --RHQIGAVfqdyTSSLH----PFQTVREI----LFEVMcqcdG---QPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSG 146
Cdd:COG1119 75 elRKRIGLV----SPALQlrfpRDETVLDVvlsgFFDSI----GlyrEPTDEQRERARELLELLGLA-HLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 147 GEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITH---DIQAATylcDQLIIFKNGKIE 223
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveEIPPGI---THVLLLKDGRVV 222
|
250
....*....|...
gi 446513169 224 EQIPTSALHKSDN 236
Cdd:COG1119 223 AAGPKEEVLTSEN 235
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-223 |
1.45e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.97 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVFKRRrtpIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-- 79
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKK---ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 --RHQIGAVFQdytsslHP-FQtvreiLFEVMCQCD--------GQPKDVMEVQAITLLEEVGLSK-AYMDKYPNMLSGG 147
Cdd:PRK13637 80 diRKKVGLVFQ------YPeYQ-----LFEETIEKDiafgpinlGLSEEEIENRVKRAMNIVGLDYeDYKDKSPFELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 148 EAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIE 223
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-231 |
1.91e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR- 79
Cdd:COG1129 4 LLEMRGISKSFGGVKA--------LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 --RHQIGAVFQDytSSLHPFQTVREILFevMCQcdgQPK-------DVMEVQAITLLEEVGLSkayMDkyPNM----LSG 146
Cdd:COG1129 76 aqAAGIAIIHQE--LNLVPNLSVAENIF--LGR---EPRrgglidwRAMRRRARELLARLGLD---ID--PDTpvgdLSV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 147 GEAQRVAIARAICINPKYILFDEAISSLDMSiQTQIL-DLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQ 225
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTER-EVERLfRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRLVGT 221
|
....*.
gi 446513169 226 IPTSAL 231
Cdd:COG1129 222 GPVAEL 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-222 |
2.52e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.34 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRmILG-IEKPDKG--------CVTLNDQ 71
Cdd:PRK10535 4 LLELKDIRRSYPSGE----EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGcLDKPTSGtyrvagqdVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 72 PMhkKKVRRHQIGAVFQDY--TSSLHPFQTVreilfEVMCQCDGQPKDVMEVQAITLLEEVGLSKAyMDKYPNMLSGGEA 149
Cdd:PRK10535 79 AL--AQLRREHFGFIFQRYhlLSHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGLEDR-VEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446513169 150 QRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYlCDQLIIFKNGKI 222
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
2.94e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.07 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAH---------VFKRRRTP-----IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGcv 66
Cdd:COG1134 4 MIEVENVSKSYRLYHepsrslkelLLRRRRTRreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 67 tlndqpmhkkKVRRH-QIGAVFqDYTSSLHPFQTVRE-ILFevMCQCDGQPKDvmEVQAitLLEEV----GLSKaYMDK- 139
Cdd:COG1134 82 ----------RVEVNgRVSALL-ELGAGFHPELTGREnIYL--NGRLLGLSRK--EIDE--KFDEIvefaELGD-FIDQp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 140 ---YpnmlSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQAATYLCDQLII 216
Cdd:COG1134 144 vktY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIW 218
|
....*....
gi 446513169 217 FKNGKIEEQ 225
Cdd:COG1134 219 LEKGRLVMD 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-236 |
4.91e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.09 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSyqsahVFKRRRTPIVK---GVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKK 77
Cdd:PRK13642 1 MNKILEVENL-----VFKYEKESDVNqlnGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 V--RRHQIGAVFQDYTSSLHPFQTVREILFEVMCQcdGQPKDVMevqaITLLEEVGLSKAYMD---KYPNMLSGGEAQRV 152
Cdd:PRK13642 76 VwnLRRKIGMVFQNPDNQFVGATVEDDVAFGMENQ--GIPREEM----IKRVDEALLAVNMLDfktREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 153 AIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYlCDQLIIFKNGK-IEEQIPTSAL 231
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEiIKEAAPSELF 228
|
....*
gi 446513169 232 HKSDN 236
Cdd:PRK13642 229 ATSED 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-189 |
8.47e-24 |
|
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: 95.42 E-value: 8.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDK---GCVTLNDQPMHKKKVRRHqIGAVFQDYTssLHPFQTV 100
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKC-VAYVRQDDI--LLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 101 RE-ILFEVM-----CQCDGQPKdvmEVQAITLLEEVGLSKAYMDKYPNmLSGGEAQRVAIARAICINPKYILFDEAISSL 174
Cdd:cd03234 99 REtLTYTAIlrlprKSSDAIRK---KRVEDVLLRDLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170
....*....|....*
gi 446513169 175 DMSIQTQILDLLIHL 189
Cdd:cd03234 175 DSFTALNLVSTLSQL 189
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-223 |
1.02e-23 |
|
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: 99.05 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 20 RRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH---KKKVRRHqIGAVFQDytSSLHP 96
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdREELGRH-IGYLPQD--VELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 97 fQTVRE-I-LFEvmcqcDGQPKDVmeVQA---------I--------TLLEEVGlskaymdkypNMLSGGEAQRVAIARA 157
Cdd:COG4618 420 -GTIAEnIaRFG-----DADPEKV--VAAaklagvhemIlrlpdgydTRIGEGG----------ARLSGGQRQRIGLARA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 158 ICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATyLCDQLIIFKNGKIE 223
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLA-AVDKLLVLRDGRVQ 545
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
1.43e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.07 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAhvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM--HKKKV 78
Cdd:PRK13636 5 ILKVEELNYNYSDG-------THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 R--RHQIGAVFQDYTSSLHPFQTVREILFEVMCQcdGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIAR 156
Cdd:PRK13636 78 MklRESVGMVFQDPDNQLFSASVYQDVSFGAVNL--KLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 157 AICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-227 |
1.43e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM-HKKKVRR 80
Cdd:PRK13536 42 IDLAGVSKSYGD--------KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQdyTSSLHPFQTVREILFEVMCQCDGQPKDVMEVQAiTLLEEVGL-SKAymDKYPNMLSGGEAQRVAIARAIC 159
Cdd:PRK13536 114 ARIGVVPQ--FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIP-SLLEFARLeSKA--DARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLReTRQLSYIFITHDIQAATYLCDQLIIFKNG-KIEEQIP 227
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRP 256
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-240 |
1.99e-23 |
|
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: 98.64 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 15 HVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--RHQIGAVFQDyts 92
Cdd:TIGR02203 338 FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVALVSQD--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 93 sLHPFQ-TVRE-ILFevmcqcdGQPKDVMEVQAITLLEEVGLsKAYMDKYPN-----------MLSGGEAQRVAIARAIC 159
Cdd:TIGR02203 415 -VVLFNdTIANnIAY-------GRTEQADRAEIERALAAAYA-QDFVDKLPLgldtpigengvLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLRETRqlSYIFITH---DIQAAtylcDQLIIFKNGKIEEQIPTSALHKSDN 236
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHrlsTIEKA----DRIVVMDDGRIVERGTHNELLARNG 559
|
....
gi 446513169 237 AYTR 240
Cdd:TIGR02203 560 LYAQ 563
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-224 |
2.49e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNdqpmhkKKVRr 80
Cdd:COG0488 315 VLELEGLSKSYGD--------KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG------ETVK- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 hqIGAVFQDyTSSLHPFQTVREILFEVMcqcdgqpKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICI 160
Cdd:COG0488 380 --IGYFDQH-QEELDPDKTVLDELRDGA-------PGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 161 NPKYILFDEAISSLDMSIQTQILDLLIhlretrqlSY----IFITHD---IQAatyLCDQLIIFKNGKIEE 224
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALD--------DFpgtvLLVSHDryfLDR---VATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
3.39e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.80 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVeksyqsaHVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-- 79
Cdd:PRK13647 5 IEVEDL-------HFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDYTSSLHPFQTVREILFEVMCQcdGQPKDVMEVQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVAIARAIC 159
Cdd:PRK13647 78 RSKVGLVFQDPDDQVFSSTVWDDVAFGPVNM--GLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-238 |
3.90e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK--KKVR 79
Cdd:TIGR00958 479 IEFQDVSFSYPN-----RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydHHYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytsslhPFQTVREILFEVMCQCDGQPKDvmEVQAITLLEEV-----GLSKAY---MDKYPNMLSGGEAQR 151
Cdd:TIGR00958 554 HRQVALVGQE------PVLFSGSVRENIAYGLTDTPDE--EIMAAAKAANAhdfimEFPNGYdteVGEKGSQLSGGQKQR 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 152 VAIARAICINPKYILFDEAISSLDmsiqTQILDLLIHLRETRQLSYIFITHDIQAATYlCDQLIIFKNGKIEEQIPTSAL 231
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
....*..
gi 446513169 232 HKSDNAY 238
Cdd:TIGR00958 701 MEDQGCY 707
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
25-222 |
4.50e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.48 E-value: 4.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--RHQIGAVFQDYTSSLHPFQTVRE 102
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRevRKFVGLVFQNPDDQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 103 ILFEvmcQCD-GQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQ 181
Cdd:PRK13652 100 IAFG---PINlGLDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446513169 182 ILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-222 |
5.78e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.87 E-value: 5.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRH 81
Cdd:PRK11000 4 VTLRNVTKAYGD--------VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYtsSLHPFQTVRE-ILFEVMCQCDGQP---KDVMEVQAITLLEEVglskayMDKYPNMLSGGEAQRVAIARA 157
Cdd:PRK11000 76 GVGMVFQSY--ALYPHLSVAEnMSFGLKLAGAKKEeinQRVNQVAEVLQLAHL------LDRKPKALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 158 ICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-231 |
7.82e-23 |
|
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: 92.50 E-value: 7.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYqsahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-- 79
Cdd:cd03224 1 LEVENLNAGY--------GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHer 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 -RHQIGAVFQDytSSLHPFQTVRE-ILFEVMCQCDGQPKDVMEvQAITL---LEEVGLSKAYMdkypnmLSGGEAQRVAI 154
Cdd:cd03224 73 aRAGIGYVPEG--RRIFPELTVEEnLLLGAYARRRAKRKARLE-RVYELfprLKERRKQLAGT------LSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446513169 155 ARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-231 |
9.32e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.72 E-value: 9.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQsaHVFKRrrtpivkgVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR 80
Cdd:PRK10771 1 MLKLTDITWLYH--HLPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQDytSSLHPFQTVREIL---FEVMCQCDGQPKDvmEVQAItlLEEVGLSkAYMDKYPNMLSGGEAQRVAIARA 157
Cdd:PRK10771 71 RPVSMLFQE--NNLFSHLTVAQNIglgLNPGLKLNAAQRE--KLHAI--ARQMGIE-DLLARLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 158 ICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-240 |
1.21e-22 |
|
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: 92.29 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAhvfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-- 79
Cdd:cd03251 1 VEFKNVTFRYPGD------GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAsl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytssLHPFQ-TVRE-ILFEVMcqcDGQPKDVMEVQAITLLEEvglskaYMDKYPN-----------MLSG 146
Cdd:cd03251 75 RRQIGLVSQD----VFLFNdTVAEnIAYGRP---GATREEVEEAARAANAHE------FIMELPEgydtvigergvKLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 147 GEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRqlSYIFITH---DIQAAtylcDQLIIFKNGKIE 223
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHrlsTIENA----DRIVVLEDGKIV 215
|
250
....*....|....*..
gi 446513169 224 EQIPTSALHKSDNAYTR 240
Cdd:cd03251 216 ERGTHEELLAQGGVYAK 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-222 |
3.94e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.75 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR 80
Cdd:PRK09536 3 MIDVSDLSVEFGD--------TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 --HQIGAVFQDYTSSLHpFqTVREIL----------FEVMCQCDGQPKDvmevQAItllEEVGLSkAYMDKYPNMLSGGE 148
Cdd:PRK09536 75 asRRVASVPQDTSLSFE-F-DVRQVVemgrtphrsrFDTWTETDRAAVE----RAM---ERTGVA-QFADRPVTSLSGGE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 149 AQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFItHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRV 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-222 |
5.44e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.81 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVFKRRRtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVT-----LNDQPMHK- 75
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKG---LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhITPETGNKn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 -KKVRRhQIGAVFQDYTSSLHPFQTVREILFEVMCQcdGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAI 154
Cdd:PRK13641 80 lKKLRK-KVSLVFQFPEAQLFENTVLKDVEFGPKNF--GFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 155 ARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-235 |
9.41e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 90.62 E-value: 9.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 28 VSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH--KKKVRRHQIGAVFQDYTSSlhPFQTVREIL- 104
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQLPAA--EGMTVRELVa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 105 ---------FEVMCQCDGQPKDvmevQAITLleeVGLsKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLD 175
Cdd:PRK10575 108 igrypwhgaLGRFGAADREKVE----EAISL---VGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 176 MSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKSD 235
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-222 |
2.57e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.76 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDqpMHKKKVR- 79
Cdd:PRK13633 4 MIKCKNVSYKYESNE--ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEEn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 ----RHQIGAVFQDYTSslhpfQTVREILFEVMC---QCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRV 152
Cdd:PRK13633 80 lwdiRNKAGMVFQNPDN-----QIVATIVEEDVAfgpENLGIPPEEIRERVDESLKKVGMYE-YRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 153 AIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYlCDQLIIFKNGKI 222
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-238 |
3.86e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.81 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK--KKVR 79
Cdd:PRK11160 339 LTLNNVSFTYPDQP------QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADysEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQdytsSLHPF-QTVREILfeVMcqcdGQPKDVMEvQAITLLEEVGLSKAYMDKYP-NM--------LSGGEA 149
Cdd:PRK11160 413 RQAISVVSQ----RVHLFsATLRDNL--LL----AAPNASDE-ALIEVLQQVGLEKLLEDDKGlNAwlgeggrqLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 150 QRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLsyIFITHDIQAATYLcDQLIIFKNGKIEEQIPTS 229
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV--LMITHRLTGLEQF-DRICVMDNGQIIEQGTHQ 558
|
....*....
gi 446513169 230 ALHKSDNAY 238
Cdd:PRK11160 559 ELLAQQGRY 567
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
25-243 |
4.13e-21 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 90.25 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKpDKGCVT-----LND------QPMHKKKVRRHQIGAVFQDYTSS 93
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTadrmrFDDidllrlSPRERRKLVGHNVSMIFQEPQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 94 LHPFQTVREILFEVMcqcDG--------QPKDVMEVQAITLLEEVGLS--KAYMDKYPNMLSGGEAQRVAIARAICINPK 163
Cdd:PRK15093 102 LDPSERVGRQLMQNI---PGwtykgrwwQRFGWRKRRAIELLHRVGIKdhKDAMRSFPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 164 YILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGK-IEEQIPTSALHKSDNAYTREL 242
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQtVETAPSKELVTTPHHPYTQAL 258
|
.
gi 446513169 243 I 243
Cdd:PRK15093 259 I 259
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-229 |
6.34e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 88.17 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKST----LSRMILGIEkpdkGC-----VTLNDQP 72
Cdd:COG1117 12 IEVRNLNVYYGDKQA--------LKDINLDIPENKVTALIGPSGCGKSTllrcLNRMNDLIP----GArvegeILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 73 MHKKKV-----RRhQIGAVFQDYTsslhPF-QTVRE-ILFevmcqcdG------QPKDVMEVQAITLLEEVGL---SKAY 136
Cdd:COG1117 80 IYDPDVdvvelRR-RVGMVFQKPN----PFpKSIYDnVAY-------GlrlhgiKSKSELDEIVEESLRKAALwdeVKDR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 137 MDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDmSIQTQ-ILDLLIHLREtrQLSYIFITHDIQAATYLCDQLI 215
Cdd:COG1117 148 LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD-PISTAkIEELILELKK--DYTIVIVTHNMQQAARVSDYTA 224
|
250
....*....|....
gi 446513169 216 IFKNGKIEEQIPTS 229
Cdd:COG1117 225 FFYLGELVEFGPTE 238
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-244 |
7.66e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.28 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM-----------HKKKVRRHQIGA 85
Cdd:PRK11831 15 FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrsrlytvRKRMSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 86 VFQDytssLHPFQTVREILFEVMcqcdGQPKDVMEVQAITLLEEVGLSKAyMDKYPNMLSGGEAQRVAIARAICINPKYI 165
Cdd:PRK11831 95 LFTD----MNVFDNVAYPLREHT----QLPAPLLHSTVMMKLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 166 LFDEAISSLD---MSIQTQILDLLIHlreTRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKSDNAYTREL 242
Cdd:PRK11831 166 MFDEPFVGQDpitMGVLVKLISELNS---ALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQF 242
|
..
gi 446513169 243 IE 244
Cdd:PRK11831 243 LD 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-204 |
8.67e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.24 E-value: 8.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHvfkrrrtPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR- 79
Cdd:PRK10908 1 MIRFEHVSKAYLGGR-------QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 ----RHQIGAVFQDytsslHPFQTVREILFEVMCQ--CDGQPKDVMEVQAITLLEEVGLskayMDK---YPNMLSGGEAQ 150
Cdd:PRK10908 74 vpflRRQIGMIFQD-----HHLLMDRTVYDNVAIPliIAGASGDDIRRRVSAALDKVGL----LDKaknFPIQLSGGEQQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446513169 151 RVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETrQLSYIFITHDI 204
Cdd:PRK10908 145 RVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDI 197
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-222 |
8.94e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 8.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 14 AHVFKRRRtpIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ-----PMHKKKvrRHQIGAVFQ 88
Cdd:PRK10895 10 AKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARA--RRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 89 DytSSLHPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAICINPKYILFD 168
Cdd:PRK10895 86 E--ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEH-LRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446513169 169 EAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-247 |
1.05e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.71 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM-HKKKVRR 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLV--------VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAVFQdyTSSLHPFQTVREILFeVMCQCDGQPKDVMEVQAITLLEEVGL-SKAymDKYPNMLSGGEAQRVAIARAIC 159
Cdd:PRK13537 80 QRVGVVPQ--FDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKLeNKA--DAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 160 INPKYILFDEAISSLDMSIQTQILDLLIHLReTRQLSYIFITHDIQAATYLCDQLIIFKNG-KIEEQIPtsalhksdnay 238
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAP----------- 222
|
....*....
gi 446513169 239 tRELIEKQL 247
Cdd:PRK13537 223 -HALIESEI 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-235 |
1.99e-20 |
|
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: 86.57 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVrr 80
Cdd:COG0410 3 MLEVENLHAGYGGIHV--------LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGA-----------VFqdytsslhPFQTVREILfEVMCQCDGQPKDVMEVqaitlLEEVglskayMDKYPNM------ 143
Cdd:COG0410 73 HRIARlgigyvpegrrIF--------PSLTVEENL-LLGAYARRDRAEVRAD-----LERV------YELFPRLkerrrq 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 144 ----LSGGEAQRVAIARAICINPKYILFDEAisSLDMS--IQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIF 217
Cdd:COG0410 133 ragtLSGGEQQMLAIGRALMSRPKLLLLDEP--SLGLAplIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVL 209
|
250
....*....|....*...
gi 446513169 218 KNGKIEEQIPTSALHKSD 235
Cdd:COG0410 210 ERGRIVLEGTAAELLADP 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-222 |
2.29e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 86.37 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQP--MHKKKVR 79
Cdd:cd03248 12 VKFQNVTFAYPT-----RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPisQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDYTSSLhpfQTVREILFEVMCQCDGQpkDVMEVQ----AITLLEEvgLSKAY---MDKYPNMLSGGEAQRV 152
Cdd:cd03248 87 HSKVSLVGQEPVLFA---RSLQDNIAYGLQSCSFE--CVKEAAqkahAHSFISE--LASGYdteVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 153 AIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRqlSYIFITHDIQAATYlCDQLIIFKNGKI 222
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-203 |
3.11e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 88.96 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--RHQIGAVFQDytssLHPFQ-T 99
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQD----AHLFDtT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 100 VRE-ILFevmcqcdGQPkDVMEVQAITLLEEVGLSKaYMDKYPN-----------MLSGGEAQRVAIARAICINPKYILF 167
Cdd:TIGR02868 425 VREnLRL-------ARP-DATDEELWAALERVGLAD-WLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 446513169 168 DEAISSLDMSIQTQILDLLihLRETRQLSYIFITHD 203
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-221 |
3.98e-20 |
|
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: 84.83 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAhvfKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQpmhkkkvrrh 81
Cdd:cd03250 1 ISVEDASFTWDSG---EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 qIGAVFQdytSSLHPFQTVRE-ILFevmcqcdGQP------KDVMEVQA----ITLLE-----EVGlskaymDKYPNmLS 145
Cdd:cd03250 68 -IAYVSQ---EPWIQNGTIREnILF-------GKPfdeeryEKVIKACAlepdLEILPdgdltEIG------EKGIN-LS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 146 GGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLI--HLRE--TRqlsyIFITHDIQAATYlCDQLIIFKNGK 221
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCIlgLLLNnkTR----ILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
40-222 |
5.55e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 40 IIGESGSGKSTLSRMILGIEKPDKGCVTLND--------------QPMHKK----KVRRHQIGAVFQDYTSSLHPFQTVR 101
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitNPYSKKiknfKELRRRVSMVFQFPEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 102 EILFEVMCQcdGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQ 181
Cdd:PRK13631 137 DIMFGPVAL--GVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446513169 182 ILDLLIHLRETRQlSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13631 215 MMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-225 |
6.17e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KK 77
Cdd:PRK11231 2 TLRTENLTVGYGT--------KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRRHQigavfqdytsSLHPFQ-------TVREI----------LFEVMCQCDGQPKDV-MEVQAITLLEEVGLSKaymdk 139
Cdd:PRK11231 74 LARRL----------ALLPQHhltpegiTVRELvaygrspwlsLWGRLSAEDNARVNQaMEQTRINHLADRRLTD----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 140 ypnmLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLlihLRETRQLSYIFIT--HDIQAATYLCDQLIIF 217
Cdd:PRK11231 139 ----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRL---MRELNTQGKTVVTvlHDLNQASRYCDHLVVL 211
|
....*...
gi 446513169 218 KNGKIEEQ 225
Cdd:PRK11231 212 ANGHVMAQ 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-246 |
7.83e-20 |
|
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: 85.23 E-value: 7.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTL--NDQPMHKKKVRRHQIGAVFQDYT---------- 91
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdgHDLALADPAWLRRQVGVVLQENVlfnrsirdni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 92 SSLHPFQTVREIlfEVMCQCDGQPKDVMEVQA--ITLLEEVGLSkaymdkypnmLSGGEAQRVAIARAICINPKYILFDE 169
Cdd:cd03252 97 ALADPGMSMERV--IEAAKLAGAHDFISELPEgyDTIVGEQGAG----------LSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 170 AISSLDMSIQTQILDLLIHLRETRqlSYIFITHDIqaATYLC-DQLIIFKNGKIEEQIPTSALHKSDNAYTReLIEKQ 246
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICAGR--TVIIIAHRL--STVKNaDRIIVMEKGRIVEQGSHDELLAENGLYAY-LYQLQ 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-231 |
9.33e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAhvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLND----QPMHKK 76
Cdd:PRK13644 1 MIRLENVSYSYPDG-------TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 KVRRhQIGAVFQDYTSSLHPfQTVREILF---EVMCqcdgQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVA 153
Cdd:PRK13644 74 GIRK-LVGIVFQNPETQFVG-RTVEEDLAfgpENLC----LPPIEIRKRVDRALAEIGLEK-YRHRSPKTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 154 IARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQaATYLCDQLIIFKNGKIE-EQIPTSAL 231
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLE-ELHDADRIIVMDRGKIVlEGEPENVL 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-222 |
1.38e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.18 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVFKRRrtpIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK------ 75
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGR---ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 -KKVRRHqIGAVFQDYTSSLHPFQTVREILFEVmcQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAI 154
Cdd:PRK13649 80 iKQIRKK-VGLVFQFPESQLFEETVLKDVAFGP--QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 155 ARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETrQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-219 |
2.07e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.01 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIE--KPDKGCVTLNDQPMHKKKVR 79
Cdd:PTZ00265 1166 IEIMDVNFRYIS-----RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlKNDHHIVFKNEHTNDMTNEQ 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQ-------------------IGAVFQDYTSslhpFQTVREILFEVMCQCDGQPKDVMEVQAI----------TLLEEV 130
Cdd:PTZ00265 1241 DYQgdeeqnvgmknvnefsltkEGGSGEDSTV----FKNSGKILLDGVDICDYNLKDLRNLFSIvsqepmlfnmSIYENI 1316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 131 GLSK--------------AYMDKY----PNM-----------LSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQ 181
Cdd:PTZ00265 1317 KFGKedatredvkrackfAAIDEFieslPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1396
|
250 260 270
....*....|....*....|....*....|....*...
gi 446513169 182 ILDLLIHLRETRQLSYIFITHDIqAATYLCDQLIIFKN 219
Cdd:PTZ00265 1397 IEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1433
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-246 |
4.09e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.05 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 22 TPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIeKPDKGCVTLNDQPMHK--KKVRRHQIGAVFQDytsSLHPFQT 99
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREldPESWRKHLSWVGQN---PQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 100 VRE-ILFevmcqcdGQPkDVMEVQAITLLEEVGLSKaYMDKYPN-----------MLSGGEAQRVAIARAICINPKYILF 167
Cdd:PRK11174 439 LRDnVLL-------GNP-DASDEQLQQALENAWVSE-FLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 168 DEAISSLDMSIQTQILDLLIHLreTRQLSYIFITHDIQaATYLCDQLIIFKNGKIEEQIPTSALHKSDNAYTRELIEKQ 246
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
1.04e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.21 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSA-----------HVFKRRRTPI--VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVT 67
Cdd:COG4586 1 IIEVENLSKTYRVYekepglkgalkGLFRREYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 68 LNDQPMHKKKVR-RHQIGAVF-QdyTSSLHP-------FQTVREIlFEVmcqcdgqPKDVMEVQAITLLEEVGLSKaYMD 138
Cdd:COG4586 81 VLGYVPFKRRKEfARRIGVVFgQ--RSQLWWdlpaidsFRLLKAI-YRI-------PDAEYKKRLDELVELLDLGE-LLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 139 KYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFK 218
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVID 229
|
....
gi 446513169 219 NGKI 222
Cdd:COG4586 230 HGRI 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
1.17e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHvfkrrrtpIVKGVSFECPIGATIAIIGESGSGKST----LSRMI-LGIEKPDKGCVTLNDQPMHKK 76
Cdd:PRK14258 8 IKVNNLSFYYDTQK--------ILEGVSMEIYQSKVTAIIGPSGCGKSTflkcLNRMNeLESEVRVEGRVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 KVR----RHQIGAVFQdyTSSLHPFQTVREILFEVMCqCDGQPK----DVME--VQAITLLEEVG--LSKAYMDkypnmL 144
Cdd:PRK14258 80 RVNlnrlRRQVSMVHP--KPNLFPMSVYDNVAYGVKI-VGWRPKleidDIVEsaLKDADLWDEIKhkIHKSALD-----L 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446513169 145 SGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-225 |
1.65e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.24 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 21 RTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--RHQIGAVFQDytsSLHPFQ 98
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQD---AGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 TVREILfEVMCQcDGQPKDVMEVQAITLLEEVGLSKAymDKYP-------NMLSGGEAQRVAIARAICINPKYILFDEAI 171
Cdd:PRK13657 424 SIEDNI-RVGRP-DATDEEMRAAAERAQAHDFIERKP--DGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 172 SSLDMSIQTQI---LDLLIHLRETrqlsyIFITH---DIQAAtylcDQLIIFKNGKIEEQ 225
Cdd:PRK13657 500 SALDVETEAKVkaaLDELMKGRTT-----FIIAHrlsTVRNA----DRILVFDNGRVVES 550
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-222 |
4.93e-18 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 79.01 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR---RHQIGAVFQD-YTSSLHPFQTV 100
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaiRAGIAYVPEDrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 101 REilfevmcqcdgqpkdvmevqAITLleevglskaymdkyPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQT 180
Cdd:cd03215 96 AE--------------------NIAL--------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446513169 181 QILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:cd03215 142 EIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-215 |
1.24e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH--KKKVRRHQIGAVFQdyTSSL 94
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIYRQQVSYCAQ--TPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 95 hpF-QTVRE-ILFEVmcQCDGQPKDVMEVQAItlLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAIS 172
Cdd:PRK10247 93 --FgDTVYDnLIFPW--QIRNQQPDPAIFLDD--LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446513169 173 SLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYlCDQLI 215
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVI 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-202 |
1.50e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 22 TPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLndqPMHKKkvrrhqigAVF--QD-YTsslhPFQ 98
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---PAGAR--------VLFlpQRpYL----PLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 TVREILfevmcqC-DGQPKDVMEVQAITLLEEVGLSK--AYMDK---YPNMLSGGEAQRVAIARAICINPKYILFDEAIS 172
Cdd:COG4178 441 TLREAL------LyPATAEAFSDAELREALEAVGLGHlaERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190
....*....|....*....|....*....|
gi 446513169 173 SLDMSIQTQILDLLihLRETRQLSYIFITH 202
Cdd:COG4178 515 ALDEENEAALYQLL--REELPGTTVISVGH 542
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-209 |
1.53e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.61 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 3 KIKDVEK-SYQSA--HVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKK--- 76
Cdd:PTZ00265 376 KLKDIKKiQFKNVrfHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinl 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 KVRRHQIGAVFQD-------------YT-SSLHPFQTVREILFE--------------VMCQCDGQPKDVM--------- 119
Cdd:PTZ00265 456 KWWRSKIGVVSQDpllfsnsiknnikYSlYSLKDLEALSNYYNEdgndsqenknkrnsCRAKCAGDLNDMSnttdsneli 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 120 ----EVQAITLLEEVGLSK---------AYMDKYPNM-------LSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQ 179
Cdd:PTZ00265 536 emrkNYQTIKDSEVVDVSKkvlihdfvsALPDKYETLvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260 270
....*....|....*....|....*....|
gi 446513169 180 TQILDLLIHLRETRQLSYIFITHDIQAATY 209
Cdd:PTZ00265 616 YLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-222 |
1.61e-17 |
|
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: 78.91 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQ-----------SAHVFKR--RRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTL 68
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligsLKSLFKRkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 69 NDQ-PMHKKKVRRHQIGAVFQDYT------SSLHPFQTVREILfevmcqcdgqpkDVMEVQAITLLEEvgLSK-----AY 136
Cdd:cd03267 81 AGLvPWKRRKKFLRRIGVVFGQKTqlwwdlPVIDSFYLLAAIY------------DLPPARFKKRLDE--LSElldleEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 137 MDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLII 216
Cdd:cd03267 147 LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLV 226
|
....*.
gi 446513169 217 FKNGKI 222
Cdd:cd03267 227 IDKGRL 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-248 |
1.74e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.12 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMI-----LGIEKPDKGCVTLNDQPMHKKKVR----RHQIGAVFQdYTSSL 94
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDpievRREVGMVFQ-YPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 95 hPFQTVRE-----ILFEVMCQCDGQPKDVME--VQAITLLEEVglsKAYMDKYPNMLSGGEAQRVAIARAICINPKYILF 167
Cdd:PRK14267 98 -PHLTIYDnvaigVKLNGLVKSKKELDERVEwaLKKAALWDEV---KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 168 DEAISSLDMSIQTQILDLLIHLREtrQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKSDNaytRELIEKQL 247
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE---HELTEKYV 248
|
.
gi 446513169 248 S 248
Cdd:PRK14267 249 T 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-222 |
1.87e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.28 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKK----VRRHQIGAVFQDYTS 92
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgllALRQQVATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 93 SLHPFQTVREILFEVMCQCDGQPKDVMEV-QAITLLEevglSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAI 171
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNLGVPEAEITRRVdEALTLVD----AQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446513169 172 SSLDMSIQTQILDLLihLRETRQLSYIFI-THDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13638 165 AGLDPAGRTQMIAII--RRIVAQGNHVIIsSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-245 |
2.55e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.42 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMI-----LGIEKPDKGCVTLNDQPMHKK 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEV--------LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 KVR--RHQIGAVFQ--DYTSSLHPFQTVR---EILFEVMCQCDGQPKDVMEVQAITLLEEVglsKAYMDKYPNMLSGGEA 149
Cdd:PRK14247 76 DVIelRRRVQMVFQipNPIPNLSIFENVAlglKLNRLVKSKKELQERVRWALEKAQLWDEV---KDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 150 QRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRetRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTS 229
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELK--KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTR 230
|
250
....*....|....*....
gi 446513169 230 ALhksdnaYTR---ELIEK 245
Cdd:PRK14247 231 EV------FTNprhELTEK 243
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-221 |
5.14e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 5.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVK---GVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR---RHQIGAVFQDytssLH- 95
Cdd:PRK11288 15 PGVKaldDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaalAAGVAIIYQE----LHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 96 -PFQTVREILFEvmcqcdGQ-P-------KDVMEVQAITLLEEVGlskayMDKYPNM----LSGGEAQRVAIARAICINP 162
Cdd:PRK11288 91 vPEMTVAENLYL------GQlPhkggivnRRLLNYEAREQLEHLG-----VDIDPDTplkyLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 163 KYILFDEAISSLDmSIQTQILDLLIH-LR-ETRQLsyIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:PRK11288 160 RVIAFDEPTSSLS-AREIEQLFRVIReLRaEGRVI--LYVSHRMEEIFALCDAITVFKDGR 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
40-222 |
7.90e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.74 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 40 IIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ--PMHKKKVR-----RHQIGAVFQDYTSSLHPFQTVREILFEVMCQcd 112
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaiPANLKKIKevkrlRKEIGLVFQFPEYQLFQETIEKDIAFGPVNL-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 113 GQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRET 192
Cdd:PRK13645 120 GENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKE 199
|
170 180 190
....*....|....*....|....*....|
gi 446513169 193 RQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13645 200 YKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-225 |
8.15e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 79.40 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH---KKKVRRHqIGAVFQDytsslhPFQT 99
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdidRHTLRQF-INYLPQE------PYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 100 VREILFEVMCQCDGQPKDVMEVQAITLLEevglSKAYMDKYP-----------NMLSGGEAQRVAIARAICINPKYILFD 168
Cdd:TIGR01193 561 SGSILENLLLGAKENVSQDEIWAACEIAE----IKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446513169 169 EAISSLDMSIQTQILDLLIHLRETrqlSYIFITHDIQAATyLCDQLIIFKNGKIEEQ 225
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQ 689
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
25-224 |
1.02e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.13 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSR-------MILGIEKpdKGCVTLNDQPMHKKKVR----RHQIGAVFQdytsS 93
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYAPDVDpvevRRRIGMVFQ----K 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 94 LHPF-QTVRE-ILFEVmcQCDGQPKDVMEV------QAItLLEEVglsKAYMDKYPNMLSGGEAQRVAIARAICINPKYI 165
Cdd:PRK14243 100 PNPFpKSIYDnIAYGA--RINGYKGDMDELverslrQAA-LWDEV---KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 166 LFDEAISSLDmSIQTQILDLLIH-LREtrQLSYIFITHDIQAATYLCDQLIIFkNGKIEE 224
Cdd:PRK14243 174 LMDEPCSALD-PISTLRIEELMHeLKE--QYTIIIVTHNMQQAARVSDMTAFF-NVELTE 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-202 |
1.06e-16 |
|
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: 74.88 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 22 TPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIekpdkgcvtlndQPMHKKKVRRHQIGAVF----QDYTsslhPF 97
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL------------WPWGSGRIGMPEGEDLLflpqRPYL----PL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 98 QTVREILFevmcqcdgqpkdvmevqaitlleevglskaymdkYP--NMLSGGEAQRVAIARAICINPKYILFDEAISSLD 175
Cdd:cd03223 78 GTLREQLI----------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*..
gi 446513169 176 MSIQTQILDLLihlrETRQLSYIFITH 202
Cdd:cd03223 124 EESEDRLYQLL----KELGITVISVGH 146
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
1.51e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.66 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVFKRRrtpIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQ-----PMHK 75
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKR---ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 kkvRRHQIGAVFQDYTSSLHPFQTVREILfeVMCQCDGQP--------KDVMEvQAITLLEEVGLS-KAYMDKYPNMLSG 146
Cdd:COG1101 78 ---RAKYIGRVFQDPMMGTAPSMTIEENL--ALAYRRGKRrglrrgltKKRRE-LFRELLATLGLGlENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 147 GEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-218 |
2.33e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.38 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 19 RRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEK--PDKGCVTLNDQPMHKKKVRRHQIGAvfqdytsslhp 96
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREASLIDAIGR----------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 97 fqtvreilfevmcqcDGQPKDVMEVqaitlLEEVGLSKAY-MDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLD 175
Cdd:COG2401 109 ---------------KGDFKDAVEL-----LNAVGLSDAVlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446513169 176 MSiQTQILDLLIHlRETRQL--SYIFITHDIQAATYLCDQLIIFK 218
Cdd:COG2401 169 RQ-TAKRVARNLQ-KLARRAgiTLVVATHHYDVIDDLQPDLLIFV 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-203 |
2.49e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 4 IKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNdqpmhkKKVRrhqI 83
Cdd:COG0488 1 LENLSKSFGG--------RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------KGLR---I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 84 GAVFQDytSSLHPFQTVREILFEV-----------------MCQCDGQPKDVMEVQAI--------------TLLEEVGL 132
Cdd:COG0488 64 GYLPQE--PPLDDDLTVLDTVLDGdaelraleaeleeleakLAEPDEDLERLAELQEEfealggweaearaeEILSGLGF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 133 SKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDmsIQTqILDLLIHLReTRQLSYIFITHD 203
Cdd:COG0488 142 PEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES-IEWLEEFLK-NYPGTVLVVSHD 208
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-225 |
2.66e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 75.22 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KKV 78
Cdd:cd03244 3 IEFKNVSLRYRPNLP------PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiglHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 RRHqIGAVFQDytsslhPF---QTVREILfevmcqcD--GQPKDVMEVQAitlLEEVGLsKAYMDKYPNML--------- 144
Cdd:cd03244 77 RSR-ISIIPQD------PVlfsGTIRSNL-------DpfGEYSDEELWQA---LERVGL-KEFVESLPGGLdtvveegge 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 145 --SGGEAQRVAIARAICINPKYILFDEAISSLDMsiQTqilDLLIH--LRET-RQLSYIFITHDIQaaTYL-CDQLIIFK 218
Cdd:cd03244 139 nlSVGQRQLLCLARALLRKSKILVLDEATASVDP--ET---DALIQktIREAfKDCTVLTIAHRLD--TIIdSDRILVLD 211
|
....*..
gi 446513169 219 NGKIEEQ 225
Cdd:cd03244 212 KGRVVEF 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-248 |
3.02e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK-KKVR 79
Cdd:PRK15439 11 LLCARSISKQYSG--------VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDYTSSLHPFQTVRE-ILFevmcqcdGQPKDVMEVQAIT-LLEEVGlSKAYMDKYPNMLSGGEAQRVAIARA 157
Cdd:PRK15439 83 AHQLGIYLVPQEPLLFPNLSVKEnILF-------GLPKRQASMQKMKqLLAALG-CQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 158 ICINPKYILFDEAISSLdMSIQTQilDLLIHLRETRQLSY--IFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKSD 235
Cdd:PRK15439 155 LMRDSRILILDEPTASL-TPAETE--RLFSRIRELLAQGVgiVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
250
....*....|....*
gi 446513169 236 --NAYTRELIEKQLS 248
Cdd:PRK15439 232 iiQAITPAAREKSLS 246
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-234 |
5.18e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.52 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--------RHQIGAVFQdyTSSLH 95
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFnyrdvlefRRRVGMLFQ--RPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 96 PFQTVREILFEVMCQcDGQPKDVMEVQAITLLEEVGLSKAYMDKY---PNMLSGGEAQRVAIARAICINPKYILFDEAIS 172
Cdd:PRK14271 114 PMSIMDNVLAGVRAH-KLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446513169 173 SLDMSIQTQILDLLIHLREtrQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKS 234
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-238 |
7.15e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.43 E-value: 7.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMI-----LGIEKPDKGCVTLNDQPMHKKKVR----RHQIGAVFQDytSSLH 95
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTDtvdlRKEIGMVFQQ--PNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 96 PFQTVREILFEVmcQCDG-QPKDVME------VQAITLLEEVglsKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFD 168
Cdd:PRK14239 99 PMSIYENVVYGL--RLKGiKDKQVLDeaveksLKGASIWDEV---KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 169 EAISSLDMSIQTQILDLLIHLREtrQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL-----HKSDNAY 238
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMfmnpkHKETEDY 246
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-217 |
1.11e-15 |
|
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: 73.98 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 35 GATIAIIGESGSGKSTLSRMILGIEKPDKGcvtlnDQPMHKKKV--RRHQIGAvfqDYTSslhpfqTVREILFEVMCQCD 112
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----DIEIELDTVsyKPQYIKA---DYEG------TVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 113 GQPKDVMEVQAITLLEEVglskayMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRET 192
Cdd:cd03237 91 THPYFKTEIAKPLQIEQI------LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170 180
....*....|....*....|....*
gi 446513169 193 RQLSYIFITHDIQAATYLCDQLIIF 217
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRLIVF 189
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-224 |
1.25e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 73.22 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYqSAHVfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-- 79
Cdd:cd03369 7 IEVENLSVRY-APDL-----PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDYT-------SSLHPFQTVREilfevmcqcdgqpKDVMEVQAITlleEVGLSkaymdkypnmLSGGEAQRV 152
Cdd:cd03369 81 RSSLTIIPQDPTlfsgtirSNLDPFDEYSD-------------EEIYGALRVS---EGGLN----------LSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 153 AIARAICINPKYILFDEAISSLDMSIqtqilDLLIH--LRETRQLSYIF-ITHDIQAATYlCDQLIIFKNGKIEE 224
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYAT-----DALIQktIREEFTNSTILtIAHRLRTIID-YDKILVMDAGEVKE 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-190 |
1.34e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.98 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRR--HQIGavfqdYTSSLHPFQTV 100
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEacHYLG-----HRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 101 REILfEVMCQCDGQPkdvmEVQAITLLEEVGLSKAYMDKYpNMLSGGEAQRVAIARAICIN-PKYILfDEAISSLDMSIQ 179
Cdd:PRK13539 91 AENL-EFWAAFLGGE----ELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNrPIWIL-DEPTAALDAAAV 163
|
170
....*....|..
gi 446513169 180 TQILDLL-IHLR 190
Cdd:PRK13539 164 ALFAELIrAHLA 175
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-238 |
1.90e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.06 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-- 79
Cdd:PRK11176 342 IEFRNVTFTYPG------KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAsl 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RHQIGAVFQDytssLHPFQ-TV-REILFEVmcqcdgqpKDVMEVQAITLLEEVGLSKAYMDKYPN-----------MLSG 146
Cdd:PRK11176 416 RNQVALVSQN----VHLFNdTIaNNIAYAR--------TEQYSREQIEEAARMAYAMDFINKMDNgldtvigengvLLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 147 GEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRqlSYIFITH---DIQAAtylcDQLIIFKNGKIE 223
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHrlsTIEKA----DEILVVEDGEIV 557
|
250
....*....|....*
gi 446513169 224 EQIPTSALHKSDNAY 238
Cdd:PRK11176 558 ERGTHAELLAQNGVY 572
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-236 |
2.87e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVFKRrrtpivkGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMhKKKVRRH 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALR-------DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-RQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQ----DYTsslhpFQTVREILfeVMCQCDG--------QPKDVMEVQAItlLEEVGLSKaYMDKYPNMLSGGEA 149
Cdd:PRK15056 79 LVAYVPQseevDWS-----FPVLVEDV--VMMGRYGhmgwlrraKKRDRQIVTAA--LARVDMVE-FRHRQIGELSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 150 QRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQAATYLCDQLIIFKnGKIEEQIPTS 229
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTE 226
|
....*..
gi 446513169 230 ALHKSDN 236
Cdd:PRK15056 227 TTFTAEN 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-229 |
4.72e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.91 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 26 KGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH---KKKVRRHQIGAVFQDYtsSLHPFQTVRE 102
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsPRDAIALGIGMVHQHF--MLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 103 --ILfevmcqcdGQPKDVMEV----QAITLLEEvgLSKAY-----MDKYPNMLSGGEAQRVAIARAICINPKYILFDEAI 171
Cdd:COG3845 100 niVL--------GLEPTKGGRldrkAARARIRE--LSERYgldvdPDAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446513169 172 SSLdmsiqT--QILDLLIHLRETRQ--LSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTS 229
Cdd:COG3845 170 AVL-----TpqEADELFEILRRLAAegKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
35-222 |
5.54e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.35 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 35 GATIAIIGESGSGKSTLSRMILGIEKPDK--GC------VTLNDQPMHKKKVR--RHQIGAVFQDYtSSLHPFQTVREIL 104
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLSGLITGDKsaGShiellgRTVQREGRLARDIRksRANTGYIFQQF-NLVNRLSVLENVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 105 FEVMCQ------CDGQPKDVMEVQAITLLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSI 178
Cdd:PRK09984 109 IGALGStpfwrtCFSWFTREQKQRALQALTRVGMVH-FAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446513169 179 QTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK09984 188 ARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-189 |
7.02e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 7.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 3 KIKDVEKSYQsahvfkrRRTpIVKGVS-FECPiGATIAIIGESGSGKSTLSRMILGIEKPD--KGCVTLNDQPMHKKKVR 79
Cdd:PLN03211 70 KISDETRQIQ-------ERT-ILNGVTgMASP-GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 80 RhqIGAVFQDytSSLHPFQTVREILfeVMCQCDGQP----KDVMEVQAITLLEEVGLSKAYMDKYPNM----LSGGEAQR 151
Cdd:PLN03211 141 R--TGFVTQD--DILYPHLTVRETL--VFCSLLRLPksltKQEKILVAESVISELGLTKCENTIIGNSfirgISGGERKR 214
|
170 180 190
....*....|....*....|....*....|....*...
gi 446513169 152 VAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHL 189
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-222 |
7.44e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.80 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 27 GVSFECPIGATIAIIGESGSGKSTLSRMILGIEkPDKGCVTLNDQPM---HKKKVRRHQ-----------IGAVFQdYTS 92
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLsdwSAAELARHRaylsqqqsppfAMPVFQ-YLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 93 sLHpfqtvreilfevmcqcdgQPKDVMEVQAITLLEEV----GLSkaymDKYPNM---LSGGEAQRVAIArAIC------ 159
Cdd:COG4138 92 -LH------------------QPAGASSEAVEQLLAQLaealGLE----DKLSRPltqLSGGEWQRVRLA-AVLlqvwpt 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 160 INP--KYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:COG4138 148 INPegQLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-189 |
1.23e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 18 KRRRTPIVKGVSFECPIGATIAIIGESGSGKSTL-----SRMILGIEKpdKGCVTLNDQPMHKKKVRRhqIGA-VFQDyt 91
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLmnalaFRSPKGVKG--SGSVLLNGMPIDAKEMRA--ISAyVQQD-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 92 SSLHPFQTVREIL-FEVMCQCDGQPKDVMEVQAIT-LLEEVGLSKAYMDK--YPNM---LSGGEAQRVAIARAICINPKY 164
Cdd:TIGR00955 108 DLFIPTLTVREHLmFQAHLRMPRRVTKKEKRERVDeVLQALGLRKCANTRigVPGRvkgLSGGERKRLAFASELLTDPPL 187
|
170 180
....*....|....*....|....*
gi 446513169 165 ILFDEAISSLDMSIQTQILDLLIHL 189
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGL 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-221 |
1.24e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 68.63 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGcvtlndqpmhkkKVRRH 81
Cdd:cd03221 1 IELENLSKTYGG--------KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------IVTWG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QigavfqdytsslhpfqtvreilfevmcqcdgqpkdvmevqaitlleevGLSKAYMDKypnmLSGGEAQRVAIARAICIN 161
Cdd:cd03221 61 S------------------------------------------------TVKIGYFEQ----LSGGEKMRLALAKLLLEN 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 162 PKYILFDEAISSLDMSIQTQILDLLIHLRETrqlsYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEYPGT----VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-225 |
3.55e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.37 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIE--KPDKGCVTLN---------- 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEV--------LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 70 ------DQPMHK----------------KKVRRH---QIGAVFQDyTSSLHPFQTVREILFEVMCQCDGQPKDVMEvQAI 124
Cdd:TIGR03269 73 erpskvGEPCPVcggtlepeevdfwnlsDKLRRRirkRIAIMLQR-TFALYGDDTVLDNVLEALEEIGYEGKEAVG-RAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 125 TLLEEVGLSKAYMdKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDI 204
Cdd:TIGR03269 151 DLIEMVQLSHRIT-HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|.
gi 446513169 205 QAATYLCDQLIIFKNGKIEEQ 225
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEE 250
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-245 |
4.83e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.63 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KKVRRhQIGAVFQDYTSslhPFQ-T 99
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyasKEVAR-RIGLLAQNATT---PGDiT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 100 VREI----------LFEVMCQCDGQP-KDVMEVQAITLLEevglskaymDKYPNMLSGGEAQRVAIARAICINPKYILFD 168
Cdd:PRK10253 98 VQELvargryphqpLFTRWRKEDEEAvTKAMQATGITHLA---------DQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 169 EAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI-EEQIPTSALhksdnayTRELIEK 245
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIvAQGAPKEIV-------TAELIER 239
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-238 |
5.78e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.13 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 19 RRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLndqpmhKKKVRRHQIGAVFQDytsslhpfQ 98
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------KGSVAYVPQQAWIQN--------D 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 TVRE-ILFevmcQCDGQPKDVMEV-QAITLLEEV-----GLSKAYMDKYPNmLSGGEAQRVAIARAICINPKYILFDEAI 171
Cdd:TIGR00957 714 SLREnILF----GKALNEKYYQQVlEACALLPDLeilpsGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446513169 172 SSLDMSIQTQILDLLIHLR-----ETRqlsyIFITHDIqaaTYL--CDQLIIFKNGKIEEQIPTSALHKSDNAY 238
Cdd:TIGR00957 789 SAVDAHVGKHIFEHVIGPEgvlknKTR----ILVTHGI---SYLpqVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
17-204 |
8.97e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 8.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRtpIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTlndqpmHKKKVRrhqIGAVFQ----DYTS 92
Cdd:PRK09544 14 FGQRR--VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLR---IGYVPQklylDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 93 SLhpfqTVREILfevMCQCDGQPKDVM----EVQAITLLEevglskAYMDKypnmLSGGEAQRVAIARAICINPKYILFD 168
Cdd:PRK09544 83 PL----TVNRFL---RLRPGTKKEDILpalkRVQAGHLID------APMQK----LSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 446513169 169 EAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDI 204
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-175 |
1.14e-13 |
|
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: 69.96 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPmhkkkvrrh 81
Cdd:TIGR03719 323 IEAENLTKAFGD--------KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDyTSSLHPFQTVREilfEVmcqCDGQpkDVMEVQAItlleEVGlSKAYM----------DKYPNMLSGGEAQR 151
Cdd:TIGR03719 386 KLAYVDQS-RDALDPNKTVWE---EI---SGGL--DIIKLGKR----EIP-SRAYVgrfnfkgsdqQKKVGQLSGGERNR 451
|
170 180
....*....|....*....|....
gi 446513169 152 VAIARAICINPKYILFDEAISSLD 175
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-220 |
1.32e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAHVfkrrrtpiVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KK 77
Cdd:PRK09700 5 YISMAGIGKSFGPVHA--------LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldhKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRRHQIGAVFQDYtsSLHPFQTVREILF------EVMCQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNmLSGGEAQR 151
Cdd:PRK09700 77 AAQLGIGIIYQEL--SVIDELTVLENLYigrhltKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-LSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 152 VAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQAATYLCDQLIIFKNG 220
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-202 |
1.52e-13 |
|
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: 67.17 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIE--KPDKGCVTLNDQ-----PMHKKKvrRHQIGAVFQDytsslhp 96
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEditdlPPEERA--RLGIFLAFQY------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 97 fqtvreilfevmcqcdgqPKDVMEVQAITLLEEVGLSkaymdkypnmLSGGEAQRVAIARAICINPKYILFDEAISSLDM 176
Cdd:cd03217 86 ------------------PPEIPGVKNADFLRYVNEG----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180
....*....|....*....|....*.
gi 446513169 177 SIQTQILDLLIHLREtRQLSYIFITH 202
Cdd:cd03217 138 DALRLVAEVINKLRE-EGKSVLIITH 162
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-222 |
2.40e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 12 QSAHVFKRRRTpIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGiEKPD---------KGCVTLNDQPMHKKKVRR-H 81
Cdd:PRK13547 5 DHLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGggaprgarvTGDVTLNGEPLAAIDAPRlA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDYTSSLHPFqTVREIlfeVMCQCDGQPKDVMEVQ------AITLLEEVGlSKAYMDKYPNMLSGGEAQRVAIA 155
Cdd:PRK13547 83 RLRAVLPQAAQPAFAF-SAREI---VLLGRYPHARRAGALThrdgeiAWQALALAG-ATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 156 RAIC---------INPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK13547 158 RVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-224 |
3.20e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.38 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKK--------VRRHQIGAVFQDYTSSLH 95
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqidaiKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 96 pFQTVREILFEVMCQcdgQPKDVMEVQAIT--LLEEVGLSKAYMDKY---PNMLSGGEAQRVAIARAICINPKYILFDEA 170
Cdd:PRK14246 105 -LSIYDNIAYPLKSH---GIKEKREIKKIVeeCLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446513169 171 ISSLDMSIQTQILDLLIHLRetRQLSYIFITHDIQAATYLCDQLIIFKNGKIEE 224
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELK--NEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-207 |
3.46e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.10 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTlndqpmhkkKVRRHQIGAVFQ--DYTSSLhPFqTV 100
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------RAGGARVAYVPQrsEVPDSL-PL-TV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 101 REILFEVMCQCDGQPK-----DVMEVQAItlLEEVG---LSKAYMDKypnmLSGGEAQRVAIARAICINPKYILFDEAIS 172
Cdd:NF040873 75 RDLVAMGRWARRGLWRrltrdDRAAVDDA--LERVGladLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*
gi 446513169 173 SLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAA 207
Cdd:NF040873 149 GLDAESRERIIALLAEEHA-RGATVVVVTHDLELV 182
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-188 |
2.08e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 28 VSFECPIGATIAIIGESGSGKSTLSRMILGIeKPDKGCVTLNDQPM-----HKKKVRR----HQIGAVFqdytsSLHPFQ 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLeawsaAELARHRaylsQQQTPPF-----AMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 tvreilFEVMCQCDGQPKDVMEVQAITLLEEVGLskayMDKYP---NMLSGGEAQRVAIArAIC------INP--KYILF 167
Cdd:PRK03695 89 ------YLTLHQPDKTRTEAVASALNEVAEALGL----DDKLGrsvNQLSGGEWQRVRLA-AVVlqvwpdINPagQLLLL 157
|
170 180
....*....|....*....|.
gi 446513169 168 DEAISSLDMSiQTQILDLLIH 188
Cdd:PRK03695 158 DEPMNSLDVA-QQAALDRLLS 177
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-218 |
3.02e-12 |
|
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: 65.58 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 34 IGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLN------------DQPMhkkKVRRHQIGAVFQDYTSSlhPFQTvr 101
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyispDYDG---TVEEFLRSANTDDFGSS--YYKT-- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 102 EILfevmcqcdgqpkdvmevqaitllEEVGLSKaYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQ 181
Cdd:COG1245 438 EII-----------------------KPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170 180 190
....*....|....*....|....*....|....*..
gi 446513169 182 ILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFK 218
Cdd:COG1245 494 VAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-188 |
6.87e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMhKKKVRRHQIGAVFQDYTSSLHP 96
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 97 FQTVRE-ILFEVMCQCDGqpkdvMEVQAITLLEEVGlskAYMDkYP-NMLSGGEAQRVAIARAICINPKYILFDEAISSL 174
Cdd:PRK13540 88 YLTLREnCLYDIHFSPGA-----VGITELCRLFSLE---HLID-YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170
....*....|....*
gi 446513169 175 D-MSIQTQILDLLIH 188
Cdd:PRK13540 159 DeLSLLTIITKIQEH 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-222 |
8.01e-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: 64.65 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 39 AIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKK-KVRRHQIGAVFQdYTSSLHPFQTVREILFevMCQCDGQPKD 117
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNlDAVRQSLGMCPQ-HNILFHHLTVAEHILF--YAQLKGRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 118 VMEVQAITLLEEVGLSKAYMDKYPNmLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLsy 197
Cdd:TIGR01257 1037 EAQLEMEAMLEDTGLHHKRNEEAQD-LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI-- 1113
|
170 180
....*....|....*....|....*
gi 446513169 198 IFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:TIGR01257 1114 IMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-225 |
1.12e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.97 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYqsahvfkRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM----HkkK 77
Cdd:PRK10790 341 IDIDNVSFAY-------RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslsH--S 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRRHQIGAVFQDytsslhPFqtvreILFEVMCQCDGQPKDVMEVQAITLLEEVGLSK----------AYMDKYPNMLSGG 147
Cdd:PRK10790 412 VLRQGVAMVQQD------PV-----VLADTFLANVTLGRDISEEQVWQALETVQLAElarslpdglyTPLGEQGNNLSVG 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 148 EAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtrQLSYIFITHDIQAATYlCDQLIIFKNGKIEEQ 225
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-222 |
1.82e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.37 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVtlndqpmhkKKVRRHQIGAVFQDYTsslHPFQTvRE 102
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV---------KWSENANIGYYAQDHA---YDFEN-DL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 103 ILFEVMCQCdGQPKDvmEVQAI-TLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDM-SIQT 180
Cdd:PRK15064 400 TLFDWMSQW-RQEGD--DEQAVrGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES 476
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446513169 181 QILDLlihlrETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK15064 477 LNMAL-----EKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-175 |
1.91e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.35 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 27 GVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRHQiGAVFQDYTSSLHPFQTVREIL-- 104
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR-GLLYLGHAPGIKTTLSVLENLrf 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 105 FEVMCQCDgqpkdvmevQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLD 175
Cdd:cd03231 97 WHADHSDE---------QVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-231 |
2.47e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.19 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 21 RTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--RHQIGAVFQDytsslhPFq 98
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQT------PF- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 tvreiLFE-------VMCQCDGQPKDVMEVQAITLLEE--VGLSKAYMDKYPN---MLSGGEAQRVAIARAICINPKYIL 166
Cdd:PRK10789 400 -----LFSdtvanniALGRPDATQQEIEHVARLASVHDdiLRLPQGYDTEVGErgvMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 167 FDEAISSLDMSIQTQILDLLIHLRETRQLsyIFITHDIQAATYlCDQLIIFKNGKIEEQIPTSAL 231
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGRTV--IISAHRLSALTE-ASEILVMQHGHIAQRGNHDQL 536
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-224 |
5.68e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--RHQIGAVFQDYtsslHpfqtvre 102
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDF----H------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 103 iLFEVMCQCDGQPKDVMEVQAitLLEEVGL-SKAYMD--KYPNM-LSGGEAQRVAIARAICINPKYILFDEAISSLD-MS 177
Cdd:PRK10522 408 -LFDQLLGPEGKPANPALVEK--WLERLKMaHKLELEdgRISNLkLSKGQKKRLALLLALAEERDILLLDEWAADQDpHF 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446513169 178 IQTQILDLLIHLRETRQLsyIF-ITHD----IQAatylcDQLIIFKNGKIEE 224
Cdd:PRK10522 485 RREFYQVLLPLLQEMGKT--IFaISHDdhyfIHA-----DRLLEMRNGQLSE 529
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-218 |
6.37e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 35 GATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLN------------DQPMhkkkvrrhqigavfqdytsslhpfqTVRE 102
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyikpDYDG-------------------------TVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 103 ILFEVmcqcdgqPKDVMEVQAIT-LLEEVGLSKaYMDKYPNMLSGGEAQRVAIarAICINPK---YILfDEAISSLDMSI 178
Cdd:PRK13409 420 LLRSI-------TDDLGSSYYKSeIIKPLQLER-LLDKNVKDLSGGELQRVAI--AACLSRDadlYLL-DEPSAHLDVEQ 488
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446513169 179 QTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFK 218
Cdd:PRK13409 489 RLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-221 |
7.80e-11 |
|
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: 61.38 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 27 GVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPD--KGCVTLNDQPMHKKKVR---RHQIGAVFQDYTssLHPFQTVR 101
Cdd:TIGR02633 19 GIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRdteRAGIVIIHQELT--LVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 102 EILF---EVMCQCDGQPKDVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSi 178
Cdd:TIGR02633 97 ENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446513169 179 QTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:TIGR02633 176 ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-221 |
8.47e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH---KKKVRRHqiGAVfqdytsslHPFQTVR 101
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpGHQIARM--GVV--------RTFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 102 eiLFEVMCQCDG-------------------------QPKDVMEvQAITLLEEVGLsKAYMDKYPNMLSGGEAQRVAIAR 156
Cdd:PRK11300 91 --LFREMTVIENllvaqhqqlktglfsgllktpafrrAESEALD-RAATWLERVGL-LEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 157 AICINPKYILFDEAISSLDMSiQTQILDLLI-HLRETRQLSYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPK-ETKELDELIaELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-244 |
9.70e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILG-IEKPDKGCVTLNDQPMHKKkvrrhQIGAVFQdytsslhpfQTVR 101
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVAYVP-----QVSWIFN---------ATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 102 E-ILFEVMCQCD--GQPKDVMEVQA---------ITLLEEVGLSkaymdkypnmLSGGEAQRVAIARAICINPKYILFDE 169
Cdd:PLN03232 697 EnILFGSDFESEryWRAIDVTALQHdldllpgrdLTEIGERGVN----------ISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 170 AISSLDMSIQTQILDLLIHlRETRQLSYIFITHDIQAATyLCDQLIIFKNGKIEEQIPTSALHKSDNAYtRELIE 244
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLP-LMDRIILVSEGMIKEEGTFAELSKSGSLF-KKLME 838
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-225 |
1.29e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfKRRRtPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGiEKP---DKGCV---TLNDQPmhk 75
Cdd:PLN03130 615 ISIKNGYFSWDS----KAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPprsDASVVirgTVAYVP--- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 76 kkvrrhQIGAVFQdytsslhpfQTVRE-ILFevmcqcdGQPKD------VMEVQAITL---------LEEVGlskaymDK 139
Cdd:PLN03130 686 ------QVSWIFN---------ATVRDnILF-------GSPFDperyerAIDVTALQHdldllpggdLTEIG------ER 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 140 YPNmLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHlRETRQLSYIFITHDIQAATYLcDQLIIFKN 219
Cdd:PLN03130 738 GVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHE 814
|
....*.
gi 446513169 220 GKIEEQ 225
Cdd:PLN03130 815 GMIKEE 820
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-175 |
1.76e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSahvfkrrRTPIvKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQpmhkkkVrrh 81
Cdd:PRK11819 325 IEAENLSKSFGD-------RLLI-DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET------V--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVFQDyTSSLHPFQTVreilFEVMcqCDGQpkDVMEVQAItlleEVGlSKAYM----------DKYPNMLSGGEAQR 151
Cdd:PRK11819 388 KLAYVDQS-RDALDPNKTV----WEEI--SGGL--DIIKVGNR----EIP-SRAYVgrfnfkggdqQKKVGVLSGGERNR 453
|
170 180
....*....|....*....|....
gi 446513169 152 VAIARAICINPKYILFDEAISSLD 175
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
2-217 |
3.80e-10 |
|
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: 57.20 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAHVfkRRRTPIVKGvsfecpiGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNdqpmhkkkvrrh 81
Cdd:cd03222 1 QLYPDCVKRYGVFFL--LVELGVVKE-------GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 qigavfqdytsslhpfqtvreilfevmcqcdgqpkdvmevqaitlleevGLSKAYMDKYPNmLSGGEAQRVAIARAICIN 161
Cdd:cd03222 60 -------------------------------------------------GITPVYKPQYID-LSGGELQRVAIAAALLRN 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 162 PKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIF 217
Cdd:cd03222 90 ATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-220 |
6.08e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 57.34 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRHQIGAVFQDYTSSLHPF---QT 99
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWllnAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 100 VRE-ILFE----------VMCQCDGQPK-DVMEVQAITLLEEVGLSkaymdkypnmLSGGEAQRVAIARAICINPKYILF 167
Cdd:cd03290 95 VEEnITFGspfnkqrykaVTDACSLQPDiDLLPFGDQTEIGERGIN----------LSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 168 DEAISSLDMSIQTQILD--LLIHLRETRQlSYIFITHDIQAATYlCDQLIIFKNG 220
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-222 |
8.62e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 20 RRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR---RHQIGAVFQD-YTSSLH 95
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaiRAGIAYVPEDrKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 96 PFQTVREILfevmcqcdgqpkdvmevqAITLL------------EEVGLSKAYMD----KYPNM------LSGGEAQRVA 153
Cdd:COG1129 343 LDLSIRENI------------------TLASLdrlsrgglldrrRERALAEEYIKrlriKTPSPeqpvgnLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446513169 154 IARAICINPKYILFDE---AIsslDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:COG1129 405 LAKWLATDPKVLILDEptrGI---DVGAKAEIYRLIRELAA-EGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-231 |
9.25e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYqsahvfkrrrtPIVKGVSFEC----PiGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKK 76
Cdd:PRK10762 4 LLQLKGIDKAF-----------PGVKALSGAAlnvyP-GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 KVRRHQ---IGAVFQDYtsSLHPFQTVREILF---EVMCQCDGQPKDVMEVQAITLLEEVGLSKAyMDKYPNMLSGGEAQ 150
Cdd:PRK10762 72 GPKSSQeagIGIIHQEL--NLIPQLTIAENIFlgrEFVNRFGRIDWKKMYAEADKLLARLNLRFS-SDKLVGELSIGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 151 RVAIARAICINPKYILFDEAISSLdmsIQTQILDLLIHLRETRQLSY--IFITHDIQAATYLCDQLIIFKNGKIEEQIPT 228
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDAL---TDTETESLFRVIRELKSQGRgiVYISHRLKEIFEICDDVTVFRDGQFIAEREV 225
|
...
gi 446513169 229 SAL 231
Cdd:PRK10762 226 ADL 228
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-224 |
1.26e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.98 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 28 VSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLndqpmhKKKVRRHQIGAVFQDYTSSLHPFQtvreiLFEV 107
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI------KGSAALIAISSGLNGQLTGIENIE-----LKGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 108 MCqcdGQPKDvmEVQAIT--LLEEVGLSKaYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDL 185
Cdd:PRK13545 112 MM---GLTKE--KIKEIIpeIIEFADIGK-FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 446513169 186 LIHLRETRQlSYIFITHDIQAATYLCDQLIIFKNGKIEE 224
Cdd:PRK13545 186 MNEFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
33-90 |
2.10e-09 |
|
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: 57.12 E-value: 2.10e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 33 PIGATIA------IIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR--RHQIGAVFQDY 90
Cdd:COG4615 350 PIDLTIRrgelvfIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREayRQLFSAVFSDF 415
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-184 |
4.82e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.46 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 22 TPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVtlndqpmhkkkvrRHQIGAVFQDYTSSLHPfQTVR 101
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSPQTSWIMP-GTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 102 E-ILFEVMCQcdgQPKDVMEVQAITLLEEVGLSkAYMDKYPNM-----LSGGEAQRVAIARAICINPKYILFDEAISSLD 175
Cdd:TIGR01271 505 DnIIFGLSYD---EYRYTSVIKACQLEEDIALF-PEKDKTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
....*....
gi 446513169 176 MSIQTQILD 184
Cdd:TIGR01271 581 VVTEKEIFE 589
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-202 |
5.56e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.91 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGI--------EKPDKGCV------------TLNDQ---PMHKKKVRR 80
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLfyvpqrpymtlgTLRDQiiyPDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 81 HQIGAvfqdytsslhpfQTVREILFEVmcqcdgQPKDVMEvqaitllEEVGLSKayMDKYPNMLSGGEAQRVAIARAICI 160
Cdd:TIGR00954 547 RGLSD------------KDLEQILDNV------QLTHILE-------REGGWSA--VQDWMDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446513169 161 NPKYILFDEAISSLDMSIQTQILDlliHLRETRqLSYIFITH 202
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYR---LCREFG-ITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-212 |
6.12e-09 |
|
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: 55.07 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKgvsfecpIGATIAIIGESGSGKSTLSRMILGIEKPDKGcvtLNDQPMHKKKVRRHQIGAVFQDYTSSL-- 94
Cdd:cd03236 15 FKLHRLPVPR-------EGQVLGLVGPNGIGKSTALKILAGKLKPNLG---KFDDPPDWDEILDEFRGSELQNYFTKLle 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 95 ------HPFQTVREI-------LFEVMCQCD--GQPKDVMEVQAITLLeevglskayMDKYPNMLSGGEAQRVAIARAIC 159
Cdd:cd03236 85 gdvkviVKPQYVDLIpkavkgkVGELLKKKDerGKLDELVDQLELRHV---------LDRNIDQLSGGELQRVAIAAALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446513169 160 INPKYILFDEAISSLDMSiQTQILDLLIHLRETRQLSYIFITHDIQAATYLCD 212
Cdd:cd03236 156 RDADFYFFDEPSSYLDIK-QRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSD 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-221 |
6.70e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIeKPD---KGCVTLNDQPMHKKKVR---RHQIGAVFQDYTssLHPFQ 98
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRdteRAGIAIIHQELA--LVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 TVREILF---EVMcqcdgqPK-----DVMEVQAITLLEEVGLSkayMDKY-PNM-LSGGEAQRVAIARAICINPKYILFD 168
Cdd:PRK13549 98 SVLENIFlgnEIT------PGgimdyDAMYLRAQKLLAQLKLD---INPAtPVGnLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446513169 169 EAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-183 |
7.26e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 18 KRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGI----EKPDkGCVTLNDQPMHKKKvRRHQIGAVFQDYTSS 93
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPYKEFA-EKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 94 LHPFQTVREiLFEVMCQCDGqpkdvmevqaitlleevglskaymDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISS 173
Cdd:cd03233 94 HFPTLTVRE-TLDFALRCKG------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170
....*....|
gi 446513169 174 LDMSIQTQIL 183
Cdd:cd03233 149 LDSSTALEIL 158
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-176 |
1.04e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 13 SAH--VFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRH-----QIGA 85
Cdd:PRK13543 13 AAHalAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFmaylgHLPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 86 VFQDYTS--SLHpfqtvreilfeVMCQCDGQPKDVMEVQAITLleeVGLSkAYMDKYPNMLSGGEAQRVAIARaICINPK 163
Cdd:PRK13543 93 LKADLSTleNLH-----------FLCGLHGRRAKQMPGSALAI---VGLA-GYEDTLVRQLSAGQKKRLALAR-LWLSPA 156
|
170
....*....|....
gi 446513169 164 YI-LFDEAISSLDM 176
Cdd:PRK13543 157 PLwLLDEPYANLDL 170
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-203 |
1.23e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLndQPMHKkkvrrhqIGAVFQDytSSLHPFQTVRE 102
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QPGIK-------VGYLPQE--PQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 103 ILFEVMcqcdGQPKDVM-EVQAIT------------LLEEVG-----------------LSKAyMD--KYP------NML 144
Cdd:TIGR03719 88 NVEEGV----AEIKDALdRFNEISakyaepdadfdkLAAEQAelqeiidaadawdldsqLEIA-MDalRCPpwdadvTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 145 SGGEAQRVAIARAICINPKYILFDEAISSLDMSiqtQILDLLIHLRETrQLSYIFITHD 203
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEY-PGTVVAVTHD 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-217 |
2.05e-08 |
|
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: 54.41 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 35 GATIAIIGESGSGKSTLSRMILGIEKPDKGCVtlnDQPMHKKKVRRHQIGAVFQDYTSSL--------HPFQTVREI--L 104
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEVLKRFRGTELQDYFKKLangeikvaHKPQYVDLIpkV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 105 FevmcqcDGQPKDVMEV-----QAITLLEEVGLSKAyMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSiq 179
Cdd:COG1245 176 F------KGTVRELLEKvdergKLDELAEKLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY-- 246
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446513169 180 tQILDLLIHLRE-TRQLSYIFIT-HDIQAATYLCDQLIIF 217
Cdd:COG1245 247 -QRLNVARLIRElAEEGKYVLVVeHDLAILDYLADYVHIL 285
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-216 |
3.50e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 17 FKRRRTPIVKgvsfecpIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVtlnDQPMHKKKVRRHQIGAVFQDYTSSL-- 94
Cdd:PRK13409 88 FKLYGLPIPK-------EGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPSWDEVLKRFRGTELQNYFKKLyn 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 95 ------HPFQ-----------TVREILfevmcqcdgqpKDVMEVQAI-TLLEEVGLSKaYMDKYPNMLSGGEAQRVAIAR 156
Cdd:PRK13409 158 geikvvHKPQyvdlipkvfkgKVRELL-----------KKVDERGKLdEVVERLGLEN-ILDRDISELSGGELQRVAIAA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 157 AICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRqlSYIFITHDIQAATYLCDQLII 216
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHI 283
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-184 |
7.54e-08 |
|
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: 52.17 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 22 TPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVtlndqpmhkkkvrRHQIGAVFQDYTSSLHPfQTVR 101
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFSWIMP-GTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 102 E-ILFEV------------MCQCDGQPKDVMEvQAITLLEEVGLSkaymdkypnmLSGGEAQRVAIARAICINPKYILFD 168
Cdd:cd03291 116 EnIIFGVsydeyryksvvkACQLEEDITKFPE-KDNTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLD 184
|
170
....*....|....*.
gi 446513169 169 EAISSLDMSIQTQILD 184
Cdd:cd03291 185 SPFGYLDVFTEKEIFE 200
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-222 |
9.85e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 22 TPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGieKPD----KGCVTLNDQPMHKK--KVRRHQ-IGAVFQ------ 88
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLepEERAHLgIFLAFQypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 89 -----DYT----SSLHPFQTVREI----LFEVMcqcdgQPKdvmevqaitlLEEVGLSKAYMDKYPNM-LSGGEAQRVAI 154
Cdd:CHL00131 98 gvsnaDFLrlayNSKRKFQGLPELdpleFLEII-----NEK----------LKLVGMDPSFLSRNVNEgFSGGEKKRNEI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 155 ARAICINPKYILFDEAISSLDMSiQTQILDLLIHLRETRQLSYIFITHDIQAATYLC-DQLIIFKNGKI 222
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDID-ALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKI 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-240 |
1.08e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSAhvfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHK---KK 77
Cdd:PLN03232 1234 SIKFEDVHLRYRPG------LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfglTD 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRR-----HQIGAVFQDYTS-SLHPFQTVREI-LFEVMCQcdGQPKDVMEVQAITLLEEVGlskaymdKYPNMLSGGEAQ 150
Cdd:PLN03232 1308 LRRvlsiiPQSPVLFSGTVRfNIDPFSEHNDAdLWEALER--AHIKDVIDRNPFGLDAEVS-------EGGENFSVGQRQ 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 151 RVAIARAICINPKYILFDEAISSLDMSIqtqilDLLIH--LRET-RQLSYIFITHDIQAATYlCDQLIIFKNGKI-EEQI 226
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVRT-----DSLIQrtIREEfKSCTMLVIAHRLNTIID-CDKILVLSSGQVlEYDS 1452
|
250
....*....|....
gi 446513169 227 PTSALHKSDNAYTR 240
Cdd:PLN03232 1453 PQELLSRDTSAFFR 1466
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
39-221 |
1.69e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 39 AIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMH---KKKVRRHQIGAVFQDYTSSLHpfQTVREILFEVMCQCDG-- 113
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVHQELNLVLQ--RSVMDNMWLGRYPTKGmf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 114 --QPKDVMEVQAItlLEEVGLSKAYMDKYPNmLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRE 191
Cdd:PRK10982 106 vdQDKMYRDTKAI--FDELDIDIDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKE 182
|
170 180 190
....*....|....*....|....*....|
gi 446513169 192 tRQLSYIFITHDIQAATYLCDQLIIFKNGK 221
Cdd:PRK10982 183 -RGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-223 |
1.71e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.94 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 6 DVEKSYQSAHVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRHQ-IG 84
Cdd:TIGR01257 1936 DILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQnMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 85 AVFQdyTSSLHPFQTVREILFeVMCQCDGQPKDVMEVQAITLLEEVGLSkAYMDKYPNMLSGGEAQRVAIARAICINPKY 164
Cdd:TIGR01257 2016 YCPQ--FDAIDDLLTGREHLY-LYARLRGVPAEEIEKVANWSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 165 ILFDEAISSLDMSIQTQILDLLIH-LRETRQLsyIFITHDIQAATYLCDQLIIFKNGKIE 223
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSiIREGRAV--VLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-212 |
2.23e-07 |
|
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: 49.63 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 25 VKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEkpdkGCVTLNDQPmhkKKVRRHQIGAVFQdytsslhpfqtvreil 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYAS----GKARLISFL---PKFSRNKLIFIDQ---------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 105 fevmcqcdgqpkdvmevqaITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILF--DEAISSLDMSIQTQI 182
Cdd:cd03238 68 -------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFilDEPSTGLHQQDINQL 128
|
170 180 190
....*....|....*....|....*....|...
gi 446513169 183 LDLLIHLRETRQlSYIFITHD---IQAATYLCD 212
Cdd:cd03238 129 LEVIKGLIDLGN-TVILIEHNldvLSSADWIID 160
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-224 |
4.47e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 24 IVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKG---CVTlndqpmhKKKVrrhqigAVFQDYTSSLHPFQTV 100
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihCGT-------KLEV------AYFDQHRAELDPEKTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 101 REILFE----VMcqCDGQPKDVM---------EVQAITLLeevglsKAymdkypnmLSGGEAQRVAIARaICINPKYIL- 166
Cdd:PRK11147 401 MDNLAEgkqeVM--VNGRPRHVLgylqdflfhPKRAMTPV------KA--------LSGGERNRLLLAR-LFLKPSNLLi 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446513169 167 FDEAISSLDmsIQTqiLDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFK-NGKIEE 224
Cdd:PRK11147 464 LDEPTNDLD--VET--LELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGR 518
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-222 |
6.73e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.72 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVeksyqSAHVFKrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPM---HKKK 77
Cdd:PRK11614 5 MLSFDKV-----SAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRRHQIGAVFQDytSSLHPFQTVREIL-----FEVMCQCDGQPKDVMEVqaITLLEEVGLSKAymdkypNMLSGGEAQRV 152
Cdd:PRK11614 77 IMREAVAIVPEG--RRVFSRMTVEENLamggfFAERDQFQERIKWVYEL--FPRLHERRIQRA------GTMSGGEQQML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 153 AIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-226 |
2.16e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 19 RRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKK---VRRHQIGAVFQDY--TSS 93
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldAVKKGMAYITESRrdNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 94 LHPFQTVREILFEVMCQcDGQPK-------DVMEVQ-AITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYI 165
Cdd:PRK09700 353 FPNFSIAQNMAISRSLK-DGGYKgamglfhEVDEQRtAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446513169 166 LFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHDIQAATYLCDQLIIFKNGKIEEQI 226
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQIL 491
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
28-224 |
2.86e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 28 VSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGcvtlndqpmhkkKVRRHQIGAVFQDYTSSLHPFQTVREILFEV 107
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG------------KVDRNGEVSVIAISAGLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 108 MCQcDGQPKDVMEVQ-AITLLEEVG-LSKAYMDKYpnmlSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDL 185
Cdd:PRK13546 111 LCM-GFKRKEIKAMTpKIIEFSELGeFIYQPVKKY----SSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDK 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 446513169 186 LIHLRETRQlSYIFITHDIQAATYLCDQLIIFKNGKIEE 224
Cdd:PRK13546 186 IYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-222 |
2.96e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 15 HVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-------------RH 81
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRerrrlgvayipedRL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 82 QIGAVfQDYtsslhpfqTVREILfeVMCQCDGQP--------KDVMEVQAITLLEEvglskayMD-KYPN------MLSG 146
Cdd:COG3845 344 GRGLV-PDM--------SVAENL--ILGRYRRPPfsrggfldRKAIRAFAEELIEE-------FDvRTPGpdtparSLSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 147 GEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-222 |
4.67e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 15 HVFKRRRTP---IVKGVSFECPIGATIAIIGESGSGKSTLSRMIL----GIEKPDKGCVTLNDQPMHKkkVRRHQIGAVF 87
Cdd:TIGR00956 64 KLKKFRDTKtfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEE--IKKHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 88 QDYTSSLH-PFQTVREIL-FEVMCQCDG-QPKDVMEVQAITLLEEV-----GLSKAYMDKYPNML----SGGEAQRVAIA 155
Cdd:TIGR00956 142 YNAETDVHfPHLTVGETLdFAARCKTPQnRPDGVSREEYAKHIADVymatyGLSHTRNTKVGNDFvrgvSGGERKRVSIA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 156 RAICINPKYILFDEAISSLDMSIQTQILDLL-IHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALkTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQ 289
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-175 |
1.41e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLndQPMHKkkvrrhqIGAVFQDytSSLHPFQTVRE 102
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--APGIK-------VGYLPQE--PQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 103 IlfevmcqcdgqpkdVME-----VQAITLLEEV----GLSKAYMDKY--------------------------------P 141
Cdd:PRK11819 90 N--------------VEEgvaevKAALDRFNEIyaayAEPDADFDALaaeqgelqeiidaadawdldsqleiamdalrcP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446513169 142 ------NMLSGGEAQRVAIARAICINPKYILFDEAISSLD 175
Cdd:PRK11819 156 pwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-212 |
1.42e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 40 IIGESGSGKSTLSRmILGIEKP-DKGCVTLN----------DQPmhkkkvrRHQIGAVFqDYTSS--------LHPFQtv 100
Cdd:PRK11147 34 LVGRNGAGKSTLMK-ILNGEVLlDDGRIIYEqdlivarlqqDPP-------RNVEGTVY-DFVAEgieeqaeyLKRYH-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 101 rEILFEVMCQC-DGQPKDVMEVQAI--------------TLLEEVGLSKaymDKYPNMLSGGEAQRVAIARAICINPKYI 165
Cdd:PRK11147 103 -DISHLVETDPsEKNLNELAKLQEQldhhnlwqlenrinEVLAQLGLDP---DAALSSLSGGWLRKAALGRALVSNPDVL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446513169 166 LFDEAISSLDmsIQTqiLDLLIHLRETRQLSYIFITHD---IQA-ATYLCD 212
Cdd:PRK11147 179 LLDEPTNHLD--IET--IEWLEGFLKTFQGSIIFISHDrsfIRNmATRIVD 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-231 |
1.80e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.43 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 28 VSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR-RHQIGAVF--QD--------------- 89
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARGLVYlpEDrqssglyldaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 90 ---YTSSLHPF--QTVRE-ILFEVMCQcdgqpkdvmevqaitlleEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPK 163
Cdd:PRK15439 362 vcaLTHNRRGFwiKPAREnAVLERYRR------------------ALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446513169 164 YILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSAL 231
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-203 |
2.91e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 35 GATIAIIGESGSGKSTLSRMILG-IEKPDKGCVTLNDQPmhkkkvrrhqigavfqdytsslhpfqtvreilfevmcqcdg 113
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGED----------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 114 qpkdvmevqaITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDL-----LIH 188
Cdd:smart00382 41 ----------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLL 110
|
170
....*....|....*
gi 446513169 189 LRETRQLSYIFITHD 203
Cdd:smart00382 111 LKSEKNLTVILTTND 125
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-222 |
3.25e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVR---RHQIGAVFQDYT-SSLHPFQ 98
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglANGIVYISEDRKrDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 99 TVREIL----FEVMCQCDGQPKDVMEVQAITlleevGLSKAYMDKYPNM------LSGGEAQRVAIARAICINPKYILFD 168
Cdd:PRK10762 346 SVKENMsltaLRYFSRAGGSLKHADEQQAVS-----DFIRLFNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446513169 169 EAISSLDMSIQTQILDlLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKI 222
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-104 |
8.77e-05 |
|
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: 42.23 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 18 KRRRTPIVKGVSFECPIGATIAIIGESGSGKSTL-----SRMILGIEkpdKGCVTLNDQPmhKKKVRRHQIGAVFQDYTS 92
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLldvlaGRKTAGVI---TGEILINGRP--LDKNFQRSTGYVEQQDVH 90
|
90
....*....|..
gi 446513169 93 SlhPFQTVREIL 104
Cdd:cd03232 91 S--PNLTVREAL 100
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-223 |
8.97e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 28 VSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCV-------TLNDQPMHKKKVRRHQIGAVFQDYTSSLHpfQTV 100
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaersiaYVPQQAWIMNATVRGNILFFDEEDAARLA--DAV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 101 ReilfevMCQCDGqpkDVMEVQAitlleevGLSKAYMDKYPNmLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQT 180
Cdd:PTZ00243 757 R------VSQLEA---DLAQLGG-------GLETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446513169 181 QILD--LLIHLR-ETRQLSyifiTHDIQAATyLCDQLIIFKNGKIE 223
Cdd:PTZ00243 820 RVVEecFLGALAgKTRVLA----THQVHVVP-RADYVVALGDGRVE 860
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-212 |
2.06e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.47 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 26 KGVSFECPIGATIAIIGESGSGKSTLS--------------------RMILG-IEKPDKGCVTlndqpmhkkkvrrhqiG 84
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayaRQFLGqMDKPDVDSIE----------------G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 85 -----AVFQDYTSSlHPFQTVREI-----LFEVMCQCDGQpkdvmeVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAI 154
Cdd:cd03270 76 lspaiAIDQKTTSR-NPRSTVGTVteiydYLRLLFARVGI------RERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446513169 155 ARAICINPKYIL--FDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITHD---IQAATYLCD 212
Cdd:cd03270 149 ATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDedtIRAADHVID 210
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-175 |
4.02e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 18 KRRrtpIVKGVSFECPIGATIAIIGESGSGKSTLsrMILGIEKPDKGCVT-----LNDQPMHKKKVRRhqIGAVFQDyts 92
Cdd:TIGR00956 775 KRV---ILNNVDGWVKPGTLTALMGASGAGKTTL--LNVLAERVTTGVITggdrlVNGRPLDSSFQRS--IGYVQQQ--- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 93 SLH-PFQTVREIL-FEVMCQcdgQPKDV-----ME-VQA-ITLLEevglskayMDKYPNMLSG--GEA------QRVAIA 155
Cdd:TIGR00956 845 DLHlPTSTVRESLrFSAYLR---QPKSVsksekMEyVEEvIKLLE--------MESYADAVVGvpGEGlnveqrKRLTIG 913
|
170 180
....*....|....*....|.
gi 446513169 156 RAICINPKYILF-DEAISSLD 175
Cdd:TIGR00956 914 VELVAKPKLLLFlDEPTSGLD 934
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-239 |
4.77e-04 |
|
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: 40.28 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 2 IKIKDVEKSYQSAhvfkrrRTPIVKGVSFECPIGATIAIIGESGSGKSTLS----RMILGIE-KPDKGCVTLNDQPMHkk 76
Cdd:cd03288 20 IKIHDLCVRYENN------LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMVDIFDgKIVIDGIDISKLPLH-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 77 kVRRHQIGAVFQDytsslhPFQTVREILFEVMCQCDGQPKDVMEVQAITLLEEV------GLSKAYMDKYPNmLSGGEAQ 150
Cdd:cd03288 92 -TLRSRLSIILQD------PILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMvkslpgGLDAVVTEGGEN-FSVGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 151 RVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYI-FITHDIQAAtylcDQLIIFKNGKI-EEQIPT 228
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIaHRVSTILDA----DLVLVLSRGILvECDTPE 239
|
250
....*....|.
gi 446513169 229 SALHKSDNAYT 239
Cdd:cd03288 240 NLLAQEDGVFA 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-231 |
4.94e-04 |
|
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: 40.96 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 4 IKDV--EKSYQSAHVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGI-EKPDKGCVTLNDQPMHKK---K 77
Cdd:TIGR02633 253 IGDVilEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRnpaQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 78 VRRHQIGAVFQDYT----------------SSLHPFQTVreilfevmcqcdGQPKDVMEVQAI-TLLEEVGLSKAYMDKY 140
Cdd:TIGR02633 333 AIRAGIAMVPEDRKrhgivpilgvgknitlSVLKSFCFK------------MRIDAAAELQIIgSAIQRLKVKTASPFLP 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 141 PNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNG 220
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
250 260
....*....|....*....|.
gi 446513169 221 KI----------EEQIPTSAL 231
Cdd:TIGR02633 480 KLkgdfvnhaltQEQVLAAAL 500
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-202 |
8.07e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.77 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 1 MIKIKDVEKSYQSahvfkrrrTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIE--KPDKGCVTLNDQPMHKKKV 78
Cdd:PRK09580 1 MLSIKDLHVSVED--------KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 79 RRHQIGAVFQdytsslhPFQTVREI------------LFEVMCQCDGQPKDVMEVQaiTLLEEvglsKAYMDKYPNML-- 144
Cdd:PRK09580 73 EDRAGEGIFM-------AFQYPVEIpgvsnqfflqtaLNAVRSYRGQEPLDRFDFQ--DLMEE----KIALLKMPEDLlt 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446513169 145 -------SGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQlSYIFITH 202
Cdd:PRK09580 140 rsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTH 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-211 |
1.40e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.74 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 28 VSFECPIgatIAIIGESGSGKSTL---SRMILGIEKPDKGCVTLNDQPMHKKKVRRHQIGAVFQDYTSslHPFQTVREI- 103
Cdd:cd03240 18 IEFFSPL---TLIVGQNGAGKTTIieaLKYALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANG--KKYTITRSLa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 104 LFE--VMCQCDgqpkdvmEVQAItLLEEVGLskaymdkypnmLSGGE------AQRVAIARAICINPKYILFDEAISSLD 175
Cdd:cd03240 93 ILEnvIFCHQG-------ESNWP-LLDMRGR-----------CSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446513169 176 M-SIQTQILDLLIHLRETRQLSYIFITHD---IQAATYLC 211
Cdd:cd03240 154 EeNIEESLAEIIEERKSQKNFQLIVITHDeelVDAADHIY 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-223 |
1.42e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 23 PIVK---GVSFECPIGATIAIIGESGSGKSTLSRMILGI------EkpdkGCVTLNDQPMHKKKVR---RHQIGAVFQDY 90
Cdd:NF040905 12 PGVKaldDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGEVCRFKDIRdseALGIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 91 tsSLHPFQTVREILFEvmcqcdGQPK--------DVMEVQAITLLEEVGLSKAymdkyPNMLSG----GEAQRVAIARAI 158
Cdd:NF040905 88 --ALIPYLSIAENIFL------GNERakrgvidwNETNRRARELLAKVGLDES-----PDTLVTdigvGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446513169 159 CINPKYILFDEAISSLDMSIQTQILDLLIHLREtRQLSYIFITHDIQAATYLCDQLIIFKNGK-IE 223
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRtIE 219
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
38-55 |
2.97e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 37.39 E-value: 2.97e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
120-176 |
5.10e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.92 E-value: 5.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446513169 120 EVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDM 176
Cdd:PLN03073 321 EARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
124-212 |
6.54e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446513169 124 ITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAI---CINPKYILfDEAISSLDMSIQTQILDLLIHLRETRQlSYIFI 200
Cdd:TIGR00630 469 LGFLIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIgsgLTGVLYVL-DEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVV 546
|
90
....*....|....*
gi 446513169 201 THD---IQAATYLCD 212
Cdd:TIGR00630 547 EHDedtIRAADYVID 561
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
26-56 |
8.33e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 8.33e-03
10 20 30
....*....|....*....|....*....|.
gi 446513169 26 KGVSFECPIGATIAIIGESGSGKSTLSRMIL 56
Cdd:COG0178 622 KNVDVEIPLGVLTCVTGVSGSGKSTLVNDIL 652
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
38-56 |
8.86e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 36.69 E-value: 8.86e-03
|
| |
