|
Name |
Accession |
Description |
Interval |
E-value |
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-249 |
3.88e-148 |
|
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: 413.43 E-value: 3.88e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPYGSLHPRHTIGDILEEPLQIHGIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVL 160
Cdd:COG1124 81 VQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 161 LLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAGqAKTDYTQMLV 240
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG-PKHPYTRELL 239
|
....*....
gi 2084886466 241 NASQQYSRE 249
Cdd:COG1124 240 AASLAFERA 248
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-242 |
3.05e-112 |
|
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: 332.25 E-value: 3.05e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEK-RNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRIS---RE 76
Cdd:COG1123 260 LLEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCRRVQMVFQDPYGSLHPRHTIGDILEEPLQIHGI---KDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARAL 153
Cdd:COG1123 340 LRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLlsrAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAgQAKT 233
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA-NPQH 498
|
....*....
gi 2084886466 234 DYTQMLVNA 242
Cdd:COG1123 499 PYTRALLAA 507
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
8.33e-108 |
|
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: 310.59 E-value: 8.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEK---RISRER 77
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 CRRVQMVFQDPYGSLHPRHTIGDILEEPLQIHGIKDRDS----RIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARAL 153
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEarkeAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-242 |
2.36e-107 |
|
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: 313.14 E-value: 2.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHW---DGELAIDGKPL----EKRI 73
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLlklsEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 74 SRERCRRVQMVFQDPYGSLHPRHTIGDILEEPLQIHGI---KDRDSRIHTLLDKVGLNRAFR--DRYPHQLSGGQRQRVA 148
Cdd:COG0444 81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGlskAEARERAIELLERVGLPDPERrlDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 149 IARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMqY-GKILDSLTVDALV 227
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM-YaGRIVEEGPVEELF 239
|
250
....*....|....*
gi 2084886466 228 AgQAKTDYTQMLVNA 242
Cdd:COG0444 240 E-NPRHPYTRALLSS 253
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-242 |
7.28e-107 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 312.05 E-value: 7.28e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKP---LEKRISRERCRRVQMVFQDPYGSLHPRHT 97
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDPYASLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 IGDILEEPLQIHGI---KDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQ 174
Cdd:COG4608 114 VGDIIAEPLRIHGLaskAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 175 AEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAgQAKTDYTQMLVNA 242
Cdd:COG4608 194 AQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYA-RPLHPYTQALLSA 260
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-243 |
7.16e-102 |
|
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: 306.23 E-value: 7.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHwDGELAIDGKPLEKRISRER---CRRVQMVFQDPYGSLHPRHT 97
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRALrplRRRMQVVFQDPFGSLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 IGDILEEPLQIHGI----KDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:COG4172 381 VGQIIAEGLRVHGPglsaAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 174 QAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAgQAKTDYTQMLVNAS 243
Cdd:COG4172 461 QAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFD-APQHPYTRALLAAA 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-243 |
5.46e-83 |
|
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: 257.69 E-value: 5.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKT----TVLKCLAGLFTHWDGELAIDGKPL----EKR 72
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglsERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 73 ISRERCRRVQMVFQDPYGSLHPRHTIGDILEEPLQIH-GIKDRD--SRIHTLLDKVGLNRAFR--DRYPHQLSGGQRQRV 147
Cdd:COG4172 86 LRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHrGLSGAAarARALELLERVGIPDPERrlDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALV 227
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
250
....*....|....*.
gi 2084886466 228 AgQAKTDYTQMLVNAS 243
Cdd:COG4172 246 A-APQHPYTRKLLAAE 260
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
11-253 |
2.86e-80 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 244.49 E-value: 2.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 11 FGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL---EKRISRERCRRVQMVFQD 87
Cdd:PRK11308 21 LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 PYGSLHPRHTIGDILEEPLQIH---GIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDE 164
Cdd:PRK11308 101 PYGSLNPRKKVGQILEEPLLINtslSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 165 PTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAgQAKTDYTQMLVNASQ 244
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFN-NPRHPYTQALLSATP 259
|
....*....
gi 2084886466 245 QYSREMARE 253
Cdd:PRK11308 260 RLNPDDRRE 268
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
1.43e-74 |
|
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: 235.57 E-value: 1.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTH---WDGELAIDGKPLEKRISRER 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 CRRVQMVFQDPYGSLHPrHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALIL 155
Cdd:COG1123 82 GRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGLsrAEARARVLELLEAVGLER-RLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 156 EPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
16-242 |
7.59e-74 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 225.87 E-value: 7.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 16 KRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPYGSLHPR 95
Cdd:COG4167 24 QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPNTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 HTIGDILEEPLQIH---GIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVS 172
Cdd:COG4167 104 LNIGQILEEPLRLNtdlTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMS 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 173 VQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAgQAKTDYTQMLVNA 242
Cdd:COG4167 184 VRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA-NPQHEVTKRLIES 252
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
3.15e-70 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 216.49 E-value: 3.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLekrisRERCRR 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPygSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQ 158
Cdd:COG1116 82 RGVVFQEP--ALLPWLTVLDNVALGLELRGVpkAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVM--QYGKILDSLTVD 224
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEIDVD 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-241 |
1.60e-69 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 217.25 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL----EKRISRE 76
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RcRRVQMVFQDPygSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:COG1135 81 R-RKIGMIFQHF--NLLSSRTVAENVALPLEIAGVpkAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAgQAKTD 234
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA-NPQSE 235
|
....*..
gi 2084886466 235 YTQMLVN 241
Cdd:COG1135 236 LTRRFLP 242
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-224 |
4.24e-69 |
|
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: 212.33 E-value: 4.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLekrisRERCRRV 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPygSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQV 159
Cdd:cd03293 76 GYVFQQD--ALLPWLTVLDNVALGLELQGVpkAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQY--GKILDSLTVD 224
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEVD 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
2.04e-68 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 210.67 E-value: 2.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL----EKRISRE 76
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCRRVQMVFQDPYgsLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:COG1136 84 RRRHIGFVFQFFN--LLPELTALENVALPLLLAGVsrKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLgVIAHLCQKVAVMQYGKI 217
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
2.67e-68 |
|
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: 210.52 E-value: 2.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKP---LEKRISRER 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 CRRVQMVFQDpYGSLHPRHTIGDIlEEPLQIHGI--KDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALIL 155
Cdd:cd03258 81 RRRIGMIFQH-FNLLSSRTVFENV-ALPLEIAGVpkAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 156 EPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTV 223
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-217 |
8.47e-68 |
|
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: 208.88 E-value: 8.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL----EKRISRER 77
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 CRRVQMVFQDPYgsLHPRHTIGDILEEPLQIHGIK--DRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALIL 155
Cdd:cd03255 81 RRHIGFVFQSFN--LLPDLTALENVELPLLLAGVPkkERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 156 EPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLgVIAHLCQKVAVMQYGKI 217
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-242 |
1.18e-66 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 209.56 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 22 DNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRIS---RERCRRVQMVFQDPYGSLHPRHTI 98
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewRAVRSDIQMIFQDPLASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 99 GDILEEPLQIH-------GIKDRdsrIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDV 171
Cdd:PRK15079 118 GEIIAEPLRTYhpklsrqEVKDR---VKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 172 SVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAgQAKTDYTQMLVNA 242
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYH-NPLHPYTKALMSA 264
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
2.81e-65 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 206.87 E-value: 2.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEkRISRERcRR 80
Cdd:COG3842 5 ALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPEK-RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDpYgSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQ 158
Cdd:COG3842 79 VGMVFQD-Y-ALFPHLTVAENVAFGLRMRGVpkAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLG---VIAHlcqKVAVMQYGKIL 218
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEealALAD---RIAVMNDGRIE 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-218 |
7.98e-65 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 201.76 E-value: 7.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL---EKRISRER 77
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdsKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 cRRVQMVFQDPygSLHPRHTIGD-ILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:COG1126 77 -RKVGMVFQQF--NLFPHLTVLEnVTLAPIKVKKMskAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDLA-KEGMTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-228 |
1.83e-64 |
|
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: 200.98 E-value: 1.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERC-- 78
Cdd:COG1127 5 MIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 -RRVQMVFQDP--YGSLhprhTIGDILEEPLQIHGIKDRD---SRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARA 152
Cdd:COG1127 81 rRRIGMLFQGGalFDSL----TVFENVAFPLREHTDLSEAeirELVLEKLELVGL-PGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 153 LILEPQVLLLDEPTSALD-VSVqAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:COG1127 156 LALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-228 |
2.10e-64 |
|
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: 200.64 E-value: 2.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRV 81
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPYGSLhprhtIGDILEE-----PLQIhGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:COG1122 78 GLVFQNPDDQL-----FAPTVEEdvafgPENL-GLprEEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-243 |
4.77e-62 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 203.40 E-value: 4.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFG--EGEKR-----NQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHwDGELAIDGKPLEKRI 73
Cdd:PRK15134 275 LLDVEQLQVAFPirKGILKrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 74 SRERC---RRVQMVFQDPYGSLHPRHTIGDILEEPLQIH----GIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQR 146
Cdd:PRK15134 354 RRQLLpvrHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqptlSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 147 VAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
250
....*....|....*..
gi 2084886466 227 VAGqAKTDYTQMLVNAS 243
Cdd:PRK15134 514 FAA-PQQEYTRQLLALS 529
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-229 |
1.62e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 193.36 E-value: 1.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRiSRERCRRV 81
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD-PAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPygSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQV 159
Cdd:COG1131 76 GYVPQEP--ALYPDLTVRENLRFFARLYGLprKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAG 229
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
2.18e-61 |
|
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: 192.35 E-value: 2.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrRV 81
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR--NI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPygSLHPRHTIGDILEEPLQIHGIK--DRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQV 159
Cdd:cd03259 75 GMVFQDY--ALFPHLTVAENIAFGLKLRGVPkaEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-223 |
5.27e-61 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 193.36 E-value: 5.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKrISRERC----RRVQMVFQDPYGSLHP 94
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK-LNRAQRkafrRDIQMVFQDSISAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 95 RHTIGDILEEPLQiHGI----KDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALD 170
Cdd:PRK10419 105 RKTVREIIREPLR-HLLsldkAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 171 VSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTV 223
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-227 |
3.47e-60 |
|
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: 190.64 E-value: 3.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:COG1120 1 MLEAENLSVGYG----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPygSLHPRHTIGDILE-------EPLQIHGIKDRDsRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARAL 153
Cdd:COG1120 77 IAYVPQEP--PAPFGLTVRELVAlgryphlGLFGRPSAEDRE-AVEEALERTGL-EHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALV 227
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-223 |
8.35e-60 |
|
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: 190.02 E-value: 8.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 17 RNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEK--RISRERCRR-VQMVFQDPYGSLH 93
Cdd:TIGR02769 23 RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldRKQRRAFRRdVQLVFQDSPSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 PRHTIGDILEEPLQIHGIKD---RDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALD 170
Cdd:TIGR02769 103 PRMTVRQIIGEPLRHLTSLDeseQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 171 VSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTV 223
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-217 |
1.32e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 187.72 E-value: 1.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGekrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEkRISRERCRR- 80
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS-AMPPPEWRRq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPYgsLhPRHTIGDILEEPLQIHGIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVL 160
Cdd:COG4619 76 VAYVPQEPA--L-WGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 161 LLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-242 |
1.74e-59 |
|
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: 188.53 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcRR 80
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPYgsLHPRHTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQ 158
Cdd:COG4555 76 IGVLPDERG--LYDRLTVRENIRYFAELYGLFDEElkKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAGQAKTDYTQM 238
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDA 231
|
....
gi 2084886466 239 LVNA 242
Cdd:COG4555 232 FVAL 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-216 |
3.08e-59 |
|
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: 186.52 E-value: 3.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 3 EINHLNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQ 82
Cdd:cd03225 1 ELKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 83 MVFQDpygslhPRH-----TIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALIL 155
Cdd:cd03225 79 LVFQN------PDDqffgpTVEEEVAFGLENLGLpeEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 156 EPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-228 |
5.41e-59 |
|
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: 186.94 E-value: 5.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERC--- 78
Cdd:cd03261 1 IELRGLTKSFGG----RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 RRVQMVFQDP--YGSLhprhTIGDILEEPLQIHGiKDRDSRIHTL----LDKVGLnRAFRDRYPHQLSGGQRQRVAIARA 152
Cdd:cd03261 77 RRMGMLFQSGalFDSL----TVFENVAFPLREHT-RLSEEEIREIvlekLEAVGL-RGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 153 LILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-244 |
1.23e-58 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 186.04 E-value: 1.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 22 DNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLF----THWDGELAIDGKPLEKriSRERCRRVQMVFQDPYGSLHPRHT 97
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLppglTQTSGEILLDGRPLLP--LSIRGRHIATIMQNPRTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 IGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNRAFR--DRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:TIGR02770 81 MGNHAIETLRSLGKlsKQARALILEALEAVGLPDPEEvlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 174 QAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAgQAKTDYTQMLVNASQ 244
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFY-NPKHETTRKLLSAHL 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-216 |
2.25e-58 |
|
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: 183.54 E-value: 2.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL--EKRISRERCR 79
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 80 RVQMVFQDPygSLHPRHTIGDILEEPLqihgikdrdsrihtlldkvglnrafrdryphqlSGGQRQRVAIARALILEPQV 159
Cdd:cd03229 77 RIGMVFQDF--ALFPHLTVLENIALGL---------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-217 |
1.84e-57 |
|
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: 182.34 E-value: 1.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL---EKRISRERc 78
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 RRVQMVFQDPYgsLHPRHTI-GDILEEPLQIHGIKDRDS--RIHTLLDKVGL-NRAfrDRYPHQLSGGQRQRVAIARALI 154
Cdd:cd03262 76 QKVGMVFQQFN--LFPHLTVlENITLAPIKVKGMSKAEAeeRALELLEKVGLaDKA--DAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-217 |
6.94e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 184.97 E-value: 6.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRIS-RERcrR 80
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPpRER--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPygSLHPRHTIGDILEEPLQI--HGIKDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQ 158
Cdd:COG1118 77 VGFVFQHY--ALFPHMTVAENIAFGLRVrpPSKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-242 |
7.21e-57 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 189.53 E-value: 7.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKT-TVLKCLAGLFT----HWDGELAIDGKPL----EK 71
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESLlhasEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 72 RISRERCRRVQMVFQDPYGSLHPRHTIGDILEEPLQIH-GIKDRDSR--IHTLLDKVGLNRAFR--DRYPHQLSGGQRQR 146
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHrGMRREAARgeILNCLDRVGIRQAAKrlTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 147 VAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250
....*....|....*.
gi 2084886466 227 VAgQAKTDYTQMLVNA 242
Cdd:PRK15134 245 FS-APTHPYTQKLLNS 259
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-223 |
1.81e-56 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 183.85 E-value: 1.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL----EKRISRE 76
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RcRRVQMVFQdpYGSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:PRK11153 81 R-RQIGMIFQ--HFNLLSSRTVFDNVALPLELAGTpkAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTV 223
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTV 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-219 |
2.27e-56 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 183.39 E-value: 2.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT---HWDGELAIDGKPL----EKRI 73
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREIlnlpEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 74 SRERCRRVQMVFQDPYGSLHPRHTIGDILEEPLQIH-GIKDRDSRIHT--LLDKVGLNRAfRDR---YPHQLSGGQRQRV 147
Cdd:PRK09473 92 NKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGMSKAEAFEESvrMLDAVKMPEA-RKRmkmYPHEFSGGMRQRV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAV------MQYGKILD 219
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVmyagrtMEYGNARD 248
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-226 |
2.89e-56 |
|
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: 179.68 E-value: 2.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGL-----FTHWDGELAIDGKPLEKRISR- 75
Cdd:cd03260 1 IELRDLNVYYGD----KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 -ERCRRVQMVFQDPYgslhP-RHTIGDILEEPLQIHGIKDR---DSRIHTLLDKVGLNRAFRDR-YPHQLSGGQRQRVAI 149
Cdd:cd03260 77 lELRRRVGMVFQKPN----PfPGSIYDNVAYGLRLHGIKLKeelDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 150 ARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-219 |
2.34e-55 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 177.17 E-value: 2.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL----EKRISRE 76
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RcRRVQMVFQDpyGSLHPRHTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:COG2884 78 R-RRIGVVFQD--FRLLPDRTVYENVALPLRVTGKSRKEirRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILD 219
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
2.94e-55 |
|
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: 175.32 E-value: 2.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 3 EINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQ 82
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 83 MVFQdpygslhprhtigdileeplqihgikdrdsrihtLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLL 162
Cdd:cd03214 77 YVPQ----------------------------------ALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 163 DEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-242 |
7.32e-54 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 174.98 E-value: 7.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAF--GEGEKRNQVLD---NVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISR 75
Cdd:PRK15112 4 LLEVRNLSKTFryRTGWFRRQTVEavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 ERCRRVQMVFQDPYGSLHPRHTIGDILEEPLQIH---GIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARA 152
Cdd:PRK15112 84 YRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNtdlEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 153 LILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILD-SLTVDALVAGQA 231
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVErGSTADVLASPLH 243
|
250
....*....|.
gi 2084886466 232 ktDYTQMLVNA 242
Cdd:PRK15112 244 --ELTKRLIAG 252
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-218 |
1.76e-53 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 176.42 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrR 80
Cdd:COG3839 3 SLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR--N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPygSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQ 158
Cdd:COG3839 77 IAMVFQSY--ALYPHMTVYENIAFPLKLRKVpkAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 159 VLLLDEPTSALD----VSVQAEIlnllVELQCESNLTYLMVTHD------LGviahlcQKVAVMQYGKIL 218
Cdd:COG3839 154 VFLLDEPLSNLDaklrVEMRAEI----KRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDGRIQ 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-217 |
4.29e-53 |
|
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: 171.65 E-value: 4.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGekrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrRV 81
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR--PV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDpYgSLHPRHTIGDILEEPLQIHGIK--DRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQV 159
Cdd:cd03300 75 NTVFQN-Y-ALFPHLTVFENIAFGLRLKKLPkaEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-219 |
2.01e-51 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 176.97 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGK---PLEKRISRERCRRVQMVFQDPYGSLHPRHT 97
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 IGDILEEPLQIHGIKDRD---SRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQ 174
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKaaaARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2084886466 175 AEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILD 219
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-218 |
1.09e-50 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 166.86 E-value: 1.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEG---EKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGK---PLEKRISR 75
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfEK--KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 ERCRRVQMVFQdpygslHPRH-----TIG-DILEEPLQIhGI--KDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRV 147
Cdd:TIGR04521 79 DLRKKVGLVFQ------FPEHqlfeeTVYkDIAFGPKNL-GLseEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-252 |
4.60e-50 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 166.84 E-value: 4.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTH----WDGELAIDGKPLEKRISRE 76
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCR----RVQMVFQDPYGSLHPRHTIGDILEEPLQIH---GIKDRDSRIHTLLDKVGL-NRAFR-DRYPHQLSGGQRQRV 147
Cdd:PRK11022 83 RRNlvgaEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHqggNKKTRRQRAIDLLNQVGIpDPASRlDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALV 227
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250 260
....*....|....*....|....*
gi 2084886466 228 AgQAKTDYTQMLVNASQQYSREMAR 252
Cdd:PRK11022 243 R-APRHPYTQALLRALPEFAQDKAR 266
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
7.87e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 163.72 E-value: 7.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRisrerCRR 80
Cdd:COG1121 6 AIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 V----QMVFQDP--------------YGSLHPrhtigdileepLQIHGIKDRDsRIHTLLDKVGLnRAFRDRYPHQLSGG 142
Cdd:COG1121 77 IgyvpQRAEVDWdfpitvrdvvlmgrYGRRGL-----------FRRPSRADRE-AVDEALERVGL-EDLADRPIGELSGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 143 QRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVM 212
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-225 |
9.02e-50 |
|
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: 163.37 E-value: 9.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL----EKRISRE 76
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCRRVQMVFQdpygSLH--PRHTIgdiLEE---PLQIHGIKDRDSRIHTLLDKVGL-NRAfrDRYPHQLSGGQRQRVAIA 150
Cdd:COG4181 88 RARHVGFVFQ----SFQllPTLTA---LENvmlPLELAGRRDARARARALLERVGLgHRL--DHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 151 RALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGvIAHLCQKVAVMQYGKILDSLTVDA 225
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-216 |
1.10e-49 |
|
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: 160.49 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 3 EINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQ 82
Cdd:cd00267 1 EIENLSFRYGG----RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 83 MVFQdpygslhprhtigdileeplqihgikdrdsrihtlldkvglnrafrdryphqLSGGQRQRVAIARALILEPQVLLL 162
Cdd:cd00267 77 YVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 163 DEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:cd00267 105 DEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-217 |
2.27e-49 |
|
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: 162.51 E-value: 2.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrRV 81
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDpYgSLHPRHTIGDILEEPLQIHGIKDRDS------RIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALIL 155
Cdd:cd03296 77 GFVFQH-Y-ALFRHMTVFDNVAFGLRVKPRSERPPeaeiraKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 156 EPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-217 |
5.11e-49 |
|
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: 159.10 E-value: 5.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRiSRERCRRV 81
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKE-PEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPygSLHPRHTIGDILEeplqihgikdrdsrihtlldkvglnrafrdryphqLSGGQRQRVAIARALILEPQVLL 161
Cdd:cd03230 76 GYLPEEP--SLYENLTVRENLK-----------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 162 LDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-251 |
7.85e-49 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 163.92 E-value: 7.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT----------HWDGelaIDgkpLE 70
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtadrfRWNG---ID---LL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 71 KRISRER----CRRVQMVFQDPYGSLHPRHTIGDILEEPLQIHGIK--------DRDSRIHTLLDKVGL--NRAFRDRYP 136
Cdd:COG4170 77 KLSPRERrkiiGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKgkwwqrfkWRKKRAIELLHRVGIkdHKDIMNSYP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 137 HQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQ 236
|
250 260 270
....*....|....*....|....*....|....*
gi 2084886466 217 ILDSLTVDALVAgQAKTDYTQMLVNASQQYSREMA 251
Cdd:COG4170 237 TVESGPTEQILK-SPHHPYTKALLRSMPDFRQPLP 270
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-220 |
9.37e-49 |
|
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: 164.12 E-value: 9.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINhLNLAFGEGEkrnqvLDnVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL---EKRISR-- 75
Cdd:COG4148 2 MLEVD-FRLRRGGFT-----LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsARGIFLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 ERcRRVQMVFQDPygSLHPRHTIGDILEEPLQIHGIKDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALIL 155
Cdd:COG4148 75 HR-RRIGYVFQEA--RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 156 EPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDS 220
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
1.41e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 160.61 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERC-- 78
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 -RRVQMVFQDPY-------------GSLH----PRHTIGDILEEplqihgikDRDsRIHTLLDKVGL-NRAFRdRyPHQL 139
Cdd:COG3638 79 rRRIGMIFQQFNlvprlsvltnvlaGRLGrtstWRSLLGLFPPE--------DRE-RALEALERVGLaDKAYQ-R-ADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 140 SGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL- 218
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVf 227
|
250
....*....|..
gi 2084886466 219 ----DSLTVDAL 226
Cdd:COG3638 228 dgppAELTDAVL 239
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-228 |
7.89e-48 |
|
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: 168.09 E-value: 7.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKrISRERCRR- 80
Cdd:COG2274 474 IELENVSFRYPGDSP--PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ-IDPASLRRq 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPY---GSL-------HPRHTIGDILE--EPLQIHG-IKDRDSRIHTLLDKVGLNrafrdryphqLSGGQRQRV 147
Cdd:COG2274 551 IGVVLQDVFlfsGTIrenitlgDPDATDEEIIEaaRLAGLHDfIEALPMGYDTVVGEGGSN----------LSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqcESNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALV 227
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELL 697
|
.
gi 2084886466 228 A 228
Cdd:COG2274 698 A 698
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-218 |
8.37e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 160.26 E-value: 8.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLeKRISRERCRR 80
Cdd:COG1125 1 MIEFENVTKRYPDGTV---AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDI-RDLDPVELRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 vQM--VFQDpyGSLHPRHTIGD-ILEEP-LQIHGIKDRDSRIHTLLDKVGLNRA-FRDRYPHQLSGGQRQRVAIARALIL 155
Cdd:COG1125 77 -RIgyVIQQ--IGLFPHMTVAEnIATVPrLLGWDKERIRARVDELLELVGLDPEeYRDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 156 EPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIV 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-167 |
1.03e-47 |
|
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: 155.11 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPygSLHPRHTIGD 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 101 ILEEPLQIHGIKDR--DSRIHTLLDKVGLNrAFRDR----YPHQLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:pfam00005 79 NLRLGLLLKGLSKRekDARAEEALEKLGLG-DLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-235 |
1.60e-47 |
|
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: 158.58 E-value: 1.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFG-----------EGEKRNQVLD---------NVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGE 61
Cdd:cd03294 1 IKIKGLYKIFGknpqkafkllaKGKSKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 62 LAIDGKPL----EKRISRERCRRVQMVFQDpYGsLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRY 135
Cdd:cd03294 81 VLIDGQDIaamsRKELRELRRKKISMVFQS-FA-LLPHRTVLENVAFGLEVQGVprAEREERAAEALELVGL-EGWEHKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 136 PHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYG 215
Cdd:cd03294 158 PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDG 237
|
250 260
....*....|....*....|
gi 2084886466 216 KILDSLTVDALVAGQAkTDY 235
Cdd:cd03294 238 RLVQVGTPEEILTNPA-NDY 256
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-230 |
3.85e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 156.71 E-value: 3.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDG-------KPLEKRIS 74
Cdd:PRK11124 3 IQLNGINCFYGA----HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 75 RERcRRVQMVFQDpYgSLHPRHT-IGDILEEPLQIHGIKDRDS--RIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIAR 151
Cdd:PRK11124 79 ELR-RNVGMVFQQ-Y-NLWPHLTvQQNLIEAPCRVLGLSKDQAlaRAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 152 ALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAGQ 230
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQ 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-220 |
4.04e-47 |
|
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: 157.59 E-value: 4.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL--EKRISRERcR 79
Cdd:TIGR04520 1 IEVENVSFSYPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldEENLWEIR-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 80 RVQMVFQDPYGSLhprhtIGDILEEP----LQIHGIkDRD---SRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARA 152
Cdd:TIGR04520 78 KVGMVFQNPDNQF-----VGATVEDDvafgLENLGV-PREemrKRVDEALKLVGME-DFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 153 LILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGViAHLCQKVAVMQYGKILDS 220
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEE-AVLADRVIVMNKGKIVAE 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-216 |
4.64e-47 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 154.08 E-value: 4.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRV 81
Cdd:cd03228 1 IEFKNVSFSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPY---GSLhpRHTIgdileeplqihgikdrdsrihtlldkvglnrafrdryphqLSGGQRQRVAIARALILEPQ 158
Cdd:cd03228 79 AYVPQDPFlfsGTI--RENI----------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELQCESnlTYLMVTHDLGVIAHlCQKVAVMQYGK 216
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-217 |
5.16e-47 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 159.86 E-value: 5.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrRV 81
Cdd:PRK10851 3 IEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR--KV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDpYGSLhpRH-TIGDILEEPLQIHGIKDR------DSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:PRK10851 77 GFVFQH-YALF--RHmTVFDNIAFGLTVLPRRERpnaaaiKAKVTQLLEMVQLAH-LADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-217 |
6.82e-47 |
|
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: 155.11 E-value: 6.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrRV 81
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR--DI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDpYgSLHPRHTIGDILEEPLQIHGIKDR--DSRIHTLLDKVGLNRAFrDRYPHQLSGGQRQRVAIARALILEPQV 159
Cdd:cd03301 75 AMVFQN-Y-ALYPHMTVYDNIAFGLKLRKVPKDeiDERVREVAELLQIEHLL-DRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-246 |
8.47e-47 |
|
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: 155.92 E-value: 8.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRV 81
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPygSLHPRHTIGDILEEPLQIHGIKD--RDSRIHTLLDKVGLNRA-FRDRYPHQLSGGQRQRVAIARALILEPQ 158
Cdd:cd03295 78 GYVIQQI--GLFPHMTVEENIALVPKLLKWPKekIRERADELLALVGLDPAeFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAGQAkTDYTQM 238
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPA-NDFVAE 234
|
....*...
gi 2084886466 239 LVNASQQY 246
Cdd:cd03295 235 FVGADRLL 242
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-218 |
9.46e-47 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 155.18 E-value: 9.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL----EKRISRER 77
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELhgasKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 cRRVQMVFQ--DPYGSLHPRHTIGDILEepLQIH-GIKDRDSRIHTLLDKVGLNRAFrDRYPHQLSGGQRQRVAIARALI 154
Cdd:TIGR02982 82 -RRIGYIFQahNLLGFLTARQNVQMALE--LQPNlSYQEARERARAMLEAVGLGDHL-NYYPHNLSGGQKQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHD---LGVIAHLCQkvavMQYGKIL 218
Cdd:TIGR02982 158 HHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDnriLDVADRILQ----MEDGKLL 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-232 |
1.25e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 155.56 E-value: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDG-------KPLEKRIS 74
Cdd:COG4161 3 IQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 75 RERcRRVQMVFQDpYgSLHPRHTIGD-ILEEPLQIHGIKDRDSRIHT--LLDKVGLNRaFRDRYPHQLSGGQRQRVAIAR 151
Cdd:COG4161 79 LLR-QKVGMVFQQ-Y-NLWPHLTVMEnLIEAPCKVLGLSKEQAREKAmkLLARLRLTD-KADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 152 ALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAGQA 231
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQPQT 233
|
.
gi 2084886466 232 K 232
Cdd:COG4161 234 E 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-217 |
2.72e-46 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 154.48 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQ--MVFQDPYgsLHPRHTIgdiLEE----PLQIHGIKDRDSR--IHTLLDKVGL-NRAfrDRYPHQLSGGQRQRVAIAR 151
Cdd:PRK09493 77 QEagMVFQQFY--LFPHLTA---LENvmfgPLRVRGASKEEAEkqARELLAKVGLaERA--HHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 152 ALILEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGviahLCQKVA----VMQYGKI 217
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIG----FAEKVAsrliFIDKGRI 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-218 |
6.59e-46 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 156.80 E-value: 6.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRER--Cr 79
Cdd:PRK11432 7 VVLKNITKRFG----SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdiC- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 80 rvqMVFQDpYgSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEP 157
Cdd:PRK11432 82 ---MVFQS-Y-ALFPHMSLGENVGYGLKMLGVpkEERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 158 QVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-231 |
9.28e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 152.99 E-value: 9.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRnqvldnVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL-EKRISRercR 79
Cdd:COG3840 1 MLRLDDLTYRYGDFPLR------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtALPPAE---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 80 RVQMVFQDpyGSLHP----RHTIGdileepLQIH-GIK----DRdSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIA 150
Cdd:COG3840 72 PVSMLFQE--NNLFPhltvAQNIG------LGLRpGLKltaeQR-AQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 151 RALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAGQ 230
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
.
gi 2084886466 231 A 231
Cdd:COG3840 222 P 222
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-217 |
3.70e-45 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 151.49 E-value: 3.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrRV 81
Cdd:TIGR00968 1 IEIANISKRFG----SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDR--KI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQdpYGSLHPRHTIGDILEEPLQI--HGIKDRDSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQV 159
Cdd:TIGR00968 75 GFVFQ--HYALFKHLTVRDNIAFGLEIrkHPKAKIKARVEELLELVQLEG-LGDRYPNQLSGGQRQRVALARALAVEPQV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:TIGR00968 152 LLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-212 |
4.03e-45 |
|
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: 150.76 E-value: 4.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 3 EINHLNLAFGEGEkrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKR---------- 72
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKErkrigyvpqr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 73 --ISRERCRRV-QMVfqdpygSLHPRHTIGdileePLQIHGIKDRDsRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAI 149
Cdd:cd03235 77 rsIDRDFPISVrDVV------LMGLYGHKG-----LFRRLSKADKA-KVDEALERVGLS-ELADRQIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 150 ARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVM 212
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-244 |
5.39e-45 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 151.78 E-value: 5.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 22 DNVNISVKEGEIYGLVGESGSGKTtvLKCLAGL------FTHWDGELAIDGKPLEKriSRERCRRVQMVFQDPYGSLHPR 95
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGRVLLDGKPVAP--CALRGRKIATIMQNPRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 HTIGDILEEPLQIHGIKDRDSRIHTLLDKVGLNRAFR--DRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:PRK10418 96 HTMHTHARETCLALGKPADDATLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 174 QAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAgQAKTDYTQMLVNASQ 244
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN-APKHAVTRSLVSAHL 245
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-217 |
6.21e-45 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 150.58 E-value: 6.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEK----RISRE 76
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlssnERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCRRVQMVFQdpYGSLHPRHTIGDILEEPLQIHGIKDRDS--RIHTLLDKVGL-NRAfrDRYPHQLSGGQRQRVAIARAL 153
Cdd:TIGR02211 81 RNKKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKSVKEAkeRAYEMLEKVGLeHRI--NHRPSELSGGERQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLcQKVAVMQYGKI 217
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-217 |
8.62e-45 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 154.04 E-value: 8.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPlekrISRE--RCR 79
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRD----ITRLppQKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 80 RVQMVFQDpYgSLHPRHTIGDILEEPLQIHGIK--DRDSRIHTLLDKVGLNRAfRDRYPHQLSGGQRQRVAIARALILEP 157
Cdd:TIGR03265 77 DYGIVFQS-Y-ALFPNLTVADNIAYGLKNRGMGraEVAERVAELLDLVGLPGS-ERKYPGQLSGGQQQRVALARALATSP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 158 QVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:TIGR03265 154 GLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-217 |
2.59e-44 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 149.80 E-value: 2.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLF-----THWDGELAIDGKP-LEKRISR 75
Cdd:COG1117 12 IEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDiYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 ERCR-RVQMVFQDPygslHP-RHTIGDILEEPLQIHGIKDR---DSRIHTLLDKVGLNRAFRDR---YPHQLSGGQRQRV 147
Cdd:COG1117 88 VELRrRVGMVFQKP----NPfPKSIYDNVAYGLRLHGIKSKselDEIVEESLRKAALWDEVKDRlkkSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 148 AIARALILEPQVLLLDEPTSALD-VSVQAeILNLLVELQceSNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELK--KDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
2.62e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 150.01 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRiSRERcrr 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-GADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 vQMVFQDpyGSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQ 158
Cdd:COG4525 79 -GVVFQK--DALLPWLNVLDNVAFGLRLRGVpkAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHD 198
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-219 |
4.83e-44 |
|
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: 148.64 E-value: 4.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrnqvLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGK-----PLEKRisre 76
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlPPEKR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 rcrRVQMVFQDPYgsLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNRAFrDRYPHQLSGGQRQRVAIARALI 154
Cdd:cd03299 72 ---DISYVPQNYA--LFPHMTVYKNIAYGLKKRKVdkKEIERKVLEIAEMLGIDHLL-NRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILD 219
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
1.34e-43 |
|
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: 147.88 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:COG0411 4 LLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 -VQMVFQDP--YGSL-------------HPRHTIGDILEEPLQIHGIKDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQR 144
Cdd:COG0411 80 gIARTFQNPrlFPELtvlenvlvaaharLGRGLLAALLRLPRARREEREARERAEELLERVGL-ADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 145 QRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-242 |
2.18e-43 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 155.01 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKR-------- 72
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRsrqviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 73 -ISRERCRRVQ-----MVFQDPYGSLHPRHTIGDILEEPLQIHGIKDRDSRI---HTLLDKVGL--NRAFRDRYPHQLSG 141
Cdd:PRK10261 92 eQSAAQMRHVRgadmaMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMveaKRMLDQVRIpeAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 142 GQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSL 221
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|.
gi 2084886466 222 TVDALVAGQAKTdYTQMLVNA 242
Cdd:PRK10261 252 SVEQIFHAPQHP-YTRALLAA 271
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
3.25e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 147.25 E-value: 3.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISR----- 75
Cdd:COG4598 8 ALEVRDLHKSFGD----LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 -------ERCR-RVQMVFQDpyGSLHPRHTI-GDILEEPLQIHGIKDRD--SRIHTLLDKVGLNRaFRDRYPHQLSGGQR 144
Cdd:COG4598 84 padrrqlQRIRtRLGMVFQS--FNLWSHMTVlENVIEAPVHVLGRPKAEaiERAEALLAKVGLAD-KRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 145 QRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNlTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-214 |
4.61e-43 |
|
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: 144.93 E-value: 4.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRisRERCRR 80
Cdd:COG4133 2 MLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA--REDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 vQMVFQDPYGSLHPRHTIGDILEEPLQIHGIKDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVL 160
Cdd:COG4133 76 -RLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 161 LLDEPTSALDVSVQAEILNLLVElQCESNLTYLMVTHDLGVIAHlCQKVAVMQY 214
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLELAA-ARVLDLGDF 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
1.29e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.97 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFgegeKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDG-----ELAIDG-KPL--EKR 72
Cdd:PRK11264 3 AIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLsqQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 73 ISRERCRRVQMVFQDpyGSLHP-RHTIGDILEEPLQIHGIKDRDS--RIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAI 149
Cdd:PRK11264 79 LIRQLRQHVGFVFQN--FNLFPhRTVLENIIEGPVIVKGEPKEEAtaRARELLAKVGLA-GKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 150 ARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-217 |
1.45e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 143.65 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEG---EKRnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDG-KPLEKRISRER 77
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKK--ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 CR-RVQMVFQDPYGSLHPRHTIGDILEEPLQIhGIKDRD--SRIHTLLDKVGLNR-AFRDRYPHQLSGGQRQRVAIARAL 153
Cdd:PRK13637 81 IRkKVGLVFQYPEYQLFEETIEKDIAFGPINL-GLSEEEieNRVKRAMNIVGLDYeDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-217 |
1.87e-41 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 140.86 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRNqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRisrERCRRVQMVFQD 87
Cdd:cd03226 4 NISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 PYgslhpRHTIGDILEEPLQIhGIKDRD---SRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDE 164
Cdd:cd03226 80 VD-----YQLFTDSVREELLL-GLKELDagnEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 165 PTSALDVSVQAEILNLLVELQCESNlTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-230 |
2.90e-41 |
|
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: 148.37 E-value: 2.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRV 81
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPY---GSLhprhtigdilEEPLQIHGIKDRDSRIHTLLDKVGLNrAFRDRYPH-----------QLSGGQRQRV 147
Cdd:COG4988 414 AWVPQNPYlfaGTI----------RENLRLGRPDASDEELEAALEAAGLD-EFVAALPDgldtplgeggrGLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALV 227
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELL 559
|
...
gi 2084886466 228 AGQ 230
Cdd:COG4988 560 AKN 562
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-219 |
3.32e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.46 E-value: 3.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRV 81
Cdd:PRK13635 6 IRVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDP----YGSlhprhTIGDILEEPLQIHGIKdRDS---RIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:PRK13635 84 GMVFQNPdnqfVGA-----TVQDDVAFGLENIGVP-REEmveRVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKILD 219
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-218 |
3.50e-41 |
|
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: 141.04 E-value: 3.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGeGEKrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR- 80
Cdd:cd03219 1 LEVRGLTKRFG-GLV---ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPygSLHPRHT------IGDILEEPLQIHGIKDRDS------RIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVA 148
Cdd:cd03219 77 IGRTFQIP--RLFPELTvlenvmVAAQARTGSGLLLARARREereareRAEELLERVGL-ADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 149 IARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-218 |
3.53e-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: 140.51 E-value: 3.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 30 EGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL---EKRI--SRERcRRVQMVFQDpyGSLHPRHTIGDILEE 104
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsRKKInlPPQQ-RKIGLVFQQ--YALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 105 PLQIHGIKDRDSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVEL 184
Cdd:cd03297 99 GLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....
gi 2084886466 185 QCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-226 |
4.13e-41 |
|
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: 140.65 E-value: 4.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR- 80
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPygSLHPRHTIgdilEEPLQIHGIKDRDSRIHTLLDKVgLN-----RAFRDRYPHQLSGGQRQRVAIARALIL 155
Cdd:cd03224 77 IGYVPEGR--RIFPELTV----EENLLLGAYARRRAKRKARLERV-YElfprlKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 156 EPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-216 |
7.34e-41 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 139.69 E-value: 7.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL----EKRISRE 76
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnrlrGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RcRRVQMVFQDpyGSLHPRHTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGL-NRAfrDRYPHQLSGGQRQRVAIARAL 153
Cdd:TIGR02673 78 R-RRIGVVFQD--FRLLPDRTVYENVALPLEVRGKKEREiqRRVGAALRQVGLeHKA--DAFPEQLSGGEQQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:TIGR02673 153 VNSPPLLLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-226 |
1.79e-40 |
|
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: 139.63 E-value: 1.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRE----R 77
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 cRRVQMVFQDPygSLHPRHT-IGDILeeplqiHGIKDRDSRIHTL---------------LDKVGLNRAFRDRyPHQLSG 141
Cdd:cd03256 78 -RQIGMIFQQF--NLIERLSvLENVL------SGRLGRRSTWRSLfglfpkeekqralaaLERVGLLDKAYQR-ADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 142 GQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL--- 218
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVfdg 227
|
250
....*....|
gi 2084886466 219 --DSLTVDAL 226
Cdd:cd03256 228 ppAELTDEVL 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-226 |
1.82e-40 |
|
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: 139.04 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRiSRERCRRV 81
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE-PREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPygSLHPRHTIGDILEEPLQIHGIK--DRDSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQV 159
Cdd:cd03265 76 GIVFQDL--SVDDELTGWENLYIHARLYGVPgaERRERIDELLDFVGLLE-AADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-226 |
1.83e-40 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 138.79 E-value: 1.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcRRV 81
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDpyGSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQV 159
Cdd:cd03263 78 GYCPQF--DALFDELTVREHLRFYARLKGLpkSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
5.11e-40 |
|
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: 137.88 E-value: 5.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDG-----KPLEKRisr 75
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEAR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 ercRRVQMVFqDPYGsLHPRHTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARAL 153
Cdd:cd03266 78 ---RRLGFVS-DSTG-LYDRLTARENLEYFAGLYGLKGDEltARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDS 220
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
23-242 |
1.36e-39 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 137.65 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 23 NVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAI---DGKPLEKRISRERCRRVQM------VFQDPYGSLH 93
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELELYQLSEAERRRLMrtewgfVHQNPRDGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 PRHTIG-DILEEPLQI---HGIKDRDSrIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSAL 169
Cdd:TIGR02323 101 MRVSAGaNIGERLMAIgarHYGNIRAT-AQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 170 DVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAlVAGQAKTDYTQMLVNA 242
Cdd:TIGR02323 180 DVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ-VLDDPQHPYTQLLVSS 251
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-228 |
1.99e-39 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 141.13 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:PRK09536 3 MIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPygSLHPRHTIGDILEEPLQIH-----GIKDRDSR-IHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:PRK09536 79 VASVPQDT--SLSFEFDVRQVVEMGRTPHrsrfdTWTETDRAaVERAMERTGVA-QFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDS------LTVDALVA 228
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAgppadvLTADTLRA 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
2.18e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.81 E-value: 2.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINhlNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:PRK13632 7 MIKVE--NVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPYGSLhprhtIGDILEEPLQIhGIKDR-------DSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARAL 153
Cdd:PRK13632 85 IGIIFQNPDNQF-----IGATVEDDIAF-GLENKkvppkkmKDIIDDLAKKVGMED-YLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGViAHLCQKVAVMQYGKI 217
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDE-AILADKVIVFSEGKL 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
3.48e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 137.67 E-value: 3.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLE---KRISRER 77
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 cRRVQMVFQDPYGSLHPRHTIGDILEEPLQIHGIKDR-DSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILE 156
Cdd:PRK13636 82 -ESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEvRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 157 PQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-218 |
3.65e-39 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 139.06 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEkrnqvLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGK-----PLEKRisr 75
Cdd:NF040840 1 MIRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKditnlPPEKR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 ercrRVQMVFQDpYgSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARAL 153
Cdd:NF040840 73 ----GIAYVYQN-Y-MLFPHKTVFENIAFGLKLRKVpkEEIERKVKEIMELLGI-SHLLHRKPRTLSGGEQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:NF040840 146 IIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLS 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-217 |
5.33e-39 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 139.31 E-value: 5.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGK-----PLEKRisre 76
Cdd:PRK09452 15 VELRGISKSFDG----KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvPAENR---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 rcrRVQMVFQDpYgSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:PRK09452 87 ---HVNTVFQS-Y-ALFPHMTVFENVAFGLRMQKTpaAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-228 |
6.69e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 142.23 E-value: 6.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLeKRISRERCRR- 80
Cdd:COG1132 340 IEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI-RDLTLESLRRq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPY---GSL-------HPRHTIGDILE--EPLQIHG-IKDRDSRIHTLLDKVGLNrafrdryphqLSGGQRQRV 147
Cdd:COG1132 416 IGVVPQDTFlfsGTIrenirygRPDATDEEVEEaaKAAQAHEfIEALPDGYDTVVGERGVN----------LSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALV 227
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELL 562
|
.
gi 2084886466 228 A 228
Cdd:COG1132 563 A 563
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-198 |
2.70e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.99 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEkrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT---HWDGELAIDGKPLEkRISRER 77
Cdd:COG4136 1 MLSLENLTITLGGRP----LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLT-ALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 cRRVQMVFQDPYgsLHPRHTIGDIL--EEPLQIHGiKDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALIL 155
Cdd:COG4136 76 -RRIGILFQDDL--LFPHLSVGENLafALPPTIGR-AQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2084886466 156 EPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHD 198
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
19-209 |
3.70e-38 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 132.35 E-value: 3.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGK---PLEKRISRERCR-RVQMVFQDpYGsLHP 94
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKFRReKLGYLFQN-FA-LIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 95 RHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVS 172
Cdd:TIGR03608 90 NETVEENLDLGLKYKKLskKEKREKKKEALEKVGLN-LKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPK 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 2084886466 173 VQAEILNLLVELQcESNLTYLMVTHDLgVIAHLCQKV 209
Cdd:TIGR03608 169 NRDEVLDLLLELN-DEGKTIIIVTHDP-EVAKQADRV 203
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-250 |
5.09e-38 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 135.70 E-value: 5.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT-HWD---GELAIDGKPLEKRISRE 76
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdNWRvtaDRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCR----RVQMVFQDPYGSLHPRHTIGDILEEPLQIHGIKD--------RDSRIHTLLDKVGL--NRAFRDRYPHQLSGG 142
Cdd:PRK15093 83 RRKlvghNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGrwwqrfgwRKRRAIELLHRVGIkdHKDAMRSFPYELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 143 QRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLT 222
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAP 242
|
250 260
....*....|....*....|....*...
gi 2084886466 223 VDALVAgQAKTDYTQMLVNASQQYSREM 250
Cdd:PRK15093 243 SKELVT-TPHHPYTQALIRAIPDFGSAM 269
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
21-240 |
6.33e-38 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 133.51 E-value: 6.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAI---DGKPLEKRISRERCRRVQM------VFQDPYGS 91
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERRRLLrtewgfVHQHPRDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 92 LHPRHTIGDILEEPLQIHGIKD----RDSRIHtLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:PRK11701 102 LRMQVSAGGNIGERLMAVGARHygdiRATAGD-WLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 168 ALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDS-LTVDALVAGQAKtdYTQMLV 240
Cdd:PRK11701 181 GLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESgLTDQVLDDPQHP--YTQLLV 252
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
6.55e-38 |
|
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: 131.93 E-value: 6.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGekrnQVLDNVNISVKEGeIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcRRV 81
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPygSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQV 159
Cdd:cd03264 75 GYLPQEF--GVYPNFTVREFLDYIAWLKGIpsKEVKARVDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-220 |
6.82e-38 |
|
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: 131.96 E-value: 6.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRIsrERCRRV 81
Cdd:cd03268 1 LKTNDLTKTYGK----KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPygSLHPRHTIGDILEEPLQIHGIkdRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLL 161
Cdd:cd03268 75 GALIEAP--GFYPNLTARENLRLLARLLGI--RKKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 162 LDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDS 220
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-217 |
8.00e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 132.97 E-value: 8.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:PRK13548 2 MLEARNLSVRLG----GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQdpYGSLHPRHTIGDILE---EPLQIHGIKDRDSrIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALI--- 154
Cdd:PRK13548 78 RAVLPQ--HSSLSFPFTVEEVVAmgrAPHGLSRAEDDAL-VAAALAQVDL-AHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 155 ---LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-217 |
1.12e-37 |
|
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: 129.86 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRE-RCRRVQMVfqdpygslhprht 97
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMV------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 igdileeplqihgikdrdsrihtlldkvglnrafrdrypHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEI 177
Cdd:cd03216 81 ---------------------------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2084886466 178 LNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03216 122 FKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-243 |
1.28e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.79 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLE---------KR 72
Cdd:PRK10619 6 LNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 73 ISRERCR----RVQMVFQdpYGSLHPRHTI-GDILEEPLQIHGIKDRDSRIHTL--LDKVGLNRAFRDRYPHQLSGGQRQ 145
Cdd:PRK10619 82 ADKNQLRllrtRLTMVFQ--HFNLWSHMTVlENVMEAPIQVLGLSKQEARERAVkyLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 146 RVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDA 225
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
250
....*....|....*...
gi 2084886466 226 LVaGQAKTDYTQMLVNAS 243
Cdd:PRK10619 239 LF-GNPQSPRLQQFLKGS 255
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-218 |
3.16e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 131.78 E-value: 3.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:COG4559 1 MLEAENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 -------VQMVFqdPYgslhprhTIGDILE---EPLQIHGIKDRDsRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIA 150
Cdd:COG4559 77 ravlpqhSSLAF--PF-------TVEEVVAlgrAPHGSSAAQDRQ-IVREALALVGL-AHLAGRSYQTLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 151 RALI-------LEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-228 |
3.88e-37 |
|
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: 133.70 E-value: 3.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 24 VNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL---EKRI--SRERcRRVQMVFQDpyGSLHPRHTI 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsRKGIflPPEK-RRIGYVFQE--ARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 99 GDILEEPLQIHGIKDRDSRIHTLLDKVGLNRAFRdRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEIL 178
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELLGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2084886466 179 NLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-228 |
8.47e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 131.01 E-value: 8.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:PRK13650 4 IIEVKNLTFKYKE-DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDP----YGSlhprhTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:PRK13650 83 IGMVFQNPdnqfVGA-----TVEDDVAFGLENKGIphEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAhLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-218 |
1.15e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 130.91 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAI------------DGKPLEKRisrercrrVQMVFQDP 88
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkknkKLKPLRKK--------VGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 89 YGSLHPRHTIGDILEEPLQIhGIKDRDS--RIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPT 166
Cdd:PRK13634 95 EHQLFEETVEKDICFGPMNF-GVSEEDAkqKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 167 SALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-218 |
1.79e-36 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 131.46 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 36 LVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrRVQMVFQDpYgSLHPRHTIGDILEEPLQIHGI--KD 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR--HINMVFQS-Y-ALFPHMTVEENVAFGLKMRKVprAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 114 RDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYL 193
Cdd:TIGR01187 77 IKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFV 155
|
170 180
....*....|....*....|....*
gi 2084886466 194 MVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIA 180
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-223 |
2.06e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.78 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERC-- 78
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAel 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 --RRVQMVFQdpYGSLHPRHTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLNRAFRDRyPHQLSGGQRQRVAIARALI 154
Cdd:PRK11629 85 rnQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPAEinSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAvMQYGKILDSLTV 223
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAELSL 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-217 |
4.76e-36 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 127.59 E-value: 4.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL----EKRISRE 76
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCRRVQMVFQDPYgsLHPRHTIGDILEEPLQIHGIKDRDSRIH--TLLDKVGLNRAFrDRYPHQLSGGQRQRVAIARALI 154
Cdd:PRK10584 86 RAKHVGFVFQSFM--LIPTLNALENVELPALLRGESSRQSRNGakALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKI 217
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-228 |
1.55e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.06 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 18 NQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR-VQMVFQDPygSLHPRH 96
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQEL--NLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 97 TIGD---ILEEPLQIHGIKDRDSRIHT--LLDKVGLNRAfrdryPHQ----LSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:COG1129 95 SVAEnifLGREPRRGGLIDWRAMRRRAreLLARLGLDID-----PDTpvgdLSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 168 ALDVSvQAEIL-NLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDS-----LTVDALVA 228
Cdd:COG1129 170 SLTER-EVERLfRIIRRLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTgpvaeLTEDELVR 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
2.63e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 126.74 E-value: 2.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEG---EKRnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRER 77
Cdd:COG1101 1 MLELKNLSKTFNPGtvnEKR--ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 CRRVQMVFQDPYGSLHPRHTIgdilEEPLQIhgiKDRDSRIHTLldKVGLNRAFRDRYPHQ------------------L 139
Cdd:COG1101 79 AKYIGRVFQDPMMGTAPSMTI----EENLAL---AYRRGKRRGL--RRGLTKKRRELFRELlatlglglenrldtkvglL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 140 SGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI-L 218
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIiL 229
|
250
....*....|....*..
gi 2084886466 219 D-------SLTVDALVA 228
Cdd:COG1101 230 DvsgeekkKLTVEDLLE 246
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-217 |
5.19e-35 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 124.53 E-value: 5.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 26 ISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGkpLEKRISRERCRRVQMVFQDP--YGSLHPRHTIGDILE 103
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRPVSMLFQENnlFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 104 EPLQIHGIkDRDsRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVE 183
Cdd:cd03298 97 PGLKLTAE-DRQ-AIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 2084886466 184 LQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-219 |
7.47e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.41 E-value: 7.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHW-----DGELAIDGKPLEKRISRE 76
Cdd:PRK14247 4 IEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCRRVQMVFQDPygSLHPRHTIGDILEEPLQIHGI----KDRDSRIHTLLDKVGLNRAFRDRY---PHQLSGGQRQRVAI 149
Cdd:PRK14247 80 LRRRVQMVFQIP--NPIPNLSIFENVALGLKLNRLvkskKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 150 ARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCEsnLTYLMVTHDLGVIAHLCQKVAVMQYGKILD 219
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-219 |
7.91e-35 |
|
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: 130.69 E-value: 7.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAI----DGKPLEKRISRERCRRVQ---MVFQDpYGsLH 93
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRGRAKRyigILHQE-YD-LY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 PRHTIGDILEEPLQIHGIKD--RDSRIHTLlDKVGLN----RAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:TIGR03269 378 PHRTVLDNLTEAIGLELPDElaRMKAVITL-KMVGFDeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 168 ALD----VSVQAEILNLLVELqcesNLTYLMVTHDLGVIAHLCQKVAVMQYGKILD 219
Cdd:TIGR03269 457 TMDpitkVDVTHSILKAREEM----EQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-219 |
8.98e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 125.16 E-value: 8.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEK-----RISRERCRR-VQMVFQDPygSLH 93
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifQIDAIKLRKeVGMVFQQP--NPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 PRHTIGDILEEPLQIHGIKDR---DSRIHTLLDKVGLNRAFRDRY---PHQLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKreiKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 168 ALDVSVQAEILNLLVELQCEsnLTYLMVTHDLGVIAHLCQKVAVMQYGKILD 219
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-226 |
1.03e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.99 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISR----- 75
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 --ERcrrvqmvfqdpygSLHPRHTIGDILEEPLQIHGIKDRDS--RIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIAR 151
Cdd:COG4152 77 peER-------------GLYPKMKVGEQLVYLARLKGLSKAEAkrRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 152 ALILEPQVLLLDEPTSALD-VSVQaEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDpVNVE-LLKDVIRELA-AKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-217 |
1.36e-34 |
|
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: 123.67 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL----EKRISRERcRRVQMVFQDpyGSLHPRH 96
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLR-RKIGVVFQD--FRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 97 TIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLNRAFRDrYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQ 174
Cdd:cd03292 94 NVYENVAFALEVTGVPPREirKRVPAALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2084886466 175 AEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03292 173 WEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-226 |
2.13e-34 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 123.40 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 3 EINHLNLAFGEGekrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR-- 80
Cdd:TIGR03410 2 EVSNLNVYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 --V---QMVFqdpygslhPRHTIgdilEEPLQI--HGIKDRDSRI-HTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARA 152
Cdd:TIGR03410 78 ayVpqgREIF--------PRLTV----EENLLTglAALPRRSRKIpDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 153 LILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
2.68e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 124.42 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLE-KRISRERCR 79
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 80 R-VQMVFQDPYGSLHPRHTIGDILEEPLQIHGIKDR-DSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEP 157
Cdd:PRK13639 78 KtVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEvEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 158 QVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLT 222
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-231 |
3.55e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 123.15 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 25 NISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPlEKRISRERcRRVQMVFQDP--YGSLHPRHTIGdil 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSR-RPVSMLFQENnlFSHLTVAQNIG--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 103 eepLQIH-GIKDRDSRIHTL---LDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEIL 178
Cdd:PRK10771 94 ---LGLNpGLKLNAAQREKLhaiARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 179 NLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL-DSLTvDALVAGQA 231
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAwDGPT-DELLSGKA 222
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
2-226 |
5.88e-34 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 125.49 E-value: 5.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGlFTHWDG---ELAIDGKPLEKRISRERc 78
Cdd:TIGR03258 6 IRIDHLRVAYGA----NTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAG-FVKAAGltgRIAIADRDLTHAPPHKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 rRVQMVFQDPygSLHPRHTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLNRAfRDRYPHQLSGGQRQRVAIARALILE 156
Cdd:TIGR03258 80 -GLALLFQNY--ALFPHLKVEDNVAFGLRAQKMPKADiaERVADALKLVGLGDA-AAHLPAQLSGGMQQRIAIARAIAIE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 157 PQVLLLDEPTSALDVSVQAEILNLLVELQCE-SNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:TIGR03258 156 PDVLLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQAL 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-224 |
7.05e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 122.86 E-value: 7.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 4 INHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKriSRERCRrvqM 83
Cdd:PRK11247 15 LNAVSKRYGE----RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE--AREDTR---L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 84 VFQDpyGSLHPRHTIGDILEepLQIHGikDRDSRIHTLLDKVGL-NRAfrDRYPHQLSGGQRQRVAIARALILEPQVLLL 162
Cdd:PRK11247 86 MFQD--ARLLPWKKVIDNVG--LGLKG--QWRDAALQALAAVGLaDRA--NEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 163 DEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI-LDsLTVD 224
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgLD-LTVD 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-224 |
9.54e-34 |
|
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: 121.80 E-value: 9.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPlekrISRERCRRVqMVFQDpYgSLHP----RH 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ----ITEPGPDRM-VVFQN-Y-SLLPwltvRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 97 TIGDILEEPLQIHGIKDRDSRIHTLLDKVGLNRAfRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAE 176
Cdd:TIGR01184 74 NIALAVDRVLPDLSKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 177 ILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYG---KILDSLTVD 224
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaaNIGQILEVP 203
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-217 |
1.17e-33 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 121.12 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 25 NISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrRVQMVFQDP--YGSLHPRHTIGDIL 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQR--PVSMLFQENnlFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 103 EEPLQIHGIKDRdsRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLV 182
Cdd:TIGR01277 96 HPGLKLNAEQQE--KVVDAAQQVGIAD-YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*
gi 2084886466 183 ELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-239 |
1.64e-33 |
|
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: 127.19 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRV 81
Cdd:COG4987 334 LELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPygslhprHTIGDILEEPLQIhgIKDR--DSRIHTLLDKVGLnRAFRDRYPH-----------QLSGGQRQRVA 148
Cdd:COG4987 412 AVVPQRP-------HLFDTTLRENLRL--ARPDatDEELWAALERVGL-GDWLAALPDgldtwlgeggrRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 149 IARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESnlTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLA 558
|
250
....*....|.
gi 2084886466 229 GQAKtdYTQML 239
Cdd:COG4987 559 QNGR--YRQLY 567
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-226 |
1.91e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.58 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDG-----KPLEKRISRERcRRVQMVFQDPYGSLH 93
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithKTKDKYIRPVR-KRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 PRHTIGDILEEPLQIH-GIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVS 172
Cdd:PRK13646 100 EDTVEREIIFGPKNFKmNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 173 VQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-199 |
2.29e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 121.35 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGeGEKrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRiSRERcrr 80
Cdd:PRK11248 1 MLQISHLYADYG-GKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP-GAER--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 vQMVFQDPygSLHPRHTIGDILEEPLQIHGIkDRDSRIHT---LLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEP 157
Cdd:PRK11248 73 -GVVFQNE--GLLPWRNVQDNVAFGLQLAGV-EKMQRLEIahqMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2084886466 158 QVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDL 199
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
4.42e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 122.27 E-value: 4.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgEKRNQ--VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAI-------------- 64
Cdd:PRK13631 21 ILRVKNLYCVFDE-KQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 65 DGKPLEKRISR-ERCRR-VQMVFQDPYGSLHPRHTIGDILEEPLQIhGIKDRDSRIHT--LLDKVGLNRAFRDRYPHQLS 140
Cdd:PRK13631 100 ITNPYSKKIKNfKELRRrVSMVFQFPEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAkfYLNKMGLDDSYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 141 GGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDS 220
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
..
gi 2084886466 221 LT 222
Cdd:PRK13631 258 GT 259
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-217 |
5.73e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 119.59 E-value: 5.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEkrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERC-- 78
Cdd:PRK10908 1 MIRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPfl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 -RRVQMVFQDPYgsLHPRHTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLNRAFRDrYPHQLSGGQRQRVAIARALIL 155
Cdd:PRK10908 78 rRQIGMIFQDHH--LLMDRTVYDNVAIPLIIAGASGDDirRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 156 EPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-217 |
7.81e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 120.96 E-value: 7.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQ--VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDG--KPLEKRISRE 76
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RcRRVQMVFQDPYGSLhprhtIGDILEEPLQIH----GIKDRD--SRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIA 150
Cdd:PRK13633 84 R-NKAGMVFQNPDNQI-----VATIVEEDVAFGpenlGIPPEEirERVDESLKKVGMYE-YRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 151 RALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKI 217
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-217 |
1.02e-32 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 119.33 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEkrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL------EKRIS 74
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgkKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 75 RercRRVQMVFQDpYGSLHPRHTIGDILEEPLQIHG--------IKDRDSRI-HTLLDKVGLNrAFRDRYPHQLSGGQRQ 145
Cdd:TIGR02315 78 R---RRIGMIFQH-YNLIERLTVLENVLHGRLGYKPtwrsllgrFSEEDKERaLSALERVGLA-DKAYQRADQLSGGQQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 146 RVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-228 |
1.06e-32 |
|
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: 119.32 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:COG0410 3 MLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 ----V---QMVFqdpygslhPRHTIgdilEEPLQIHGIKDRD-SRIHTLLDKVgLN-----RAFRDRYPHQLSGGQRQRV 147
Cdd:COG0410 79 gigyVpegRRIF--------PSLTV----EENLLLGAYARRDrAEVRADLERV-YElfprlKERRRQRAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALV 227
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
.
gi 2084886466 228 A 228
Cdd:COG0410 225 A 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-212 |
1.08e-32 |
|
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: 124.71 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFgegEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRV 81
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPY---GS------LHPRHTIGDILEEPLQIHG----IKDRDSRIHTLLDKVGlnrafrdrypHQLSGGQRQRVA 148
Cdd:TIGR02857 399 AWVPQHPFlfaGTiaenirLARPDASDAEIREALERAGldefVAALPQGLDTPIGEGG----------AGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 149 IARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGViAHLCQKVAVM 212
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLAL-AALADRIVVL 529
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-220 |
1.24e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 120.29 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLF---THWDGELAIDGKPLEKRISRERC 78
Cdd:PRK13640 6 VEFKHVSFTYPDSKK--PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 RRVQMVFQDP----YGSlhprhTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARA 152
Cdd:PRK13640 84 EKVGIVFQNPdnqfVGA-----TVGDDVAFGLENRAVPRPEmiKIVRDVLADVGMLD-YIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 153 LILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGViAHLCQKVAVMQYGKILDS 220
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQ 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-218 |
1.27e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 120.32 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL-----EKRISRERcRRVQMVFQDPYGSLH 93
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKKLR-KKVSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 PRHTIGDILEEPLQIhGIKDRDSRIHTL--LDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDV 171
Cdd:PRK13641 100 ENTVLKDVEFGPKNF-GFSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2084886466 172 SVQAEILNLLVELQCESNlTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-216 |
1.42e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 122.25 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFgEGEkrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrR 80
Cdd:PRK11607 19 LLEIRNLTKSF-DGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDpYgSLHPRHTIgdilEEPLQIHGIKDR------DSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALI 154
Cdd:PRK11607 93 INMMFQS-Y-ALFPHMTV----EQNIAFGLKQDKlpkaeiASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 155 LEPQVLLLDEPTSALDVSV----QAEILNLLVELqcesNLTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-218 |
1.48e-32 |
|
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: 118.97 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGK-PLEKRIsrERCRRVQMVF---QDPYGSLHPR 95
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRK--KFLRRIGVVFgqkTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 htigDILEEPLQIHGIKDRD--SRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:cd03267 114 ----DSFYLLAAIYDLPPARfkKRLDELSELLDLEE-LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2084886466 174 QAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-217 |
1.82e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 121.68 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 23 NVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrRVQMVFQDpYgSLHPRHTIGDIL 102
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER--GVGMVFQS-Y-ALYPHLSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 103 EEPLQIHGIK--DRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALD----VSVQAE 176
Cdd:PRK11000 97 SFGLKLAGAKkeEINQRVNQVAEVLQLA-HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2084886466 177 ILNLLVELQCesnlTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PRK11000 176 ISRLHKRLGR----TMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-217 |
2.37e-32 |
|
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: 116.76 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR-VQMVFQDpygslhpRHTI 98
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPED-------RKRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 99 GDILEEPlqihgikdrdsrihtlldkVGLNRAFrdryPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEIL 178
Cdd:cd03215 88 GLVLDLS-------------------VAENIAL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 2084886466 179 NLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03215 145 RLIRELA-DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-228 |
3.05e-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: 3.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 18 NQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDP---YGSLHP 94
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPvlfDGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 95 RHTIGD---ILEEPLQIHGIKDRDSRIHTLLDK----VGlNRAFrdryphQLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:cd03249 96 NIRYGKpdaTDEEVEEAAKKANIHDFIMSLPDGydtlVG-ERGS------QLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 168 ALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:cd03249 169 ALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-228 |
3.14e-32 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 117.71 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKrISRERCR-R 80
Cdd:cd03254 3 IEFENVNFSYDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD-ISRKSLRsM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPY---GSL-------HPRHTIGDILEEPLQIHgikdrdsrIHTLLDKV--GLNRAFRDRyPHQLSGGQRQRVA 148
Cdd:cd03254 79 IGVVLQDTFlfsGTImenirlgRPNATDEEVIEAAKEAG--------AHDFIMKLpnGYDTVLGEN-GGNLSQGERQLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 149 IARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-217 |
3.28e-32 |
|
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: 117.31 E-value: 3.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 18 NQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDP---YGSLHP 94
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVtlfYGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 95 RHTIGDILEEplqihgikdrDSRIHTLLDKVGLNrAFRDRYPH-----------QLSGGQRQRVAIARALILEPQVLLLD 163
Cdd:cd03245 97 NITLGAPLAD----------DERILRAAELAGVT-DFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 164 EPTSALDVSVQAEILNLLVELQCESnlTYLMVTHDLGVIAhLCQKVAVMQYGKI 217
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-217 |
3.32e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 120.72 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 18 NQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrRVQMVFQDpYgSLHPRHT 97
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR--DIAMVFQN-Y-ALYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 IGDILEEPLQIHGIK--DRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALD----V 171
Cdd:PRK11650 93 VRENMAYGLKIRGMPkaEIEERVAEAARILELE-PLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2084886466 172 SVQAEILnllvELQCESNLTYLMVTHDlGVIAH-LCQKVAVMQYGKI 217
Cdd:PRK11650 172 QMRLEIQ----RLHRRLKTTSLYVTHD-QVEAMtLADRVVVMNGGVA 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
5.29e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 118.30 E-value: 5.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRV 81
Cdd:PRK13647 5 IEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPYGSLHPRHTIGDILEEPLQIH-GIKDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVL 160
Cdd:PRK13647 82 GLVFQDPDDQVFSSTVWDDVAFGPVNMGlDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 161 LLDEPTSALDVSVQAEILNLLVELQCESNlTYLMVTHDLGVIAHLCQKVAVMQYGKIL----DSLTVDALVAGQA 231
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLaegdKSLLTDEDIVEQA 234
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
8-228 |
1.54e-31 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 122.36 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKrISRERCRR-VQMVFQ 86
Cdd:TIGR03796 482 NITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREE-IPREVLANsVAMVDQ 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 87 DPY---GSLHPRHTIGD--ILEEPL-------QIHG-IKDRDSRIHTLLDKVGLNrafrdryphqLSGGQRQRVAIARAL 153
Cdd:TIGR03796 561 DIFlfeGTVRDNLTLWDptIPDADLvrackdaAIHDvITSRPGGYDAELAEGGAN----------LSGGQRQRLEIARAL 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCesnlTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:TIGR03796 631 VRNPSILILDEATSALDPETEKIIDDNLRRRGC----TCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWA 700
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-228 |
1.68e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 122.37 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEK-RISRERcRR 80
Cdd:TIGR03797 452 IEVDRVTFRYRPDG--PLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGlDVQAVR-RQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDpyGSLHPrhtiGDILE--------------EPLQIHG----IKDRDSRIHTLLDKVGLNrafrdryphqLSGG 142
Cdd:TIGR03797 529 LGVVLQN--GRLMS----GSIFEniaggapltldeawEAARMAGlaedIRAMPMGMHTVISEGGGT----------LSGG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 143 QRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqcesNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLT 222
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
....*.
gi 2084886466 223 VDALVA 228
Cdd:TIGR03797 668 YDELMA 673
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-218 |
1.79e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.65 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgeKRnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:PRK11231 2 TLRTENLTVGYGT--KR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VqmvfqdpygSLHPRHtigdileePLQIHGIKDRD---------------------SRIHTLLDKVGLNrAFRDRYPHQL 139
Cdd:PRK11231 78 L---------ALLPQH--------HLTPEGITVRElvaygrspwlslwgrlsaednARVNQAMEQTRIN-HLADRRLTDL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 140 SGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNlTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-217 |
2.56e-31 |
|
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: 115.07 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISR------ 75
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrigylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 -ERcrrvqmvfqdpygSLHPRHTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARA 152
Cdd:cd03269 77 eER-------------GLYPKMKVIDQLVYLAQLKGLKKEEarRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 153 LILEPQVLLLDEPTSALDVsVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03269 143 VIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-228 |
4.57e-31 |
|
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: 121.00 E-value: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLeKRISRERCRR- 80
Cdd:TIGR01193 474 IVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL-KDIDRHTLRQf 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPY---GSLHPRHTIG-------DILEEPLQIHGIKDRDSRI----HTLLDKVGLNrafrdryphqLSGGQRQR 146
Cdd:TIGR01193 550 INYLPQEPYifsGSILENLLLGakenvsqDEIWAACEIAEIKDDIENMplgyQTELSEEGSS----------ISGGQKQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 147 VAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcesNLTYLMVTHDLGViAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSV-AKQSDKIIVLDHGKIIEQGSHDEL 695
|
..
gi 2084886466 227 VA 228
Cdd:TIGR01193 696 LD 697
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-226 |
7.71e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 115.95 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAI---DGKPLEKRISRERC----------------- 78
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKVleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 ----RRVQMVFQDPYGSLHPRHTIGDILEEPLQIhGIKDRDS--RIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARA 152
Cdd:PRK13651 101 keirRRVGVVFQFAEYQLFEQTIEKDIIFGPVSM-GVSKEEAkkRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 153 LILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL-DSLTVDAL 226
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIkDGDTYDIL 253
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-219 |
1.18e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 114.55 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLF-----THWDGELAIDGK--------P 68
Cdd:PRK14267 5 IETVNLRVYYG----SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRniyspdvdP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 69 LEKRisrercRRVQMVFQdpYGSLHPRHTIGDILEEPLQIHGI----KDRDSRIHTLLDKVGLNRAFRDR---YPHQLSG 141
Cdd:PRK14267 81 IEVR------REVGMVFQ--YPNPFPHLTIYDNVAIGVKLNGLvkskKELDERVEWALKKAALWDEVKDRlndYPSNLSG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 142 GQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCEsnLTYLMVTHDLGVIAHLCQKVAVMQYGKILD 219
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-218 |
1.20e-30 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 119.59 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLeKRISRERCRR-VQMVFQDP---YGSLhpR 95
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI-RQIDPADLRRnIGYVPQDPrlfYGTL--R 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 HTIgdILEEPLQihgikdRDSRIHTLLDKVGLNRaFRDRYPH-----------QLSGGQRQRVAIARALILEPQVLLLDE 164
Cdd:TIGR03375 557 DNI--ALGAPYA------DDEEILRAAELAGVTE-FVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDE 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 165 PTSALDVSVQAEILNLLVELQCESnlTYLMVTHDLGVIAhLCQKVAVMQYGKIL 218
Cdd:TIGR03375 628 PTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLD-LVDRIIVMDNGRIV 678
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-252 |
1.59e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.06 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGE-----------GEKRNQVLDNVNIS---------VKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGE 61
Cdd:PRK10070 5 LEIKNLYKIFGEhpqrafkyieqGLSKEQILEKTGLSlgvkdaslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 62 LAIDGKPLEK----RISRERCRRVQMVFQDpyGSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNRaFRDRY 135
Cdd:PRK10070 85 VLIDGVDIAKisdaELREVRRKKIAMVFQS--FALMPHMTVLDNTAFGMELAGInaEERREKALDALRQVGLEN-YAHSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 136 PHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYG 215
Cdd:PRK10070 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2084886466 216 KILDSLTVDALVAGQAkTDYTQML---VNASQQYS-REMAR 252
Cdd:PRK10070 242 EVVQVGTPDEILNNPA-NDYVRTFfrgVDISQVFSaKDIAR 281
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-228 |
1.87e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 114.42 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQvLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPYGSLhPRHTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQ 158
Cdd:PRK13642 83 IGMVFQNPDNQF-VGATVEDDVAFGMENQGIPREEmiKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-224 |
2.91e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.13 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPYGSLHPRHTI 98
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 99 GDILEEPLQIhGIKDR--DSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAE 176
Cdd:PRK13652 98 QDIAFGPINL-GLDEEtvAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2084886466 177 ILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVD 224
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
3.77e-30 |
|
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: 112.14 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAF---GEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIdgkplekrisRER 77
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV----------RHD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 78 CRRVQMVFQDPYGSLHPR-HTIG---------------DILEEPLQIHGIkDRDS---RIHTLLDKVGLNRAFRDRYPHQ 138
Cdd:COG4778 74 GGWVDLAQASPREILALRrRTIGyvsqflrviprvsalDVVAEPLLERGV-DREEaraRARELLARLNLPERLWDLPPAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 139 LSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQ 213
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-220 |
4.33e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 113.69 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL-----EKRISRERcRRVQMVFQDPYGSLHPR 95
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstskNKDIKQIR-KKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 HTIGDILEEPlQIHGI--KDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:PRK13649 102 TVLKDVAFGP-QNFGVsqEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2084886466 174 QAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDS 220
Cdd:PRK13649 181 RKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-224 |
5.35e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.05 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRE-RCRRVQMVFQDPygSLHPRHTIg 99
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHF--MLVPNLTV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 100 diLE------EPLQiHGIKDRDS---RIHTLLDKVGLNRAFrDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALd 170
Cdd:COG3845 98 --AEnivlglEPTK-GGRLDRKAaraRIRELSERYGLDVDP-DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 171 vsVQAEILNLLVELQ--CESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVD 224
Cdd:COG3845 173 --TPQEADELFEILRrlAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-238 |
8.32e-30 |
|
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: 111.55 E-value: 8.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLeKRISRERCRR- 80
Cdd:cd03253 1 IEFENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-REVTLDSLRRa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDP------------YGSlhPRHTIGDILE--EPLQIHGikdrdsRIHTLLD----KVGlNRAFRdryphqLSGG 142
Cdd:cd03253 77 IGVVPQDTvlfndtigynirYGR--PDATDEEVIEaaKAAQIHD------KIMRFPDgydtIVG-ERGLK------LSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 143 QRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLT 222
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
250
....*....|....*.
gi 2084886466 223 VDALVAGQAKtdYTQM 238
Cdd:cd03253 219 HEELLAKGGL--YAEM 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-217 |
1.02e-29 |
|
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: 109.61 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQD 87
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 pygslhprhtigDILEEplqihgikdrdsriHTLLDKVglnrafrdryphqLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:cd03246 85 ------------DELFS--------------GSIAENI-------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2084886466 168 ALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAhLCQKVAVMQYGKI 217
Cdd:cd03246 126 HLDVEGERALNQAIAALK-AAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-239 |
1.66e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 116.36 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 18 NQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPY---GSLhp 94
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVlfsGSV-- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 95 RHTIGdileeplqiHGIKDRDSRIHTLLDKVGLNRAFRDRYPH-----------QLSGGQRQRVAIARALILEPQVLLLD 163
Cdd:TIGR00958 572 RENIA---------YGLTDTPDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 164 EPTSALDVSVQAeilnLLVELQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVAGQakTDYTQML 239
Cdd:TIGR00958 643 EATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ--GCYKHLV 711
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-199 |
2.87e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 115.15 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 18 NQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPygslhprHT 97
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDA-------HL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 IGDILEEPLQIHGIKDRDSRIHTLLDKVGLNRAFRDRyPH-----------QLSGGQRQRVAIARALILEPQVLLLDEPT 166
Cdd:TIGR02868 421 FDTTVRENLRLARPDATDEELWAALERVGLADWLRAL-PDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|...
gi 2084886466 167 SALDVSVQAEILNLLveLQCESNLTYLMVTHDL 199
Cdd:TIGR02868 500 EHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-217 |
3.64e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 3.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 4 INHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGElaidgkplekrISRERCRRVQM 83
Cdd:COG0488 1 LENLSKSFGG----RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE-----------VSIPKGLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 84 VFQDPYgsLHPRHTIGDI----------------------------------LEEPLQIHGIKDRDSRIHTLLDKVGLNR 129
Cdd:COG0488 66 LPQEPP--LDDDLTVLDTvldgdaelraleaeleeleaklaepdedlerlaeLQEEFEALGGWEAEARAEEILSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 130 AFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDV-SVQ--AEILNllvelqcESNLTYLMVTHDLGVIAHLC 206
Cdd:COG0488 144 EDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEwlEEFLK-------NYPGTVLVVSHDRYFLDRVA 216
|
250
....*....|.
gi 2084886466 207 QKVAVMQYGKI 217
Cdd:COG0488 217 TRILELDRGKL 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-217 |
4.39e-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: 108.17 E-value: 4.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRisrERCRRv 81
Cdd:cd03247 1 LSINNVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL---EKALS- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 qmvfqdpygslhprHTIGDILEEPLQIHGikdrdsrihTLLDKVGLnrafrdryphQLSGGQRQRVAIARALILEPQVLL 161
Cdd:cd03247 75 --------------SLISVLNQRPYLFDT---------TLRNNLGR----------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 162 LDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHLcQKVAVMQYGKI 217
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVL--KDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-217 |
4.71e-29 |
|
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: 109.48 E-value: 4.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPY---GSLH-- 93
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVlfaRSLQdn 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 -----PRHTIGDILEEPLQIHG---IKDRDSRIHTLLDKVGlnrafrdrypHQLSGGQRQRVAIARALILEPQVLLLDEP 165
Cdd:cd03248 108 iayglQSCSFECVKEAAQKAHAhsfISELASGYDTEVGEKG----------SQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 166 TSALDVSVQAEILNLLveLQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKI 217
Cdd:cd03248 178 TSALDAESEQQVQQAL--YDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-218 |
5.48e-29 |
|
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: 109.12 E-value: 5.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLeKRISRERCR-R 80
Cdd:cd03244 3 IEFKNVSLRYRPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI-SKIGLHDLRsR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPY---GSLhpRHTIgdileEPLQIHGikdrDSRIHTLLDKVGLNRAFRDRYPH----------QLSGGQRQRV 147
Cdd:cd03244 80 ISIIPQDPVlfsGTI--RSNL-----DPFGEYS----DEELWQALERVGLKEFVESLPGGldtvveeggeNLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVElqCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKIL 218
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-218 |
7.63e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 110.95 E-value: 7.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGK-PLEKRisRERCRRVQMVF----QdpygsLHPR 95
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKRR--KEFARRIGVVFgqrsQ-----LWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 HTIGDILEEPLQIHGIKDRD--SRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:COG4586 111 LPAIDSFRLLKAIYRIPDAEykKRLDELVELLDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2084886466 174 QAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:COG4586 190 KEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-220 |
1.08e-28 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 108.40 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 26 ISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPlekriSRERCRRVQMVFQdpygslhpRHTIGdiLEEP 105
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQ--------RHEFA--WDFP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 106 LQIHG--IKDRDSRIHTL--------------LDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSAL 169
Cdd:TIGR03771 66 ISVAHtvMSGRTGHIGWLrrpcvadfaavrdaLRRVGLTE-LADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 170 DVSVQAEILNLLVELQCESNlTYLMVTHDLGVIAHLCQKVAVMQYGKILDS 220
Cdd:TIGR03771 145 DMPTQELLTELFIELAGAGT-AILMTTHDLAQAMATCDRVVLLNGRVIADG 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-218 |
2.17e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.44 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEK-RNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLF-----THWDGELAIDGKPLEKRIS 74
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqptegKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 75 RERcRRVQMVFQDPYGSLHPRHTIGDILEEPLQIHGIKDRDSRIHT-LLDKVGLNRAFRDRYPHQLSGGQRQRVAIARAL 153
Cdd:PRK13643 81 PVR-KKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAeKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-238 |
3.19e-28 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 107.32 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQD 87
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 PY---GSLH-------PRHTIGDILEEPLQIHG---IKDRDSRIHTLLDKVGLNrafrdryphqLSGGQRQRVAIARALI 154
Cdd:cd03251 85 VFlfnDTVAeniaygrPGATREEVEEAARAANAhefIMELPEGYDTVIGERGVK----------LSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVAgqAKTD 234
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA--QGGV 229
|
....
gi 2084886466 235 YTQM 238
Cdd:cd03251 230 YAKL 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-219 |
3.85e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.56 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISR----ERCRR-VQMVFQDPYGSLH 93
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevKRLRKeIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 PRHTIGDILEEPLQIHGIKDRD-SRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVS 172
Cdd:PRK13645 105 QETIEKDIAFGPVNLGENKQEAyKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2084886466 173 VQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILD 219
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-217 |
1.08e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 108.81 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 23 NVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL---EKRIS--RERcRRVQMVFQDpyGSLHPRHT 97
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaEKGIClpPEK-RRIGYVFQD--ARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 I-GDILeeplqiHGIKDRD----SRIHTLLdkvGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVS 172
Cdd:PRK11144 93 VrGNLR------YGMAKSMvaqfDKIVALL---GI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2084886466 173 VQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-218 |
1.09e-27 |
|
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: 104.94 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 14 GEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGL--FTHWDGELAIDGKPLEKRISRercRRVQMVFQDPYgs 91
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFR---KIIGYVPQDDI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 92 LHPRHTIgdilEEPLQIH-GIKdrdsrihtlldkvglnrafrdryphQLSGGQRQRVAIARALILEPQVLLLDEPTSALD 170
Cdd:cd03213 93 LHPTLTV----RETLMFAaKLR-------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2084886466 171 VSVQAEILNLLVELqCESNLTYLMVTHDL-GVIAHLCQKVAVMQYGKIL 218
Cdd:cd03213 144 SSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-205 |
1.17e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 106.66 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFgegeKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLfTHWDGELAIDGKP-------LEKRIS 74
Cdd:PRK14258 8 IKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVeffnqniYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 75 RERCRR-VQMVFQDP------------YG----SLHPRHTIGDILEEplqihGIKDRD--SRIHTLLDKVGLnrafrdry 135
Cdd:PRK14258 83 LNRLRRqVSMVHPKPnlfpmsvydnvaYGvkivGWRPKLEIDDIVES-----ALKDADlwDEIKHKIHKSAL-------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 136 phQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHL 205
Cdd:PRK14258 150 --DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRL 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-203 |
1.90e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.24 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 17 RNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFthwdgelaidgKPLEKRISRERCRRVQMVFQdpygslhpRH 96
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL-----------RPTSGTVRRAGGARVAYVPQ--------RS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 97 TIGDIL---------------EEPLQIHGIKDRdSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLL 161
Cdd:NF040873 65 EVPDSLpltvrdlvamgrwarRGLWRRLTRDDR-AAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2084886466 162 LDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIA 203
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-217 |
2.58e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.99 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPYGSLhprhtIGD 100
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQF-----VGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 101 ILEEP----LQIHGI--KDRDSRIHTLLDKVG-LNRAfrDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:PRK13648 100 IVKYDvafgLENHAVpyDEMHRRVSEALKQVDmLERA--DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2084886466 174 QAEILNLLVELQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKI 217
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-204 |
3.77e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.51 E-value: 3.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEkrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAidgkplekrisreRCRR 80
Cdd:COG4178 362 ALALEDLTLRTPDGR---PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-------------RPAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVF--QDPY---GSLHprhtigDILEEPLQIHGIKDrdSRIHTLLDKVGL-NRAFR----DRYPHQLSGGQRQRVAIA 150
Cdd:COG4178 426 ARVLFlpQRPYlplGTLR------EALLYPATAEAFSD--AELREALEAVGLgHLAERldeeADWDQVLSLGEQQRLAFA 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 151 RALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESnlTYLMVTHDLGVIAH 204
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT--TVISVGHRSTLAAF 549
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-228 |
5.14e-27 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 109.04 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRV 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDR--PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQD------------PYGSLH--PRHTIGDILEEPLQIHGIKDRDSRIHTlldKVGLNRAfrdryphQLSGGQRQRV 147
Cdd:TIGR02203 409 ALVSQDvvlfndtianniAYGRTEqaDRAEIERALAAAYAQDFVDKLPLGLDT---PIGENGV-------LLSGGQRQRL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALV 227
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELL 555
|
.
gi 2084886466 228 A 228
Cdd:TIGR02203 556 A 556
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-227 |
5.22e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 104.78 E-value: 5.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:COG4604 1 MIEIKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPygSLHPRHTIGDILEeplqiHG--------IKDRDSR-IHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIAR 151
Cdd:COG4604 77 LAILRQEN--HINSRLTVRELVA-----FGrfpyskgrLTAEDREiIDEAIAYLDLE-DLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 152 ALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALV 227
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
16-228 |
5.63e-27 |
|
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: 104.16 E-value: 5.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 16 KRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR-VQMVFQDPygSLHP 94
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEA--SIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 95 RHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALD-V 171
Cdd:cd03218 89 KLTVEENILAVLEIRGLskKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 172 SVQaEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:cd03218 168 AVQ-DIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-230 |
6.11e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 108.76 E-value: 6.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINhlNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAglfTHWD---GELAIDGKPLEKriSRERC 78
Cdd:PRK11160 339 LTLN--NVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT---RAWDpqqGEILLNGQPIAD--YSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 RRVQM--VFQDPygslhprHTIGDILEEPLQIHGIKDRDSRIHTLLDKVGLNRAFRDRYP---------HQLSGGQRQRV 147
Cdd:PRK11160 412 LRQAIsvVSQRV-------HLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggRQLSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqCEsNLTYLMVTHDLGVIAHLcQKVAVMQYGKILDSLTVDALV 227
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQ-NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELL 561
|
...
gi 2084886466 228 AGQ 230
Cdd:PRK11160 562 AQQ 564
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-218 |
8.91e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 104.30 E-value: 8.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQD 87
Cdd:PRK10253 12 QLTLGYGKY--TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 PYgslhprhTIGDIL-----------EEPLQIHGIKDRDSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILE 156
Cdd:PRK10253 90 AT-------TPGDITvqelvargrypHQPLFTRWRKEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 157 PQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
18-213 |
1.67e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 18 NQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKrISRERCRR-VQMVFQDP--YGSlhp 94
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST-LKPEIYRQqVSYCAQTPtlFGD--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 95 rhTIGDILEEPLQIHGIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQ 174
Cdd:PRK10247 96 --TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2084886466 175 AEILNLLVELQCESNLTYLMVTHDLGVIAHlCQKVAVMQ 213
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-217 |
1.83e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 17 RNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR-VQMVFQDpygslhpR 95
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgIAYVPED-------R 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 HTIGDILEEP------------LQIHGIKDRdSRIHTLLDKVGlnRAFRDRYPH------QLSGGQRQRVAIARALILEP 157
Cdd:COG1129 337 KGEGLVLDLSirenitlasldrLSRGGLLDR-RRERALAEEYI--KRLRIKTPSpeqpvgNLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 158 QVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-199 |
2.48e-26 |
|
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: 102.86 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLftHW---DGELAIDGKP--------L 69
Cdd:COG1119 3 LLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD--LPptyGNDVRLFGERrggedvweL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 70 EKRI------------SRERCRrvQMVFQDPYGSLHPRHTIGDILEEplqihgikdrdsRIHTLLDKVGLnRAFRDRYPH 137
Cdd:COG1119 77 RKRIglvspalqlrfpRDETVL--DVVLSGFFDSIGLYREPTDEQRE------------RARELLELLGL-AHLADRPFG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 138 QLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDL 199
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHV 203
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-228 |
2.00e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.10 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGegeKRnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPlekrISR----E 76
Cdd:COG1137 3 TLEAENLVKSYG---KR-TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED----ITHlpmhK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCRR-VQMVFQDPygSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARAL 153
Cdd:COG1137 75 RARLgIGYLPQEA--SIFRKLTVEDNILAVLELRKLskKEREERLEELLEEFGITH-LRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 154 ILEPQVLLLDEPTSALD-VSVqAEILNLLVELQcESNLTYLMVTHD----LGViahlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVLITDHNvretLGI----CDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-216 |
2.02e-25 |
|
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: 97.52 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGlfthwdgelaiDGKPLEKRISRercrrv 81
Cdd:cd03221 1 IELENLSKTYGG----KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-----------ELEPDEGIVTW------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 qmvfqdpygslHPRHTIGdileeplqihgikdrdsrihtlldkvglnrafrdrYPHQLSGGQRQRVAIARALILEPQVLL 161
Cdd:cd03221 60 -----------GSTVKIG-----------------------------------YFEQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 162 LDEPTSALDV-SVQAeILNLLVELQCesnlTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:cd03221 94 LDEPTNHLDLeSIEA-LEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-216 |
2.33e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.86 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTH--WDGELAIDGKPLEKRISRERCRR-VQMVFQDPygSLHPRHT 97
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEELQASNIRDTERAgIAIIHQEL--ALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 IGDIL---EEPLQiHGIKDRD---SRIHTLLDKVGLnrafrDRYPH----QLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:PRK13549 99 VLENIflgNEITP-GGIMDYDamyLRAQKLLAQLKL-----DINPAtpvgNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2084886466 168 ALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:PRK13549 173 SLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-245 |
2.81e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.16 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGlFTHWDGELAIDGKPLeKRISRERCRR- 80
Cdd:PRK11174 350 IEAEDLEILSPDG---KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIEL-RELDPESWRKh 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDP---YGSLHPRHTIGDIleeplQIHgikdrDSRIHTLLDKVGLNRaFRDRYPH-----------QLSGGQRQR 146
Cdd:PRK11174 425 LSWVGQNPqlpHGTLRDNVLLGNP-----DAS-----DEQLQQALENAWVSE-FLPLLPQgldtpigdqaaGLSVGQAQR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 147 VAIARALILEPQVLLLDEPTSALDVSVQAEILNLLveLQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDAL 226
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL--NAASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAEL 570
|
250
....*....|....*....
gi 2084886466 227 VagQAKTDYTQMLVNASQQ 245
Cdd:PRK11174 571 S--QAGGLFATLLAHRQEE 587
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-203 |
8.10e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.88 E-value: 8.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEK----RISRE 76
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCRRVQMVFQDPYgsLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNRAFrDRYPHQLSGGQRQRVAIARALI 154
Cdd:PRK10535 84 RREHFGFIFQRYH--LLSHLTAAQNVEVPAVYAGLerKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIA 203
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAA 208
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
8-230 |
1.13e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 102.51 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQD 87
Cdd:TIGR01846 460 NIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQE 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 PYgsLHPRHTIGDI-LEEP----------LQIHGIKDRDSRI----HTLLDKVGLNrafrdryphqLSGGQRQRVAIARA 152
Cdd:TIGR01846 540 NV--LFSRSIRDNIaLCNPgapfehvihaAKLAGAHDFISELpqgyNTEVGEKGAN----------LSGGQRQRIAIARA 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 153 LILEPQVLLLDEPTSALDVSVQAEILNLLVELqCEsNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVAGQ 230
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREI-CR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLALQ 682
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-239 |
1.48e-24 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 97.94 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDpyGSLHPRHTIG 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQE--NVLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 100 DI--------LEEPLQIHGIKDRDSRIHTLldKVGLNRAFRDRyPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDV 171
Cdd:cd03252 95 NIaladpgmsMERVIEAAKLAGAHDFISEL--PEGYDTIVGEQ-GAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 172 SVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVAGQAKTDYTQML 239
Cdd:cd03252 172 ESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-218 |
1.90e-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: 97.34 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 16 KRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWD---GELAIDGKPLEKRISRERCRRVQmvfQDPYgsL 92
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKCVAYVR---QDDI--L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 93 HPRHTIGDILEEPLQIHGIKDRDSRIHTLLDKVGL-----NRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLlrdlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 168 ALDVSVQAEILNLLVELqCESNLTYLMVTHDLGV-IAHLCQKVAVMQYGKIL 218
Cdd:cd03234 173 GLDSFTALNLVSTLSQL-ARRNRIVILTIHQPRSdLFRLFDRILLLSSGEIV 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-228 |
2.07e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.58 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKrISRERCRR-VQMVFQ 86
Cdd:PRK13657 339 DVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT-VTRASLRRnIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 87 DPygSLHPRhTIGDIL--------EEPL-------QIHG-IKDRDSRIHTLLDKVGLnrafrdryphQLSGGQRQRVAIA 150
Cdd:PRK13657 417 DA--GLFNR-SIEDNIrvgrpdatDEEMraaaeraQAHDfIERKPDGYDTVVGERGR----------QLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 151 RALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVA 558
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-218 |
3.39e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 97.37 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 22 DNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR-VQMVFQDP--YGSL------ 92
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQHVrlFREMtvienl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 93 ----HpRHT----IGDILEEPLQIHGIKDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDE 164
Cdd:PRK11300 102 lvaqH-QQLktglFSGLLKTPAFRRAESEALDRAATWLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 165 PTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-218 |
4.03e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 96.83 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHwDGELAIDGKPLEK----RISRERCRRVQ-------M-VFQdp 88
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDwsaaELARHRAYLSQqqsppfaMpVFQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 89 YGSLH-PRHTIGDILEeplqihgikdrdSRIHTLLDKVGLNrafrDRYP---HQLSGGQRQRVAIARALI-------LEP 157
Cdd:COG4138 89 YLALHqPAGASSEAVE------------QLLAQLAEALGLE----DKLSrplTQLSGGEWQRVRLAAVLLqvwptinPEG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 158 QVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:COG4138 153 QLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-197 |
6.98e-24 |
|
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: 94.14 E-value: 6.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGelaidgkplekRISRERCRRV 81
Cdd:cd03223 1 IELENLSLATPDG---RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG-----------RIGMPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPY---GSLhprhtigdileeplqihgikdRDSRIhtlldkvglnrafrdrYP--HQLSGGQRQRVAIARALILE 156
Cdd:cd03223 67 LFLPQRPYlplGTL---------------------REQLI----------------YPwdDVLSGGEQQRLAFARLLLHK 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2084886466 157 PQVLLLDEPTSALDVSVQAEILNLLVELQCesnlTYLMVTH 197
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKELGI----TVISVGH 146
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-217 |
8.08e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 -VQMVFQDPYGSLhprhtIGDILEE------------PLQIHGIKDRdsrihtLLDKVGLNRaFRDRYPHQLSGGQRQRV 147
Cdd:PRK13644 78 lVGIVFQNPETQF-----VGRTVEEdlafgpenlclpPIEIRKRVDR------ALAEIGLEK-YRHRSPKTLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIaHLCQKVAVMQYGKI 217
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-219 |
1.23e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.61 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLfTHWDGELAIDGKPL--EKRISRERC 78
Cdd:PRK14239 5 ILQVSDLSVYYN----KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM-NDLNPEVTITGSIVynGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 RRVQ------MVFQDPygslHP-RHTIGDILEEPLQIHGIKDR---DSRIHTLLDKVGLNRAFRDRYpHQ----LSGGQR 144
Cdd:PRK14239 80 DTVDlrkeigMVFQQP----NPfPMSIYENVVYGLRLKGIKDKqvlDEAVEKSLKGASIWDEVKDRL-HDsalgLSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 145 QRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHLCQKVAVMQYGKILD 219
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDGDLIE 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
1.81e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcRRV 81
Cdd:PRK13537 8 IDFRNVEKRYGD----KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-QRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQdpYGSLHPRHTIgdilEEPLQIHG------IKDRDSRIHTLLDKVGL-NRAfrDRYPHQLSGGQRQRVAIARALI 154
Cdd:PRK13537 83 GVVPQ--FDNLDPDFTV----RENLLVFGryfglsAAAARALVPPLLEFAKLeNKA--DAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-228 |
2.15e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.76 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQ------------------VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLF--THwdG 60
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILepTS--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 61 ELAIDGK---PLEkrisrercrrVQMVFqdpygslHPRHT-------IGdileeplQIHGIKDRDsrIHTLLDKV----G 126
Cdd:COG1134 82 RVEVNGRvsaLLE----------LGAGF-------HPELTgreniylNG-------RLLGLSRKE--IDEKFDEIvefaE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 127 LNRAFrDRyP-HQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHL 205
Cdd:COG1134 136 LGDFI-DQ-PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRL 212
|
250 260
....*....|....*....|...
gi 2084886466 206 CQKVAVMQYGKILDSLTVDALVA 228
Cdd:COG1134 213 CDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-216 |
2.58e-23 |
|
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: 97.97 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTH--WDGELAIDGKPLEKRISRERC 78
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSPLKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 RR-VQMVFQDPygSLHPRHTI-------------GDILEEPLQIHgikdrdsRIHTLLDKVGLNRAFRDRYPHQLSGGQR 144
Cdd:TIGR02633 77 RAgIVIIHQEL--TLVPELSVaeniflgneitlpGGRMAYNAMYL-------RAKNLLRELQLDADNVTRPVGDYGGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 145 QRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:TIGR02633 148 QLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-201 |
1.12e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 92.04 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPL-EKRISRERcrrvQMVFQ 86
Cdd:TIGR01189 5 NLACSRGERM--LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHE----NILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 87 DPYGSLHPRHTIGDILEEPLQIHGIKDRDsrIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPT 166
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFWAAIHGGAQRT--IEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 2084886466 167 SALDVSVQAeILNLLVELQCESNLTYLMVTH-DLGV 201
Cdd:TIGR01189 156 TALDKAGVA-LLAGLLRAHLARGGIVLLTTHqDLGL 190
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-230 |
1.26e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.31 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 31 GEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQD--PYGSLHPRHTIGdILEEP--- 105
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlpAAEGMTVRELVA-IGRYPwhg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 106 -LQIHGIKDRDsRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVEL 184
Cdd:PRK10575 116 aLGRFGAADRE-KVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2084886466 185 QCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAGQ 230
Cdd:PRK10575 194 SQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-202 |
1.52e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 96.24 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 3 EINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVlkclAGLFTHW----DGELAIDGKPLEK-RIS--R 75
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI----ANLLTRFydidEGEILLDGHDLRDyTLAslR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 76 ERCRRV-QMV--FQD------PYGSlHPRHTIGDILEEPLQIHG---IKDRDSRIHTLldkVGLNRAFrdryphqLSGGQ 143
Cdd:PRK11176 417 NQVALVsQNVhlFNDtianniAYAR-TEQYSREQIEEAARMAYAmdfINKMDNGLDTV---IGENGVL-------LSGGQ 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 144 RQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVI 202
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTI 542
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-218 |
1.98e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.15 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLE--KRISRERCRRVQMVFQDPYGSLHPRH 96
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 97 TIGDILEEpLQIHGIKDRD--SRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQ 174
Cdd:PRK13638 95 IDSDIAFS-LRNLGVPEAEitRRVDEALTLVDAQH-FRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2084886466 175 AEILNLLVELQCESNLTyLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-219 |
2.27e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.85 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 7 LNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT-----HWDGELAIDGKPL-EKRISRERCRR 80
Cdd:PRK14271 25 VNLTLGFAGK--TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIfNYRDVLEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPygSLHPRHTIGDILEEpLQIHGI---KDRDSRIHTLLDKVGLNRAFRDRY---PHQLSGGQRQRVAIARALI 154
Cdd:PRK14271 103 VGMLFQRP--NPFPMSIMDNVLAG-VRAHKLvprKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHLCQKVAVMQYGKILD 219
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-225 |
2.77e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 95.24 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTH--WDGELAIDGKPLE-KRISRERCRRVQMVFQD----PYGSlh 93
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVCRfKDIRDSEALGIVIIHQElaliPYLS-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 prhtigdILE------EPLQiHGIKDRD---SRIHTLLDKVGLNRAfrdryPHQLSG----GQRQRVAIARALILEPQVL 160
Cdd:NF040905 95 -------IAEniflgnERAK-RGVIDWNetnRRARELLAKVGLDES-----PDTLVTdigvGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 161 LLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDA 225
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELK-AQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-217 |
3.85e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.61 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT-HWDGELAIDGKPLEKRISRERCRR-VQMVFQD--PYG----- 90
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQgIAMVPEDrkRDGivpvm 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 91 --------SLHPRHTIGDILEEPLQIHGIKDRDSRIH----TLLDKVGlnrafrdryphQLSGGQRQRVAIARALILEPQ 158
Cdd:PRK13549 357 gvgknitlAALDRFTGGSRIDDAAELKTILESIQRLKvktaSPELAIA-----------RLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-220 |
4.56e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.87 E-value: 4.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRV---------------QMVF 85
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVpqseevdwsfpvlveDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 86 QDPYGSLHPrhtigdileepLQIHGIKDRdSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEP 165
Cdd:PRK15056 103 MGRYGHMGW-----------LRRAKKRDR-QIVTAALARVDMVE-FRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 166 TSALDVSVQAEILNLLVELQCESNlTYLMVTHDLGVIAHLCQkVAVMQYGKILDS 220
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCD-YTVMVKGTVLAS 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-238 |
5.12e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 94.78 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEkRISRERCRR- 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQg 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPY---GSLHPRHTIG-DILE-------EPLQIHG-IKDRDSRIHTLLDKVGLNrafrdryphqLSGGQRQRVA 148
Cdd:PRK10790 417 VAMVQQDPVvlaDTFLANVTLGrDISEeqvwqalETVQLAElARSLPDGLYTPLGEQGNN----------LSVGQKQLLA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 149 IARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVR--EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLA 563
|
250
....*....|
gi 2084886466 229 GQAKtdYTQM 238
Cdd:PRK10790 564 AQGR--YWQM 571
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-199 |
6.69e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.94 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFthwdgelaidgKPLEKRISRERCRR 80
Cdd:PRK09544 4 LVSLENVSVSFGQ----RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV-----------APDEGVIKRNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQdpygSLHPRHTIGDILEEPLQIH-GIKDRDsrIHTLLDKVglNRAFRDRYPHQ-LSGGQRQRVAIARALILEPQ 158
Cdd:PRK09544 69 IGYVPQ----KLYLDTTLPLTVNRFLRLRpGTKKED--ILPALKRV--QAGHLIDAPMQkLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDL 199
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-220 |
7.46e-22 |
|
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: 89.89 E-value: 7.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGL--FTHWDGELAIDGKPLEKRISRERCR 79
Cdd:cd03217 1 LEIKDLHVSVGGKE----ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 80 R-VQMVFQdpygslhprhtigdileEPLQIHGIKDRDsrihtLLDKVGLNrafrdryphqLSGGQRQRVAIARALILEPQ 158
Cdd:cd03217 77 LgIFLAFQ-----------------YPPEIPGVKNAD-----FLRYVNEG----------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHL-CQKVAVMQYGKILDS 220
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLR-EEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKS 186
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-217 |
9.56e-22 |
|
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: 89.78 E-value: 9.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgeKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKrISRERCRR- 80
Cdd:cd03369 7 IEVENLSVRYAP--DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIST-IPLEDLRSs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPY---GSLhpRHTIgDILEEplqihgikDRDSRIHTLLdKV---GLNrafrdryphqLSGGQRQRVAIARALI 154
Cdd:cd03369 84 LTIIPQDPTlfsGTI--RSNL-DPFDE--------YSDEEIYGAL-RVsegGLN----------LSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084886466 155 LEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDLGVIAHlCQKVAVMQYGKI 217
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEF--TNSTILTIAHRLRTIID-YDKILVMDAGEV 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-230 |
1.53e-21 |
|
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: 92.97 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVlDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT-HWDGELAIDGKPLEKRISRERCR 79
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 80 R-VQMVFQDpygslHPRHTIGDIL--------------EEPLQIHGIKDRDSrIHTLLDKVGLNRAFRDRYPHQLSGGQR 144
Cdd:TIGR02633 336 AgIAMVPED-----RKRHGIVPILgvgknitlsvlksfCFKMRIDAAAELQI-IGSAIQRLKVKTASPFLPIGRLSGGNQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 145 QRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESnLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVD 224
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNH 488
|
....*.
gi 2084886466 225 ALVAGQ 230
Cdd:TIGR02633 489 ALTQEQ 494
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-201 |
2.01e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQmvFQD 87
Cdd:PRK13539 7 DLACVRGGR--VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 PygsLHPRHTIGDILEEPLQIHGikDRDSRIHTLLDKVGLNRAFRDRYPHqLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:PRK13539 83 A---MKPALTVAENLEFWAAFLG--GEELDIAAALEAVGLAPLAHLPFGY-LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2084886466 168 ALDVSVQAEILNlLVELQCESNLTYLMVTH-DLGV 201
Cdd:PRK13539 157 ALDAAAVALFAE-LIRAHLAQGGIVIAATHiPLGL 190
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-199 |
2.06e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.21 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINhlNLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKrISRERC-- 78
Cdd:PRK11831 7 LVDMR--GVSFTRGNR--CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPA-MSRSRLyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 --RRVQMVFQDpyGSLHPRHTIGDILEEPLQIHgIKDRDSRIHTL----LDKVGLnRAFRDRYPHQLSGGQRQRVAIARA 152
Cdd:PRK11831 82 vrKRMSMLFQS--GALFTDMNVFDNVAYPLREH-TQLPAPLLHSTvmmkLEAVGL-RGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2084886466 153 LILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDL 199
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-230 |
3.56e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAfgEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:PRK10895 1 MATLTAKNLA--KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 -VQMVFQDPygSLHPRHTIGDILEEPLQIH---GIKDRDSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILE 156
Cdd:PRK10895 79 gIGYLPQEA--SIFRRLSVYDNLMAVLQIRddlSAEQREDRANELMEEFHIEH-LRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 157 PQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVAGQ 230
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-217 |
3.96e-21 |
|
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: 88.36 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 5 NHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFthwdgelaidgKPLEKRIsrERCRRVQMV 84
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIY-----------PPDSGTV--TVRGRVSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 85 FqDPYGSLHPRHTIGDILEEPLQIHGI--KDRDSRIHTLLDKVGLNRAFRDRYPHqLSGGQRQRVAIARALILEPQVLLL 162
Cdd:cd03220 89 L-GLGGGFNPELTGRENIYLNGRLLGLsrKEIDEKIDEIIEFSELGDFIDLPVKT-YSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 163 DEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-218 |
9.54e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.07 E-value: 9.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 27 SVKEGEIYGLVGESGSGKTTVLKCLAGLFTHwDGELAIDGKPLEK----RISRERCRRVQM--------VFQdpYGSLHp 94
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAwsaaELARHRAYLSQQqtppfampVFQ--YLTLH- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 95 rhtigdiLEEPLQIHGIKDRDSRIHTLL---DKVGlnrafrdRYPHQLSGGQRQRVAIA-------RALILEPQVLLLDE 164
Cdd:PRK03695 94 -------QPDKTRTEAVASALNEVAEALgldDKLG-------RSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 165 PTSALDVSVQAeILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK03695 160 PMNSLDVAQQA-ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-204 |
1.58e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.40 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINhlNLAFGEGEKRnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEkrisreRCRr 80
Cdd:PRK13538 1 MLEAR--NLACERDERI--LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR------RQR- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 vqmvfQDPYGSL----HprHT-IGDIL--EEPLQ----IHGIKDRDsRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAI 149
Cdd:PRK13538 70 -----DEYHQDLlylgH--QPgIKTELtaLENLRfyqrLHGPGDDE-ALWEALAQVGL-AGFEDVPVRQLSAGQQRRVAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 150 ARaLILEPQVL-LLDEPTSALDVSVQAEILNLLVElQCESNLTYLMVTH-DLGVIAH 204
Cdd:PRK13538 141 AR-LWLTRAPLwILDEPFTAIDKQGVARLEALLAQ-HAEQGGMVILTTHqDLPVASD 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-198 |
1.74e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGlfthwdgELAID-GKplekrisRERCR 79
Cdd:COG0488 315 VLELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-------ELEPDsGT-------VKLGE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 80 RVQMVF--QDpYGSLHPRHTIGDILEEplqiHGIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEP 157
Cdd:COG0488 377 TVKIGYfdQH-QEELDPDKTVLDELRD----GAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2084886466 158 QVLLLDEPTSALDVsvqaEILNLLVELqcesnL-----TYLMVTHD 198
Cdd:COG0488 452 NVLLLDEPTNHLDI----ETLEALEEA-----LddfpgTVLLVSHD 488
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-216 |
1.77e-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: 85.98 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGE-KRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIdgkplekrisrerCRR 80
Cdd:cd03250 1 ISVEDASFTWDSGEqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPY---GSLhpRHTI--GDILEEPLQIHGIK----DRDSRIHTLLDKV-----GLNrafrdryphqLSGGQRQR 146
Cdd:cd03250 68 IAYVSQEPWiqnGTI--RENIlfGKPFDEERYEKVIKacalEPDLEILPDGDLTeigekGIN----------LSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 147 VAIARALILEPQVLLLDEPTSALDVSVQAEILNLLV--ELQCESnlTYLMVTHDLGVIAHlCQKVAVMQYGK 216
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCIlgLLLNNK--TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
8-255 |
2.34e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 89.88 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLeKRISRERCRR-VQMVFQ 86
Cdd:COG5265 362 NVSFGYDPER-PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQASLRAaIGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 87 DP------------YGslHPRHTIGDILE--EPLQIHGIkdrdsrIHTLLD----KVGlNRAFRdryphqLSGGQRQRVA 148
Cdd:COG5265 440 DTvlfndtiayniaYG--RPDASEEEVEAaaRAAQIHDF------IESLPDgydtRVG-ERGLK------LSGGEKQRVA 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 149 IARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqcESNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLA 581
|
250 260
....*....|....*....|....*..
gi 2084886466 229 GQAKtdYTQMLvnASQQYSREMAREVA 255
Cdd:COG5265 582 QGGL--YAQMW--ARQQEEEEAEEALA 604
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-201 |
3.22e-20 |
|
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: 85.62 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEkRISRERCRRVQMVFQDP--YGSLHPRht 97
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-FQRDSIARGLLYLGHAPgiKTTLSVL-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 igdileEPLQIHGIKDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEI 177
Cdd:cd03231 92 ------ENLRFWHADHSDEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|....*
gi 2084886466 178 LNLLVElQCESNLTYLMVTH-DLGV 201
Cdd:cd03231 165 AEAMAG-HCARGGMVVLTTHqDLGL 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-199 |
5.72e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.99 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKC------------LAGLFTHWDGEL-AIDGKP 68
Cdd:PRK14243 11 LRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlipgfrVEGKVTFHGKNLyAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 69 LEKRisrercRRVQMVFQDPYGslHPRhTIGDILEEPLQIHGIK-DRDSRIHTLLDKVGLNRAFRDRYPHQ---LSGGQR 144
Cdd:PRK14243 87 VEVR------RRIGMVFQKPNP--FPK-SIYDNIAYGARINGYKgDMDELVERSLRQAALWDEVKDKLKQSglsLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 145 QRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQceSNLTYLMVTHDL 199
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK--EQYTIIIVTHNM 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-216 |
5.82e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 5.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcRRVQMVFQdpYGSLHPRHTIG 99
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR-ARIGVVPQ--FDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 100 DILEEPLQIHGIKDRDSR--IHTLLDKVGLNRAFRDRYPhQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEI 177
Cdd:PRK13536 133 ENLLVFGRYFGMSTREIEavIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190
....*....|....*....|....*....|....*....
gi 2084886466 178 LNLLVELQCESNlTYLMVTHDLGVIAHLCQKVAVMQYGK 216
Cdd:PRK13536 212 WERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-205 |
7.96e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.01 E-value: 7.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 10 AFGEGEKRNQ--VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGlfthwdgelaidgkplekrisRERCRRVQMVFQD 87
Cdd:COG2401 33 AFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---------------------ALKGTPVAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 PYGSLHPRHTIGDILeeplqihgikDRDSRIHT---LLDKVGLNRA--FRDRYPHqLSGGQRQRVAIARALILEPQVLLL 162
Cdd:COG2401 92 PDNQFGREASLIDAI----------GRKGDFKDaveLLNAVGLSDAvlWLRRFKE-LSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2084886466 163 DEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHL 205
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-228 |
1.10e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.87 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 22 DNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcRRVQMVFQ--DPYGSLHPRhtig 99
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR-RRVGYMSQafSLYGELTVR---- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 100 dileEPLQIH------GIKDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:NF033858 358 ----QNLELHarlfhlPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 174 QAEILNLLVELQCESNLTYLMVTHDLGViAHLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:NF033858 433 RDMFWRLLIELSREDGVTIFISTHFMNE-AERCDRISLMHAGRVLASDTPAALVA 486
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-216 |
1.43e-19 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 84.73 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 27 SVKEGEIYGLVGESGSGKTTVLKCLAGLFT----------HWDGEL-AIDGKPLEKRISRERCRRVQMVFQDPYGSLHPR 95
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKpnlgkfddppDWDEILdEFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 H---TIGDILEEplqihgiKDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVS 172
Cdd:cd03236 102 AvkgKVGELLKK-------KDERGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2084886466 173 VQAEILNLLVELQCESNlTYLMVTHDLGVIAHLCQKVAVMqYGK 216
Cdd:cd03236 174 QRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL-YGE 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-228 |
1.46e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.55 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGL--FTHWDGEL----------------A 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 64 IDGKP-----------------LEKRISRERCRRVQMVFQDPYgSLHPRHTIGDILEEPLQIHGIKDRDS--RIHTLLDK 124
Cdd:TIGR03269 77 KVGEPcpvcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTF-ALYGDDTVLDNVLEALEEIGYEGKEAvgRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 125 VGLNRafrdRYPH---QLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGV 201
Cdd:TIGR03269 156 VQLSH----RITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|....*..
gi 2084886466 202 IAHLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-231 |
2.33e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.16 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEK----RISRE 76
Cdd:PRK11614 5 MLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtaKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCRRVqmvfqdPYGS-LHPRHTIgdilEEPLQIHGI-------KDRDSRIHTLLDKVGLNRAFRdryPHQLSGGQRQRVA 148
Cdd:PRK11614 81 AVAIV------PEGRrVFSRMTV----EENLAMGGFfaerdqfQERIKWVYELFPRLHERRIQR---AGTMSGGEQQMLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 149 IARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVA 228
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLR-EQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
...
gi 2084886466 229 GQA 231
Cdd:PRK11614 227 NEA 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-217 |
2.70e-19 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 86.73 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQD 87
Cdd:COG4618 335 NLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 PygSLHPrHTIGD-I--LEEPlqihgikDRD--------SRIHTLLDKvglnraFRDRY-------PHQLSGGQRQRVAI 149
Cdd:COG4618 415 V--ELFD-GTIAEnIarFGDA-------DPEkvvaaaklAGVHEMILR------LPDGYdtrigegGARLSGGQRQRIGL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 150 ARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHlCQKVAVMQYGKI 217
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSLLAA-VDKLLVLRDGRV 544
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-218 |
2.75e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.49 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAfgegEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT--------HWDGELAIDGKPLeKR 72
Cdd:PRK13547 1 MLTADHLHVA----RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPL-AA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 73 ISRERCRRVQMVFQ-----------DPYGSL----HPR------HTIGDILEEPLQIHGIKDRDSRIHTlldkvglnraf 131
Cdd:PRK13547 76 IDAPRLARLRAVLPqaaqpafafsaREIVLLgrypHARragaltHRDGEIAWQALALAGATALVGRDVT----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 132 rdryphQLSGGQRQRVAIARAL---------ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVI 202
Cdd:PRK13547 145 ------TLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLA 218
|
250
....*....|....*.
gi 2084886466 203 AHLCQKVAVMQYGKIL 218
Cdd:PRK13547 219 ARHADRIAMLADGAIV 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-226 |
2.78e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 3 EINHLNLAfgeGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcRRVQ 82
Cdd:COG3845 259 EVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER-RRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 83 MVF--QDPYGS-LHPRHTIGD--ILE----EPLQIHGIKDRDsRIHTLLDKvgLNRAFRDRYPH------QLSGGQRQRV 147
Cdd:COG3845 335 VAYipEDRLGRgLVPDMSVAEnlILGryrrPPFSRGGFLDRK-AIRAFAEE--LIEEFDVRTPGpdtparSLSGGNQQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 148 AIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-224 |
4.15e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.19 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 3 EINHLNLAFGEGEkrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGlftHW-----DGELAIDGKP-LEKRISrE 76
Cdd:COG0396 2 EIKNLHVSVEGKE----ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG---HPkyevtSGSILLDGEDiLELSPD-E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 77 RCRR-VQMVFQDPygslhP-----------RHTIGDILEEPLqihGIKDRDSRIHTLLDKVGLNRAFRDRYPHQ-LSGGQ 143
Cdd:COG0396 74 RARAgIFLAFQYP-----VeipgvsvsnflRTALNARRGEEL---SAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 144 RQRVAIARALILEPQVLLLDEPTSALDV-SVQ--AEILNLLVelqcESNLTYLMVTHdlgviahlcqkvavmqYGKILDS 220
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIdALRivAEGVNKLR----SPDRGILIITH----------------YQRILDY 205
|
....
gi 2084886466 221 LTVD 224
Cdd:COG0396 206 IKPD 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-226 |
6.05e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 12 GEGEKrnqvldNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRvQMVF--QDpy 89
Cdd:PRK15439 276 GEGFR------NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR-GLVYlpED-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 90 gslhpRHTIGDILEEPLQ------IHGIKdrdsrihTLLDKVGLNRAFRDRYPHQ--------------LSGGQRQRVAI 149
Cdd:PRK15439 347 -----RQSSGLYLDAPLAwnvcalTHNRR-------GFWIKPARENAVLERYRRAlnikfnhaeqaartLSGGNQQKVLI 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 150 ARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:PRK15439 415 AKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-197 |
8.51e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLF---THWDGELAIDGKPLEKRISRERC 78
Cdd:TIGR00955 22 QLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPIDAKEMRAIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 RRVQmvfQDP--YGSLHPRHTIGDILEEPLQIHGIKD-RDSRIHTLLDKVGLNRAFRDR--YPHQ---LSGGQRQRVAIA 150
Cdd:TIGR00955 102 AYVQ---QDDlfIPTLTVREHLMFQAHLRMPRRVTKKeKRERVDEVLQALGLRKCANTRigVPGRvkgLSGGERKRLAFA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2084886466 151 RALILEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTH 197
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIH 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-230 |
9.29e-19 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 82.77 E-value: 9.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAG--LFTHWDGELAIDGKPLEKRISRERC 78
Cdd:CHL00131 7 ILEIKNLHASVNE----NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 RR-VQMVFQDP---------------YGSLHPRHTIGDIleEPLQIHGIkdrdsrIHTLLDKVGLNRAFRDRYPHQ-LSG 141
Cdd:CHL00131 83 HLgIFLAFQYPieipgvsnadflrlaYNSKRKFQGLPEL--DPLEFLEI------INEKLKLVGMDPSFLSRNVNEgFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 142 GQRQRVAIARALILEPQVLLLDEPTSALDVS---VQAEILNLLVelqcESNLTYLMVTHDLGVIAHLC-QKVAVMQYGKI 217
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLM----TSENSIILITHYQRLLDYIKpDYVHVMQNGKI 230
|
250
....*....|...
gi 2084886466 218 LdsLTVDALVAGQ 230
Cdd:CHL00131 231 I--KTGDAELAKE 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-211 |
2.77e-18 |
|
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: 81.30 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 27 SVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDG-----KPleKRISRERCRRVQ-MVFQDPYGSLHPRHTIGD 100
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsyKP--QYIKADYEGTVRdLLSSITKDFYTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 101 ILEePLQIHGIKDRDSRihtlldkvglnrafrdryphQLSGGQRQRVAIARALILEPQVLLLDEPTSALDV---SVQAEI 177
Cdd:cd03237 99 IAK-PLQIEQILDREVP--------------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMASKV 157
|
170 180 190
....*....|....*....|....*....|....
gi 2084886466 178 LNLLVElqcESNLTYLMVTHDLGVIAHLCQKVAV 211
Cdd:cd03237 158 IRRFAE---NNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-228 |
8.52e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 8.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPlekrisrercrrvqMVFQDPYGSLHprHTI 98
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--------------MRFASTTAALA--AGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 99 GDILEEpLQI------------------HGIKDRD---SRIHTLLDKVGLnrafrDRYPHQ----LSGGQRQRVAIARAL 153
Cdd:PRK11288 82 AIIYQE-LHLvpemtvaenlylgqlphkGGIVNRRllnYEAREQLEHLGV-----DIDPDTplkyLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 154 ILEPQVLLLDEPTSALDvSVQAEIL-NLLVELQCESNLTyLMVTHDLGVIAHLCQKVAVMQYGKILDS------LTVDAL 226
Cdd:PRK11288 156 ARNARVIAFDEPTSSLS-AREIEQLfRVIRELRAEGRVI-LYVSHRMEEIFALCDAITVFKDGRYVATfddmaqVDRDQL 233
|
..
gi 2084886466 227 VA 228
Cdd:PRK11288 234 VQ 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-171 |
1.38e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.92 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR 80
Cdd:PRK11147 3 LISIHGAWLSFSD----APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQ-MVF-------QDPYGSLHPRHTIGDILE---------------EPLQIHGIKDRDSRIHTLLDKVGLNRafrDRYPH 137
Cdd:PRK11147 79 VEgTVYdfvaegiEEQAEYLKRYHDISHLVEtdpseknlnelaklqEQLDHHNLWQLENRINEVLAQLGLDP---DAALS 155
|
170 180 190
....*....|....*....|....*....|....
gi 2084886466 138 QLSGGQRQRVAIARALILEPQVLLLDEPTSALDV 171
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
8-219 |
1.54e-17 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 81.63 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLeKRISRERC-RRVQMVFQ 86
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL-KQWDRETFgKHIGYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 87 DPygSLHPRHTIGDI--LEEPLQIHGIKD--RDSRIHTLLDKV--GLNRAFRDRyPHQLSGGQRQRVAIARALILEPQVL 160
Cdd:TIGR01842 400 DV--ELFPGTVAENIarFGENADPEKIIEaaKLAGVHELILRLpdGYDTVIGPG-GATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 161 LLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAhLCQKVAVMQYGKILD 219
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITHRPSLLG-CVDKILVLQDGRIAR 533
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-218 |
2.67e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.90 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 17 RNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT---HWDGELAIDGKPLEK--RISRE-RCRRVQM--VFQDp 88
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVQRegRLARDiRKSRANTgyIFQQ- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 89 yGSLHPRHT------IGDILEEPLQIHGIK----DRDSRIHTLLDKVGLNRaFRDRYPHQLSGGQRQRVAIARALILEPQ 158
Cdd:PRK09984 95 -FNLVNRLSvlenvlIGALGSTPFWRTCFSwftrEQKQRALQALTRVGMVH-FAHQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKIL 218
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-217 |
3.41e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 6 HLNLAfgEGEKRNQV-------LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKR------ 72
Cdd:PRK10762 248 RLDKA--PGEVRLKVdnlsgpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdgl 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 73 ------ISRERCR---------RVQMV------FQDPYGSLH---PRHTIGDILeeplQIHGIK--DRDSRIhtlldkvG 126
Cdd:PRK10762 326 angivyISEDRKRdglvlgmsvKENMSltalryFSRAGGSLKhadEQQAVSDFI----RLFNIKtpSMEQAI-------G 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 127 LnrafrdryphqLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESnLTYLMVTHDLGVIAHLC 206
Cdd:PRK10762 395 L-----------LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMS 462
|
250
....*....|.
gi 2084886466 207 QKVAVMQYGKI 217
Cdd:PRK10762 463 DRILVMHEGRI 473
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-181 |
4.10e-17 |
|
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: 76.90 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 16 KRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT--HWDGELAIDGKPLEKRISRercrrvqmvfqdpygslh 93
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQR------------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 prhTIGDILEEPLQIHGIKDRDS-RIHTLLdkvglnRAfrdryphqLSGGQRQRVAIARALILEPQVLLLDEPTSALDVS 172
Cdd:cd03232 80 ---STGYVEQQDVHSPNLTVREAlRFSALL------RG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
....*....
gi 2084886466 173 VQAEILNLL 181
Cdd:cd03232 143 AAYNIVRFL 151
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-237 |
1.01e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.00 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRR-VQMVFQDpYGSLHPRHTIG 99
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQE-LNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 100 DI------LEEPLQIHGIKDRDSRihTLLDKVGLNRAFRDRYPhQLSGGQRQRVAIARALILEPQVLLLDEPTSAL---D 170
Cdd:PRK10982 93 NMwlgrypTKGMFVDQDKMYRDTK--AIFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 171 VSVQAEILNLLVELQCesNLTYlmVTHDLGVIAHLCQKVAVMQYGKILDS-----LTVDALVAGQAKTDYTQ 237
Cdd:PRK10982 170 VNHLFTIIRKLKERGC--GIVY--ISHKMEEIFQLCDEITILRDGQWIATqplagLTMDKIIAMMVGRSLTQ 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-222 |
1.04e-16 |
|
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: 79.67 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERcrrvQMVFQDPYGSLHPRH-TIG 99
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR----QSLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 100 DILEEPLQIHGIKDRDSRI--HTLLDKVGLNRAfRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEI 177
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLemEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2084886466 178 LNLLveLQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLT 222
Cdd:TIGR01257 1101 WDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-211 |
3.85e-16 |
|
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: 77.52 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 27 SVKEGEIYGLVGESGSGKTTVLKCLAGLFT----HWDGELAIDGKPleKRISRERCRRVQMVFqdpygslhpRHTIGDIL 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKpdegEVDEDLKISYKP--QYISPDYDGTVEEFL---------RSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 103 EeplqihgikdrDSRIHT-LLDKVGLNRAFrDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVS---VQAEIL 178
Cdd:COG1245 431 G-----------SSYYKTeIIKPLGLEKLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAI 498
|
170 180 190
....*....|....*....|....*....|...
gi 2084886466 179 NLLVElqcESNLTYLMVTHDLGVIAHLCQKVAV 211
Cdd:COG1245 499 RRFAE---NRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-222 |
4.08e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.26 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 24 VNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMvfqdpygsLHP--RHTIGDI 101
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIM--------LCPedRKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 102 leeplQIHGIKDR---DSRIHTLLDKVGLNRAFR----DRY----------PHQ----LSGGQRQRVAIARALILEPQVL 160
Cdd:PRK11288 344 -----PVHSVADNiniSARRHHLRAGCLINNRWEaenaDRFirslniktpsREQlimnLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 161 LLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLT 222
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA 479
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-202 |
1.61e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 16 KRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCR-RVQMVFQDP------ 88
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRsKIGVVSQDPllfsns 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 89 ------YG--SLHPRHTIGDILEEPLQ--------------------------------IHGIKD----RDSRIHTLLDK 124
Cdd:PTZ00265 476 iknnikYSlySLKDLEALSNYYNEDGNdsqenknkrnscrakcagdlndmsnttdsnelIEMRKNyqtiKDSEVVDVSKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 125 VGLN---RAFRDRY-------PHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLM 194
Cdd:PTZ00265 556 VLIHdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITII 635
|
....*...
gi 2084886466 195 VTHDLGVI 202
Cdd:PTZ00265 636 IAHRLSTI 643
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-222 |
1.63e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 14 GEKRNQVlDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRE----------RCRRVQM 83
Cdd:PRK09700 273 SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgmayitESRRDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 84 VFqdPYGSLHPRHTIGDILEE-----PLQIHGIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQ 158
Cdd:PRK09700 352 FF--PNFSIAQNMAISRSLKDggykgAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 159 VLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLT 222
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-202 |
2.70e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.84 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIY-----GLVGESGSGKTTVLKCLAGLFTHWDGE----LAIDGKPleKRISRERCRRVQMVFQ---DP 88
Cdd:PRK13409 350 LGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEvdpeLKISYKP--QYIKPDYDGTVEDLLRsitDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 89 YGSLHPRHTIGdileEPLQIHGIKDRDSRihtlldkvglnrafrdryphQLSGGQRQRVAIARALILEPQVLLLDEPTSA 168
Cdd:PRK13409 428 LGSSYYKSEII----KPLQLERLLDKNVK--------------------DLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
170 180 190
....*....|....*....|....*....|....*..
gi 2084886466 169 LDVS---VQAEILNLLVElqcESNLTYLMVTHDLGVI 202
Cdd:PRK13409 484 LDVEqrlAVAKAIRRIAE---EREATALVVDHDIYMI 517
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-228 |
2.80e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.75 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 10 AFGEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEK-RISRERcRRVQMVFQDP 88
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWR-SRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 89 Y-------GSL---HPRHTIGDIlEEPLQIHGIKDRDSRIHTLLD-KVGlNRAFrdryphQLSGGQRQRVAIARALILEP 157
Cdd:PRK10789 399 FlfsdtvaNNIalgRPDATQQEI-EHVARLASVHDDILRLPQGYDtEVG-ERGV------MLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 158 QVLLLDEPTSALDVSVQAEILNLLVelQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-198 |
3.15e-15 |
|
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: 74.59 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGE-LAIDGkplekrisrercRRVQMVFQDPYgsLHPRHT 97
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEaRPQPG------------IKVGYLPQEPQ--LDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 IGDILEEPLQ-IHGIKDR-----------DSRIHTLLDKVG-------------LNR-------AFR----DRYPHQLSG 141
Cdd:TIGR03719 85 VRENVEEGVAeIKDALDRfneisakyaepDADFDKLAAEQAelqeiidaadawdLDSqleiamdALRcppwDADVTKLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 142 GQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCesnlTYLMVTHD 198
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-215 |
5.05e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKP---LEKRISRErcRRVQMVFQD----PYGS 91
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQ--LGIGIIYQElsviDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 92 LHPRHTIGDILEEplQIHGI-----KDRDSRIHTLLDKVGLNRAFrDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPT 166
Cdd:PRK09700 97 VLENLYIGRHLTK--KVCGVniidwREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2084886466 167 SALDVSVQAEILNLLVELQCESNlTYLMVTHDLGVIAHLCQKVAVMQYG 215
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-216 |
8.71e-15 |
|
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: 73.28 E-value: 8.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 29 KEGEIYGLVGESGSGKTTVLKCLAGL----FTHWDGELAID-------GKPLE---KRISRERCR---RVQMVfqdpygS 91
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElkpnLGDYDEEPSWDevlkrfrGTELQdyfKKLANGEIKvahKPQYV------D 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 92 LHPRH---TIGDILEeplqihGIKDRDsRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSA 168
Cdd:COG1245 171 LIPKVfkgTVRELLE------KVDERG-KLDELAEKLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2084886466 169 LDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMqYGK 216
Cdd:COG1245 243 LDIYQRLNVARLIRELA-EEGKYVLVVEHDLAILDYLADYVHIL-YGE 288
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
12-164 |
9.77e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 73.29 E-value: 9.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 12 GEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRiSRERCRrvQM---VFQDP 88
Cdd:COG4615 339 GEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD-NREAYR--QLfsaVFSDF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 89 YgslhprhtigdILEEPLQIHGIKDrDSRIHTLLDKVGL-------NRAFRDRyphQLSGGQRQRVAIARALILEPQVLL 161
Cdd:COG4615 416 H-----------LFDRLLGLDGEAD-PARARELLERLELdhkvsveDGRFSTT---DLSQGQRKRLALLVALLEDRPILV 480
|
...
gi 2084886466 162 LDE 164
Cdd:COG4615 481 FDE 483
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-217 |
1.11e-14 |
|
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: 70.37 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKRN--QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHW---DGELAIDGKPLEKriSRERCRRvQ 82
Cdd:cd03233 8 NISFTTGKGRSkiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKE--FAEKYPG-E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 83 MVFQDPYGSLHPRHTIGDILEEPLQIHGikdrdsrihtlldkvglnrafrDRYPHQLSGGQRQRVAIARALILEPQVLLL 162
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKG----------------------NEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 163 DEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGV-IAHLCQKVAVMQYGKI 217
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQ 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-216 |
1.68e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 28 VKEGEIYGLVGESGSGKTTVLKCLAGL----FTHWDGELAID-------GKPLEKRISRERCRRVQMVFQDPYGSLHPRH 96
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGElipnLGDYEEEPSWDevlkrfrGTELQNYFKKLYNGEIKVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 97 ---TIGDILEEPLQiHGIKDRdsrihtLLDKVGLnRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:PRK13409 176 fkgKVRELLKKVDE-RGKLDE------VVERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2084886466 174 QAEILNLLVELQceSNLTYLMVTHDLGVIAHLCQKVAVMqYGK 216
Cdd:PRK13409 248 RLNVARLIRELA--EGKYVLVVEHDLAVLDYLADNVHIA-YGE 287
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-184 |
2.53e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.22 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLF--THWDGELAIDGKPLEKRIsrerCRRVQMVFQDP--YGSLHPR 95
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANNRKPTKQI----LKRTGFVTQDDilYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 HTIgdILEEPLQIHGIKDRDSRI---HTLLDKVGL----NRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSA 168
Cdd:PLN03211 159 ETL--VFCSLLRLPKSLTKQEKIlvaESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170
....*....|....*.
gi 2084886466 169 LDVSVQAEILNLLVEL 184
Cdd:PLN03211 237 LDATAAYRLVLTLGSL 252
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-170 |
6.68e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGegekRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRER-CRR 80
Cdd:NF033858 2 ARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQ-MvfqdPYG---SLHPRHTIgdilEEPLQI------HGIKDRDSRIHTLLDKVGLnRAFRDRYPHQLSGGQRQRVAIA 150
Cdd:NF033858 78 IAyM----PQGlgkNLYPTLSV----FENLDFfgrlfgQDAAERRRRIDELLRATGL-APFADRPAGKLSGGMKQKLGLC 148
|
170 180
....*....|....*....|
gi 2084886466 151 RALILEPQVLLLDEPTSALD 170
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVD 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-198 |
1.09e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 14 GEKRnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGE-LAIDGkplekrisrercRRVQMVFQDPYgsL 92
Cdd:PRK11819 17 PPKK-QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPG------------IKVGYLPQEPQ--L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 93 HPRHTIGDILEEPLQ-IHGIKDR-----------DSRIHTLLDKVG-----------------LNRAFrD--RYPH---- 137
Cdd:PRK11819 82 DPEKTVRENVEEGVAeVKAALDRfneiyaayaepDADFDALAAEQGelqeiidaadawdldsqLEIAM-DalRCPPwdak 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 138 --QLSGGQRQRVAIARALILEPQVLLLDEPTSALDvsvqAEILNLLvelqcESNL-----TYLMVTHD 198
Cdd:PRK11819 161 vtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWL-----EQFLhdypgTVVAVTHD 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-184 |
1.41e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 13 EGEKRnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLA-----GLFThwDGELAIDGKPLEKRISReRCRRVQMvfQD 87
Cdd:TIGR00956 772 KKEKR-VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervttGVIT--GGDRLVNGRPLDSSFQR-SIGYVQQ--QD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 pygsLH-PRHTIGDILE------EPLQIhGIKDRDSRIHTLLDKVGLnrafrDRYPHQLSG--------GQRQRVAIARA 152
Cdd:TIGR00956 846 ----LHlPTSTVRESLRfsaylrQPKSV-SKSEKMEYVEEVIKLLEM-----ESYADAVVGvpgeglnvEQRKRLTIGVE 915
|
170 180 190
....*....|....*....|....*....|...
gi 2084886466 153 LILEPQVLL-LDEPTSALDVSVQAEILNLLVEL 184
Cdd:TIGR00956 916 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-204 |
1.58e-13 |
|
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: 67.74 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLF------THWDGELAiDGKPLEKRISRERcRRVQMVFQDPYgslhp 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMqtlegkVHWSNKNE-SEPSFEATRSRNR-YSVAYAAQKPW----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 95 rhTIGDILEEPLqIHGIKDRDSRIHTLLDKVGLNRAFrDRYPH-----------QLSGGQRQRVAIARALILEPQVLLLD 163
Cdd:cd03290 90 --LLNATVEENI-TFGSPFNKQRYKAVTDACSLQPDI-DLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2084886466 164 EPTSALDVSV-----QAEILNLLVelqcESNLTYLMVTHDLGVIAH 204
Cdd:cd03290 166 DPFSALDIHLsdhlmQEGILKFLQ----DDKRTLVLVTHKLQYLPH 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-215 |
1.76e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.04 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRercrrvqmVFQDpYGSLHPRHTIGD 100
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD--------VHQN-MGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 101 IL--EEPL----QIHGI--KDRDSRIHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVS 172
Cdd:TIGR01257 2026 LLtgREHLylyaRLRGVpaEEIEKVANWSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2084886466 173 VQAEILNLLVELQCESNlTYLMVTHDLGVIAHLCQKVAVMQYG 215
Cdd:TIGR01257 2105 ARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-226 |
4.54e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPlekrisrercrrvqMVFQDPYGS------- 91
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE--------------VTFNGPKSSqeagigi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 92 ------LHPRHTIGDIL---EEPLQIHGIKDRD---SRIHTLLDKVGLNRAFRdRYPHQLSGGQRQRVAIARALILEPQV 159
Cdd:PRK10762 84 ihqelnLIPQLTIAENIflgREFVNRFGRIDWKkmyAEADKLLARLNLRFSSD-KLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084886466 160 LLLDEPTSALDVSVQAEILNLLVELQCES-NLTYlmVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGrGIVY--ISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-202 |
6.87e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 15 EKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLkclaglFTHwDGELAIDGKPLEKRISRERCRRVQMVFQDPY---GS 91
Cdd:PTZ00265 1239 EQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTV------FKN-SGKILLDGVDICDYNLKDLRNLFSIVSQEPMlfnMS 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 92 LHPRHTIGD---ILEEPLQIHGIKDRDSRIHTLLDKVGLNRAfrdRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSA 168
Cdd:PTZ00265 1312 IYENIKFGKedaTREDVKRACKFAAIDEFIESLPNKYDTNVG---PYGKSLSGGQKQRIAIARALLREPKILLLDEATSS 1388
|
170 180 190
....*....|....*....|....*....|....
gi 2084886466 169 LDVSVQAEILNLLVELQCESNLTYLMVTHDLGVI 202
Cdd:PTZ00265 1389 LDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-217 |
7.25e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.05 E-value: 7.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKrISRERCR-RVQMVFQDPY---GSLhpR 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK-IGLHDLRfKITIIPQDPVlfsGSL--R 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 HTIgdileEPLQIHGikdrDSRIHTLLDKVGLN---RAFRDRYPHQ-------LSGGQRQRVAIARALILEPQVLLLDEP 165
Cdd:TIGR00957 1378 MNL-----DPFSQYS----DEEVWWALELAHLKtfvSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 166 TSALDVSVQaEILNLLVELQCEsNLTYLMVTHDLGVIAHLcQKVAVMQYGKI 217
Cdd:TIGR00957 1449 TAAVDLETD-NLIQSTIRTQFE-DCTVLTIAHRLNTIMDY-TRVIVLDKGEV 1497
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-227 |
1.15e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 66.03 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFtHWDGELAIDGKPLEKrISRERCRRV 81
Cdd:cd03289 3 MTVKDLTAKYTEGG--NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNS-VPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 -----QMVF---------QDPYGslhprhtigdileeplqihgiKDRDSRIHTLLDKVGLnRAFRDRYPHQ--------- 138
Cdd:cd03289 79 fgvipQKVFifsgtfrknLDPYG---------------------KWSDEEIWKVAEEVGL-KSVIEQFPGQldfvlvdgg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 139 --LSGGQRQRVAIARALILEPQVLLLDEPTSALDvSVQAEILNLLVElQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGK 216
Cdd:cd03289 137 cvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQVIRKTLK-QAFADCTVILSEHRIEAMLE-CQRFLVIEENK 213
|
250
....*....|.
gi 2084886466 217 ILDSLTVDALV 227
Cdd:cd03289 214 VRQYDSIQKLL 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-228 |
2.31e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPY---GSLH--- 93
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVlfsGTVRfni 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 ---PRHTIGDILEEPLQIHgIKDRDSRihtllDKVGLNRAFRDRyPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALD 170
Cdd:PLN03232 1331 dpfSEHNDADLWEALERAH-IKDVIDR-----NPFGLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 171 VSVQAEILNLLVE--LQCesnlTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:PLN03232 1404 VRTDSLIQRTIREefKSC----TMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-217 |
2.36e-12 |
|
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: 66.51 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGK----PLEKRISRERCRRvQMVFQDPYGSLHPRH 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvPQQAWIQNDSLRE-NILFGKALNEKYYQQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 97 TI-GDILEEPLQIHGIKDRdsrihTLLDKVGLNrafrdryphqLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQA 175
Cdd:TIGR00957 733 VLeACALLPDLEILPSGDR-----TEIGEKGVN----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2084886466 176 EIL-NLLVELQCESNLTYLMVTHDlgvIAHLCQK--VAVMQYGKI 217
Cdd:TIGR00957 798 HIFeHVIGPEGVLKNKTRILVTHG---ISYLPQVdvIIVMSGGKI 839
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-228 |
9.60e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLeKRISRERCRR--VQMVFQDPYgsLHPRHT 97
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-ARLTPAKAHQlgIYLVPQEPL--LFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 IGDILEEPLQIHgiKDRDSRIHTLLDKVG--LNrafrdryPHQLSG----GQRQRVAIARALILEPQVLLLDEPTSALdv 171
Cdd:PRK15439 103 VKENILFGLPKR--QASMQKMKQLLAALGcqLD-------LDSSAGslevADRQIVEILRGLMRDSRILILDEPTASL-- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084886466 172 sVQAEILNLLVELQC--ESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI-----LDSLTVDALVA 228
Cdd:PRK15439 172 -TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIalsgkTADLSTDDIIQ 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-221 |
1.08e-11 |
|
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: 64.55 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHwDGELAIDGKPLEKrISRERCRRV 81
Cdd:TIGR01271 1218 MDVQGLTAKYTEAG--RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNS-VTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 -----QMVF---------QDPYGSLhprhtigdileeplqihgikdRDSRIHTLLDKVGLnRAFRDRYPHQ--------- 138
Cdd:TIGR01271 1294 fgvipQKVFifsgtfrknLDPYEQW---------------------SDEEIWKVAEEVGL-KSVIEQFPDKldfvlvdgg 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 139 --LSGGQRQRVAIARALILEPQVLLLDEPTSALDvSVQAEILNLLVElQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGK 216
Cdd:TIGR01271 1352 yvLSNGHKQLMCLARSILSKAKILLLDEPSAHLD-PVTLQIIRKTLK-QSFSNCTVILSEHRVEALLE-CQQFLVIEGSS 1428
|
....*..
gi 2084886466 217 I--LDSL 221
Cdd:TIGR01271 1429 VkqYDSI 1435
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-171 |
1.30e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.80 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIdGKPlekrisrercrrV 81
Cdd:TIGR03719 323 IEAENLTKAFGD----KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET------------V 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPY-GSLHPRHTIgdiLEEplqIHGIKDrdsriHTLLDKVGLN-RAFRDRYPH----------QLSGGQRQRVAI 149
Cdd:TIGR03719 386 KLAYVDQSrDALDPNKTV---WEE---ISGGLD-----IIKLGKREIPsRAYVGRFNFkgsdqqkkvgQLSGGERNRVHL 454
|
170 180
....*....|....*....|..
gi 2084886466 150 ARALILEPQVLLLDEPTSALDV 171
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDV 476
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-228 |
1.91e-11 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 62.23 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPY---GS----L 92
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIlfsGSirfnL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 93 HP-RHTIGDILEEPLQIHGIKDRDSRIHTLLDKV----GLNrafrdryphqLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:cd03288 116 DPeCKCTDDRLWEALEIAQLKNMVKSLPGGLDAVvtegGEN----------FSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 168 ALDVSVQaEILNLLVeLQCESNLTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA 228
Cdd:cd03288 186 SIDMATE-NILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-197 |
2.25e-11 |
|
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: 63.23 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKplekrisrercRR 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDV---LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 VQMVFQDPYGSLHprhTIGDILEEPLQIHGIKDR---DSRIHTLLDKVGLNR---------AFRDrYPHQLSGGQRQRVA 148
Cdd:TIGR00954 517 LFYVPQRPYMTLG---TLRDQIIYPDSSEDMKRRglsDKDLEQILDNVQLTHilereggwsAVQD-WMDVLSGGEKQRIA 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2084886466 149 IARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqcesNLTYLMVTH 197
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-213 |
3.82e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 60.28 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 28 VKEGEIYGLVGESGSGKTTVLKCLAGLFthwdgelaidgKPLEKRISRERCRrvqmvfqdpygslhprhtigdILEEPLQ 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQL-----------IPNGDNDEWDGIT---------------------PVYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 108 IhgikdrdsrihtlldkvglnrafrdryphQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCE 187
Cdd:cd03222 70 I-----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*.
gi 2084886466 188 SNLTYLMVTHDLGVIAHLCQKVAVMQ 213
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-198 |
6.96e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 24 VNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDpygsLHP-RHTIGDIL 102
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTD----FHLfDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 103 EEP--------LQIHGIKDR----DSRIHTLldkvglnrafrdryphQLSGGQRQRVAIARALILEPQVLLLDEPTSALD 170
Cdd:PRK10522 418 KPAnpalvekwLERLKMAHKleleDGRISNL----------------KLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180
....*....|....*....|....*...
gi 2084886466 171 VSVQAEILNLLVELQCESNLTYLMVTHD 198
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-199 |
1.14e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.46 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGkplekRISRerCRRV----------QMVFQDPY 89
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----RISF--SPQTswimpgtikdNIIFGLSY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 90 GSLHPRHTIGDI-LEEPLQIHGIKDRdsrihTLLDKVGLNrafrdryphqLSGGQRQRVAIARALILEPQVLLLDEPTSA 168
Cdd:TIGR01271 514 DEYRYTSVIKACqLEEDIALFPEKDK-----TVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190
....*....|....*....|....*....|...
gi 2084886466 169 LDVSVQAEILNLLVelqCE--SNLTYLMVTHDL 199
Cdd:TIGR01271 579 LDVVTEKEIFESCL---CKlmSNKTRILVTSKL 608
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-198 |
1.18e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 8 NLAFGEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGlfthwdgELaidgKPLEKRIsreRC-RRVQMVFQ 86
Cdd:PRK11147 324 NVNYQIDGK--QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG-------QL----QADSGRI---HCgTKLEVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 87 DPY-GSLHPRHTIGDILEEPLQ---IHGiKDRdsriHTLldkvGLNRAF-----RDRYP-HQLSGGQRQRVAIARaLILE 156
Cdd:PRK11147 388 DQHrAELDPEKTVMDNLAEGKQevmVNG-RPR----HVL----GYLQDFlfhpkRAMTPvKALSGGERNRLLLAR-LFLK 457
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2084886466 157 PQVLL-LDEPTSALDVsvqaEILNLLVELQCESNLTYLMVTHD 198
Cdd:PRK11147 458 PSNLLiLDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-171 |
1.29e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIdGKPlekrisrercrrV 81
Cdd:PRK11819 325 IEAENLSKSFGD----RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GET------------V 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPY-GSLHPRHTIGDILEEPLQIHGIKDRD--SRIHtlldkVGlnrAFRDRYPHQ------LSGGQRQRVAIARA 152
Cdd:PRK11819 388 KLAYVDQSrDALDPNKTVWEEISGGLDIIKVGNREipSRAY-----VG---RFNFKGGDQqkkvgvLSGGERNRLHLAKT 459
|
170
....*....|....*....
gi 2084886466 153 LILEPQVLLLDEPTSALDV 171
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLDV 478
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-217 |
1.91e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNlafgegEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRr 80
Cdd:PRK10982 250 ILEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAIN- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 81 vqmvfqdpygslhprHTIGDILEEPLQ--IHGIKDRD-----SRIHTLLDKVGL--NR-----------AFRDRYP-HQ- 138
Cdd:PRK10982 323 ---------------HGFALVTEERRStgIYAYLDIGfnsliSNIRNYKNKVGLldNSrmksdtqwvidSMRVKTPgHRt 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 139 ----LSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQY 214
Cdd:PRK10982 388 qigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSN 466
|
...
gi 2084886466 215 GKI 217
Cdd:PRK10982 467 GLV 469
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-217 |
1.97e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTvlkcLA-GLF-----THWDGELAIDGKPLEKRISRERCRR-VQMVFQDpygs 91
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTE----LAmSVFgrsygRNISGTVFKDGKEVDVSTVSDAIDAgLAYVTED---- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 92 lhpRHTIGDILEEPLQI------------HGIKD-----------RDS---RIHTLLDKVGlnrafrdryphQLSGGQRQ 145
Cdd:NF040905 346 ---RKGYGLNLIDDIKRnitlanlgkvsrRGVIDeneeikvaeeyRKKmniKTPSVFQKVG-----------NLSGGNQQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 146 RVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELqCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-215 |
1.99e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.95 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPY---GSLhpRH 96
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVlfdGTV--RQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 97 TIGDILE-------EPLQIHGIKDR--------DSRIHtlldKVGLNrafrdryphqLSGGQRQRVAIARALILEPQ-VL 160
Cdd:PTZ00243 1403 NVDPFLEassaevwAALELVGLRERvasesegiDSRVL----EGGSN----------YSVGQRQLMCMARALLKKGSgFI 1468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084886466 161 LLDEPTS----ALDVSVQAEILNLLvelqceSNLTYLMVTHDLGVIAHlCQKVAVMQYG 215
Cdd:PTZ00243 1469 LMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQ-YDKIIVMDHG 1520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-171 |
2.56e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.26 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISV------KEGEI-------YGLVGESGSGKTTVLKCLAglfTHwdgelAIDGKP------------------- 68
Cdd:PLN03073 180 MENFSISVggrdliVDASVtlafgrhYGLVGRNGTGKTTFLRYMA---MH-----AIDGIPkncqilhveqevvgddtta 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 69 ----LEKRISR-----ERCRRVQMVFQDPYGSLHPRH---TIGDILEEPL--QIHGIKDR---------DSRIHTLLDKV 125
Cdd:PLN03073 252 lqcvLNTDIERtqlleEEAQLVAQQRELEFETETGKGkgaNKDGVDKDAVsqRLEEIYKRlelidaytaEARAASILAGL 331
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2084886466 126 GLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDV 171
Cdd:PLN03073 332 SFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-226 |
3.41e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.36 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTvlkclAGLFTHWDGELA-----------IDGKPLE 70
Cdd:NF000106 14 VEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**R-----GALPAHV*GPDAgrrpwrf*twcANRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 71 KRISRERCRRVQMvfQDPYGSLHPRHTIGDILEEPLqihgiKDRDSRIHTLLDKVGLNRAfRDRYPHQLSGGQRQRVAIA 150
Cdd:NF000106 85 RTIG*HRPVR*GR--RESFSGRENLYMIGR*LDLSR-----KDARARADELLERFSLTEA-AGRAAAKYSGGMRRRLDLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 151 RALILEPQVLLLDEPTSALDVSVQAEILNlLVELQCESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDAL 226
Cdd:NF000106 157 ASMIGRPAVLYLDEPTTGLDPRTRNEVWD-EVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-199 |
3.90e-10 |
|
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: 58.71 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 18 NQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGkplekRISRerCRRV----------QMVFQD 87
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----RISF--SSQFswimpgtikeNIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 88 PYGSLHPRHTIGDI-LEEPLQIHGIKDrdsriHTLLDKVGLNrafrdryphqLSGGQRQRVAIARALILEPQVLLLDEPT 166
Cdd:cd03291 123 SYDEYRYKSVVKACqLEEDITKFPEKD-----NTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190
....*....|....*....|....*....|....*
gi 2084886466 167 SALDVSVQAEILNLLVelqCE--SNLTYLMVTHDL 199
Cdd:cd03291 188 GYLDVFTEKEIFESCV---CKlmANKTRILVTSKM 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-170 |
4.97e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPlEKRISRERcrrvQMVFQDPYGSLHPRHTIG 99
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRSR----FMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 100 DILEEPLQIHGIKDRDSRiHTLLDKVGLNrAFRDRYPHQLSGGQRQRVAIARaLILEPQVL-LLDEPTSALD 170
Cdd:PRK13543 101 ENLHFLCGLHGRRAKQMP-GSALAIVGLA-GYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-220 |
5.80e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGL--FTHWDGELAIDGKPLEKRISRERC 78
Cdd:PRK09580 1 MLSIKDLHVSVED----KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 79 -RRVQMVFQDP---------------------YGSLHP--RHTIGDILEEPLQIHGIKDrdsrihTLLDKvGLNRAFrdr 134
Cdd:PRK09580 77 gEGIFMAFQYPveipgvsnqfflqtalnavrsYRGQEPldRFDFQDLMEEKIALLKMPE------DLLTR-SVNVGF--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 135 yphqlSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQK-VAVMQ 213
Cdd:PRK09580 147 -----SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLR-DGKRSFIIVTHYQRILDYIKPDyVHVLY 220
|
....*..
gi 2084886466 214 YGKILDS 220
Cdd:PRK09580 221 QGRIVKS 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-253 |
9.96e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISRERCRRVQMVFQDPY---GS----L 92
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVlfsGTvrfnL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 93 HP--RHTIGDILEEPLQIHgIKDRDSRIHTLLD----KVGLNrafrdryphqLSGGQRQRVAIARALILEPQVLLLDEPT 166
Cdd:PLN03130 1334 DPfnEHNDADLWESLERAH-LKDVIRRNSLGLDaevsEAGEN----------FSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 167 SALDVSVQAEILNLLVE--LQCesnlTYLMVTHDLGVIAHlCQKVAVMQYGKILDSLTVDALVA-------------GQA 231
Cdd:PLN03130 1403 AAVDVRTDALIQKTIREefKSC----TMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSnegsafskmvqstGAA 1477
|
250 260
....*....|....*....|..
gi 2084886466 232 KTDYTQMLVNASQQysREMARE 253
Cdd:PLN03130 1478 NAQYLRSLVFGGDE--DRLARE 1497
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-202 |
1.52e-09 |
|
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: 55.07 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 31 GEIYGLVGESGSGKTTVLKCLAGLFthwdgelaidgkplekrisRERCRRVQMVfqdpygslhprhtigdileeplqihg 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAREL-------------------GPPGGGVIYI-------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 111 ikdrDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQC---- 186
Cdd:smart00382 37 ----DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllk 112
|
170
....*....|....*..
gi 2084886466 187 -ESNLTYLMVTHDLGVI 202
Cdd:smart00382 113 sEKNLTVILTTNDEKDL 129
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-228 |
1.64e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAG-LFTHWDGELAIDGK----PLEKRISRERCRRvQMVFQDPYGSLHPR 95
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTvayvPQVSWIFNATVRD-NILFGSPFDPERYE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 HTIgDI--LEEPLQIHGIKDrdsriHTLLDKVGLNrafrdryphqLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:PLN03130 712 RAI-DVtaLQHDLDLLPGGD-----LTEIGERGVN----------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 174 QAEILNLLV--ELQcesNLTYLMVTHDLGVIAHLcQKVAVMQYGKILDSLTVDALVA 228
Cdd:PLN03130 776 GRQVFDKCIkdELR---GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-217 |
1.88e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 25 NISVK--EGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAID-----GKPLEKRISRERCRRVQMVFQDpygslhprHT 97
Cdd:PRK15064 19 NISVKfgGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKLRQDQFAFEEFTVLDTVIMG--------HT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 98 -IGDILEEPLQIH---------GIKDRD--------------SRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARAL 153
Cdd:PRK15064 91 eLWEVKQERDRIYalpemseedGMKVADlevkfaemdgytaeARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 154 ILEPQVLLLDEPTSALDVSV---QAEILNllvelqcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINTirwLEDVLN-------ERNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-218 |
1.99e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 19 QVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHW----DGELAIDGKPLEKRISRERCRRVQMVFQDpygsLH- 93
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKKHYRGDVVYNAETD----VHf 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 PRHTIGDILEEPLQIHGIK------DRDSRI--------------HTLLDKVGlNRAFRDryphqLSGGQRQRVAIARAL 153
Cdd:TIGR00956 151 PHLTVGETLDFAARCKTPQnrpdgvSREEYAkhiadvymatyglsHTRNTKVG-NDFVRG-----VSGGERKRVSIAEAS 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084886466 154 ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNLTYLMVTHDLGVIAH-LCQKVAVMQYGKIL 218
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYEGYQI 290
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-217 |
3.33e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGEL----AIDGKPLEKRISRERCRRvQMVFQDPYGS--LH 93
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSIAYVPQQAWIMNATVRG-NILFFDEEDAarLA 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 94 PRHTIGDiLEEPLQIHGikdrdSRIHTLLDKVGLNrafrdryphqLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSV 173
Cdd:PTZ00243 754 DAVRVSQ-LEADLAQLG-----GGLETEIGEKGVN----------LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2084886466 174 QAEILN--LLVELQCEsnlTYLMVTHDLGVIAHlCQKVAVMQYGKI 217
Cdd:PTZ00243 818 GERVVEecFLGALAGK---TRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-217 |
4.75e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 23 NVNISVKEGEIYGLVGESGSGKTTVLKCLAGlfthwdgelaiDGKPLEKRISRERCRRVQMVFQdpygslhpRHTIG-DI 101
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISG-----------ELQPSSGTVFRSAKVRMAVFSQ--------HHVDGlDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 102 LEEPLQ-----IHGIKDRDSRIHtlLDKVGL--NRAFRDRYphQLSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQ 174
Cdd:PLN03073 588 SSNPLLymmrcFPGVPEQKLRAH--LGSFGVtgNLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV 663
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2084886466 175 AEILNLLVELQCesnlTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PLN03073 664 EALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-244 |
5.55e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 18 NQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHW-DGELAIDGK----PLEKRISRERCRRVQMVFQDPYGSL 92
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSvayvPQVSWIFNATVRENILFGSDFESER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 93 HPRHTIGDILEEPLQIHGIKDRdsrihTLLDKVGLNrafrdryphqLSGGQRQRVAIARALILEPQVLLLDEPTSALDVS 172
Cdd:PLN03232 710 YWRAIDVTALQHDLDLLPGRDL-----TEIGERGVN----------ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 173 VQAEILNLLVELQCESNlTYLMVTHDLGVIAhLCQKVAVMQYGKILDSLTVDALvaGQAKTDYTQMLVNASQ 244
Cdd:PLN03232 775 VAHQVFDSCMKDELKGK-TRVLVTNQLHFLP-LMDRIILVSEGMIKEEGTFAEL--SKSGSLFKKLMENAGK 842
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-170 |
1.29e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEgekrNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKrisrERCR- 79
Cdd:PRK13540 1 MLDVIELDFDYHD----QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTy 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 80 RVQMVFQDPYGSLHPRHTigdileepLQIHGIKDrdsrIHTLLDKVGLNRAFR-------DRYP-HQLSGGQRQRVAIAR 151
Cdd:PRK13540 73 QKQLCFVGHRSGINPYLT--------LRENCLYD----IHFSPGAVGITELCRlfslehlIDYPcGLLSSGQKRQVALLR 140
|
170
....*....|....*....
gi 2084886466 152 ALILEPQVLLLDEPTSALD 170
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALD 159
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-212 |
1.79e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 1 MIEINHLNLAFGEGEKRNQVLDNVNISvkEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELA--------IDGKPLEKR 72
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQsqfshitrLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 73 ISRERCRR---VQMVFQDPYGslhprHTIGDILEEplqihGIKDRDsRIHTLLDKVG----LNRAFRdryphQLSGGQRQ 145
Cdd:PRK10938 79 VSDEWQRNntdMLSPGEDDTG-----RTTAEIIQD-----EVKDPA-RCEQLAQQFGitalLDRRFK-----YLSTGETR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 146 RVAIARALILEPQVLLLDEPTSALDVSVQAEILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVM 212
Cdd:PRK10938 143 KTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-249 |
1.96e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.51 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISrercrrvqmvfqdpyGSLHPRHTIGD 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS---------------SGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 101 ILEEPLQIHGIKDRdsRIHTLLDKVgLNRAFRDRYPHQ----LSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAE 176
Cdd:PRK13545 105 NIELKGLMMGLTKE--KIKEIIPEI-IEFADIGKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 177 ILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKILDSLTVDALVA--GQAKTDYTQMLVNASQQYSRE 249
Cdd:PRK13545 182 CLDKMNEFK-EQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDhyDEFLKKYNQMSVEERKDFREE 255
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-217 |
4.27e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.51 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAIDGKPLEKRISrercrrvqmvfqdpyGSLHPRHTIGD 100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAIS---------------AGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 101 ILEEPLQIHGIKDRDsrIHTLLDKVgLNRAFRDRYPHQ----LSGGQRQRVAIARALILEPQVLLLDEPTSALDVSVQAE 176
Cdd:PRK13546 105 NIEFKMLCMGFKRKE--IKAMTPKI-IEFSELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2084886466 177 ILNLLVELQcESNLTYLMVTHDLGVIAHLCQKVAVMQYGKI 217
Cdd:PRK13546 182 CLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-171 |
4.70e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCL-------AGLFTH-------WDGE--LAIDGKPLEKRISRER-CRRVQ 82
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadGGSYTFpgnwqlaWVNQetPALPQPALEYVIDGDReYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 83 MVFQDPyGSLHPRHTIGdileeplQIHGIKDR------DSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILE 156
Cdd:PRK10636 96 AQLHDA-NERNDGHAIA-------TIHGKLDAidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICR 167
|
170
....*....|....*
gi 2084886466 157 PQVLLLDEPTSALDV 171
Cdd:PRK10636 168 SDLLLLDEPTNHLDL 182
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-175 |
5.35e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 12 GEGEKRNQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFT--HWDGELAIDGKPLEK----RISrERCRrvQMVF 85
Cdd:PLN03140 887 GVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQetfaRIS-GYCE--QNDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 86 QDPYGSLHPRHTIGDILEEPLQIhGIKDRDSRIHTLLDKVGLNRaFRDR---YP--HQLSGGQRQRVAIARALILEPQVL 160
Cdd:PLN03140 964 HSPQVTVRESLIYSAFLRLPKEV-SKEEKMMFVDEVMELVELDN-LKDAivgLPgvTGLSTEQRKRLTIAVELVANPSII 1041
|
170
....*....|....*
gi 2084886466 161 LLDEPTSALDVSVQA 175
Cdd:PLN03140 1042 FMDEPTSGLDARAAA 1056
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-202 |
1.47e-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: 50.01 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVlkCLAGLFthwdgelaidgKPLEKRISRERcrrvqmvfqdpygSLHPRHTIgd 100
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY-----------ASGKARLISFL-------------PKFSRNKL-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 101 ILEEPLQihgikdrdsrihtLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQ--VLLLDEPTSALDVSVQAEIL 178
Cdd:cd03238 63 IFIDQLQ-------------FLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLL 129
|
170 180
....*....|....*....|....
gi 2084886466 179 NLLVELQCESNlTYLMVTHDLGVI 202
Cdd:cd03238 130 EVIKGLIDLGN-TVILIEHNLDVL 152
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
137-203 |
9.38e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.35 E-value: 9.38e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084886466 137 HQLSGGQRQRVAIARALIL----EPQVLLLDEPTSALDVSVQAEILNLLVELQCESNlTYLMVTHDLGVIA 203
Cdd:cd03227 76 LQLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGA-QVIVITHLPELAE 145
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-204 |
2.38e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.25 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTV-------------LKCLAGLFTHWDGEL------AIDGkpLEKRISRERCRrv 81
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQMdkpdvdSIEG--LSPAIAIDQKT-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 qmvfqdpyGSLHPRHTIGDILEeplqIH----------GIKdrdSRIHTLLDkVGLNRAFRDRYPHQLSGGQRQRVAIAR 151
Cdd:cd03270 87 --------TSRNPRSTVGTVTE----IYdylrllfarvGIR---ERLGFLVD-VGLGYLTLSRSAPTLSGGEAQRIRLAT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084886466 152 AL--ILEPQVLLLDEPTSALDVSVQAEILNLLVELQCESNlTYLMVTHDLGVIAH 204
Cdd:cd03270 151 QIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRA 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
122-170 |
6.09e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 6.09e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2084886466 122 LDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTSALD 170
Cdd:PRK10938 385 LDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-198 |
1.07e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 2 IEINHLNLAFGEGEkrnqVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELaidgKPLEKrisrercRRV 81
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSEN-------ANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 82 QMVFQDPYGSLHPRHTIGDILEeplQIHGIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLL 161
Cdd:PRK15064 385 GYYAQDHAYDFENDLTLFDWMS---QWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190
....*....|....*....|....*....|....*...
gi 2084886466 162 LDEPTSALDV-SVQAeiLNLLVELqceSNLTYLMVTHD 198
Cdd:PRK15064 462 MDEPTNHMDMeSIES--LNMALEK---YEGTLIFVSHD 494
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-198 |
1.78e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 12 GEGEKrnQVLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFTHWDGELAidgkpLEKRISRERCRRVQMVFQDPYgs 91
Cdd:PRK10636 321 GYGDR--IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG-----LAKGIKLGYFAQHQLEFLRAD-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 92 lhprhtigdilEEPLQiH----GIKDRDSRIHTLLDKVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQVLLLDEPTS 167
Cdd:PRK10636 392 -----------ESPLQ-HlarlAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190
....*....|....*....|....*....|.
gi 2084886466 168 ALDVSVQAEILNLLVELqcESNLtyLMVTHD 198
Cdd:PRK10636 460 HLDLDMRQALTEALIDF--EGAL--VVVSHD 486
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-198 |
1.80e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 36 LVGESGSGKTTVLKCL-AGLFthWDGELAIDGKPLEKRISRERCRRVQ--MVFQDPYGSLHPRHTIGDILEEPLQIHgik 112
Cdd:cd03240 27 IVGQNGAGKTTIIEALkYALT--GELPPNSKGGAHDPKLIREGEVRAQvkLAFENANGKKYTITRSLAILENVIFCH--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 113 DRDSRiHTLLDKVGlnrafrdryphQLSGGQRQ------RVAIARALILEPQVLLLDEPTSALDV-SVQAEILNLLVELQ 185
Cdd:cd03240 102 QGESN-WPLLDMRG-----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERK 169
|
170
....*....|...
gi 2084886466 186 CESNLTYLMVTHD 198
Cdd:cd03240 170 SQKNFQLIVITHD 182
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
36-205 |
1.19e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.29 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 36 LVGESGSGKTTVLKCLAGLFTHWDGELA-IDGKPLEKRISRERCRRVQMVFQDPYGSL--HPRHTIGDILEEPLQ----I 108
Cdd:COG3950 30 LVGENGSGKTTLLEAIALALSGLLSRLDdVKFRKLLIRNGEFGDSAKLILYYGTSRLLldGPLKKLERLKEEYFSrldgY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 109 HGIKDRDSRIHTLLDKV--------------------GLNRAFRDRYPH--------------------------QLSGG 142
Cdd:COG3950 110 DSLLDEDSNLREFLEWLreyledlenklsdeldekleAVREALNKLLPDfkdiridrdpgrlvildkngeelplnQLSDG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084886466 143 QRQRVAIA--------------RALILEPQVLLLDEPTSALDVSVQAEILNLLVELQCesNLTYLMVTHDLGVIAHL 205
Cdd:COG3950 190 ERSLLALVgdlarrlaelnpalENPLEGEGIVLIDEIDLHLHPKWQRRILPDLRKIFP--NIQFIVTTHSPLILSSL 264
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
21-203 |
9.26e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.52 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 21 LDNVNISVKEGEIYGLVGESGSGKTTVL-----KCLAGLFTHwdgeLAIDGKPLEKRISRERCRRVQMVFQDPYGSlHPR 95
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHL----KKEQPGNHDRIEGLEHIDKVIVIDQSPIGR-TPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 96 -------------------------------------HTIGDILEEPL-----------QIHgikdrdSRIHTLLDkVGL 127
Cdd:cd03271 86 snpatytgvfdeirelfcevckgkrynretlevrykgKSIADVLDMTVeealeffenipKIA------RKLQTLCD-VGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 128 NRAFRDRYPHQLSGGQRQRVAIARALILE---PQVLLLDEPTSAL---DVSVQAEILNLLVELqceSNlTYLMVTHDLGV 201
Cdd:cd03271 159 GYIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVKKLLEVLQRLVDK---GN-TVVVIEHNLDV 234
|
..
gi 2084886466 202 IA 203
Cdd:cd03271 235 IK 236
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
102-209 |
1.72e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 102 LEEPLQihGIKdrdSRIHTLLDkVGLNRAFRDRYPHQLSGGQRQRVAIARALILEPQ--VLLLDEPTSALDVSVQAEILN 179
Cdd:PRK00635 446 IEEVLQ--GLK---SRLSILID-LGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLIN 519
|
90 100 110
....*....|....*....|....*....|
gi 2084886466 180 LLVELQCESNlTYLMVTHDLGVIAhLCQKV 209
Cdd:PRK00635 520 VIKKLRDQGN-TVLLVEHDEQMIS-LADRI 547
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
20-155 |
2.95e-03 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 38.63 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 20 VLDNVNISVKEGEIYGLVGESGSGKTTVLKCLAGLFthwdgelaidgkplekrISRERCRRVQMVFQDPY--GSLHPRHT 97
Cdd:PRK14723 174 VLRDEDALLAQGGVLALVGPTGVGKTTTTAKLAARC-----------------VAREGADQLALLTTDSFriGALEQLRI 236
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084886466 98 IGDILEEPlqIHGIKD----RD------SRIHTLLDKVGLNRafRDRYPHQ----LSGGQRQrvaIARALIL 155
Cdd:PRK14723 237 YGRILGVP--VHAVKDaadlRFalaalgDKHLVLIDTVGMSQ--RDRNVSEqiamLCGVGRP---VRRLLLL 301
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-202 |
4.30e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 4.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 139 LSGGQRQRVAIARALILEPQ---VLLLDEPTSAL---DVSVQAEILNLLVELqceSNlTYLMVTHDLGVI 202
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRKLLEVLHRLVDK---GN-TVVVIEHNLDVI 892
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-202 |
7.44e-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: 7.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084886466 139 LSGGQRQRVAIARALILE---PQVLLLDEPTSAL---DVSVQAEILNLLVELqceSNlTYLMVTHDLGVI 202
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK---GN-TVVVIEHNLDVI 895
|
|
| |
