|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-238 |
7.25e-96 |
|
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: 285.02 E-value: 7.25e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKE----IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGSEVIGAADRTLA 78
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 DLRGRYTGMVFQNPGASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGL--PADVAAKFPHELSGGQRQRVGI 156
Cdd:COG0444 82 KIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdPERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 157 ATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAA 236
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241
|
..
gi 1566271202 237 PQ 238
Cdd:COG0444 242 PR 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-262 |
2.15e-88 |
|
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: 272.71 E-value: 2.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGG----KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLP-PDVTVAGSVMLGGSEVIGAADRTLA 78
Cdd:COG4172 8 SVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 DLRGRYTGMVFQNPGASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGL--PADVAAKFPHELSGGQRQRVGI 156
Cdd:COG4172 88 RIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIpdPERRLDAYPHQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 157 ATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAA 236
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAA 247
|
250 260
....*....|....*....|....*.
gi 1566271202 237 PQDERTARLVRAARTLTLRASREGAD 262
Cdd:COG4172 248 PQHPYTRKLLAAEPRGDPRPVPPDAP 273
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-255 |
6.24e-86 |
|
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: 266.00 E-value: 6.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNP 92
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT---SGSILFDGKDLTKLSRRSLRELR-RRVQMVFQDP 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:COG1123 352 YSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEP 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRAARTL 252
Cdd:COG1123 432 TSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSL 511
|
...
gi 1566271202 253 TLR 255
Cdd:COG1123 512 DPA 514
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-255 |
1.16e-83 |
|
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: 251.26 E-value: 1.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIG----GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRtla 78
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW---SGEVTFDGRPVTRRRRK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 DLRGRyTGMVFQNPGASLNPVLPVGRQVELPLRLHYdltRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIAT 158
Cdd:COG1124 76 AFRRR-VQMVFQDPYASLHPRHTVDRILAEPLRIHG---LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQ 238
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
250
....*....|....*..
gi 1566271202 239 DERTARLVRAARTLTLR 255
Cdd:COG1124 232 HPYTRELLAASLAFERA 248
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-228 |
2.21e-83 |
|
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: 249.73 E-value: 2.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGK----EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAaDRTLA 78
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT---SGSIIFDGKDLLKL-SRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 DLRGRYTGMVFQNPGASLNPVLPVGRQVELPLRLHYDLTRSE-RVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIA 157
Cdd:cd03257 78 KIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEaRKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 158 TALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-249 |
4.82e-76 |
|
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: 240.74 E-value: 4.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvaGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNPGASLN 97
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE----GEIRFDGQDLDGLSRRALRPLR-RRMQVVFQDPFGSLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLPVGRQVELPLRLHY-DLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTAL 176
Cdd:COG4172 377 PRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 177 DSITQRQIVDLSVSLVDEAGASMLFITHDFSVLtRATT-RCVVLDEGSVVETGETAAMLAAPQDERTARLVRAA 249
Cdd:COG4172 457 DVSVQAQILDLLRDLQREHGLAYLFISHDLAVV-RALAhRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAA 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-261 |
2.43e-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: 235.95 E-value: 2.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAI--GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGSEVIGAADRtladL 80
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEA----L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTGMVFQNPGASLNPVlPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATAL 160
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNPV-TVGDQIAEALENL-GLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 161 ITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDE 240
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
250 260
....*....|....*....|.
gi 1566271202 241 RTARLVRAARTLTLRASREGA 261
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAE 258
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-238 |
8.47e-74 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 228.85 E-value: 8.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNPGASLN 97
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPT---SGEILFDGQDITGLSGRELRPLR-RRMQMVFQDPYASLN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALD 177
Cdd:COG4608 110 PRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 178 -SItQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQ 238
Cdd:COG4608 190 vSI-QAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-237 |
1.91e-66 |
|
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: 207.14 E-value: 1.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRG 82
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD---SGEILVDGQDITGLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYtGMVFQNpGA---SLNpvlpVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPaDVAAKFPHELSGGQRQRVGIATA 159
Cdd:COG1127 83 RI-GMLFQG-GAlfdSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 160 LITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-248 |
3.08e-61 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 196.85 E-value: 3.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPpdvTVAGSVMLGGSEVIGAADRTLADLRGRYTgMVFQNPGASLN 97
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK---ATDGEVAWLGKDLLGMKDDEWRAVRSDIQ-MIFQDPLASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLPVGRQVELPLRLHY-DLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTAL 176
Cdd:PRK15079 113 PRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 177 DSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRA 248
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSA 264
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
16-226 |
9.11e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 192.18 E-value: 9.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKS----MIAramlGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQN 91
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKStllnILG----GLDRPT---SGEVLIDGQDISSLSERELARLRRRHIGFVFQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 92 PGasLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADE 171
Cdd:COG1136 95 FN--LLPELTALENVALPLLLA-GVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 172 PTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVE 226
Cdd:COG1136 171 PTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARA-DRVIRLRDGRIVS 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-272 |
8.86e-59 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 190.18 E-value: 8.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNPGASLN 97
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETP---TGGELYYQGQDLLKADPEAQKLLR-QKIQIVFQNPYGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALD 177
Cdd:PRK11308 107 PRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 178 SITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRAARTLTLRAS 257
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRLNPDDR 266
|
250
....*....|....*
gi 1566271202 258 REgadRETDRGAAPS 272
Cdd:PRK11308 267 RE---RIKLTGELPS 278
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
15-222 |
1.88e-57 |
|
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: 183.46 E-value: 1.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNPGa 94
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT---SGEVRVDGTDISKLSEKELAAFRRRHIGFVFQSFN- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 sLNPVLPVGRQVELPLRLHYdLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTT 174
Cdd:cd03255 93 -LLPDLTALENVELPLLLAG-VPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1566271202 175 ALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEG 222
Cdd:cd03255 170 NLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYA-DRIIELRDG 216
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
15-258 |
1.96e-57 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 185.04 E-value: 1.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadrTLAD--LRGRYTGMVFQNP 92
Cdd:COG4167 26 FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPT---SGEILINGHKL------EYGDykYRCKHIRMIFQDP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:COG4167 97 NTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRAARTL 252
Cdd:COG4167 177 LAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLIESHFGE 256
|
....*.
gi 1566271202 253 TLRASR 258
Cdd:COG4167 257 ALTADA 262
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-238 |
3.38e-57 |
|
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: 183.47 E-value: 3.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD---SGEVLIDGEDISGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYtGMVFQNpGA---SLNpvlpVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADvAAKFPHELSGGQRQRVGIATA 159
Cdd:cd03261 78 RM-GMLFQS-GAlfdSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGA-EDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 160 LITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQ 238
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
17-249 |
3.41e-57 |
|
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: 183.34 E-value: 3.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 17 IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVT-VAGSVMLGGSEVIGAAdrtladLRGRYTGMVFQNPGAS 95
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTqTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 96 LNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAkVGL--PADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPT 173
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSKQARALILEALEA-VGLpdPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 174 TALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRAA 249
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAH 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-248 |
1.62e-56 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 189.92 E-value: 1.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAI--GG--KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLP--PDVTVAGSVMLGGSEVIGAADRTL 77
Cdd:PRK15134 7 AIENLSVAFrqQQtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVVYPSGDIRFHGESLLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 78 ADLRGRYTGMVFQNPGASLNPVLPVGRQVELPLRLHYDLTR-SERVERVNAmLAKVGL--PADVAAKFPHELSGGQRQRV 154
Cdd:PRK15134 87 RGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRReAARGEILNC-LDRVGIrqAAKRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAML 234
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
250
....*....|....
gi 1566271202 235 AAPQDERTARLVRA 248
Cdd:PRK15134 246 SAPTHPYTQKLLNS 259
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-238 |
5.04e-56 |
|
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: 180.22 E-value: 5.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQNP 92
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT---SGEVLVDGKDI---TKKNLRELR-RKVGLVFQNP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GASLnpVLP-VGRQVELPLRlHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADE 171
Cdd:COG1122 85 DDQL--FAPtVEEDVAFGPE-NLGLPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 172 PTTALDSITQRQIVDLSVSLvDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQ 238
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-244 |
7.19e-55 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 177.49 E-value: 7.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsEVIGAADRTLADLRG 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPD---SGTITVDG-EDLTDSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RyTGMVFQNpgASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:COG1126 78 K-VGMVFQQ--FNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERT 242
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERT 232
|
..
gi 1566271202 243 AR 244
Cdd:COG1126 233 RA 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-205 |
6.40e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 170.66 E-value: 6.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDL----RIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAadrt 76
Cdd:COG1116 6 PALELRGVskrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT---SGEVLVDGKPVTGP---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 77 ladlrGRYTGMVFQNPgaSLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGI 156
Cdd:COG1116 79 -----GPDRGVVFQEP--ALLPWLTVLDNVALGLELR-GVPKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1566271202 157 ATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHD 205
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-228 |
9.48e-52 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 172.22 E-value: 9.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKE----IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGSEVIGAADRTLAD 79
Cdd:PRK09473 14 DVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 80 LRGRYTGMVFQNPGASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPAdvAAK----FPHELSGGQRQRVG 155
Cdd:PRK09473 94 LRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPE--ARKrmkmYPHEFSGGMRQRVM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 156 IATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:PRK09473 172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-249 |
1.76e-51 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 171.63 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAI----GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTV-AGSVMLGGSEVIGAADRTLA 78
Cdd:COG4170 5 DIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVtADRFRWNGIDLLKLSPRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 DLRGRYTGMVFQNPGASLNPVLPVGRQVE--LP---LRLHYDLTRSERVERVNAMLAKVGL--PADVAAKFPHELSGGQR 151
Cdd:COG4170 85 KIIGREIAMIFQEPSSCLDPSAKIGDQLIeaIPswtFKGKWWQRFKWRKKRAIELLHRVGIkdHKDIMNSYPHELTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 152 QRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETA 231
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTE 244
|
250
....*....|....*...
gi 1566271202 232 AMLAAPQDERTARLVRAA 249
Cdd:COG4170 245 QILKSPHHPYTKALLRSM 262
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-238 |
3.39e-51 |
|
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: 167.76 E-value: 3.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNPG-- 93
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT---SGSVLVDGTDLTLLSGKELRKAR-RRIGMIFQHFNll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLNpvlpVGRQVELPLRLHYdLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPT 173
Cdd:cd03258 95 SSRT----VFENVALPLEIAG-VPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 174 TALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQ 238
Cdd:cd03258 169 SALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
18-247 |
1.27e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 169.49 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNPG--AS 95
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPT---SGSVLVDGVDLTALSERELRAAR-RKIGMIFQHFNllSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 96 LNpvlpVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTA 175
Cdd:COG1135 97 RT----VAENVALPLEIA-GVPKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 176 LDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVR 247
Cdd:COG1135 171 LDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLP 242
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-235 |
3.26e-50 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 166.40 E-value: 3.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 8 LRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGM 87
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS---QGNVSWRGEPLAKLNRAQRKAFR-RDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 88 VFQNPGASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLI 167
Cdd:PRK10419 94 VFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 168 VADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLA 235
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-249 |
5.73e-50 |
|
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: 165.75 E-value: 5.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEViGAADRTLADLRGRYTGMVFQNPGA 94
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKP---AQGTVSFRGQDL-YQLDRKQRRAFRRDVQLVFQDSPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 SLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTT 174
Cdd:TIGR02769 100 AVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 175 ALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDerTARLVRAA 249
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHP--AGRNLQSA 252
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-229 |
5.93e-49 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 161.76 E-value: 5.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNp 92
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT---SGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gASLNPVLPVGRQVELPLRLHYdLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:COG2884 88 -FRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 173 TTALDSITQRQIVDLsvsLVD--EAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGE 229
Cdd:COG2884 165 TGNLDPETSWEIMEL---LEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-205 |
9.20e-49 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 161.10 E-value: 9.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTladlrgrytGMVFQNP 92
Cdd:cd03293 15 GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT---SGEVLVDGEPVTGPGPDR---------GYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gaSLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:cd03293 83 --ALLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEAGASMLFITHD 205
Cdd:cd03293 159 FSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-222 |
1.06e-47 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 158.01 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKE--IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRG 82
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT---SGEVLVDGKDL---TKLSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RyTGMVFQNPGASL-NPVlpVGRQVELPLRlHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALI 161
Cdd:cd03225 76 K-VGLVFQNPDDQFfGPT--VEEEVAFGLE-NLGLPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEG 222
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-246 |
1.10e-47 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 159.96 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvagsvmlGGSEVIGAADRTLAD--LRGRYTGMVFQNPG 93
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT---------SGELLIDDHPLHFGDysYRSQRIRMIFQDPS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPT 173
Cdd:PRK15112 98 TSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 174 TALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLV 246
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-246 |
6.09e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 160.26 E-value: 6.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIG-AADRtladlr 81
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD---SGRILLDGRDVTGlPPEK------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 82 gRYTGMVFQNPgaSLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALI 161
Cdd:COG3842 77 -RNVGMVFQDY--ALFPHLTVAENVAFGLRMR-GVPKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFS-VLTRAtTRCVVLDEGSVVETGETAAMLAAPQDE 240
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeALALA-DRIAVMNDGRIEQVGTPEEIYERPATR 230
|
....*.
gi 1566271202 241 RTARLV 246
Cdd:COG3842 231 FVADFI 236
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-252 |
7.06e-47 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 157.55 E-value: 7.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 2 GVDIRDLRIAIGGkEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVT-VAGSVMLGGSEVIGAadrtlaDL 80
Cdd:PRK10418 4 QIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRqTAGRVLLDGKPVAPC------AL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTGMVFQNPGASLNPVLPVGRQVELPLRLhydLTRSERVERVNAMLAKVGL--PADVAAKFPHELSGGQRQRVGIAT 158
Cdd:PRK10418 77 RGRKIATIMQNPRSAFNPLHTMHTHARETCLA---LGKPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQ 238
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
250
....*....|....
gi 1566271202 239 DERTARLVRAARTL 252
Cdd:PRK10418 234 HAVTRSLVSAHLAL 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-249 |
8.55e-47 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 164.11 E-value: 8.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 8 LRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvaGSVMLGGSEVIGAADRTLADLRGRYTgM 87
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ----GEIWFDGQPLHNLNRRQLLPVRHRIQ-V 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 88 VFQNPGASLNPVLPVGRQVELPLRLHY-DLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRL 166
Cdd:PRK15134 367 VFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 167 IVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLV 246
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
...
gi 1566271202 247 RAA 249
Cdd:PRK15134 527 ALS 529
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-236 |
1.02e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.38 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLrg 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT---SGEVRVLGEDVARDPAEVRRRI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 rytGMVFQNPGasLNPVLPVGRQVELPLRLhYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:COG1131 76 ---GYVPQEPA--LYPDLTVRENLRFFARL-YGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAA 236
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-230 |
3.46e-46 |
|
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: 154.65 E-value: 3.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGL--LPPDVTVAGSVMLGGSEvIGAADRTLADL 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndLIPGAPDEGEVLLDGKD-IYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RgRYTGMVFQNPgaslNPV-LPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAK-FPHELSGGQRQRVGIAT 158
Cdd:cd03260 80 R-RRVGMVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEagASMLFITHDFSVLTRATTRCVVLDEGSVVETGET 230
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-228 |
9.86e-46 |
|
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: 153.06 E-value: 9.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsevigaADRTLADLRG 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD---SGEILIDG------RDVTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNPgaSLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLPaDVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:cd03259 72 RNIGMVFQDY--ALFPHLTVAENIAFGLKLR-GVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-248 |
2.68e-45 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 155.28 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLP-PDVTVAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNPGASL 96
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 97 NPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPaDVAAK---FPHELSGGQRQRVGIATALITSPRLIVADEPT 173
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIP-DPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 174 TALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRA 248
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRA 256
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
15-222 |
3.76e-45 |
|
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: 151.71 E-value: 3.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQnpGA 94
Cdd:TIGR02982 18 KQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQ---EGSLKVLGQELHGASKKQLVQLR-RRIGYIFQ--AH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 SLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTT 174
Cdd:TIGR02982 92 NLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGL-GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1566271202 175 ALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEG 222
Cdd:TIGR02982 171 ALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVA-DRILQMEDG 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-247 |
1.53e-44 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 151.64 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNPGasLN 97
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPT---SGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFA--LL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALD 177
Cdd:cd03294 115 PHRTVLENVAFGLEVQ-GVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 178 SITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVR 247
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFR 262
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
13-225 |
7.27e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 149.44 E-value: 7.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGRyTGMVFQNP 92
Cdd:COG3638 14 GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGEILVDGQDVTALRGRALRRLRRR-IGMIFQQF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GasLNPVLPV------GR--QVELPLRLHYDLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSP 164
Cdd:COG3638 90 N--LVPRLSVltnvlaGRlgRTSTWRSLLGLFPPEDR-ERALEALERVGL-ADKAYQRADQLSGGQQQRVAIARALVQEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 165 RLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVV 225
Cdd:COG3638 166 KLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-205 |
6.33e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 147.32 E-value: 6.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIG-AADRtladlrgrytGMVFQNPG 93
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS---SGEITLDGVPVTGpGADR----------GVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 asLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPT 173
Cdd:COG4525 87 --LLPWLNVLDNVAFGLRLR-GVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170 180 190
....*....|....*....|....*....|..
gi 1566271202 174 TALDSITQRQIVDLSVSLVDEAGASMLFITHD 205
Cdd:COG4525 163 GALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-249 |
1.54e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.80 E-value: 1.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEI--VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQ 90
Cdd:PRK11153 14 GGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPT---SGRVLVDGQDLTALSEKELRKAR-RQIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 91 --NPGASLNpvlpVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIV 168
Cdd:PRK11153 90 hfNLLSSRT----VFDNVALPLELA-GTPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 169 ADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRA 248
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243
|
.
gi 1566271202 249 A 249
Cdd:PRK11153 244 T 244
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-222 |
3.84e-42 |
|
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: 143.82 E-value: 3.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsEVIGAADRTLADLRg 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD---SGTIIIDG-LKLTDDKKNINELR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNpgASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:cd03262 76 QKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEG 222
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-234 |
6.13e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 144.42 E-value: 6.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLAdlrgRY 84
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS---SGEVLLDGRDLASLSRRELA----RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 TGMVFQNPGASLNpvLPVGRQVEL---PLRLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALI 161
Cdd:COG1120 77 IAYVPQEPPAPFG--LTVRELVALgryPHLGLFGRPSAEDREAVEEALERTGL-EHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAML 234
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-248 |
1.34e-41 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 151.16 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPpdvTVAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNPGASLN 97
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE---SQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDPYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALD 177
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 178 SITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRA 248
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-248 |
5.64e-41 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 149.62 E-value: 5.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLP-PDVTVAGSVML---GGSEVIGAADRTLA---DLRGRYTGMVFQ 90
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEqAGGLVQCDKMLlrrRSRQVIELSEQSAAqmrHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 91 NPGASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLP--ADVAAKFPHELSGGQRQRVGIATALITSPRLIV 168
Cdd:PRK10261 112 EPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 169 ADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRA 248
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAA 271
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-222 |
5.84e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.72 E-value: 5.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRGRy 84
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT---SGEIYLDGKPL---SAMPPPEWRRQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 TGMVFQNPGASLNPVlpvGRQVELPLRLHydlTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSP 164
Cdd:COG4619 76 VAYVPQEPALWGGTV---RDNLPFPFQLR---ERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 165 RLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEG 222
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-242 |
6.01e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 6.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadrtlaDLRG 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT---SGTVRLFGKPP---------RRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNpgASLNPVLPV--------GRQVELPLRLHYdlTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRV 154
Cdd:COG1121 75 RRIGYVPQR--AEVDWDFPItvrdvvlmGRYGRRGLFRRP--SRADR-EAVDEALERVGL-EDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGsVVETGETAAML 234
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVL 226
|
....*...
gi 1566271202 235 AAPQDERT 242
Cdd:COG1121 227 TPENLSRA 234
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
16-226 |
2.49e-40 |
|
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: 139.41 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLlppDVTVAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNpgAS 95
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGL---DNPTSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQF--HH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 96 LNPVLPVGRQVELPLrLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTA 175
Cdd:TIGR02211 94 LLPDFTALENVAMPL-LIGKKSVKEAKERAYEMLEKVGL-EHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 176 LDSITQRQIVDLSVSLVDEAGASMLFITHDFSvLTRATTRCVVLDEGSVVE 226
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQLFN 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-252 |
2.68e-40 |
|
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: 140.13 E-value: 2.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKS----MIARamlgLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMV 88
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTttmkMINR----LIEPT---SGEIFIDGEDI---REQDPVELR-RKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 89 FQNPGasLNPVLPVGRQVEL-PLRLHYDltRSERVERVNAMLAKVGL-PADVAAKFPHELSGGQRQRVGIATALITSPRL 166
Cdd:cd03295 81 IQQIG--LFPHMTVEENIALvPKLLKWP--KEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 167 IVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLV 246
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
....*.
gi 1566271202 247 RAARTL 252
Cdd:cd03295 237 GADRLL 242
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-228 |
3.04e-40 |
|
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: 140.64 E-value: 3.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 17 IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGaaDRTLADLRgRYTGMVFQNPGASL 96
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPT---SGKVTVDGLDTLD--EENLWEIR-KKVGMVFQNPDNQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 97 npvlpVGRQVE-----------LPlrlhydltRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPR 165
Cdd:TIGR04520 91 -----VGATVEddvafglenlgVP--------REEMRKRVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 166 LIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETG 228
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLA-DRVIVMNKGKIVAEG 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-222 |
4.34e-40 |
|
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: 137.32 E-value: 4.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsEVIGAADRTLADLRg 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD---SGSILIDG-EDLTDLEDELPPLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNPGasLNPVLPVGRQVELPLrlhydltrservervnamlakvglpadvaakfphelSGGQRQRVGIATALIT 162
Cdd:cd03229 76 RRIGMVFQDFA--LFPHLTVLENIALGL------------------------------------SGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEG 222
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
16-232 |
2.74e-39 |
|
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: 137.18 E-value: 2.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNpgAS 95
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPT---SGTVRLAGQDLFALDEDARARLRARHVGFVFQS--FQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 96 LNPVLPVGRQVELPLRLhydLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTA 175
Cdd:COG4181 101 LLPTLTALENVMLPLEL---AGRRDARARARALLERVGL-GHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 176 LDSITQRQIVDLSVSLVDEAGASMLFITHDfSVLTRATTRCVVLDEGSVVETGETAA 232
Cdd:COG4181 177 LDAATGEQIIDLLFELNRERGTTLVLVTHD-PALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-225 |
9.88e-39 |
|
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: 135.77 E-value: 9.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGRyTGMVFQNP 92
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGSVLIDGTDINKLKGKALRQLRRQ-IGMIFQQF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GasLNPVLPVGRQVeLPLRLHY---------DLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITS 163
Cdd:cd03256 88 N--LIERLSVLENV-LSGRLGRrstwrslfgLFPKEEK-QRALAALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVV 225
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-230 |
1.12e-38 |
|
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: 136.81 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 19 HGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsEVIGAADRT-LADLRGRyTGMVFQNPGASL- 96
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPT---SGTVTIDG-RDITAKKKKkLKDLRKK-VGLVFQFPEHQLf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 97 -NPVLpvgRQVEL-PLRLhyDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTT 174
Cdd:TIGR04521 97 eETVY---KDIAFgPKNL--GLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 175 ALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGET 230
Cdd:TIGR04521 172 GLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTP 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-246 |
1.34e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.93 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGL--LPPDVTVAGSVMLGGSEvIGAADRTLADL 80
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGARVEGEILLDGED-IYDPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RgRYTGMVFQNPgaslNPvLP--VGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKF---PHELSGGQRQRVG 155
Cdd:COG1117 91 R-RRVGMVFQKP----NP-FPksIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLkksALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 156 IATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEagASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLA 235
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFT 242
|
250
....*....|.
gi 1566271202 236 APQDERTARLV 246
Cdd:COG1117 243 NPKDKRTEDYI 253
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
3-248 |
7.27e-38 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 136.09 E-value: 7.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAI----GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVM-LGGSEVIGAADRTL 77
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMrFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 78 ADLRGRYTGMVFQNPGASLNPVLPVGRQV--ELP---------LRLHYdltrseRVERVNAMLAKVGL--PADVAAKFPH 144
Cdd:PRK15093 84 RKLVGHNVSMIFQEPQSCLDPSERVGRQLmqNIPgwtykgrwwQRFGW------RKRRAIELLHRVGIkdHKDAMRSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 145 ELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSV 224
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250 260
....*....|....*....|....
gi 1566271202 225 VETGETAAMLAAPQDERTARLVRA 248
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQALIRA 261
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-246 |
2.81e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 134.89 E-value: 2.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIgaadrTLADL 80
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPD---SGRIVLNGRDLF-----TNLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTGMVFQNPGasLNPVLPVGRQVELPLRlHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATAL 160
Cdd:COG1118 73 RERRVGFVFQHYA--LFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 161 ITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHD----FSVltraTTRCVVLDEGSVVETGETAAMLAA 236
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDqeeaLEL----ADRVVVMNQGRIEQVGTPDEVYDR 224
|
250
....*....|
gi 1566271202 237 PQDERTARLV 246
Cdd:COG1118 225 PATPFVARFL 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-246 |
1.32e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 133.27 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIG--AADRTLAdl 80
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT---SGEILIGGRDVTDlpPKDRNIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 rgrytgMVFQNPGasLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATAL 160
Cdd:COG3839 79 ------MVFQSYA--LYPHMTVYENIAFPLKLR-KVPKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 161 ITSPRLIVADEPTTALD----SITQRQIVDlsvsLVDEAGASMLFITHDFS-VLTRAtTRCVVLDEGSVVETGETAAMLA 235
Cdd:COG3839 149 VREPKVFLLDEPLSNLDaklrVEMRAEIKR----LHRRLGTTTIYVTHDQVeAMTLA-DRIAVMNDGRIQQVGTPEELYD 223
|
250
....*....|.
gi 1566271202 236 APQDERTARLV 246
Cdd:COG3839 224 RPANLFVAGFI 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-241 |
2.15e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 129.83 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLlppDVTVAGSVMLGGSEVIGAAdrtlADLRG--RYTGMVFQ 90
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL---EEITSGDLIVDGLKVNDPK----VDERLirQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 91 NpgASLNPVLPVGRQVEL-PLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVA 169
Cdd:PRK09493 85 Q--FYLFPHLTALENVMFgPLRVR-GASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 170 DEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDER 241
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQR 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-228 |
2.70e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.52 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQNP----- 92
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE---AGTITVGGMVL---SEETVWDVR-RQVGMVFQNPdnqfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GASlnpvlpVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:PRK13635 96 GAT------VQDDVAFGLENI-GVPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETG 228
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQA-DRVIVMNKGEILEEG 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-242 |
3.47e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 129.48 E-value: 3.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPD---VTVaGSVMLGGSEVIGAADRTLAD 79
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtIRV-GDITIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 80 LRgRYTGMVFQNpgASLNPVLPVGRQV-ELPLRLHYDlTRSERVERVNAMLAKVGLPADVAAkFPHELSGGQRQRVGIAT 158
Cdd:PRK11264 83 LR-QHVGFVFQN--FNLFPHRTVLENIiEGPVIVKGE-PKEEATARARELLAKVGLAGKETS-YPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAgASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQ 238
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
....
gi 1566271202 239 DERT 242
Cdd:PRK11264 237 QPRT 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-224 |
4.36e-36 |
|
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: 126.74 E-value: 4.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLadlrg 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD---SGEIKVLGKDIKKEPEEVK----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNPgaslnpvlpvgrqvelplRLHYDLTrserverVNAMLakvglpadvaakfphELSGGQRQRVGIATALIT 162
Cdd:cd03230 73 RRIGYLPEEP------------------SLYENLT-------VRENL---------------KLSGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSV 224
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-220 |
6.15e-36 |
|
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: 127.65 E-value: 6.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 7 DLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadrtlaDLRGRYTG 86
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT---SGSIRVFGKPL---------EKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 87 MVFQNpgASLNPVLPV-GRQVEL-----PLRLHYDLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATAL 160
Cdd:cd03235 72 YVPQR--RSIDRDFPIsVRDVVLmglygHKGLFRRLSKADK-AKVDEALERVGL-SELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 161 ITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLD 220
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-241 |
8.35e-36 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 128.76 E-value: 8.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEV---------IGAA 73
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPD---SGEIRVGGEEIrlkpdrdgeLVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 74 D-RTLADLRGRyTGMVFQNpgASLNPVLPVGRQV-ELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQR 151
Cdd:COG4598 86 DrRQLQRIRTR-LGMVFQS--FNLWSHMTVLENViEAPVHVL-GRPKAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 152 QRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETA 231
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
250
....*....|
gi 1566271202 232 AMLAAPQDER 241
Cdd:COG4598 240 EVFGNPKSER 249
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-205 |
2.34e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 126.06 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGSEVigaadRTLADLRgRY 84
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRL-----TALPAEQ-RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 TGMVFQNPgaSLNPVLPVGRQveLPLRLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSP 164
Cdd:COG4136 78 IGILFQDD--LLFPHLSVGEN--LAFALPPTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1566271202 165 RLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHD 205
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-247 |
4.17e-35 |
|
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: 133.42 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQNP 92
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT---SGRILIDGIDL---RQIDPASLR-RQIGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 ---GASL--NpvlpvgrqvelpLRLHYDLTRSERVERVnamLAKVGLpADVAAKFPH-----------ELSGGQRQRVGI 156
Cdd:COG2274 559 flfSGTIreN------------ITLGDPDATDEEIIEA---ARLAGL-HDFIEALPMgydtvvgeggsNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 157 ATALITSPRLIVADEPTTALDSITQRQIVDlsvSLVD-EAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETGETAAMLA 235
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILE---NLRRlLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEELLA 698
|
250
....*....|..
gi 1566271202 236 apQDERTARLVR 247
Cdd:COG2274 699 --RKGLYAELVQ 708
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-245 |
5.84e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.64 E-value: 5.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 22 DLSIGDGERVGLIGSSGSGKS----MIAramlGLLPPDvtvAGSVMLGGSEVIGA--ADRTLAdlrgrytgMVFQ--Npg 93
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKStllnLIA----GFLPPD---SGRILWNGQDLTALppAERPVS--------MLFQenN-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 asLNPVLPVGRQVELPLRLHYDLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPT 173
Cdd:COG3840 82 --LFPHLTVAQNIGLGLRPGLKLTAEQR-AQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 174 TALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARL 245
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-235 |
5.87e-35 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 126.13 E-value: 5.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVtvaGSVMLGGSEVIGAADRTLADLrgry 84
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS---GSILIDGEDVRKEPREARRQI---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 tGMVFQNPGaslnpvLPVGRQVELPLRLH---YDLTRSERVERVNAMLAKVGLPADVAAKFpHELSGGQRQRVGIATALI 161
Cdd:COG4555 77 -GVLPDERG------LYDRLTVRENIRYFaelYGLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLA 235
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-232 |
6.14e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 126.26 E-value: 6.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNp 92
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS---SGSILLEGTDITKLRGKKLRKLR-RRIGMIFQH- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gASLNPVLPVGRQVeLPLRLHYD---------LTRSERVERVNAmLAKVGLpADVAAKFPHELSGGQRQRVGIATALITS 163
Cdd:TIGR02315 88 -YNLIERLTVLENV-LHGRLGYKptwrsllgrFSEEDKERALSA-LERVGL-ADKAYQRADQLSGGQQQRVAIARALAQQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAA 232
Cdd:TIGR02315 164 PDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE 232
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-212 |
6.34e-35 |
|
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: 125.04 E-value: 6.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARaMLGLL-PPDvtvAGSVMLGGSEVIGAADRTLADLRGR 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLN-IIGLLeKFD---SGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 YTGMVFQNPGasLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLPADVAAKfPHELSGGQRQRVGIATALITS 163
Cdd:TIGR03608 77 KLGYLFQNFA--LIENETVEENLDLGLKYK-KLSKKEKREKKKEALEKVGLNLKLKQK-IYELSGGEQQRVALARAILKP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRA 212
Cdd:TIGR03608 153 PPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQA 200
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-228 |
8.80e-35 |
|
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: 123.70 E-value: 8.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGr 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS---SGEILLDGKDLASLSPKELARKIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 ytgmvfqnpgaslnpVLPvgrQVelplrlhydltrservervnamLAKVGLpADVAAKFPHELSGGQRQRVGIATALITS 163
Cdd:cd03214 77 ---------------YVP---QA----------------------LELLGL-AHLADRPFNELSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
13-222 |
1.72e-34 |
|
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: 123.90 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNp 92
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPS---RGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gASLNPVLPVGRQVELPLRLHYDLTRSERvERVNAMLAKVGLPaDVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:TIGR02673 88 -FRLLPDRTVYENVALPLEVRGKKEREIQ-RRVGAALRQVGLE-HKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1566271202 173 TTALDSITQRQIVDLsVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEG 222
Cdd:TIGR02673 165 TGNLDPDLSERILDL-LKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-228 |
3.11e-34 |
|
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: 123.89 E-value: 3.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAadrtlaDLRG 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT---SGEILLDGKDITNL------PPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNpgASLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:cd03300 72 RPVNTVFQN--YALFPHLTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 163 SPRLIVADEPTTALDSITQRQI-VDLSvSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMqLELK-RLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-243 |
3.15e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 124.35 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARaMLGLLppDVTVAGSVMLGGSEV---IGAADRTL 77
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLL--ETPDSGQLNIAGHQFdfsQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 78 ADLRgRYTGMVFQNpgASLNPVLPVGRQ-VELPLRLhYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGI 156
Cdd:COG4161 78 RLLR-QKVGMVFQQ--YNLWPHLTVMENlIEAPCKV-LGLSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 157 ATALITSPRLIVADEPTTALDSITQRQIVDLSVSLvDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGeTAAMLAA 236
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQ 230
|
....*..
gi 1566271202 237 PQDERTA 243
Cdd:COG4161 231 PQTEAFA 237
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-222 |
3.39e-34 |
|
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: 121.58 E-value: 3.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRY 84
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---SGEILIDGKDI---AKLPLEELR-RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 TGMVFQnpgaslnpvlpvgrqvelplrlhydltrservervnamlakvglpadvaakfpheLSGGQRQRVGIATALITSP 164
Cdd:cd00267 75 IGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 165 RLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEG 222
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-174 |
4.01e-34 |
|
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: 121.22 E-value: 4.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRGRyTGMVFQNPgaSLN 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT---EGTILLDGQDL---TDDERKSLRKE-IGYVFQDP--QLF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLPVGRQVELPLRLhYDLTRSERVERVNAMLAKVGLP---ADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTT 174
Cdd:pfam00005 72 PRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-242 |
8.04e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.35 E-value: 8.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAM--LGLLPPDVTVAGSVMLGGSEVIGAADRTLaDLRg 82
Cdd:PRK14239 8 VSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIYSPRTDTV-DLR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNPgaslNPV-LPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFpHE----LSGGQRQRVGIA 157
Cdd:PRK14239 86 KEIGMVFQQP----NPFpMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRL-HDsalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 158 TALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEagASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
....*
gi 1566271202 238 QDERT 242
Cdd:PRK14239 239 KHKET 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-227 |
9.11e-34 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 123.27 E-value: 9.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIG-AADRtladlrgrytGMVFQN 91
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGSITLDGKPVEGpGAER----------GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 92 PGasLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADE 171
Cdd:PRK11248 79 EG--LLPWRNVQDNVAFGLQLA-GVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 172 PTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVL--DEGSVVET 227
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVER 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-246 |
1.12e-33 |
|
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: 124.91 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 33 LIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadrTLADLRGRYTGMVFQNpgASLNPVLPVGRQVELPLRL 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD---SGSIMLDGEDV------TNVPPHLRHINMVFQS--YALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 113 HyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLV 192
Cdd:TIGR01187 70 R-KVPRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 193 DEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLV 246
Cdd:TIGR01187 148 EQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-228 |
1.54e-33 |
|
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: 121.63 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 27 DGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsevigaadRTLADLR--------GRYTGMVFQNpgASLNP 98
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPD---GGTIVLNG--------TVLFDSRkkinlppqQRKIGLVFQQ--YALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 99 VLPVGRQVELPLRLHydlTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDS 178
Cdd:cd03297 89 HLNVRENLAFGLKRK---RNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1566271202 179 ITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-238 |
2.11e-33 |
|
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: 122.06 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadrTLADL 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD---SGTILFGGEDA------TDVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTGMVFQNpgASLNPVLPVGRQVELPLRLHYDLTR---SERVERVNAMLAKVGLPAdVAAKFPHELSGGQRQRVGIA 157
Cdd:cd03296 72 QERNVGFVFQH--YALFRHMTVFDNVAFGLRVKPRSERppeAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 158 TALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
.
gi 1566271202 238 Q 238
Cdd:cd03296 229 A 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-246 |
1.09e-32 |
|
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: 120.13 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIaIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsevigaADRTLADLRG 82
Cdd:cd03299 1 LKVENLSK-DWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD---SGKILLNG------KDITNLPPEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNpgASLNPVLPVGRQVELPLRlHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:cd03299 71 RDISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERT 242
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
....
gi 1566271202 243 ARLV 246
Cdd:cd03299 227 AEFL 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-225 |
3.69e-32 |
|
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: 117.74 E-value: 3.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGsEVIGAADRTladlrgRYTGMVFQNP 92
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE---SSGSILLNG-KPIKAKERR------KSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GASLnpvlpVGRQVELPLRLHYDLTrSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:cd03226 81 DYQL-----FTDSVREELLLGLKEL-DAGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVV 225
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-243 |
4.17e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.58 E-value: 4.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARaMLGLLP-PD---VTVAGSVMLGGSEvigAADRT 76
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRsgtLNIAGNHFDFSKT---PSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 77 LADLRgRYTGMVFQNpgASLNPVLPVGRQ-VELPLRLhYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVG 155
Cdd:PRK11124 77 IRELR-RNVGMVFQQ--YNLWPHLTVQQNlIEAPCRV-LGLSKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 156 IATALITSPRLIVADEPTTALD-SITQrQIVDLSVSLvDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGeTAAML 234
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDpEITA-QIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCF 228
|
....*....
gi 1566271202 235 AAPQDERTA 243
Cdd:PRK11124 229 TQPQTEAFK 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-246 |
6.06e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.48 E-value: 6.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGL--LPPDVTVAGSVMLGGSEVIgaaDRTLADL 80
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVSGEVYLDGQDIF---KMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRyTGMVFQNPgaslNPV--LPVGRQVELPLRLHYDL-TRSERVERVNAMLAKVGLPADVAAKF---PHELSGGQRQRV 154
Cdd:PRK14247 81 RRR-VQMVFQIP----NPIpnLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEagASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAML 234
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
250
....*....|..
gi 1566271202 235 AAPQDERTARLV 246
Cdd:PRK14247 234 TNPRHELTEKYV 245
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-224 |
1.11e-31 |
|
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: 116.74 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 19 HGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQNpgASLNP 98
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP---TSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 99 VLPVGRQVELPLRLHYDLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDS 178
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIR-KRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1566271202 179 ITQRQIVDLSVSlVDEAGASMLFITHDFSVLTRATTRCVVLDEGSV 224
Cdd:cd03292 170 DTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-249 |
2.82e-31 |
|
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: 116.68 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKS----MIAramlGLLPPDvtvAGSVMLGGSEVIGAADRTLAD 79
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTtlfnLIT----GFYRPT---SGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 80 LrgrytGMV--FQNPGaslnpVLP---------VGRQVELPLRLHYDLTRSERV--------ERVNAMLAKVGLpADVAA 140
Cdd:COG0411 79 L-----GIArtFQNPR-----LFPeltvlenvlVAAHARLGRGLLAALLRLPRArreerearERAEELLERVGL-ADRAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 141 KFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLD 220
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLD 227
|
250 260
....*....|....*....|....*....
gi 1566271202 221 EGSVVETGETAAMLAAPQdertarlVRAA 249
Cdd:COG0411 228 FGRVIAEGTPAEVRADPR-------VIEA 249
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-222 |
6.91e-31 |
|
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: 113.25 E-value: 6.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQNP 92
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT---SGEILIDGVDL---RDLDLESLR-KNIAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gaslnpVLpvgrqvelplrlhYDLTRSERVervnamlakvglpadvaakfpheLSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:cd03228 86 ------FL-------------FSGTIRENI-----------------------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1566271202 173 TTALDSITQRQIVDLSVSLvdEAGASMLFITHDFSVLTRAtTRCVVLDEG 222
Cdd:cd03228 124 TSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-236 |
9.16e-31 |
|
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: 120.25 E-value: 9.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIA-IGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLR 81
Cdd:COG4988 337 IELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY---SGSILINGVDL---SDLDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 82 GRyTGMVFQNPgaslnpVLPVG--RQVelpLRLhYDLTRSErvERVNAMLAKVGLpADVAAKFPHE-----------LSG 148
Cdd:COG4988 411 RQ-IAWVPQNP------YLFAGtiREN---LRL-GRPDASD--EELEAALEAAGL-DEFVAALPDGldtplgeggrgLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 149 GQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVdeAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETG 228
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLALLAQA-DRILVLDDGRIVEQG 553
|
....*...
gi 1566271202 229 ETAAMLAA 236
Cdd:COG4988 554 THEELLAK 561
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-237 |
1.30e-30 |
|
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: 117.51 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsevigaadRTLADLRGRYT--------GMVFQNp 92
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD---SGRIRLGG--------EVLQDSARGIFlpphrrriGYVFQE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLakvGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:COG4148 86 -ARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
3-237 |
1.73e-30 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 114.13 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSevigaaDRTLADLRG 82
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPD---SGRIRLNGQ------DATRVHARD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNpgASLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:TIGR00968 72 RKIGFVFQH--YALFKHLTVRDNIAFGLEIR-KHPKAKIKARVEELLELVQL-EGLGDRYPNQLSGGQRQRVALARALAV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:TIGR00968 148 EPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHP 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-239 |
1.79e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.50 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGgSEVI--GAADRTLADLRgRYTGMVFQNPGASLnp 98
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQP---TSGTVTIG-ERVItaGKKNKKLKPLR-KKVGIVFQFPEHQL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 99 vlpVGRQVELPL---RLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTA 175
Cdd:PRK13634 99 ---FEETVEKDIcfgPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 176 LDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQD 239
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-249 |
2.32e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 114.68 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEV---------IGAA 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPS---EGSIVVNGQTInlvrdkdgqLKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 74 DRT-LADLRGRYTgMVFQNpgASLNPVLPVGRQV-ELPLRLhYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQR 151
Cdd:PRK10619 83 DKNqLRLLRTRLT-MVFQH--FNLWSHMTVLENVmEAPIQV-LGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 152 QRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETA 231
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
250
....*....|....*...
gi 1566271202 232 AMLAAPQDERTARLVRAA 249
Cdd:PRK10619 238 QLFGNPQSPRLQQFLKGS 255
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-228 |
2.79e-30 |
|
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: 113.12 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEV--IGAADRTLAdl 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT---SGRIYIGGRDVtdLPPKDRDIA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 rgrytgMVFQNpgASLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATAL 160
Cdd:cd03301 76 ------MVFQN--YALYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 161 ITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-228 |
7.42e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.74 E-value: 7.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGSEVigaADRTLADLRGRyTGMVFQNP-- 92
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITL---TAKTVWDIREK-VGIVFQNPdn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 ---GASlnpvlpVGRQVELPLRlHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVA 169
Cdd:PRK13640 96 qfvGAT------VGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 170 DEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETG 228
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMA-DQVLVLDDGKLLAQG 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-238 |
3.62e-29 |
|
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: 110.60 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLrgr 83
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT---SGSVLFDGEDITGLPPHEIARL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 ytGMV--FQN----PGASLNPVLPVGRQVELPLRLHYDLTRSER---VERVNAMLAKVGLpADVAAKFPHELSGGQRQRV 154
Cdd:cd03219 76 --GIGrtFQIprlfPELTVLENVMVAAQARTGSGLLLARARREEreaRERAEELLERVGL-ADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAML 234
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
....
gi 1566271202 235 AAPQ 238
Cdd:cd03219 232 NNPR 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-229 |
4.97e-29 |
|
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: 110.25 E-value: 4.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 20 GVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAA-DRTLadlrgrytgmVFQNpgASLNP 98
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQP---TSGGVILEGKQITEPGpDRMV----------VFQN--YSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 99 VLPVGRQVELPL-RLHYDLTRSERVERVNAMLAKVGLPAdVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALD 177
Cdd:TIGR01184 68 WLTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGLTE-AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 178 SITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGE 229
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQ 198
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-237 |
5.39e-29 |
|
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: 112.90 E-value: 5.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNpgASLNPVL 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPD---EGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 101 PVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLpadvAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSIT 180
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSERRISFERVIELLGIGHL----LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 181 QRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
21-245 |
7.76e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 7.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRGRyTGMVFQNPGASLnpvl 100
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ---SGEIKIDGITI---SKENLKEIRKK-IGIIFQNPDNQF---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 101 pVGRQVE------LPLRLhydLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTT 174
Cdd:PRK13632 97 -IGATVEddiafgLENKK---VPPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 175 ALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETGETAAMLAAPQDERTARL 245
Cdd:PRK13632 172 MLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILA-DKVIVFSEGKLIAQGKPKEILNNKEILEKAKI 241
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-249 |
8.98e-29 |
|
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: 110.31 E-value: 8.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGSEV----IGAADRTLA 78
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 dLRGRYtGMVFQNPGASLNPVLPVGRQV-ELPLRL---HYDLTRSERVErvnaMLAKVGLPADVAAKFPHELSGGQRQRV 154
Cdd:TIGR02323 84 -MRTEW-GFVHQNPRDGLRMRVSAGANIgERLMAIgarHYGNIRATAQD----WLEEVEIDPTRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAML 234
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVL 237
|
250
....*....|....*
gi 1566271202 235 AAPQDERTARLVRAA 249
Cdd:TIGR02323 238 DDPQHPYTQLLVSSI 252
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-248 |
1.36e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.49 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRGRyTGMVFQ-- 90
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT---SGRILIDGVDI---RDLTLESLRRQ-IGVVPQdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 91 --------------NPGASLnpvlpvgrqvelplrlhydltrsERVERVnamLAKVGLpADVAAKFPH-----------E 145
Cdd:COG1132 424 flfsgtirenirygRPDATD-----------------------EEVEEA---AKAAQA-HEFIEALPDgydtvvgergvN 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 146 LSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDlsvSLVDE-AGASMLFITHDFSVLTRAtTRCVVLDEGSV 224
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE---ALERLmKGRTTIVIAHRLSTIRNA-DRILVLDDGRI 552
|
250 260
....*....|....*....|....
gi 1566271202 225 VETGeTAAMLAApQDERTARLVRA 248
Cdd:COG1132 553 VEQG-THEELLA-RGGLYARLYRL 574
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-211 |
1.75e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 108.75 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLlppDVTVAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNpgAS 95
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQF--HH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 96 LNPVLPVGRQVELPLrLHYDLTRSERVERVNAMLAKVGLPADVAAKfPHELSGGQRQRVGIATALITSPRLIVADEPTTA 175
Cdd:PRK11629 98 LLPDFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1566271202 176 LDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTR 211
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-228 |
7.40e-28 |
|
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: 106.81 E-value: 7.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 22 DLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvagsvmlGGSEVIGAADRTLADLRGRYTGMVFQNpgASLNPVLP 101
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQ---------SGRVLINGVDVTAAPPADRPVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 102 VGRQVELPLRLHYDLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQ 181
Cdd:cd03298 87 VEQNVGLGLSPGLKLTAEDR-QAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1566271202 182 RQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-234 |
1.14e-27 |
|
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: 107.09 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvTVAGSVMLGGsEVIGAADrtLADLRG 82
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPP--TYGNDVRLFG-ERRGGED--VWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYtGMVfqnpGASLNPVLPV---GRQVELP-----LRLHYDLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRV 154
Cdd:COG1119 79 RI-GLV----SPALQLRFPRdetVLDVVLSgffdsIGLYREPTDEQR-ERARELLELLGL-AHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAML 234
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-228 |
2.29e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.10 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADrtLADLRGRyTGMVFQNPGA 94
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPS---EGKVYVDGLDTSDEEN--LWDIRNK-AGMVFQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 SLnpvlpVGRQVEL-----PLRLhyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVA 169
Cdd:PRK13633 97 QI-----VATIVEEdvafgPENL--GIPPEEIRERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 170 DEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETG 228
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEG 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-249 |
3.10e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.08 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGL--LPPDVTVAGSVMLGGSEVIgAADRTLADL 80
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEARVEGEVRLFGRNIY-SPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RgRYTGMVFQNPGASlnPVLPVGRQVELPLRLHyDLTRS--ERVERVNAMLAKVGLPADVAAK---FPHELSGGQRQRVG 155
Cdd:PRK14267 84 R-REVGMVFQYPNPF--PHLTIYDNVAIGVKLN-GLVKSkkELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 156 IATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEagASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLA 235
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|....
gi 1566271202 236 APQDERTARLVRAA 249
Cdd:PRK14267 238 NPEHELTEKYVTGA 251
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-226 |
4.77e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.86 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 17 IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLlppDVTVAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNpgASL 96
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGL---DDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQS--FML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 97 NPVLPVGRQVELPLRLHYDLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTAL 176
Cdd:PRK10584 100 IPTLNALENVELPALLRGESSRQSR-NGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1566271202 177 DSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVE 226
Cdd:PRK10584 178 DRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARC-DRRLRLVNGQLQE 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-205 |
5.21e-27 |
|
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: 104.10 E-value: 5.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadRTLADL 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS---AGEVLWNGEPI-----RDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTGMVFQNPGasLNPVLPVGRQVELPLRLHYDLTRSERVErvnAMLAKVGLpADVAAKFPHELSGGQRQRVGIATAL 160
Cdd:COG4133 73 YRRRLAYLGHADG--LKPELTVRENLRFWAALYGLRADREAID---EALEAVGL-AGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1566271202 161 ITSPRLIVADEPTTALDSITQRQIVDLSVSLVdEAGASMLFITHD 205
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHL-ARGGAVLLTTHQ 190
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-224 |
6.72e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.14 E-value: 6.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvagsvmlGGSEVIGAAdrTLADLRGRy 84
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS---------AGELLAGTA--PLAEARED- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 TGMVFQNpgASLNPVLPVGRQVELPLRLHYdltrserveRVNAM--LAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:PRK11247 83 TRLMFQD--ARLLPWKKVIDNVGLGLKGQW---------RDAALqaLAAVGL-ADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSV 224
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-246 |
7.61e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.61 E-value: 7.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGsevigaADRTLADLRG 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---TAGQIMLDG------VDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNpgASLNPVLPVGRQVELPLRlHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:PRK11607 91 RPINMMFQS--YALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERT 242
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
....
gi 1566271202 243 ARLV 246
Cdd:PRK11607 247 AEFI 250
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-225 |
8.09e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 104.19 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 12 IGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgRYTGMVFQN 91
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPS---AGKIWFSGHDITRLKNREVPFLR-RQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 92 PGASLNPVlpVGRQVELPLRLHYDLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADE 171
Cdd:PRK10908 88 HHLLMDRT--VYDNVAIPLIIAGASGDDIR-RRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 172 PTTALDSITQRQIVDLSVSLvDEAGASMLFITHDFSVLTRATTRCVVLDEGSVV 225
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-237 |
8.59e-27 |
|
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: 109.09 E-value: 8.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQNP 92
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ---SGSITLGGVDL---RDLDEDDLR-RRIAVVPQRP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 ---GASL--NpvLPVGRQvelplrlhyDLTRservERVNAMLAKVGLpADVAAKFPH-----------ELSGGQRQRVGI 156
Cdd:COG4987 419 hlfDTTLreN--LRLARP---------DATD----EELWAALERVGL-GDWLAALPDgldtwlgeggrRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 157 ATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVdeAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETGETAAMLAA 236
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQ 559
|
.
gi 1566271202 237 P 237
Cdd:COG4987 560 N 560
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-246 |
9.89e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 105.01 E-value: 9.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSV---MLGGSEV----IGAADRTL 77
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD---AGEVhyrMRDGQLRdlyaLSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 78 AdLRGRYtGMVFQNPGASLNPVLPVGRQVELPLRL----HYDLTRSERVErvnaMLAKVGLPADVAAKFPHELSGGQRQR 153
Cdd:PRK11701 86 L-LRTEW-GFVHQHPRDGLRMQVSAGGNIGERLMAvgarHYGDIRATAGD----WLERVEIDAARIDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 154 VGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAM 233
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQV 239
|
250
....*....|...
gi 1566271202 234 LAAPQDERTARLV 246
Cdd:PRK11701 240 LDDPQHPYTQLLV 252
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-235 |
1.84e-26 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 103.28 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLADLrgr 83
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP---RSGSIRFDGRDITGLPPHERARA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 ytGMVFQNPGASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMlakvglpadvaakFP----------HELSGGQRQR 153
Cdd:cd03224 76 --GIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYEL-------------FPrlkerrkqlaGTLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 154 VGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAM 233
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
..
gi 1566271202 234 LA 235
Cdd:cd03224 220 LA 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-245 |
2.11e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.39 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEvIGAADRTLADLRgRYTGMVFQNPG 93
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT---SGEVLIKGEP-IKYDKKSLLEVR-KTVGIVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASL-NPVlpVGRQVEL-PLRLhyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADE 171
Cdd:PRK13639 89 DQLfAPT--VEEDVAFgPLNL--GLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 172 PTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARL 245
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANL 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
14-260 |
3.24e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAAdRTLADLRgRYTGMVFQNPG 93
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP---SSGRILFDGKPIDYSR-KGLMKLR-ESVGMVFQDPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLNPVlPVGRQVEL-PLRLHydLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:PRK13636 93 NQLFSA-SVYQDVSFgAVNLK--LPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTA--RLVRAAR 250
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVnlRLPRIGH 248
|
250
....*....|
gi 1566271202 251 TLTLRASREG 260
Cdd:PRK13636 249 LMEILKEKDG 258
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-228 |
4.07e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.71 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAA-DRTLADLRGRyTGMVFQNPG 93
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP---TTGTVTVDDITITHKTkDKYIRPVRKR-IGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLNPVlPVGRQVEL-PLRLHYDLtrSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:PRK13646 96 SQLFED-TVEREIIFgPKNFKMNL--DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-235 |
4.87e-26 |
|
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: 106.81 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSV-MLGGSEVIGAADRTLaDLRGR---YTGMVFQN-- 91
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEP---TSGEVnVRVGDEWVDMTKPGP-DGRGRakrYIGILHQEyd 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 92 --PGASLNPVLPVGRQVELPlrlhYDLTRSERVervnAMLAKVGLPADVAA----KFPHELSGGQRQRVGIATALITSPR 165
Cdd:TIGR03269 376 lyPHRTVLDNLTEAIGLELP----DELARMKAV----ITLKMVGFDEEKAEeildKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 166 LIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLA 235
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-250 |
5.14e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.59 E-value: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEvIGAADRTLADLRGRyTGMVFQNPGASLNPVl 100
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT---SGKIIIDGVD-ITDKKVKLSDIRKK-VGLVFQYPEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 101 PVGRQVEL-PLRLhyDLTRSERVERVNAMLAKVGLPADVAA-KFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDS 178
Cdd:PRK13637 100 TIEKDIAFgPINL--GLSEEEIENRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 179 ITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAM-----------LAAPQderTARLVR 247
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVfkevetlesigLAVPQ---VTYLVR 254
|
...
gi 1566271202 248 AAR 250
Cdd:PRK13637 255 KLR 257
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
13-223 |
9.30e-26 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 101.36 E-value: 9.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEI--VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVML----GGSEVIGAADRTLADLRGRYTG 86
Cdd:COG4778 20 GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPD---SGSILVrhdgGWVDLAQASPREILALRRRTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 87 MVFQnpgaSLNpVLPvgRQ-----VELPLRLHyDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALI 161
Cdd:COG4778 97 YVSQ----FLR-VIP--RVsaldvVAEPLLER-GVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 162 TSPRLIVADEPTTALDSiTQRQIVdlsVSLVDEA---GASMLFITHDFSVLTRATTRCVVLDEGS 223
Cdd:COG4778 169 ADPPLLLLDEPTASLDA-ANRAVV---VELIEEAkarGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-235 |
1.17e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.20 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 22 DLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsevigaADRTLADLRGRYTGMVFQNpgASLNPVLP 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA---SGSLTLNG------QDHTTTPPSRRPVSMLFQE--NNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 102 VGRQVELPLRLHYDLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQ 181
Cdd:PRK10771 88 VAQNIGLGLNPGLKLNAAQR-EKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 182 RQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLA 235
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-238 |
1.92e-25 |
|
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: 100.83 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLADLrgr 83
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPP---RSGSIRFDGEDITGLPPHRIARL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 ytGMVFqnpgaslnpvLPVGRQV----------ELPLRLHYDLTR-SERVERVNAMlakvglpadvaakFPH-------- 144
Cdd:COG0410 79 --GIGY----------VPEGRRIfpsltveenlLLGAYARRDRAEvRADLERVYEL-------------FPRlkerrrqr 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 145 --ELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEG 222
Cdd:COG0410 134 agTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERG 212
|
250
....*....|....*.
gi 1566271202 223 SVVETGETAAMLAAPQ 238
Cdd:COG0410 213 RIVLEGTAAELLADPE 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-228 |
2.56e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 99.97 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEvIGAADRtlADLRGRYtGMVFQNPG---A 94
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT---SGSVLLDGTD-IRQLDP--ADLRRNI-GYVPQDVTlfyG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 SLNPVLPVGRQvelplrlhydLTRSERVERVnAMLAKVGlpaDVAAKFPH-----------ELSGGQRQRVGIATALITS 163
Cdd:cd03245 93 TLRDNITLGAP----------LADDERILRA-AELAGVT---DFVNKHPNgldlqigergrGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVD-LSVSLVDEAgasMLFITHDFSVLTRAtTRCVVLDEGSVVETG 228
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKErLRQLLGDKT---LIIITHRPSLLDLV-DRIIVMDSGRIVADG 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-241 |
2.57e-25 |
|
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: 105.33 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadRTL--ADLRgRYTGMVFQNPG-- 93
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPT---EGSVLLDGVDI-----RQIdpADLR-RNIGYVPQDPRlf 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 -ASLNPVLPVGRQvelplrlhydLTRSERVERVnAMLAKVGlpaDVAAKFPH-----------ELSGGQRQRVGIATALI 161
Cdd:TIGR03375 552 yGTLRDNIALGAP----------YADDEEILRA-AELAGVT---EFVRRHPDgldmqigergrSLSGGQRQAVALARALL 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVdeAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETGETAAMLAAPQDER 241
Cdd:TIGR03375 618 RDPPILLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQVLEALRKGR 694
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-212 |
2.73e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.19 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKSMIARaMLGLLppDVTVAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNpgAS 95
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCL--DKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQR--YH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 96 LNPVLPVGRQVELPlRLHYDLTRSERVERVNAMLAKVGLPADVAAKfPHELSGGQRQRVGIATALITSPRLIVADEPTTA 175
Cdd:PRK10535 97 LLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1566271202 176 LDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRA 212
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQA 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-230 |
3.21e-25 |
|
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: 99.94 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 22 DLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTladlrgRYTGMVFQNpgASLNPVLP 101
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEP---ASGSIKVNDQSHTGLAPYQ------RPVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 102 VGRQVELPLRLHYDLTRSERvERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQ 181
Cdd:TIGR01277 87 VRQNIGLGLHPGLKLNAEQQ-EKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1566271202 182 RQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGET 230
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-236 |
6.49e-25 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 99.48 E-value: 6.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 7 DLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEvIGAADrtLADLRgRYTG 86
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE---NGRVLVDGHD-LALAD--PAWLR-RQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 87 MVFQ----------------NPGASLNPVLPVGRQVE-----LPLRLHYDLTRSERvervnamlaKVGLpadvaakfphe 145
Cdd:cd03252 80 VVLQenvlfnrsirdnialaDPGMSMERVIEAAKLAGahdfiSELPEGYDTIVGEQ---------GAGL----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 146 lSGGQRQRVGIATALITSPRLIVADEPTTALD----SITQRQIVDLSvslvdeAGASMLFITHDFSVLTRAtTRCVVLDE 221
Cdd:cd03252 140 -SGGQRQRIAIARALIHNPRILIFDEATSALDyeseHAIMRNMHDIC------AGRTVIIIAHRLSTVKNA-DRIIVMEK 211
|
250
....*....|....*
gi 1566271202 222 GSVVETGETAAMLAA 236
Cdd:cd03252 212 GRIVEQGSHDELLAE 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-228 |
7.76e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.57 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEvIGAADRT----LA 78
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD---SGEVLWDGEP-LDPEDRRrigyLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 DLRGRYTGMvfqnpgaslnpvlPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIAT 158
Cdd:COG4152 78 EERGLYPKM-------------KVGEQLVYLARLK-GLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-226 |
9.54e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 9.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIG-AADRTLADLRgRYTGMVFQNPGASL--N 97
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS---SGTITIAGYHITPeTGNKNLKKLR-KKVSLVFQFPEAQLfeN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLpvgRQVEL-PLrlHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTAL 176
Cdd:PRK13641 102 TVL---KDVEFgPK--NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1566271202 177 DSITQRQIVDLSVSLvDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVE 226
Cdd:PRK13641 177 DPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-228 |
1.03e-24 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 98.60 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIgaadRTLADLRg 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT---SGRATVAGHDVV----REPREVR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNPgaSLNPVLPVGRQVELPLRLhYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:cd03265 73 RRIGIVFQDL--SVDDELTGWENLYIHARL-YGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-228 |
1.11e-24 |
|
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: 98.06 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaaDRTLADLRg 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD---SGEITFDGKSY----QKNIEALR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 rYTGMVFQNPGasLNPVLPVGRQVELPLRLHydLTRSERVERVnamLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:cd03268 73 -RIGALIEAPG--FYPNLTARENLRLLARLL--GIRKKRIDEV---LDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-237 |
1.57e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 99.29 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsevIGAADRT-LADLRgRYTGMVFQNP 92
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ---KGKVLVSG---IDTGDFSkLQGIR-KLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GASLnpvlpVGRQVELPLRLHYD---LTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVA 169
Cdd:PRK13644 87 ETQF-----VGRTVEEDLAFGPEnlcLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 170 DEPTTALDSITQRQIVDlSVSLVDEAGASMLFITHDFSVLtRATTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLE-RIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-231 |
2.26e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 97.58 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKE--IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadRTLADL 80
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT---SGTAYINGYSI-----RTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTGMVFQNpgASLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLPaDVAAKFPHELSGGQRQRVGIATAL 160
Cdd:cd03263 73 ARQSLGYCPQF--DALFDELTVREHLRFYARLK-GLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 161 ITSPRLIVADEPTTALDSITQRQIVDLSVSLVdeAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETA 231
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-205 |
3.47e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.02 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGA-ADRtladlr 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD---SGRIMLDGQDITHVpAEN------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 82 gRYTGMVFQNpgASLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALI 161
Cdd:PRK09452 86 -RHVNTVFQS--YALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHD 205
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-224 |
4.16e-24 |
|
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: 95.75 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 7 DLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVigaaDRTLADLRGRYTG 86
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP---TSGRVRLDGADI----SQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 87 MVFQNpgaslnpvlpvgrqVELplrlhYDLTRSERVervnamlakvglpadvaakfpheLSGGQRQRVGIATALITSPRL 166
Cdd:cd03246 80 YLPQD--------------DEL-----FSGSIAENI-----------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 167 IVADEPTTALDSITQRQIVDLSVSLvDEAGASMLFITHDFSVLTRAtTRCVVLDEGSV 224
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-235 |
6.43e-24 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 96.92 E-value: 6.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLppDVTvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQ--- 90
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFY--DVS-SGSILIDGQDI---REVTLDSLR-RAIGVVPQdtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 91 -------------NPGASlnpvlpvgrqvelplrlhydltrSERVERVnamlAKVGLPADVAAKFPH-----------EL 146
Cdd:cd03253 86 lfndtigynirygRPDAT-----------------------DEEVIEA----AKAAQIHDKIMRFPDgydtivgerglKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 147 SGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVdeAGASMLFITHDFSVLTRAtTRCVVLDEGSVVE 226
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVNA-DKIIVLKDGRIVE 215
|
....*....
gi 1566271202 227 TGETAAMLA 235
Cdd:cd03253 216 RGTHEELLA 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-228 |
1.07e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.76 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgr 83
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD---SGEVRLNGRPLADWSPAELARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 ytGMVFQNpgASLNPVLPVGRQVELPlRLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALI-- 161
Cdd:PRK13548 79 --AVLPQH--SSLSFPFTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDL-AHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 162 ----TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-246 |
1.52e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.70 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 7 DLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAmLGLLPPDVT---VAGSVMLGGSEVIGAadRTLADLRgR 83
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRT-LNRMNDKVSgyrYSGDVLLGGRSIFNY--RDVLEFR-R 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 YTGMVFQNPgaslNPV-LPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGL---PADVAAKFPHELSGGQRQRVGIATA 159
Cdd:PRK14271 102 RVGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 160 LITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEagASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQD 239
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
....*..
gi 1566271202 240 ERTARLV 246
Cdd:PRK14271 256 AETARYV 262
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-263 |
1.59e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.57 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNpgASLN 97
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALD 177
Cdd:PRK10070 119 PHMTVLDNTAFGMELA-GINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 178 SITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRAARTLTLRAS 257
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSA 276
|
....*.
gi 1566271202 258 REGADR 263
Cdd:PRK10070 277 KDIARR 282
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-228 |
2.24e-23 |
|
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: 94.57 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGeRVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRtladLRG 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS---SGTIRIDGQDVLKQPQK----LRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RyTGMVFQNPGASlnPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:cd03264 73 R-IGYLPQEFGVY--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 163 SPRLIVADEPTTALDsITQRQIVDlsvSLVDEAGASMLFI--THDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03264 148 DPSILIVDEPTAGLD-PEERIRFR---NLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-228 |
2.32e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.97 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQNPGASLnpvl 100
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK---SGEIFYNNQAI---TDDNFEKLR-KHIGIVFQNPDNQF---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 101 pVGRQVElplrlhYDLT---------RSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADE 171
Cdd:PRK13648 97 -VGSIVK------YDVAfglenhavpYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 172 PTTALDSITQRQIVDLSVSLVDEAGASMLFITHDfsvLTRA--TTRCVVLDEGSVVETG 228
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISITHD---LSEAmeADHVIVMNKGTVYKEG 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-246 |
2.37e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.88 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLP---PDVTVAGSVMLGGSEVIgaadRTLADL 80
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGKVLYFGKDIF----QIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTGMVFQNPGASlnPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKF---PHELSGGQRQRVGIA 157
Cdd:PRK14246 88 LRKEVGMVFQQPNPF--PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 158 TALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEagASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
....*....
gi 1566271202 238 QDERTARLV 246
Cdd:PRK14246 244 KNELTEKYV 252
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-245 |
2.95e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.03 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDL-RIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAadrTLADLR 81
Cdd:PRK13652 4 IETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT---SGSVLIRGEPITKE---NIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 82 gRYTGMVFQNPGASL-NPVlpVGRQVEL-PLRLHYDltrSERVE-RVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIAT 158
Cdd:PRK13652 78 -KFVGLVFQNPDDQIfSPT--VEQDIAFgPINLGLD---EETVAhRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQ 238
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
....*..
gi 1566271202 239 DERTARL 245
Cdd:PRK13652 231 LLARVHL 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-235 |
3.00e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.69 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDV-------------TVAGSVMLGGSEVIGAADRT-----LAD 79
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTgtiewifkdeknkKKTKEKEKVLEKLVIQKTRFkkikkIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 80 LRGRyTGMVFQNPGASL-----------NPVlpvgrqvelplrlHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSG 148
Cdd:PRK13651 103 IRRR-VGVVFQFAEYQLfeqtiekdiifGPV-------------SMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 149 GQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
....*..
gi 1566271202 229 ETAAMLA 235
Cdd:PRK13651 248 DTYDILS 254
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-236 |
5.53e-23 |
|
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: 94.22 E-value: 5.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKE--IVHGVDLSIGDGERVGLIGSSGSGKSMIARamlgLLPP--DVTvAGSVMLGGSEVigaADRTLA 78
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVN----LIPRfyDVD-SGRILIDGHDV---RDYTLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 DLRgRYTGMVFQN----------------PGASLNPVLPVGRQVELplrlHYDLTRSErvERVNAMLAKVGLpadvaakf 142
Cdd:cd03251 73 SLR-RQIGLVSQDvflfndtvaeniaygrPGATREEVEEAARAANA----HEFIMELP--EGYDTVIGERGV-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 143 phELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVdeAGASMLFITHDFSVLTRAtTRCVVLDEG 222
Cdd:cd03251 138 --KLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLSTIENA-DRIVVLEDG 212
|
250
....*....|....
gi 1566271202 223 SVVETGETAAMLAA 236
Cdd:cd03251 213 KIVERGTHEELLAQ 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-240 |
6.99e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.18 E-value: 6.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQNPGA 94
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGQIIIDGDLL---TEENVWDIR-HKIGMVFQNPDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 SLnpvlpVGRQVELPLRLHYD---LTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADE 171
Cdd:PRK13650 93 QF-----VGATVEDDVAFGLEnkgIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 172 PTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTrATTRCVVLDEGSvVETGETAAMLAAPQDE 240
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VESTSTPRELFSRGND 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-224 |
8.66e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 8.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIG------------- 71
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD---SGEVSIPKGLRIGylpqeppldddlt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 72 ------AADRTLADLRGRYTGMVFQNPGASLNPVlpvgRQVELPLRLH----YDLTRserveRVNAMLAKVGLPADVAAK 141
Cdd:COG0488 78 vldtvlDGDAELRALEAELEELEAKLAEPDEDLE----RLAELQEEFEalggWEAEA-----RAEEILSGLGFPEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 142 FPHELSGGQRQRVGIATALITSPRLIVADEPTTALDsitqrqiVDlSVS-----LVDEAGAsMLFITHDFSVLTRATTRC 216
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LE-SIEwleefLKNYPGT-VLVVSHDRYFLDRVATRI 219
|
....*...
gi 1566271202 217 VVLDEGSV 224
Cdd:COG0488 220 LELDRGKL 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-248 |
1.26e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.92 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGSEViGAADRTLADLRGR--YTGMVFQ----- 90
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTV-QREGRLARDIRKSraNTGYIFQqfnlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 91 NPGASLNPVLpVGRQVELPL-RLHYDLTRSERVERVNAMLAKVGLpadvaAKFPHE----LSGGQRQRVGIATALITSPR 165
Cdd:PRK09984 99 NRLSVLENVL-IGALGSTPFwRTCFSWFTREQKQRALQALTRVGM-----VHFAHQrvstLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 166 LIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMlaapQDERTARL 245
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF----DNERFDHL 248
|
...
gi 1566271202 246 VRA 248
Cdd:PRK09984 249 YRS 251
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-246 |
1.59e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.90 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 8 LRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLAdlrgRYTGM 87
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---AHGHVWLDGEHIQHYASKEVA----RRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 88 VFQN---PG-ASLNPVLPVGRQVELPLRLHYdltRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITS 163
Cdd:PRK10253 86 LAQNattPGdITVQELVARGRYPHQPLFTRW---RKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGetaamlaAPQDERTA 243
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTA 234
|
...
gi 1566271202 244 RLV 246
Cdd:PRK10253 235 ELI 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-228 |
2.39e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.92 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 22 DLSIGDGERVGLIGSSGSGKSMIARAMLGLLppdVTVAGSVMLGGSEVIGAADRT--LADLRgRYTGMVFQNPGASLNPV 99
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI---ISETGQTIVGDYAIPANLKKIkeVKRLR-KEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 100 lPVGRQVEL-PLRLHYDltRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDS 178
Cdd:PRK13645 107 -TIEKDIAFgPVNLGEN--KQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1566271202 179 ITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-225 |
2.82e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.84 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKS----MIAramlGLLPPDvtvAGSVMLGGSEVIGAADrtlaDLRGRYTGMVFQ 90
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKStllnAIA----GSLPPD---SGSILIDGKDVTKLPE----YKRAKYIGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 91 NP--G--ASL----NPVLPVGRQVELPLRLHydLTRSER---VERV--------NAMLAKVGLpadvaakfpheLSGGQR 151
Cdd:COG1101 88 DPmmGtaPSMtieeNLALAYRRGKRRGLRRG--LTKKRRelfRELLatlglgleNRLDTKVGL-----------LSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 152 QRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDfsvLTRAT---TRCVVLDEGSVV 225
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN---MEQALdygNRLIMMHEGRII 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-239 |
3.09e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 94.71 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 2 GVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLlpPDVTvAGSVMLGGSEV--IGAADRTLad 79
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL--EDIT-SGDLFIGEKRMndVPPAERGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 80 lrgrytGMVFQNpgASLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMlAKVGLPADVAAKFPHELSGGQRQRVGIATA 159
Cdd:PRK11000 78 ------GMVFQS--YALYPHLSVAENMSFGLKLA-GAKKEEINQRVNQV-AEVLQLAHLLDRKPKALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 160 LITSPRLIVADEPTTALDSITQRQI-VDLSvSLVDEAGASMLFITHD-FSVLTRAtTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMrIEIS-RLHKRLGRTMIYVTHDqVEAMTLA-DKIVVLDAGRVAQVGKPLELYHYP 225
|
..
gi 1566271202 238 QD 239
Cdd:PRK11000 226 AN 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-239 |
3.96e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.02 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVigaadrTLADLRG 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKP---TEGQIFIDGEDV------THRSIQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNpgASLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:PRK11432 78 RDICMVFQS--YALFPHMSLGENVGYGLKML-GVPKEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVEtgetaamLAAPQD 239
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQ-------IGSPQE 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-236 |
5.59e-22 |
|
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: 95.20 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEvIGAADRtlaDLRGRYTGMVFQnp 92
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP---TAGSVRLDGAD-LSQWDR---EELGRHIGYLPQ-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gaslnpvlpvgrQVELplrlhYDLTRSErvervN-AMLAKVGlPADV--AAKFP--HE-------------------LSG 148
Cdd:COG4618 414 ------------DVEL-----FDGTIAE-----NiARFGDAD-PEKVvaAAKLAgvHEmilrlpdgydtrigeggarLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 149 GQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLsVSLVDEAGASMLFITHDFSVLtRATTRCVVLDEGSVVETG 228
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAA-IRALKARGATVVVITHRPSLL-AAVDKLLVLRDGRVQAFG 548
|
....*...
gi 1566271202 229 ETAAMLAA 236
Cdd:COG4618 549 PRDEVLAR 556
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-239 |
6.95e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.46 E-value: 6.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPpdvTVAGSVMLGGSEVIGaadRTLADLRgRYTGMVFQNPGASLn 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE---EFEGKVKIDGELLTA---ENVWNLR-RKIGMVFQNPDNQF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 pvlpVGRQVELPLRLHYD---LTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTT 174
Cdd:PRK13642 95 ----VGATVEDDVAFGMEnqgIPREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 175 ALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVlTRATTRCVVLDEGSVVETGETAAMLAAPQD 239
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDE-AASSDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-233 |
1.17e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 90.66 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLrgry 84
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVK---SGSIRLDGEDITKLPPHERARA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 tGMVFqnpgaslnpvLPVGRQVeLPLrlhydLTRSERVERVNAMLAKVG--LPADVAAKFP--HE--------LSGGQRQ 152
Cdd:TIGR03410 76 -GIAY----------VPQGREI-FPR-----LTVEENLLTGLAALPRRSrkIPDEIYELFPvlKEmlgrrggdLSGGQQQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 153 RVGIATALITSPRLIVADEPTTALD-SITQrQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETA 231
Cdd:TIGR03410 139 QLAIARALVTRPKLLLLDEPTEGIQpSIIK-DIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGD 217
|
..
gi 1566271202 232 AM 233
Cdd:TIGR03410 218 EL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-226 |
1.23e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRG 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD---SGTVKLGETVKIGYFDQHQEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTgmVFQNpgasLNPVLPVGRQVElplrlhydltrserverVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:COG0488 393 DKT--VLDE----LRDGAPGGTEQE-----------------VRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLsvsLVDEAGAsMLFITHDFSVLTRATTRCVVLDEGSVVE 226
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEA---LDDFPGT-VLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-229 |
1.26e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 20 GVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVtvaGSVMLGGSEVI-GAADRTLADLRgRYTGMVFQNPGASL-- 96
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQ---GSVRVDDTLITsTSKNKDIKQIR-KKVGLVFQFPESQLfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 97 NPVL---PVGRQvelplrlHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPT 173
Cdd:PRK13649 101 ETVLkdvAFGPQ-------NFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 174 TALDSITQRQIVDLSVSLvDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGE 229
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-228 |
1.60e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 89.65 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADL-- 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD---SGEVLFDGKPLDIAARNRIGYLpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 -RGRYtgmvfqnpgaslnPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATA 159
Cdd:cd03269 78 eRGLY-------------PKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 160 LITSPRLIVADEPTTALDSITQRQIVDLSVSLVDeAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-247 |
2.20e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.46 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLAdl 80
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP---QSGTVFLGDKPISMLSSRQLA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 rgRYTGMVFQNP----GASLNPVLPVGRQVELPL--RLHydltrSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRV 154
Cdd:PRK11231 76 --RRLALLPQHHltpeGITVRELVAYGRSPWLSLwgRLS-----AEDNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGetaaml 234
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG------ 220
|
250
....*....|...
gi 1566271202 235 aAPQDERTARLVR 247
Cdd:PRK11231 221 -TPEEVMTPGLLR 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-239 |
2.57e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.07 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLlppDVTVAGSVMLGGSEVigaaDRTLAdl 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL---EHQTSGHIRFHGTDV----SRLHA-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTGMVFQNpgASLNPVLPVGRQVELPLRLhydLTRSERV------ERVNAMLAKVGLpADVAAKFPHELSGGQRQRV 154
Cdd:PRK10851 72 RDRKVGFVFQH--YALFRHMTVFDNIAFGLTV---LPRRERPnaaaikAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGetaaml 234
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG------ 219
|
....*
gi 1566271202 235 aAPQD 239
Cdd:PRK10851 220 -TPDQ 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-237 |
2.72e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 89.52 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadrTLADLRGR- 83
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGKILLDGQDI------TKLPMHKRa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 YTGMVFQNPGASLNPVLPVGRQVELPLRLHYDlTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITS 163
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 164 PRLIVADEPTTALDSIT----QRQIVDLSvslvdEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAvqdiQKIIKILK-----DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-237 |
4.46e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.83 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLadl 80
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT---AGTVLVAGDDVEALSARAA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 rGRYTGMVFQNPGASLN----PVLPVGRQvelPLRLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGI 156
Cdd:PRK09536 76 -SRRVASVPQDTSLSFEfdvrQVVEMGRT---PHRSRFDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 157 ATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFItHDFSVLTRATTRCVVLDEGSVVETGETAAMLAA 236
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
.
gi 1566271202 237 P 237
Cdd:PRK09536 230 D 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-236 |
4.71e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 92.58 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLppDVTvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQ----- 90
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY--DVT-SGRILIDGQDI---RDVTQASLR-AAIGIVPQdtvlf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 91 -----------NPGASLNPVLPVGRQVelplRLH---------YDLTRSERvervnamlakvGLpadvaakfphELSGGQ 150
Cdd:COG5265 445 ndtiayniaygRPDASEEEVEAAARAA----QIHdfieslpdgYDTRVGER-----------GL----------KLSGGE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 151 RQRVGIATALITSPRLIVADEPTTALDSITQRQIVD--LSVSlvdeAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETG 228
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAalREVA----RGRTTLVIAHRLSTIVDA-DEILVLEAGRIVERG 574
|
....*...
gi 1566271202 229 ETAAMLAA 236
Cdd:COG5265 575 THAELLAQ 582
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-236 |
5.72e-21 |
|
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: 88.75 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 23 LSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEvigaadrtlADLRGRYTGMVFQNPGASLNPVLPV 102
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPP---AKGTVKVAGAS---------PGKGWRHIGYVPQRHEFAWDFPISV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 103 GRQVELPLRLHYDLTRSERVE---RVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSI 179
Cdd:TIGR03771 69 AHTVMSGRTGHIGWLRRPCVAdfaAVRDALRRVGL-TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 180 TQRQIVDLSVSLVdEAGASMLFITHDFSVLTRATTRcVVLDEGSVVETGETAAMLAA 236
Cdd:TIGR03771 148 TQELLTELFIELA-GAGTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQLQDP 202
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-228 |
8.95e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.02 E-value: 8.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRGRyTGMVFQNPG 93
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ---RGRVKVMGREV---NAENEKWVRSK-VGLVFQDPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLNPVlPVGRQVEL-PLRLhyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:PRK13647 90 DQVFSS-TVWDDVAFgPVNM--GLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 173 TTALDSITQRQIVDLSVSLvDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-228 |
1.20e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.20 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLlpPDVTV-AGSVMLGGSEVIGAA--DRTLADLr 81
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKYEVtSGSILLDGEDILELSpdERARAGI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 82 grytGMVFQNPgaslnpvlpvgrqVELP-------LRLHYDLTRSERV------ERVNAMLAKVGLPADVAAKFPHE-LS 147
Cdd:COG0396 80 ----FLAFQYP-------------VEIPgvsvsnfLRTALNARRGEELsareflKLLKEKMKELGLDEDFLDRYVNEgFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 148 GGQRQRVGIATALITSPRLIVADEPTTALDsITQRQIVDLSVSLVDEAGASMLFITH-----DFSVLTRAttrcVVLDEG 222
Cdd:COG0396 143 GGEKKRNEILQMLLLEPKLAILDETDSGLD-IDALRIVAEGVNKLRSPDRGILIITHyqrilDYIKPDFV----HVLVDG 217
|
....*.
gi 1566271202 223 SVVETG 228
Cdd:COG0396 218 RIVKSG 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-228 |
1.98e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 87.39 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLrgrytGMVF-QNPG 93
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT---SGEVRVAGLVPWKRRKKFLRRI-----GVVFgQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLNpvLPVGRQVELpLRLHYDLTRSE---RVERVNAMLaKVGLPADVAAKfphELSGGQRQRVGIATALITSPRLIVAD 170
Cdd:cd03267 106 LWWD--LPVIDSFYL-LAAIYDLPPARfkkRLDELSELL-DLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 171 EPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-228 |
2.81e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.49 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGsEVIGAADRTladlrgRYTGMVFQNpga 94
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNG-MPIDAKEMR------AISAYVQQD--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 SLN-PVLPVGRQ--VELPLRLHYDLTRSERVERVNAMLAKVGL----------PADVAAkfpheLSGGQRQRVGIATALI 161
Cdd:TIGR00955 108 DLFiPTLTVREHlmFQAHLRMPRRVTKKEKRERVDEVLQALGLrkcantrigvPGRVKG-----LSGGERKRLAFASELL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-238 |
4.10e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 86.62 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadrtlADL 80
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGRIFLDGEDI--------THL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 ----RGRYtGM--------VFQNpgaslnpvLPVGRQVELPLRLHYdLTRSERVERVNAMLAKVGLpADVAAKFPHELSG 148
Cdd:COG1137 71 pmhkRARL-GIgylpqeasIFRK--------LTVEDNILAVLELRK-LSKKEREERLEELLEEFGI-THLRKSKAYSLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 149 GQRQRVGIATALITSPRLIVADEPTTALDSIT----QRQIVDLSvslvdEAGASMLfIThDFSVltRAT----TRCVVLD 220
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEPFAGVDPIAvadiQKIIRHLK-----ERGIGVL-IT-DHNV--RETlgicDRAYIIS 210
|
250
....*....|....*...
gi 1566271202 221 EGSVVETGETAAMLAAPQ 238
Cdd:COG1137 211 EGKVLAEGTPEEILNNPL 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-228 |
4.31e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 85.06 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKE--IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadRTLADLRG 82
Cdd:cd03247 3 INNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ---QGEITLDGVPV-----SDLEKALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNPgaslnpvlpvgrqvelplrlH-YDLTrservervnaMLAKVGLPadvaakfpheLSGGQRQRVGIATALI 161
Cdd:cd03247 75 SLISVLNQRP--------------------YlFDTT----------LRNNLGRR----------FSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEagASMLFITHDFSVLTRAtTRCVVLDEGSVVETG 228
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-234 |
4.90e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.71 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGr 83
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS---SGEVRLNGRPLAAWSPWELARRRA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 ytgmvfqnpgaslnpVLPVGRQVELPL---------RLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRV 154
Cdd:COG4559 79 ---------------VLPQHSSLAFPFtveevvalgRAPHGSSAAQDRQIVREALALVGL-AHLAGRSYQTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALI-------TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVET 227
Cdd:COG4559 143 QLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQ 221
|
....*..
gi 1566271202 228 GETAAML 234
Cdd:COG4559 222 GTPEEVL 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-222 |
6.34e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 83.65 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGaadrtladlrg 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD---EGIVTWGSTVKIG----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 rytgmvfqnpgaslnpvlpvgrqvelplrlhYdltrservervnamlakvglpadvaakFPHeLSGGQRQRVGIATALIT 162
Cdd:cd03221 67 -------------------------------Y---------------------------FEQ-LSGGEKMRLALAKLLLE 87
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLsvsLVDEAGAsMLFITHDFSVLTRATTRCVVLDEG 222
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEA---LKEYPGT-VILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-236 |
6.84e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.17 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTladlRG 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD---AGSISLCGEPVPSRARHA----RQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RyTGMV--FQNpgasLNPVLPVgRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFpHELSGGQRQRVGIATAL 160
Cdd:PRK13537 81 R-VGVVpqFDN----LDPDFTV-RENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 161 ITSPRLIVADEPTTALDSITQRQIVDLSVSLVdEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAA 236
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-228 |
2.02e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.73 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLlpPDVTVA-GSVMLGGSEVIGAA--DRTLADLr 81
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTeGEILFKGEDITDLPpeERARLGI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 82 grytGMVFQNPgaslnpvlpvgrqVELP-LRLHyDLTRServerVNamlakVGlpadvaakfpheLSGGQRQRVGIATAL 160
Cdd:cd03217 80 ----FLAFQYP-------------PEIPgVKNA-DFLRY-----VN-----EG------------FSGGEKKRNEILQLL 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 161 ITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITH-----DFSVLTRATtrcvVLDEGSVVETG 228
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHyqrllDYIKPDRVH----VLYDGRIVKSG 187
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-204 |
2.10e-19 |
|
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: 83.75 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAI------GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdVTVAGSVMLGGSevigaaD 74
Cdd:cd03213 2 VTLSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTG-LGVSGEVLINGR------P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 75 RTLADLRGRYtGMVFQNpgaslnpvlpvgrqvelpLRLHYDLTRSERVervnamlakvglpaDVAAKFpHELSGGQRQRV 154
Cdd:cd03213 75 LDKRSFRKII-GYVPQD------------------DILHPTLTVRETL--------------MFAAKL-RGLSGGERKRV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITH 204
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIH 169
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-219 |
4.19e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.67 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMlggseviGAADRTLADLRGRytgmvfqnp 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPT---SGTVR-------RAGGARVAYVPQR--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gASLNPVLP--VGRQVEL----PLRLHYDLTRSERVeRVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRL 166
Cdd:NF040873 64 -SEVPDSLPltVRDLVAMgrwaRRGLWRRLTRDDRA-AVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 167 IVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRAtTRCVVL 219
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRA-DPCVLL 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-246 |
4.36e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.14 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKS----MIAramlGLLPPDvtvAGSVMLGGseVIGAADRTlaDLRGRYtGMVF- 89
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSttikMLT----GILVPT---SGEVRVLG--YVPFKRRK--EFARRI-GVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 90 ---QnpgasLNPVLPVGRQVELpLRLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRL 166
Cdd:COG4586 103 qrsQ-----LWWDLPAIDSFRL-LKAIYRIPDAEYKKRLDELVELLDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 167 IVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLV 246
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLE 255
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-234 |
6.25e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 6.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVtvagsvmlGGSEVIGAADRTLADL 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA--------GKITVLGVPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTGMV--FQNpgasLNPVLPVgRQVELPLRLHYDLTRSERVERVNAML--AKVGLPADVAAKfphELSGGQRQRVGI 156
Cdd:PRK13536 112 ARARIGVVpqFDN----LDLEFTV-RENLLVFGRYFGMSTREIEAVIPSLLefARLESKADARVS---DLSGGMKRRLTL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 157 ATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAML 234
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-228 |
6.37e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLADLRGRYTGMVFQNPGASL--NP 98
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQP---TEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLfeET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 99 VL---PVGRQvelplrlHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTA 175
Cdd:PRK13643 102 VLkdvAFGPQ-------NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 176 LDSITQRQIVDLSVSlVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:PRK13643 175 LDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-234 |
1.19e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.82 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKS----MIARamlgLLPPDvtvAGSVMLGGSEVIGAAD---- 74
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKStllsMISR----LLPPD---SGEVLVDGLDVATTPSrela 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 75 RTLADLRgrytgmvfQNPgaSLNPVLPV-------------GRqvelplrlhydLTRSERvERVNAMLAKVGLpADVAAK 141
Cdd:COG4604 75 KRLAILR--------QEN--HINSRLTVrelvafgrfpyskGR-----------LTAEDR-EIIDEAIAYLDL-EDLADR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 142 FPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDE 221
Cdd:COG4604 132 YLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKD 211
|
250
....*....|...
gi 1566271202 222 GSVVETGETAAML 234
Cdd:COG4604 212 GRVVAQGTPEEII 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-228 |
1.22e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.54 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLAdlrgRYTGMVFQNPga 94
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT---GGQVLLDGVPLVQYDHHYLH----RQVALVGQEP-- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 slnpVLPVGRQVElplRLHYDLTRSERVERVNAmlAKVGLPADVAAKFPH-----------ELSGGQRQRVGIATALITS 163
Cdd:TIGR00958 565 ----VLFSGSVRE---NIAYGLTDTPDEEIMAA--AKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVDLSVSlvdeAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETG 228
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESRSR----ASRTVLLIAHRLSTVERA-DQILVLKKGSVVEMG 695
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
11-236 |
1.46e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 85.09 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 11 AIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLadlrGRYTGMVFQ 90
Cdd:TIGR01842 327 PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP---TSGSVRLDGADLKQWDRETF----GKHIGYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 91 npGASLNPvlpvGRQVELPLRLHYDLTRSERVERvnAMLAKVglpADVAAKFPH-----------ELSGGQRQRVGIATA 159
Cdd:TIGR01842 400 --DVELFP----GTVAENIARFGENADPEKIIEA--AKLAGV---HELILRLPDgydtvigpggaTLSGGQRQRIALARA 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 160 LITSPRLIVADEPTTALDSITQRQIVDLSVSLvDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETGETAAMLAA 236
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-249 |
1.70e-18 |
|
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: 82.20 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRGRYtGMVFQNP--- 92
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPT---SGEILLDGVDI---RDLNLRWLRSQI-GLVSQEPvlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GASLNPVLPVGRqvelplrlhYDLTRSErVERVnamlAKVGLPADVAAKFPH-----------ELSGGQRQRVGIATALI 161
Cdd:cd03249 90 DGTIAENIRYGK---------PDATDEE-VEEA----AKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDlsvsLVDEA--GASMLFITHDFSVLTRAtTRCVVLDEGSVVETGETAAMLAapQD 239
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQE----ALDRAmkGRTTIVIAHRLSTIRNA-DLIAVLQNGQVVEQGTHDELMA--QK 228
|
250
....*....|
gi 1566271202 240 ERTARLVRAA 249
Cdd:cd03249 229 GVYAKLVKAQ 238
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-228 |
2.21e-18 |
|
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: 81.65 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLrgrytGMVFQNPGasLN 97
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD---AGFATVDGFDVVKEPAEARRRL-----GFVSDSTG--LY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALD 177
Cdd:cd03266 91 DRLTARENLEYFAGLY-GLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 178 SITQRQIVDLsVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03266 169 VMATRALREF-IRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-227 |
2.25e-18 |
|
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: 80.17 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRG 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD---SGEILVDGKEV---SFASPRDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQnpgaslnpvlpvgrqvelplrlhydltrservervnamlakvglpadvaakfpheLSGGQRQRVGIATALIT 162
Cdd:cd03216 75 AGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVET 227
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-212 |
2.51e-18 |
|
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: 84.65 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAadrtLADLRGRYTGMVFQNP 92
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIAVNGVPLADA----DADSWRDQIAWVPQHP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 G---ASLNPVLPVGRQVELPLRLhydltrSERVERVNAMLAKVGLPADVAAKF---PHELSGGQRQRVGIATALITSPRL 166
Cdd:TIGR02857 406 FlfaGTIAENIRLARPDASDAEI------REALERAGLDEFVAALPQGLDTPIgegGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1566271202 167 IVADEPTTALDSITQRQIVDLSVSLVDeaGASMLFITHDFSVLTRA 212
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA 523
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-233 |
2.97e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 19 HGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRGRYTGMVFQNPgaSLNP 98
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD---SGEILLDGEPV---RFRSPRDAQAAGIAIIHQEL--NLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 99 VLPV------GRQVELPLRLHYDLTRservERVNAMLAKVGLPADVAAKFpHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:COG1129 93 NLSVaeniflGREPRRGGLIDWRAMR----RRARELLARLGLDIDPDTPV-GDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 173 TTALdsiTQRQIVDLsVSLVDE---AGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAM 233
Cdd:COG1129 168 TASL---TEREVERL-FRIIRRlkaQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-241 |
3.11e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.12 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRG 82
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD---HGEILFDGENIPAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTgMVFQNpGAsLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPAdvAAKF-PHELSGGQRQRVGIATALI 161
Cdd:PRK11831 85 RMS-MLFQS-GA-LFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRG--AAKLmPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDF-SVLTRATTRCVVLDEGSVVETgeTAAMLAAPQDE 240
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHG--SAQALQANPDP 237
|
.
gi 1566271202 241 R 241
Cdd:PRK11831 238 R 238
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-223 |
3.40e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.09 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 2 GVDIRDLRIAI-GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtvagsvmlggsevigaadrtladl 80
Cdd:COG4178 362 ALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPY-------------------------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 rgrYTGMVFQNPGASL-----NPVLPVGRqvelpLR--LHY---DLTRSErvERVNAMLAKVGLPA-----DVAAKFPHE 145
Cdd:COG4178 416 ---GSGRIARPAGARVlflpqRPYLPLGT-----LReaLLYpatAEAFSD--AELREALEAVGLGHlaerlDEEADWDQV 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 146 LSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLsvsLVDE-AGASMLFITHDfSVLTRATTRCVVLDEGS 223
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREElPGTTVISVGHR-STLAAFHDRVLELTGDG 560
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
9-247 |
6.41e-18 |
|
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: 83.47 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 9 RIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVigaADRTLADLRgRYTGMV 88
Cdd:TIGR03797 460 RYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETP---ESGSVFYDGQDL---AGLDVQAVR-RQLGVV 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 89 FQN----PGASLNpvlpvgrqvelplrlhyDLTRSERVERVNAMLA--KVGLPADVAAkFP---H--------ELSGGQR 151
Cdd:TIGR03797 533 LQNgrlmSGSIFE-----------------NIAGGAPLTLDEAWEAarMAGLAEDIRA-MPmgmHtvisegggTLSGGQR 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 152 QRVGIATALITSPRLIVADEPTTALDSITQRqIVdlSVSLvDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETGETA 231
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSALDNRTQA-IV--SESL-ERLKVTRIVIAHRLSTIRNA-DRIYVLDAGRVVQQGTYD 669
|
250
....*....|....*.
gi 1566271202 232 AMLAAPQdeRTARLVR 247
Cdd:TIGR03797 670 ELMAREG--LFAQLAR 683
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-228 |
6.77e-18 |
|
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: 80.23 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 8 LRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEV--IGaadrtLADLRGRYT 85
Cdd:cd03244 10 LRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL---SSGSILIDGVDIskIG-----LHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 86 gMVFQNPgaslnpVLPVG--RQVELPLRLHYDltrservERVNAMLAKVGLPADVAAKFPHE----------LSGGQRQR 153
Cdd:cd03244 82 -IIPQDP------VLFSGtiRSNLDPFGEYSD-------EELWQALERVGLKEFVESLPGGLdtvveeggenLSVGQRQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 154 VGIATALITSPRLIVADEPTTALDSITQRQIvdlsVSLVDE--AGASMLFITHdfsvltRATT-----RCVVLDEGSVVE 226
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALI----QKTIREafKDCTVLTIAH------RLDTiidsdRILVLDKGRVVE 217
|
..
gi 1566271202 227 TG 228
Cdd:cd03244 218 FD 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
7-241 |
6.98e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 6.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 7 DLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvagsvmlGGSEVIGAADRTLADLRGR-YT 85
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD---------AGNIIIDDEDISLLPLHARaRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 86 GMVFQNPGASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPR 165
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 166 LIVADEPTTALDSITQRQIVDLSVSLVDeAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDER 241
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-236 |
9.31e-18 |
|
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: 82.84 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQNP- 92
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD---SGQILLDGHDL---ADYTLASLR-RQVALVSQDVv 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 --GASLNPVLPVGRQVELPlrlhydltrSERVERV----NAMLAKVGLPADVAAKFPHE---LSGGQRQRVGIATALITS 163
Cdd:TIGR02203 417 lfNDTIANNIAYGRTEQAD---------RAEIERAlaaaYAQDFVDKLPLGLDTPIGENgvlLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVDLSVSLVDeaGASMLFITHDFSVLTRAtTRCVVLDEGSVVETGETAAMLAA 236
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKA-DRIVVMDDGRIVERGTHNELLAR 557
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-248 |
2.56e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.31 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 2 GVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAM--LGLLPPDVTVAGSVMLGGSEVIgaaDR--TL 77
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVEGRVEFFNQNIY---ERrvNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 78 ADLRgRYTGMVFQNPgaSLNPvLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPH---ELSGGQRQRV 154
Cdd:PRK14258 84 NRLR-RQVSMVHPKP--NLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsalDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDE-----GSVVETGE 229
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGL 239
|
250
....*....|....*....
gi 1566271202 230 TAAMLAAPQDERTARLVRA 248
Cdd:PRK14258 240 TKKIFNSPHDSRTREYVLS 258
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
17-247 |
3.50e-17 |
|
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: 81.14 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 17 IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGsevigaadRTLADL-RGRYTG---MVFQNp 92
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQP---WSGEILFDG--------IPREEIpREVLANsvaMVDQD- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gaslnpVLPVGRQVELPLRLhYDLTRSE-RVERV--NAMLAKV------GLPADVAakfphE----LSGGQRQRVGIATA 159
Cdd:TIGR03796 562 ------IFLFEGTVRDNLTL-WDPTIPDaDLVRAckDAAIHDVitsrpgGYDAELA-----EgganLSGGQRQRLEIARA 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 160 LITSPRLIVADEPTTALDSITQRQIVDlsvsLVDEAGASMLFITHDFSVLtRATTRCVVLDEGSVVETGETAAMLAapQD 239
Cdd:TIGR03796 630 LVRNPSILILDEATSALDPETEKIIDD----NLRRRGCTCIIVAHRLSTI-RDCDEIIVLERGKVVQRGTHEELWA--VG 702
|
....*...
gi 1566271202 240 ERTARLVR 247
Cdd:TIGR03796 703 GAYARLIR 710
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-246 |
4.99e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.67 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 6 RDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAM--LGLLPPDVTVAGSVMLGGSEvIGAADRTLADLRGR 83
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFRVEGKVTFHGKN-LYAPDVDPVEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 yTGMVFQNP-------------GASLNpvlpvGRQVELPLRLHYDLTRSERVERVNAMLAKVGLpadvaakfphELSGGQ 150
Cdd:PRK14243 93 -IGMVFQKPnpfpksiydniayGARIN-----GYKGDMDELVERSLRQAALWDEVKDKLKQSGL----------SLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 151 RQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEagASMLFITHDFSVLTRATTRC----VVLDE----- 221
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTaffnVELTEgggry 234
|
250 260
....*....|....*....|....*
gi 1566271202 222 GSVVETGETAAMLAAPQDERTARLV 246
Cdd:PRK14243 235 GYLVEFDRTEKIFNSPQQQATRDYV 259
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-228 |
5.10e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.49 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLADLrgry 84
Cdd:PRK11300 8 VSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKP---TGGTILLRGQHIEGLPGHQIARM---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 tGMV--FQNP------GASLNPVLPVGRQVELPLrLH-------YDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGG 149
Cdd:PRK11300 81 -GVVrtFQHVrlfremTVIENLLVAQHQQLKTGL-FSgllktpaFRRAESEALDRAATWLERVGL-LEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 150 QRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-228 |
5.17e-17 |
|
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: 78.04 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRGRYtGMVFQNP 92
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ---KGQILIDGIDI---RDISRKSLRSMI-GVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GaslnpVLPvgRQVELPLRLHYDLTRSERVERvnamLAKVGLPADVAAKFP-----------HELSGGQRQRVGIATALI 161
Cdd:cd03254 87 F-----LFS--GTIMENIRLGRPNATDEEVIE----AAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVDeaGASMLFITHDFSVLTRATtRCVVLDEGSVVETG 228
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNAD-KILVLDDGKIIEEG 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
33-228 |
6.21e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 33 LIGSSGSGKSMIARAMLGLLPP---DVTV----AGSVMLGGSEVIGAADRTLAD---LRgRYTGMVFQNPGASLnpvlpV 102
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSkygTIQVgdiyIGDKKNNHELITNPYSKKIKNfkeLR-RRVSMVFQFPEYQL-----F 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 103 GRQVEL-----PLRLhyDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALD 177
Cdd:PRK13631 131 KDTIEKdimfgPVAL--GVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 178 SITQRQIVDLsVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:PRK13631 209 PKGEHEMMQL-ILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-231 |
7.65e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 20 GVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRGRYTGMVFQNPgaSLNPV 99
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPD---SGEILIDGKPV---RIRSPRDAIALGIGMVHQHF--MLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 100 LPVgrqVE-----LPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKfPHELSGGQRQRVGIATALITSPRLIVADEPTT 174
Cdd:COG3845 95 LTV---AEnivlgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAK-VEDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 175 ALdsiTQRQIVDLSV---SLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETA 231
Cdd:COG3845 171 VL---TPQEADELFEilrRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-228 |
1.50e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 76.42 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPD---VTVAGSVmlggSEVIGAadrtladlrgrytgmvf 89
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDsgtVTVRGRV----SSLLGL----------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 90 qnpGASLNPVLPVGRQVELPLRLhYDLTRSERVERVNAMLAKVGLPADVAAKFPHeLSGGQRQRVGIATALITSPRLIVA 169
Cdd:cd03220 92 ---GGGFNPELTGRENIYLNGRL-LGLSRKEIDEKIDEIIEFSELGDFIDLPVKT-YSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 170 DEPTTALDSITQRQIVDLSVSLVdEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-229 |
2.13e-16 |
|
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: 78.69 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGL--LPPDvtvAGSVM--LGGSEVIGAADRTLA 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPT---SGRIIyhVALCEKCGYVERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 DLR------GRYTGMV--FQNPGASLNPvlPVGRQVELPLRLHYDLTRSERV-ERVNAMLAKVGLPADVA---------- 139
Cdd:TIGR03269 78 VGEpcpvcgGTLEPEEvdFWNLSDKLRR--RIRKRIAIMLQRTFALYGDDTVlDNVLEALEEIGYEGKEAvgravdliem 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 140 AKFPH-------ELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRA 212
Cdd:TIGR03269 156 VQLSHrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250
....*....|....*..
gi 1566271202 213 TTRCVVLDEGSVVETGE 229
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGT 252
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
16-245 |
4.17e-16 |
|
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: 78.25 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEViGAADRtlADLRgRYTGMVFQ----- 90
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQ---HGQVLVDGVDL-AIADP--AWLR-RQMGVVLQenvlf 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 91 -----------NPGASLNPVLPVGR-----QVELPLRLHYDltrSERVERVNAmlakvglpadvaakfpheLSGGQRQRV 154
Cdd:TIGR01846 544 srsirdnialcNPGAPFEHVIHAAKlagahDFISELPQGYN---TEVGEKGAN------------------LSGGQRQRI 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 155 GIATALITSPRLIVADEPTTALD----SITQRQIVDLSvslvdeAGASMLFITHDFSVLtRATTRCVVLDEGSVVETGET 230
Cdd:TIGR01846 603 AIARALVGNPRILIFDEATSALDyeseALIMRNMREIC------RGRTVIIIAHRLSTV-RACDRIIVLEKGQIAESGRH 675
|
250
....*....|....*
gi 1566271202 231 AAMLAapQDERTARL 245
Cdd:TIGR01846 676 EELLA--LQGLYARL 688
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-226 |
4.70e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.19 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 2 GVDIRDLRIAIGGK-EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLlpPDVTvAGSVMLGGSEV--IGAADRTLA 78
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL--ERIT-SGEIWIGGRVVneLEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 dlrgrytgMVFQNpgASLNPVLPVGRQVELPLRLHyDLTRSERVERVNAMLAKVGLPADVAAKfPHELSGGQRQRVGIAT 158
Cdd:PRK11650 80 --------MVFQN--YALYPHMSVRENMAYGLKIR-GMPKAEIEERVAEAARILELEPLLDRK-PRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 159 ALITSPRLIVADEPTTALDS---ITQR-QIVDLSVSLvdeaGASMLFITHDfsvLTRATT---RCVVLDEGsVVE 226
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAklrVQMRlEIQRLHRRL----KTTSLYVTHD---QVEAMTladRVVVMNGG-VAE 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-241 |
8.10e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRI-AIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPpdvtVAGSVMLGGSEVigaADRTLADLR 81
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP----YQGSLKINGIEL---RELDPESWR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 82 gRYTGMVFQNP---GASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLP-ADVAAKfpheLSGGQRQRVGIA 157
Cdd:PRK11174 423 -KHLSWVGQNPqlpHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPiGDQAAG----LSVGQAQRLALA 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 158 TALITSPRLIVADEPTTALDSITQRQIVDlsvSLVDEA-GASMLFITHDFSVLTRATTrCVVLDEGSVVETG-------- 228
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHSEQLVMQ---ALNAASrRQTTLMVTHQLEDLAQWDQ-IWVMQDGQIVQQGdyaelsqa 573
|
250
....*....|....*
gi 1566271202 229 --ETAAMLAAPQDER 241
Cdd:PRK11174 574 ggLFATLLAHRQEEI 588
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-236 |
9.42e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.07 E-value: 9.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAI-GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLAdlr 81
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT---EGEIRLDGRPLSSLSHSVLR--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 82 gRYTGMVFQNP---GASLNPVLPVGRQVelplrlhydltrSErvERVNAMLAKVGLpADVAAKFP-----------HELS 147
Cdd:PRK10790 415 -QGVAMVQQDPvvlADTFLANVTLGRDI------------SE--EQVWQALETVQL-AELARSLPdglytplgeqgNNLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 148 GGQRQRVGIATALITSPRLIVADEPTTALDSITQrQIVDLSVSLVDEAgASMLFITHDFSVLTRATTrCVVLDEGSVVET 227
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSGTE-QAIQQALAAVREH-TTLVVIAHRLSTIVEADT-ILVLHRGQAVEQ 555
|
....*....
gi 1566271202 228 GETAAMLAA 236
Cdd:PRK10790 556 GTHQQLLAA 564
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-204 |
1.18e-15 |
|
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: 73.55 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 6 RDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadRTLADLRGRYT 85
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPD---SGEVRWNGTPL-----AEQRDEPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 86 GMVFQNPGasLNPVLPVGRQVELPLRLHYDLTRServerVNAMLAKVGLP--ADVAAkfpHELSGGQRQRVGIATALITS 163
Cdd:TIGR01189 76 LYLGHLPG--LKPELSALENLHFWAAIHGGAQRT-----IEDALAAVGLTgfEDLPA---AQLSAGQQRRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1566271202 164 PRLIVADEPTTALDsitqRQIVDLSVSLVDE---AGASMLFITH 204
Cdd:TIGR01189 146 RPLWILDEPTTALD----KAGVALLAGLLRAhlaRGGIVLLTTH 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-234 |
1.54e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.11 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 20 GVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQNpgASLNPV 99
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG----QGEILLNGRPL---SDWSAAELA-RHRAYLSQQ--QSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 100 LPVGrQVelpLRLHY-DLTRSERVERVNAMLA-KVGLpADVAAKFPHELSGGQRQRVGIATALIT-------SPRLIVAD 170
Cdd:COG4138 84 MPVF-QY---LALHQpAGASSEAVEQLLAQLAeALGL-EDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 171 EPTTALDsITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAML 234
Cdd:COG4138 159 EPMNSLD-VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-237 |
1.69e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARaMLGLLPPdvTVAGSVMLGGSEVIGAADRTLADLRGRY 84
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQP--PSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 TGMVFQNPGASLNPVLPVGRqvelpLRLHYDLTR--SERVERVNAMLAKVGLPAdVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGR-----YPWHGALGRfgAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAP 237
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-265 |
1.83e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.15 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSmiarAMLGLL----PPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQNPG 93
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKS----TLINLLqrvfDPQ---SGRILIDGTDI---RTVTRASLR-RNIAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ---ASLNPVLPVGRQVELPLRLHydlTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVAD 170
Cdd:PRK13657 420 lfnRSIEDNIRVGRPDATDEEMR---AAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 171 EPTTALDSITQRQIVDlsvsLVDEA--GASMLFITHDFSVLtRATTRCVVLDEGSVVETGETAAMLAapQDERTARLVRA 248
Cdd:PRK13657 497 EATSALDVETEAKVKA----ALDELmkGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFDELVA--RGGRFAALLRA 569
|
250
....*....|....*..
gi 1566271202 249 ARTLTLRASREGADRET 265
Cdd:PRK13657 570 QGMLQEDERRKQPAAEG 586
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-235 |
2.51e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsEVIGAADRTLADLRgRYTGMVFQNPGA 94
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ---KGAVLWQG-KPLDYSKRGLLALR-QQVATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 SLNpVLPVGRQVELPLRlHYDLTRSERVERVNAMLAKVGlpadvAAKFPHE----LSGGQRQRVGIATALITSPRLIVAD 170
Cdd:PRK13638 89 QIF-YTDIDSDIAFSLR-NLGVPEAEITRRVDEALTLVD-----AQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 171 EPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLA 235
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-235 |
2.89e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEI--VHGVDLSIGDGERVGLIGSSGSGKSMIAramlGLLPP--DVTvAGSVMLGGSEVigaADRTLA 78
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIA----NLLTRfyDID-EGEILLDGHDL---RDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 DLRgrytgmvfqnpgaslNPVLPVGRQVEL-----------PLRLHYdlTRsERVERVnamlAKVGLPADVAAKFPH--- 144
Cdd:PRK11176 414 SLR---------------NQVALVSQNVHLfndtianniayARTEQY--SR-EQIEEA----ARMAYAMDFINKMDNgld 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 145 --------ELSGGQRQRVGIATALI-TSPRLIVaDEPTTALDSITQRQIvdlsVSLVDE--AGASMLFITHDFSVLTRAt 213
Cdd:PRK11176 472 tvigengvLLSGGQRQRIAIARALLrDSPILIL-DEATSALDTESERAI----QAALDElqKNRTSLVIAHRLSTIEKA- 545
|
250 260
....*....|....*....|..
gi 1566271202 214 TRCVVLDEGSVVETGETAAMLA 235
Cdd:PRK11176 546 DEILVVEDGEIVERGTHAELLA 567
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-228 |
4.70e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 72.30 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGSEVigaadrtLADLRGRYTGMVFQNpgA 94
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPR-------KPDQFQKCVAYVRQD--D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 SLNPVLPVGRQVE--LPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:cd03234 91 ILLPGLTVRETLTytAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-187 |
4.95e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGseviGAADRTLADL 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP---AAGTIKLDG----GDIDDPDVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTGmvFQNPgasLNPVLPVGRQVELPLRLhydltRSERVERVNAMLAKVGLP--ADVAAKfphELSGGQRQRVGIAT 158
Cdd:PRK13539 74 ACHYLG--HRNA---MKPALTVAENLEFWAAF-----LGGEELDIAAALEAVGLAplAHLPFG---YLSAGQKRRVALAR 140
|
170 180
....*....|....*....|....*....
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQIVDL 187
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAVALFAEL 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-233 |
5.01e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.86 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvTVAGSVMLGGSEVIGAADRTLADlrgryTGMVFQNP 92
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG-TWDGEIYWSGSPLKASNIRDTER-----AGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GASLNPVLPV------GRQVELP-LRLHYDltrsERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPR 165
Cdd:TIGR02633 86 ELTLVPELSVaeniflGNEITLPgGRMAYN----AMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 166 LIVADEPTTALDSITQRQIVDLSVSLvDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAM 233
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-225 |
5.52e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 22 DLSIGDGERVGLIGSSGSGKSMIARAMLGLLP---------PDVTVA-----------GSVMLGGSEVIGAadrtLADLR 81
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLlddgriiyeQDLIVArlqqdpprnveGTVYDFVAEGIEE----QAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 82 GRY---TGMVFQNPGAS-LNPVLPVGRQVElplrlHYDLTRSErvERVNAMLAKVGLPADVAAKfphELSGGQRQRVGIA 157
Cdd:PRK11147 99 KRYhdiSHLVETDPSEKnLNELAKLQEQLD-----HHNLWQLE--NRINEVLAQLGLDPDAALS---SLSGGWLRKAALG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 158 TALITSPRLIVADEPTTALDSITqrqIVDLSVSLVDEAGaSMLFITHDFSVLTRATTRCVVLDEGSVV 225
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-205 |
9.42e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVtvaGSVMLGGSEVIgaadrTLADLRGR- 83
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS---GTLLFEGEDIS-----TLKPEIYRq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 YTGMVFQNPgaslnpVLpVGRQVELPLRLHYDLtRSERVE--RVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALI 161
Cdd:PRK10247 82 QVSYCAQTP------TL-FGDTVYDNLIFPWQI-RNQQPDpaIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHD 205
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-225 |
1.13e-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: 70.75 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 12 IGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGSEVIGAADRTLADLrgrytgmVFQN 91
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEI-------IYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 92 PGASLNPVLPVGRQVELPLRLhydltrserveRVNAMLAKVglpadvaakfphelSGGQRQRVGIATALITSPRLIVADE 171
Cdd:cd03233 90 EEDVHFPTLTVRETLDFALRC-----------KGNEFVRGI--------------SGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 172 PTTALDSITQRQIVDLSVSLVDEAGASMLF--------ITHDFSvltrattRCVVLDEGSVV 225
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLKTTTFVslyqasdeIYDLFD-------KVLVLYEGRQI 199
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-236 |
1.98e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.44 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRD--LRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIAramLGLLPPDVTVAGSVMLGGsevIGAADRTLADL 80
Cdd:TIGR00957 1285 VEFRNycLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDG---LNIAKIGLHDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRYTgMVFQNPgaslnpVLPVGRqvelpLRLHYDLTRSERVERVNAMLAKVGLPADVAA---KFPHE-------LSGGQ 150
Cdd:TIGR00957 1359 RFKIT-IIPQDP------VLFSGS-----LRMNLDPFSQYSDEEVWWALELAHLKTFVSAlpdKLDHEcaeggenLSVGQ 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 151 RQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEagASMLFITHDFSVLTRaTTRCVVLDEGSVVETGET 230
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMD-YTRVIVLDKGEVAEFGAP 1503
|
....*.
gi 1566271202 231 AAMLAA 236
Cdd:TIGR00957 1504 SNLLQQ 1509
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-188 |
2.00e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKS--MiarAML-GLLPPDvtvAGSVMLGGSEViGAADRtlaDLRGR--YTGMVFqnp 92
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSttM---KMLtGLLPAS---EGEAWLFGQPV-DAGDI---ATRRRvgYMSQAF--- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gaSLNPVLPVGRQVELPLRLhYDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:NF033858 349 --SLYGELTVRQNLELHARL-FHLPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180
....*....|....*....|
gi 1566271202 173 TTALDSITQ----RQIVDLS 188
Cdd:NF033858 425 TSGVDPVARdmfwRLLIELS 444
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-204 |
2.68e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 69.83 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 6 RDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsevigaadRTLADLRGRYT 85
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL---AGRVLLNG--------GPLDFQRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 86 -GMVFQNPGASLNPVLpvgrQVELPLRLHYDLTRSERVERVnamLAKVGLPA--DVAAkfpHELSGGQRQRVGIATALIT 162
Cdd:cd03231 73 rGLLYLGHAPGIKTTL----SVLENLRFWHADHSDEQVEEA---LARVGLNGfeDRPV---AQLSAGQQRRVALARLLLS 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVdEAGASMLFITH 204
Cdd:cd03231 143 GRPLWILDEPTTALDKAGVARFAEAMAGHC-ARGGMVVLTTH 183
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-224 |
2.74e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 69.38 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGgkeiVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRG 82
Cdd:cd03215 5 LEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA---SGEITLDGKPV---TRRSPRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RytGMVFqnpgaslnpvLPVGRQVELplrLHYDLTRSErvervNAMLakvglpadvaakfPHELSGGQRQRVGIATALIT 162
Cdd:cd03215 75 A--GIAY----------VPEDRKREG---LVLDLSVAE-----NIAL-------------SSLLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSV 224
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-228 |
2.80e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 35 GSSGSGKSMIARAMLGLLPPDVtvaGSVMLGgsevigaaDRTLADLRG--------RYTGMVFQNpgASLNPVLPV-GRq 105
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQK---GRIVLN--------GRVLFDAEKgiclppekRRIGYVFQD--ARLFPHYKVrGN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 106 velplrLHYDLTRSERVE--RVNAMLAKVGLpadvAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQ 183
Cdd:PRK11144 97 ------LRYGMAKSMVAQfdKIVALLGIEPL----LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1566271202 184 IVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-205 |
2.93e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLadlrg 82
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVIKRNGKLRIGYVPQKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 rytgmvfqnpgaSLNPVLPVgrQVELPLRLHYDLTRSE---RVERVNAmlakvglpADVAAKFPHELSGGQRQRVGIATA 159
Cdd:PRK09544 77 ------------YLDTTLPL--TVNRFLRLRPGTKKEDilpALKRVQA--------GHLIDAPMQKLSGGETQRVLLARA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1566271202 160 LITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHD 205
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-205 |
3.56e-14 |
|
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: 72.01 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 2 GVDIRDLRIAIGGKEIV-HGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGsevIGAADRTLADL 80
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGEVTLDG---VPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 RGRyTGMVFQNP---GASLNPVLPVGRQvelplrlhyDLTRSErverVNAMLAKVGLpADVAAKFPH-----------EL 146
Cdd:TIGR02868 408 RRR-VSVCAQDAhlfDTTVRENLRLARP---------DATDEE----LWAALERVGL-ADWLRALPDgldtvlgeggaRL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 147 SGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIvdLSVSLVDEAGASMLFITHD 205
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADEL--LEDLLAALSGRTVVLITHH 529
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-223 |
8.30e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 8.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGllppdvTVAGSVMLGgseVIGAADRTLADLRGRY 84
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG------RIQGNNFTG---TILANNRKPTKQILKR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 TGMVFQNPgaSLNPVLPVGRQVELP--LRLHYDLTRSERVERVNAMLAKVGLP----ADVAAKFPHELSGGQRQRVGIAT 158
Cdd:PLN03211 142 TGFVTQDD--ILYPHLTVRETLVFCslLRLPKSLTKQEKILVAESVISELGLTkcenTIIGNSFIRGISGGERKRVSIAH 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAG---------ASMLFITHDfSVLTRATTRCVVLDEGS 223
Cdd:PLN03211 220 EMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKtivtsmhqpSSRVYQMFD-SVLVLSEGRCLFFGKGS 292
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-245 |
1.31e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.62 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 19 HGVDLSIGDGERVGLIGSSGSGKS----MIARAMlgllppDVTvAGSVMLGGSEVigaADRTLADLRGRYT--------- 85
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKStllqLLTRAW------DPQ-QGEILLNGQPI---ADYSEAALRQAISvvsqrvhlf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 86 ------GMVFQNPGASLNPVLPVGRQVELPlrlhyDLTRSErvERVNAMLAKVGLPadvaakfpheLSGGQRQRVGIATA 159
Cdd:PRK11160 427 satlrdNLLLAAPNASDEALIEVLQQVGLE-----KLLEDD--KGLNAWLGEGGRQ----------LSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 160 LITSPRLIVADEPTTALDSITQRQIVDLsvsLVDEA-GASMLFITHDFSVLTRaTTRCVVLDEGSVVETGETAAMLAapQ 238
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILEL---LAEHAqNKTVLMITHRLTGLEQ-FDRICVMDNGQIIEQGTHQELLA--Q 563
|
....*..
gi 1566271202 239 DERTARL 245
Cdd:PRK11160 564 QGRYYQL 570
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-228 |
8.67e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGllPPDVTV-AGSVMLGGSEVIGAADRTLADLrG 82
Cdd:CHL00131 9 EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYKIlEGDILFKGESILDLEPEERAHL-G 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGmvFQNPgaslnpvlpvgrqVELP-------LRLHYDLTRSER----------VERVNAMLAKVGLPADVAAKFPHE 145
Cdd:CHL00131 86 IFLA--FQYP-------------IEIPgvsnadfLRLAYNSKRKFQglpeldplefLEIINEKLKLVGMDPSFLSRNVNE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 146 -LSGGQRQRVGIATALITSPRLIVADEPTTALDsITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCV-VLDEGS 223
Cdd:CHL00131 151 gFSGGEKKRNEILQMALLDSELAILDETDSGLD-IDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVhVMQNGK 229
|
....*
gi 1566271202 224 VVETG 228
Cdd:CHL00131 230 IIKTG 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-235 |
1.12e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 20 GVDLSIGDGERVGLIGSSGSGKSmiarAMLGLlppdvtVAGSVML--GGSEVIGA--ADRT-LADLRGRYTGMVfQNPGA 94
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKS----SLLSL------IAGARKIqqGRVEVLGGdmADARhRRAVCPRIAYMP-QGLGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 SLNPVLPVGRQVELPLRLhYDLTRSERVERVNAMLAKVGLpadvaAKFPH----ELSGGQRQRVGIATALITSPRLIVAD 170
Cdd:NF033858 88 NLYPTLSVFENLDFFGRL-FGQDAAERRRRIDELLRATGL-----APFADrpagKLSGGMKQKLGLCCALIHDPDLLILD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 171 EPTTALDSITQRQIVDLsVSLVDEAGASMlfithdfSVLTrATT---------RCVVLDEGSVVETGETAAMLA 235
Cdd:NF033858 162 EPTTGVDPLSRRQFWEL-IDRIRAERPGM-------SVLV-ATAymeeaerfdWLVAMDAGRVLATGTPAELLA 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-224 |
1.14e-12 |
|
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: 65.96 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 17 IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLAdlrgRYTGMVFQNP---G 93
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ---GGQVLLDGKPISQYEHKYLH----SKVSLVGQEPvlfA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLN-------PVLPVGRQVELPLRLHYDltrserverVNAMLAKVGLPADVAAKfPHELSGGQRQRVGIATALITSPRL 166
Cdd:cd03248 102 RSLQdniayglQSCSFECVKEAAQKAHAH---------SFISELASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 167 IVADEPTTALDSITQRQIVDLSVSlvDEAGASMLFITHDFSVLTRAtTRCVVLDEGSV 224
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-236 |
2.73e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVmlggsevigaadrtlaDLRGRYTGMVfqNPGA 94
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT---SGRV----------------EVNGRVSALL--ELGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 SLNPvlpvgrqvelplrlhyDLTRSERVeRVNAMLAkvGLP-ADVAAKFPH-----EL-----------SGGQRQRVGIA 157
Cdd:COG1134 98 GFHP----------------ELTGRENI-YLNGRLL--GLSrKEIDEKFDEivefaELgdfidqpvktySSGMRARLAFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 158 TALITSPRLIVADEPTT---------ALDSITQRQivdlsvslvdEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETG 228
Cdd:COG1134 159 VATAVDPDILLVDEVLAvgdaafqkkCLARIRELR----------ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDG 228
|
....*...
gi 1566271202 229 ETAAMLAA 236
Cdd:COG1134 229 DPEEVIAA 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-228 |
2.91e-12 |
|
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: 64.36 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 16 EIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEvIGAADrtLADLRGRYTgMVFQnpgas 95
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE---EGKIEIDGID-ISTIP--LEDLRSSLT-IIPQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 96 lNPVLPVGrqvelPLRLHYDLTRSERVERVNAML--AKVGLpadvaakfphELSGGQRQRVGIATALITSPRLIVADEPT 173
Cdd:cd03369 90 -DPTLFSG-----TIRSNLDPFDEYSDEEIYGALrvSEGGL----------NLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 174 TALDSITQRQIvdlSVSLVDE-AGASMLFITHDFSVLTRAtTRCVVLDEGSVVETG 228
Cdd:cd03369 154 ASIDYATDALI---QKTIREEfTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
13-235 |
3.09e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGllPPDVTvAGSVMLGGSevigaadrtlaDLRGRYTGMVFQNP 92
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRAT-SGRIVFDGK-----------DITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GAslnpVLPVGRQVELPLRLHYDLTR----------SERVERVNAMLAKVglpADVAAKFPHELSGGQRQRVGIATALIT 162
Cdd:PRK11614 82 VA----IVPEGRRVFSRMTVEENLAMggffaerdqfQERIKWVYELFPRL---HERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDlSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLA 235
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFD-TIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-233 |
4.45e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVigAADRTLADLRgryTGMVFqnpgaslnpvL 100
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA---RGGRIMLNGKEI--NALSTAQRLA---RGLVY----------L 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 101 PVGRQV-----ELPLR------LHYDLTRSERVERVNAMLAkvGLPADVAAKFPHE------LSGGQRQRVGIATALITS 163
Cdd:PRK15439 344 PEDRQSsglylDAPLAwnvcalTHNRRGFWIKPARENAVLE--RYRRALNIKFNHAeqaartLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVDLSVSLVdEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAM 233
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-250 |
6.82e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 59 AGSVMLGGSEVigaADRTLADLRGRYTgMVFQNP---GASLNPVLPVGRQvelplrlhyDLTRsERVERVNAMLAKVGLP 135
Cdd:PTZ00265 1276 SGKILLDGVDI---CDYNLKDLRNLFS-IVSQEPmlfNMSIYENIKFGKE---------DATR-EDVKRACKFAAIDEFI 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 136 ADVAAKF-----PH--ELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSV 208
Cdd:PTZ00265 1342 ESLPNKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIAS 1421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1566271202 209 LTRaTTRCVVLDE----GSVVETGETAAMLAAPQDERTARLVRAAR 250
Cdd:PTZ00265 1422 IKR-SDKIVVFNNpdrtGSFVQAHGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-205 |
7.14e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGL------------------------LPPDVTVAGSVMLGGSE 68
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfngearpqpgikvgylpqepqLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 69 VIGAADRTLAdlrgryTGMVFQNPGASLNPVLpvGRQVELPLRLH----YDLTRseRVERvnAMLAkVGLP---ADVAak 141
Cdd:TIGR03719 96 IKDALDRFNE------ISAKYAEPDADFDKLA--AEQAELQEIIDaadaWDLDS--QLEI--AMDA-LRCPpwdADVT-- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 142 fphELSGGQRQRVGIATALITSPRLIVADEPTTALDSITqrqIVDLSVSLVDEAGAsMLFITHD 205
Cdd:TIGR03719 161 ---KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPGT-VVAVTHD 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-177 |
1.41e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIaiggkeIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRgrY 84
Cdd:PRK13538 10 ERDERI------LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPD---AGEVLWQGEPIRRQRDEYHQDLL--Y 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 85 TGMVfqnpgASLNPVLPVGRQVELPLRLHYDLTRservERVNAMLAKVGLP--ADVAAkfpHELSGGQRQRVGIATALIT 162
Cdd:PRK13538 79 LGHQ-----PGIKTELTALENLRFYQRLHGPGDD----EALWEALAQVGLAgfEDVPV---RQLSAGQQRRVALARLWLT 146
|
170
....*....|....*
gi 1566271202 163 SPRLIVADEPTTALD 177
Cdd:PRK13538 147 RAPLWILDEPFTAID 161
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-238 |
1.92e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 28 GERVGLIGSSGSGKSMIARAMLGLLPPdvtvAGSVMLGGSEVIGAADRTLADLRGrYtgMVFQNPGASLNPVLPVgrqve 107
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLLPG----SGSIQFAGQPLEAWSAAELARHRA-Y--LSQQQTPPFAMPVFQY----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 108 lpLRLH-YDLTRSERVERVNAMLA-KVGLpADVAAKFPHELSGGQRQRVGIATALI-----TSP--RLIVADEPTTALDs 178
Cdd:PRK03695 90 --LTLHqPDKTRTEAVASALNEVAeALGL-DDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLD- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 179 ITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQ 238
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-231 |
2.27e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEViGAADRTLADLRGryTGMVFQNP 92
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP---TKGTITINNINY-NKLDHKLAAQLG--IGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 GA----SLNPVLPVGRqveLPLRLHYDLT---RSERVERVNAMLAKVGLPADVAAKFPhELSGGQRQRVGIATALITSPR 165
Cdd:PRK09700 90 SVidelTVLENLYIGR---HLTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVA-NLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 166 LIVADEPTTaldSITQRQiVDLSVSLVDE---AGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETA 231
Cdd:PRK09700 166 VIIMDEPTS---SLTNKE-VDYLFLIMNQlrkEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-273 |
2.81e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 17 IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGMVFQnpgasl 96
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE---RGRILIDGCDI---SKFGLMDLR-KVLGIIPQ------ 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 97 NPVLPVG--RQVELPLRLHYDLTRSERVERvnAMLAKV------GLPADVaAKFPHELSGGQRQRVGIATALITSPRLIV 168
Cdd:PLN03130 1321 APVLFSGtvRFNLDPFNEHNDADLWESLER--AHLKDVirrnslGLDAEV-SEAGENFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 169 ADEPTTAL----DSITQRQIVDLSVSlvdeagASMLFITHdfsvltRATT-----RCVVLDEGSVVETGETAAMLAapqD 239
Cdd:PLN03130 1398 LDEATAAVdvrtDALIQKTIREEFKS------CTMLIIAH------RLNTiidcdRILVLDAGRVVEFDTPENLLS---N 1462
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1566271202 240 ERTA--RLVRA-----ARTLTLRASREGADRETDRGAAPSD 273
Cdd:PLN03130 1463 EGSAfsKMVQStgaanAQYLRSLVFGGDEDRLAREESKALD 1503
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-279 |
2.89e-11 |
|
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: 63.88 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVigaadRTLADLRGRYTGMVFQNpg 93
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLVGGKDI-----ETNLDAVRQSLGMCPQH-- 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLNPVLPVGRQVELPLRLHYDLTRSERVErVNAMLAKVGLPADVAAKfPHELSGGQRQRVGIATALITSPRLIVADEPT 173
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLE-MEAMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 174 TALDSITQRQIVDLSVSLvdEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMLAAPQDERTARLVRAARTL- 252
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIq 1167
|
250 260
....*....|....*....|....*..
gi 1566271202 253 TLRASREGADRETDRGAAPSDDATADE 279
Cdd:TIGR01257 1168 SQRGGCEGTCSCTSKGFSTRCPARVDE 1194
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-214 |
3.32e-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: 63.42 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRG 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPD---SGTIEIGETVKLAYVDQSRDALDP 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTgmVFQNPGASLNpVLPVGRqVELPLRLHydltrserVERVNAMLA----KVGlpadvaakfphELSGGQRQRVGIAT 158
Cdd:TIGR03719 400 NKT--VWEEISGGLD-IIKLGK-REIPSRAY--------VGRFNFKGSdqqkKVG-----------QLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQIVDlsvSLVDEAGASMLfITHDFSVLTRATT 214
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEE---ALLNFAGCAVV-ISHDRWFLDRIAT 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-232 |
3.45e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 20 GVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEvigaadrtladlrgrytgMVFQNPGASLN-- 97
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD---AGSILIDGQE------------------MRFASTTAALAag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 -----------PVLPVGRQV---ELPLRLHYdLTRSERVERVNAMLAKVGLPADVAAKFPHeLSGGQRQRVGIATALITS 163
Cdd:PRK11288 81 vaiiyqelhlvPEMTVAENLylgQLPHKGGI-VNRRLLNYEAREQLEHLGVDIDPDTPLKY-LSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAA 232
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMA 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-282 |
3.59e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.83 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 2 GVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGsgksmiARAMLGLLP-----PDVTVAGSVMLGGSEVIGAADRT 76
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*G------AA**RGALPahv*gPDAGRRPWRF*TWCANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 77 LADLRGRYTGMvfQNPGASLNPVLPVGRQVelplrlhyDLTRSERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGI 156
Cdd:NF000106 87 IG*HRPVR*GR--RESFSGRENLYMIGR*L--------DLSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 157 ATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETaamlaa 236
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV------ 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 237 pqDERTARLvrAARTLTLRASREGA-DRETDRGAAPSDD----ATADEHEG 282
Cdd:NF000106 229 --DELKTKV--GGRTLQIRPAHAAElDRMVGAIAQAGLDgiagATADHEDG 275
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-229 |
3.78e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.73 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTvAGSVMLGGSEVIGAADRTLAdlrG 82
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVT-GGTVEFKGKDLLELSPEDRA---G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQN----PGASLNPVLPVGRQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHE-LSGGQRQRVGIA 157
Cdd:PRK09580 78 EGIFMAFQYpveiPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 158 TALITSPRLIVADEPTTALDsITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCV-VLDEGSVVETGE 229
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSGD 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-242 |
3.97e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 8 LRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLL-----PPDVTVAGSVMLGGSEVIGAADRTLADLRG 82
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaPRGARVTGDVTLNGEPLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTGMVFQNPGASLNPVLPVGRQVELplRLHYDLTRSERvERVNAMLAKVGLPAdVAAKFPHELSGGQRQRVGIATAL-- 160
Cdd:PRK13547 87 VLPQAAQPAFAFSAREIVLLGRYPHA--RRAGALTHRDG-EIAWQALALAGATA-LVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 161 -------ITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAM 233
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
....*....
gi 1566271202 234 LAAPQDERT 242
Cdd:PRK13547 243 LTPAHIARC 251
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-258 |
4.33e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADrTLADLRG 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD---SGTLEIGGNPCARLTP-AKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYtgMVFQNPgaSLNPVLPVGRQVELPLRLHYDLTRserveRVNAMLAKVG--LPADVAAKfphELSGGQRQRVGIATAL 160
Cdd:PRK15439 88 IY--LVPQEP--LLFPNLSVKENILFGLPKRQASMQ-----KMKQLLAALGcqLDLDSSAG---SLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 161 ITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAAMlaaPQDE 240
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL---STDD 231
|
250
....*....|....*...
gi 1566271202 241 RTARLVRAARTLTLRASR 258
Cdd:PRK15439 232 IIQAITPAAREKSLSASQ 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-233 |
5.87e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.35 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIA-IGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGR 83
Cdd:COG3845 260 VENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA---SGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 Y-------TGMVfqnPGASL--NPVLpvGRQVELPLRLHYDLTRSERVERVNAMLAKvglpADVAAKFPHE----LSGGQ 150
Cdd:COG3845 337 YipedrlgRGLV---PDMSVaeNLIL--GRYRRPPFSRGGFLDRKAIRAFAEELIEE----FDVRTPGPDTparsLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 151 RQRVGIATALITSPRLIVADEPTTALD--SITQ--RQIVDLSvslvdEAGASMLFITHDFSVLTRATTRCVVLDEGSVVE 226
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDvgAIEFihQRLLELR-----DAGAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
....*..
gi 1566271202 227 TGETAAM 233
Cdd:COG3845 483 EVPAAEA 489
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-225 |
6.30e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 12 IGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEV----IGAA----------DRtl 77
Cdd:COG1129 262 LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAD---SGEIRLDGKPVrirsPRDAiragiayvpeDR-- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 78 adlrgRYTGMVfqnPGASL--NPVLPVGRQVELPLRLHydltRSERVERVNAMLAKVGL-PADVAAKfPHELSGGQRQRV 154
Cdd:COG1129 337 -----KGEGLV---LDLSIreNITLASLDRLSRGGLLD----RRRERALAEEYIKRLRIkTPSPEQP-VGNLSGGNQQKV 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 155 GIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSVV 225
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-241 |
6.51e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLlppdvtvagsVMLGGSEVIGAADRTLADLRGRYTGMVFQNPG 93
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF----------VRLASGKISILGQPTRQALQKNLVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLN-PVLpVGRQVELPLRLHYDLTR---SERVERVNAMLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVA 169
Cdd:PRK15056 89 VDWSfPVL-VEDVVMMGRYGHMGWLRrakKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 170 DEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDfsvLTRATTRC--VVLDEGSVVETGETAAMLAAPQDER 241
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHN---LGSVTEFCdyTVMVKGTVLASGPTETTFTAENLEL 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-226 |
2.74e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 8 LRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaADRTLADLRgRYTGM 87
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE---KGRIMIDDCDV---AKFGLTDLR-RVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 88 VFQnpgaslNPVLPVG--RQVELPLRLHYDLTRSERVERVNAMLA----KVGLPADVaAKFPHELSGGQRQRVGIATALI 161
Cdd:PLN03232 1315 IPQ------SPVLFSGtvRFNIDPFSEHNDADLWEALERAHIKDVidrnPFGLDAEV-SEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 162 TSPRLIVADEPTTAL----DSITQRQIVDlsvslvDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVE 226
Cdd:PLN03232 1388 RRSKILVLDEATASVdvrtDSLIQRTIRE------EFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLE 1449
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-204 |
2.80e-10 |
|
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: 57.93 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 5 IRDLRIAIG-GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPpdvtvagsvmLGGSEVIGAADRTLADLRGR 83
Cdd:cd03223 3 LENLSLATPdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP----------WGSGRIGMPEGEDLLFLPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 ytgmvfqnpgaslnPVLPVGRqvelpLR--LHYdltrservervnamlakvglPADvaakfpHELSGGQRQRVGIATALI 161
Cdd:cd03223 73 --------------PYLPLGT-----LReqLIY--------------------PWD------DVLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1566271202 162 TSPRLIVADEPTTALDSITQRQIVDlsvsLVDEAGASMLFITH 204
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQ----LLKELGITVISVGH 146
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-223 |
5.22e-10 |
|
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: 57.86 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 17 IVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSevigaadrtladlrgryTGMVFQNP---G 93
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK---LSGSVSVPGS-----------------IAYVSQEPwiqN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASL--NPVLpvGRQvelplrlhYDltrSERVERVnamLAKVGLPADVAAkFPH-------E----LSGGQRQRVGIATAL 160
Cdd:cd03250 80 GTIreNILF--GKP--------FD---EERYEKV---IKACALEPDLEI-LPDgdlteigEkginLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 161 ITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEGS 223
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-209 |
5.35e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRiaiggKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPpDVTVAGSVMLggsevigaadrtladl 80
Cdd:COG2401 34 FGVELRVVE-----RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-GTPVAGCVDV---------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 81 rgrytgmvfqnpgaslnPVLPVGRQVELPLRLHYDLTRSERVERVNAmlakVGLpADVAAKF--PHELSGGQRQRVGIAT 158
Cdd:COG2401 92 -----------------PDNQFGREASLIDAIGRKGDFKDAVELLNA----VGL-SDAVLWLrrFKELSTGQKFRFRLAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRqIVDLSVS-LVDEAGASMLFITHDFSVL 209
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAK-RVARNLQkLARRAGITLVVATHHYDVI 200
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-220 |
1.10e-09 |
|
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: 57.42 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 24 SIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGS----EVIGAADRTLADL-----RGRYTGMVFQNpga 94
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRDLlssitKDFYTHPYFKT--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 slnpvlpvgrQVELPLRLHYDLTRserveRVNamlakvglpadvaakfphELSGGQRQRVGIATALITSPRLIVADEPTT 174
Cdd:cd03237 98 ----------EIAKPLQIEQILDR-----EVP------------------ELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1566271202 175 ALDSiTQRQIVDLSVS-LVDEAGASMLFITHDFSVLTRATTRCVVLD 220
Cdd:cd03237 145 YLDV-EQRLMASKVIRrFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-284 |
1.55e-09 |
|
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: 58.42 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPpdvTVAGSVMLGGSEVIGAADRTLadlrgrytgmvfQNpgASLN 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD---KVEGHVHMKGSVAYVPQQAWI------------QN--DSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 PVLPVGRQVELPlrlhydltRSERVERVNAMLAKVG-LPADVAAKFPHE---LSGGQRQRVGIATALITSPRLIVADEPT 173
Cdd:TIGR00957 717 ENILFGKALNEK--------YYQQVLEACALLPDLEiLPSGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 174 TALDSITQRQIVDLSVSLVDE-AGASMLFITHDFSVLTRaTTRCVVLDEGSVVETGETAAMLAapqdertarlvraartl 252
Cdd:TIGR00957 789 SAVDAHVGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQ----------------- 850
|
250 260 270
....*....|....*....|....*....|..
gi 1566271202 253 tlrasREGADRETDRGAAPSDDATADEHEGEA 284
Cdd:TIGR00957 851 -----RDGAFAEFLRTYAPDEQQGHLEDSWTA 877
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-223 |
2.20e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.10 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 28 GERVGLIGSSGSGKSMIARAMLG---LLPPDVTVAG-SVMLGGSEVigaadrtladlrgrYTGMVFQNPGASLNPVLpVG 103
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGdttVTSGDATVAGkSILTNISDV--------------HQNMGYCPQFDAIDDLL-TG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 104 RQvELPLRLHYDLTRSERVERV-NAMLAKVGLPAdVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQR 182
Cdd:TIGR01257 2030 RE-HLYLYARLRGVPAEEIEKVaNWSIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1566271202 183 QIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGS 223
Cdd:TIGR01257 2108 MLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-176 |
2.76e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvTVAGSVMLGGSEVIGaadRTLADLRGRYTGMVFQNp 92
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHG-TYEGEIIFEGEELQA---SNIRDTERAGIAIIHQE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 93 gASLNPVLPV------GRQVELPLRLHYDltrsERVERVNAMLAKVGLPADVAAKFpHELSGGQRQRVGIATALITSPRL 166
Cdd:PRK13549 91 -LALVKELSVleniflGNEITPGGIMDYD----AMYLRAQKLLAQLKLDINPATPV-GNLGLGQQQLVEIAKALNKQARL 164
|
170
....*....|
gi 1566271202 167 IVADEPTTAL 176
Cdd:PRK13549 165 LILDEPTASL 174
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-205 |
1.80e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGL------------------------LPPDVTVAGSVMLGGSE 68
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkefegearpapgikvgylpqepqLDPEKTVRENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 69 VIGAADRtLADLrgrytGMVFQNPGASLNPVLPvgRQVELPLRLH----YDLTRseRVERvnAMLAkVGLP---ADVAak 141
Cdd:PRK11819 98 VKAALDR-FNEI-----YAAYAEPDADFDALAA--EQGELQEIIDaadaWDLDS--QLEI--AMDA-LRCPpwdAKVT-- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 142 fphELSGGQRQRVGIATALITSPRLIVADEPTTALDSitqrqivdLSVS-----LVDEAGAsMLFITHD 205
Cdd:PRK11819 163 ---KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------ESVAwleqfLHDYPGT-VVAVTHD 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-209 |
3.76e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 7 DLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTVAGSVMLGGseviGAADRTLAdlrgRYTG 86
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNG----RPLDSSFQ----RSIG 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 87 MVFQN----PGASLNPVLpvgrQVELPLRLHYDLTRSERVERVNAMLAKVGLP--ADVAAKFPHE-LSGGQRQRVGIATA 159
Cdd:TIGR00956 840 YVQQQdlhlPTSTVRESL----RFSAYLRQPKSVSKSEKMEYVEEVIKLLEMEsyADAVVGVPGEgLNVEQRKRLTIGVE 915
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 160 LITSPRLIV-ADEPTTALDSITQRQIVDLSVSLVDeAGASMLFITHDFSVL 209
Cdd:TIGR00956 916 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSAI 965
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-185 |
9.52e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARamlgllppdvTVAGSV---MLGGSEVIGAADRTLADLRGRYTGMVFQN 91
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLK----------TIASNTdgfHIGVEGVITYDGITPEEIKKHYRGDVVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 92 PGASLN-PVLPVGRQVELPLRLH-----YD-LTRSERVERVNAM-LAKVGLP----ADVAAKFPHELSGGQRQRVGIATA 159
Cdd:TIGR00956 144 AETDVHfPHLTVGETLDFAARCKtpqnrPDgVSREEYAKHIADVyMATYGLShtrnTKVGNDFVRGVSGGERKRVSIAEA 223
|
170 180
....*....|....*....|....*.
gi 1566271202 160 LITSPRLIVADEPTTALDSITQRQIV 185
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFI 249
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-228 |
1.16e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTvaGSVMLGGS-----EVIGAADRTLADlrgrytGMVFqnpGAS 95
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET--SSVVIRGSvayvpQVSWIFNATVRE------NILF---GSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 96 LNP------VLPVGRQVELPLRLHYDLTrsERVER-VNamlakvglpadvaakfpheLSGGQRQRVGIATALITSPRLIV 168
Cdd:PLN03232 705 FESerywraIDVTALQHDLDLLPGRDLT--EIGERgVN-------------------ISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 169 ADEPTTALDSITQRQIVDlsvSLVDEA--GASMLFITHDFSVLTRaTTRCVVLDEGSVVETG 228
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFD---SCMKDElkGKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEG 821
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-229 |
1.25e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADrtlADLRGRYTGMvfqnpgaslnpvl 100
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN---KGTVDIKGSAALIAIS---SGLNGQLTGI------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 101 pvgRQVELPlRLHYDLTRservERVNAMLAKVGLPADVaAKFPHE----LSGGQRQRVGIATALITSPRLIVADEPTTAL 176
Cdd:PRK13545 104 ---ENIELK-GLMMGLTK----EKIKEIIPEIIEFADI-GKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 177 DSITQRQIVDlSVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGE 229
Cdd:PRK13545 175 DQTFTKKCLD-KMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGD 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-228 |
1.89e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvTVAGSVMLGGS-----EVIGAADRTLADlrgrytGMVFQNP--G 93
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP--RSDASVVIRGTvayvpQVSWIFNATVRD------NILFGSPfdP 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLNPVLPV-GRQVELPLRLHYDLTrsERVER-VNamlakvglpadvaakfpheLSGGQRQRVGIATALITSPRLIVADE 171
Cdd:PLN03130 708 ERYERAIDVtALQHDLDLLPGGDLT--EIGERgVN-------------------ISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 172 PTTALDSITQRQIVDlsVSLVDE-AGASMLFITHDFSVLTRaTTRCVVLDEGSVVETG 228
Cdd:PLN03130 767 PLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQ-VDRIILVHEGMIKEEG 821
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-237 |
3.54e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.25 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 1 MGVDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIaramLGLLPP--DVTvAGSVMLGGsevIGAADRTLA 78
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTL----LSLIQRhfDVS-EGDIRFHD---IPLTKLQLD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 DLRGRYTgMVFQNPGASLNPV---LPVGRQvelplrlhyDLTRSErVERVnAMLAKV---------GLPADVAAKFPHeL 146
Cdd:PRK10789 386 SWRSRLA-VVSQTPFLFSDTVannIALGRP---------DATQQE-IEHV-ARLASVhddilrlpqGYDTEVGERGVM-L 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 147 SGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIV-DLSVSlvdEAGASMLFITHDFSVLTRAtTRCVVLDEGSVV 225
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILhNLRQW---GEGRTVIISAHRLSALTEA-SEILVMQHGHIA 528
|
250
....*....|..
gi 1566271202 226 ETGETAAMLAAP 237
Cdd:PRK10789 529 QRGNHDQLAQQS 540
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-214 |
3.74e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPP---DVTVAGSVMLGGsevigAADRTLADLRGRytgmvf 89
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPvsgEIGLAKGIKLGY-----FAQHQLEFLRAD------ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 90 qnpgaslnpvlpvgrqvELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVA 169
Cdd:PRK10636 392 -----------------ESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1566271202 170 DEPTTALDsITQRQIvdLSVSLVDEAGAsMLFITHDFSVLtRATT 214
Cdd:PRK10636 455 DEPTNHLD-LDMRQA--LTEALIDFEGA-LVVVSHDRHLL-RSTT 494
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-177 |
4.06e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 2 GVDIRDLR-----IAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAM----LGLLPP--------------DVTV 58
Cdd:PLN03073 172 GPAIKDIHmenfsISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaIDGIPKncqilhveqevvgdDTTA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 59 AGSVM--------LGGSEV-IGAADRTLADLRGRYTGMVFQNPGASLNPVlpVGRQVELPLRLhyDLTRSERVE-RVNAM 128
Cdd:PLN03073 252 LQCVLntdiertqLLEEEAqLVAQQRELEFETETGKGKGANKDGVDKDAV--SQRLEEIYKRL--ELIDAYTAEaRAASI 327
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1566271202 129 LAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALD 177
Cdd:PLN03073 328 LAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-205 |
4.23e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 28 GERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLG----------GSEVIGAADRTLADLRGRYTGMVFQNpgasln 97
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPD---EGEVDPElkisykpqyiKPDYDGTVEDLLRSITDDLGSSYYKS------ 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 98 pvlpvgrqvEL--PLRLHYDLTRserveRVNamlakvglpadvaakfphELSGGQRQRVGIATALITSPRLIVADEPTTA 175
Cdd:PRK13409 436 ---------EIikPLQLERLLDK-----NVK------------------DLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
170 180 190
....*....|....*....|....*....|....*
gi 1566271202 176 LDsITQRqivdLSVS-----LVDEAGASMLFITHD 205
Cdd:PRK13409 484 LD-VEQR----LAVAkairrIAEEREATALVVDHD 513
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-184 |
4.62e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.85 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvaGSVMLGGsevIGAADRTLADLR---GRYTGMVF 89
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE----GDIQIDG---VSWNSVPLQKWRkafGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 90 QNPGaslnpvlpvgrqvelPLRLHYDLTRSERVERVNAMLAKVGLPAdVAAKFPHE-----------LSGGQRQRVGIAT 158
Cdd:cd03289 88 IFSG---------------TFRKNLDPYGKWSDEEIWKVAEEVGLKS-VIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 151
|
170 180
....*....|....*....|....*.
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQI 184
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVI 177
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-224 |
5.94e-07 |
|
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: 50.21 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 18 VHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvTVAGSVMLGGSEVigaADRTLADLRGRYTGMVFQN-PGASL 96
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG--KFEGNVFINGKPV---DIRNPAQAIRAGIAMVPEDrKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 97 NPVLPVGRQVELP-LRLHYDLTRSERVERVNAMLAKVG-LPADVAAKF--PHELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:TIGR02633 351 VPILGVGKNITLSvLKSFCFKMRIDAAAELQIIGSAIQrLKVKTASPFlpIGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSV 224
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-178 |
6.40e-07 |
|
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: 48.78 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSmiarAMLGLLPPDVT---VAGSVMLGGSEVigaaDRTLAdlrgRYTGMVF 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKT----TLLDVLAGRKTagvITGEILINGRPL----DKNFQ----RSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 90 QNPgaslnpVLPVGRQVELPLRLHYDLtrservervnamlakvglpadvaakfpHELSGGQRQRVGIATALITSPRLIVA 169
Cdd:cd03232 86 QQD------VHSPNLTVREALRFSALL---------------------------RGLSVEQRKRLTIGVELAAKPSILFL 132
|
....*....
gi 1566271202 170 DEPTTALDS 178
Cdd:cd03232 133 DEPTSGLDS 141
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-205 |
7.13e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 4 DIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRGR 83
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQAD---SGRIHCGTKLEVAYFDQHRAELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 YTgmVFQNPGASLNPVLPVGRQVELPLRLHYDLTRSERvervnAMlakvglpADVAAkfpheLSGGQRQRVGIATALITS 163
Cdd:PRK11147 398 KT--VMDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKR-----AM-------TPVKA-----LSGGERNRLLLARLFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1566271202 164 PRLIVADEPTTALDSITqrqiVDLSVSLVDEAGASMLFITHD 205
Cdd:PRK11147 459 SNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-180 |
7.63e-07 |
|
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: 50.29 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 13 GGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvaGSVMLGGsevIGAADRTLADLR---GRYTGMVF 89
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE----GEIQIDG---VSWNSVTLQTWRkafGVIPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 90 QNPGA---SLNPvlpvgrqvelplrlhYDLTRSERVERVNamlAKVGLPAdVAAKFPHE-----------LSGGQRQRVG 155
Cdd:TIGR01271 1303 IFSGTfrkNLDP---------------YEQWSDEEIWKVA---EEVGLKS-VIEQFPDKldfvlvdggyvLSNGHKQLMC 1363
|
170 180
....*....|....*....|....*
gi 1566271202 156 IATALITSPRLIVADEPTTALDSIT 180
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVT 1388
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-284 |
7.89e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLppDVTvAGSVMlggsevigaADRTLA-----------DLRGR 83
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF--EIS-EGRVW---------AERSIAyvpqqawimnaTVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 84 ytgMVFQNPgaslnpvlpvgrqvELPLRLHyDLTRSERVERVNAMLAKvGLPADVAAKFPHeLSGGQRQRVGIATALITS 163
Cdd:PTZ00243 741 ---ILFFDE--------------EDAARLA-DAVRVSQLEADLAQLGG-GLETEIGEKGVN-LSGGQKARVSLARAVYAN 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 164 PRLIVADEPTTALDSITQRQIVDlSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVETGETAAMLAAPQDErta 243
Cdd:PTZ00243 801 RDVYLLDDPLSALDAHVGERVVE-ECFLGALAGKTRVLATHQVHVVPRA-DYVVALGDGRVEFSGSSADFMRTSLYA--- 875
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1566271202 244 rlvraartlTLRAsrEGADRETDRGA-APSDDATADEHEGEA 284
Cdd:PTZ00243 876 ---------TLAA--ELKENKDSKEGdADAEVAEVDAAPGGA 906
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
146-212 |
1.56e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.32 E-value: 1.56e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 146 LSGGQRQRVGIATALITSPR--LIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRA 212
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSSA 155
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-205 |
1.73e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIGAADRTLADLRG 82
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPD---SGTIKIGETVKLAYVDQSRDALDP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RYTgmVFQNPGASLNpVLPVGrQVELPLRLHydltrserVERVNAMLA----KVGlpadvaakfphELSGGQRQRVGIAT 158
Cdd:PRK11819 402 NKT--VWEEISGGLD-IIKVG-NREIPSRAY--------VGRFNFKGGdqqkKVG-----------VLSGGERNRLHLAK 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1566271202 159 ALITSPRLIVADEPTTALDSITQRQivdLSVSLVDEAGASMLfITHD 205
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVETLRA---LEEALLEFPGCAVV-ISHD 501
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-214 |
2.66e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 2.66e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 145 ELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATT 214
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANT 648
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-212 |
3.13e-06 |
|
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: 46.94 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPpdvTVAGSVMLGgSEVIGAADRTLADLRGRYTGMVFQNPGASLNPVL 100
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVHWS-NKNESEPSFEATRSRNRYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 101 PVGRQVELPLRlhydltrserVERVNAMLAKVGLPADVAAkFPH-----------ELSGGQRQRVGIATALITSPRLIVA 169
Cdd:cd03290 96 EENITFGSPFN----------KQRYKAVTDACSLQPDIDL-LPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1566271202 170 DEPTTALD-SITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRA 212
Cdd:cd03290 165 DDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHA 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
119-204 |
3.64e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 119 SERvERVNAM--LAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQ---RQIVDLsvsLVD 193
Cdd:PRK10938 374 SDR-QQKLAQqwLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDV---LIS 449
|
90
....*....|.
gi 1566271202 194 EAGASMLFITH 204
Cdd:PRK10938 450 EGETQLLFVSH 460
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
145-209 |
6.82e-06 |
|
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: 47.09 E-value: 6.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 145 ELSGGQRQRVGIATALITSPRLIVADEPTTALDsITQRqivdLSVS-----LVDEAGASMLFITHDFSVL 209
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQR----LAVAkairrFAENRGKTAMVVDHDIYLI 519
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-223 |
7.80e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.21 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtvagsvmlggsevigaadrtlADLRGRYTGMVFQNPG 93
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEP-----------------------SEGKIKHSGRISFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLnpVLPVGRQVELPLRLHYDLTRSERVerVNAmlakVGLPADVAaKFPHE-----------LSGGQRQRVGIATALIT 162
Cdd:TIGR01271 495 TSW--IMPGTIKDNIIFGLSYDEYRYTSV--IKA----CQLEEDIA-LFPEKdktvlgeggitLSGGQRARISLARAVYK 565
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVdEAGASMLFITHDFSVLTRAtTRCVVLDEGS 223
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKEIFESCLCKL-MSNKTRILVTSKLEHLKKA-DKILLLHEGV 624
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-243 |
1.12e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.50 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVigaADRTLADLRGRYTGmVFQNpgaslnpvl 100
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP---QSGEILLDGKPV---TAEQPEDYRKLFSA-VFTD--------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 101 pvgrqVELPLRLHYDLTRSERVERVNAMLAKVGLpadvAAKFPHE--------LSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:PRK10522 406 -----FHLFDQLLGPEGKPANPALVEKWLERLKM----AHKLELEdgrisnlkLSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566271202 173 TTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRAtTRCVVLDEGSVVE-TGETAAMLAAPQDERTA 243
Cdd:PRK10522 477 AADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHA-DRLLEMRNGQLSElTGEERDAASRDAVARTA 547
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
145-226 |
1.23e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 145 ELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSV 224
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
..
gi 1566271202 225 VE 226
Cdd:PRK09700 488 TQ 489
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
145-220 |
1.56e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.49 E-value: 1.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566271202 145 ELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEAGASMLFITHDFSVLTRATTRCVVLD 220
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
145-209 |
1.56e-05 |
|
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: 45.44 E-value: 1.56e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 145 ELSGGQRQRVGIATALITSPRLIVADEPTTALDsITQRQIVDLSVSLVDEAGASMLFITHDFSVL 209
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLD-IKQRLNAARLIRELAEDDNYVLVVEHDLAVL 202
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-223 |
1.91e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 45.23 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVmlggsevigaadrtladlrgRYTGMVFQNPG 93
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS---EGKI--------------------KHSGRISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 94 ASLnpVLPVGRQVELPLRLHYDLTRSERVervnamLAKVGLPADVAaKFPHE-----------LSGGQRQRVGIATALIT 162
Cdd:cd03291 106 FSW--IMPGTIKENIIFGVSYDEYRYKSV------VKACQLEEDIT-KFPEKdntvlgeggitLSGGQRARISLARAVYK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDLSVSLVdEAGASMLFITHDFSVLTRAtTRCVVLDEGS 223
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTEKEIFESCVCKL-MANKTRILVTSKMEHLKKA-DKILILHEGS 235
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-205 |
2.25e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVIG----------A 72
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPD---SGTVKWSENANIGyyaqdhaydfE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 73 ADRTLADLRGRYTgmvfqNPGaslnpvlpvgrqvelplrlHYDLTrserverVNAMLAKVGLPADVAAKFPHELSGGQRQ 152
Cdd:PRK15064 397 NDLTLFDWMSQWR-----QEG-------------------DDEQA-------VRGTLGRLLFSQDDIKKSVKVLSGGEKG 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1566271202 153 RVGIATALITSPRLIVADEPTTALDsitQRQIVDLSVSLVDEAGaSMLFITHD 205
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD---MESIESLNMALEKYEG-TLIFVSHD 494
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
146-212 |
2.98e-05 |
|
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: 45.39 E-value: 2.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 146 LSGGQRQRVGIATAL---ITSPRLIVADEPTTALDSITQRQIVDLSVSLVDeAGASMLFITHDFSVLTRA 212
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVD-KGNTVVVIEHNLDVIKTA 898
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
120-178 |
4.04e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 4.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 120 ERVERVNAMLAKVGLPADVAakfpheLSGGQRQRVGIATALITSPRLIVADEPTTALDS 178
Cdd:PLN03140 1000 ELVELDNLKDAIVGLPGVTG------LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
15-248 |
4.88e-05 |
|
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: 43.74 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 15 KEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLppDVtVAGSVMLGGsevIGAADRTLADLRGRYTgMVFQNPga 94
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV--DI-FDGKIVIDG---IDISKLPLHTLRSRLS-IILQDP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 95 slnpVLPVG--RQVELPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFPH---ELSGGQRQRVGIATALITSPRLIVA 169
Cdd:cd03288 105 ----ILFSGsiRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEggeNFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566271202 170 DEPTTALDSITQRqiVDLSVSLVDEAGASMLFITHDFSVLTRATTrCVVLDEGSVVETgETAAMLAAPQDERTARLVRA 248
Cdd:cd03288 181 DEATASIDMATEN--ILQKVVMTAFADRTVVTIAHRVSTILDADL-VLVLSRGILVEC-DTPENLLAQEDGVFASLVRT 255
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
145-209 |
4.89e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.76 E-value: 4.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1566271202 145 ELSGGQRQRVGIATALI---TSPRLIVADEPTTALDSITQRQIVDLSVSLVDeAGASMLFITHDFSVL 209
Cdd:cd03271 169 TLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVD-KGNTVVVIEHNLDVI 235
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-235 |
7.35e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 22 DLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSV-----------------------------MLGGSEviga 72
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPL---LSGERqsqfshitrlsfeqlqklvsdewqrnntdMLSPGE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 73 aDRTladlrGRYTGMVFQNPgaslnpvlpvgrqvelplrlHYDLTRSERVErvnamlAKVGLPADVAAKFPHeLSGGQRQ 152
Cdd:PRK10938 96 -DDT-----GRTTAEIIQDE--------------------VKDPARCEQLA------QQFGITALLDRRFKY-LSTGETR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 153 RVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLvDEAGASMLFITHDFSVLTRATTRCVVLDEGSVVETGETAA 232
Cdd:PRK10938 143 KTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASL-HQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREE 221
|
...
gi 1566271202 233 MLA 235
Cdd:PRK10938 222 ILQ 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-215 |
8.01e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 28 GERVGLIGSSGSGKSMIARAMLGLLPPDvtvagsvmlGGSEVIGAADRTLADLRGRYTGMVFqnpgaslnpvlpvgrqve 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPP---------GGGVIYIDGEDILEEVLDQLLLIIV------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 108 lplrlhydltrservervnamlakvglpadvaAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDL 187
Cdd:smart00382 55 --------------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLL 102
|
170 180 190
....*....|....*....|....*....|...
gi 1566271202 188 SVSLVD-----EAGASMLFITHDFSVLTRATTR 215
Cdd:smart00382 103 EELRLLlllksEKNLTVILTTNDEKDLGPALLR 135
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
146-230 |
8.28e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 146 LSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATTRCVVLDEGSV- 224
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVa 470
|
....*...
gi 1566271202 225 --VETGET 230
Cdd:PRK10982 471 giVDTKTT 478
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-214 |
1.08e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566271202 144 HELSGGQRQRVGIATALI---TSPR-LIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVLTRATT 214
Cdd:cd03227 76 LQLSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAELADK 149
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
146-229 |
1.55e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.68 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 146 LSGGQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLsVSLVDEAGASMLFITHDFSVLTRATTRCVVLDEGSVv 225
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQL-INQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI- 473
|
....
gi 1566271202 226 eTGE 229
Cdd:PRK10762 474 -SGE 476
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-209 |
1.65e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 27 DGERVGLIGSSGSGKSMIARAMLGLLPPDvtvagsvmLGGSEVIGAADRTLAdlrgRYTGMVFQN-----PGASLNPVLP 101
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPN--------LGDYEEEPSWDEVLK----RFRGTELQNyfkklYNGEIKVVHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 102 VgRQVELpLRLHYDLTRSERVERVNamlaKVGLPADVAAKFP---------HELSGGQRQRVGIATALITSPRLIVADEP 172
Cdd:PRK13409 166 P-QYVDL-IPKVFKGKVRELLKKVD----ERGKLDEVVERLGlenildrdiSELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1566271202 173 TTALDsITQRqivdLSVS-LVDE--AGASMLFITHDFSVL 209
Cdd:PRK13409 240 TSYLD-IRQR----LNVArLIRElaEGKYVLVVEHDLAVL 274
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
145-209 |
2.13e-04 |
|
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: 42.46 E-value: 2.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 145 ELSGGQRQRVGIATALITSPRLIVADEPTTALDsITQR-----QIVDLSvslvdEAGASMLFITHDFSVL 209
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-IYQRlnvarLIRELA-----EEGKYVLVVEHDLAIL 275
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
33-54 |
2.23e-04 |
|
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.
Pssm-ID: 426032 [Multi-domain] Cd Length: 207 Bit Score: 41.37 E-value: 2.23e-04
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-228 |
2.38e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 17 IVHGVDLSIGDGERVGLIGSSGSGKSMIaraMLGLLPPDVTVAGSVMLGGSEvIGAADrtLADLRgRYTGMVFQnpgasl 96
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTL---LLTFMRMVEVCGGEIRVNGRE-IGAYG--LRELR-RQFSMIPQ------ 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 97 NPVLPVGrqvelPLRLHYDLTRSERVERVNAMLAKVGLPADVAAKFP----------HELSGGQRQRVGIATALIT-SPR 165
Cdd:PTZ00243 1392 DPVLFDG-----TVRQNVDPFLEASSAEVWAALELVGLRERVASESEgidsrvleggSNYSVGQRQLMCMARALLKkGSG 1466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566271202 166 LIVADEPTTALDSITQRQIvdlsVSLVDEAGASMLFITHDFSVLTRAT-TRCVVLDEGSVVETG 228
Cdd:PTZ00243 1467 FILMDEATANIDPALDRQI----QATVMSAFSAYTVITIAHRLHTVAQyDKIIVMDHGAVAEMG 1526
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-176 |
2.52e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 20 GVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaadrtladlrgrytgmVFQNPGASLNPV 99
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRD---AGSILYLGKEV------------------TFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 100 LPVGRQvelPLRLHYDLTRSERV----ERVNAM---------------LAKVGLPADvAAKFPHELSGGQRQRVGIATAL 160
Cdd:PRK10762 81 IGIIHQ---ELNLIPQLTIAENIflgrEFVNRFgridwkkmyaeadklLARLNLRFS-SDKLVGELSIGEQQMVEIAKVL 156
|
170
....*....|....*.
gi 1566271202 161 ITSPRLIVADEPTTAL 176
Cdd:PRK10762 157 SFESKVIIMDEPTDAL 172
|
|
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
33-54 |
8.78e-04 |
|
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440371 [Multi-domain] Cd Length: 502 Bit Score: 40.41 E-value: 8.78e-04
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
118-227 |
9.29e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 118 RSERVERVNAMLAKVGLPADvaakfPHELSG----GQRQRVGIATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVD 193
Cdd:NF040905 113 WNETNRRARELLAKVGLDES-----PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA 187
|
90 100 110
....*....|....*....|....*....|....
gi 1566271202 194 EAGASMLfITHDFSVLTRATTRCVVLDEGSVVET 227
Cdd:NF040905 188 QGITSII-ISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
26-205 |
9.56e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 26 GDGERVGLIGSSGSGKSMIARAMLGLLPP------------------------DVTVAGSVMLGGSEVIGAA---DRtla 78
Cdd:PRK15064 25 GGGNRYGLIGANGCGKSTFMKILGGDLEPsagnvsldpnerlgklrqdqfafeEFTVLDTVIMGHTELWEVKqerDR--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 79 dlrgrytgmVFQNPGASLNPVLPVGrqvELPLRL-HYDLTRSErvERVNAMLAKVGLPADVAAKFPHELSGGQRQRVGIA 157
Cdd:PRK15064 102 ---------IYALPEMSEEDGMKVA---DLEVKFaEMDGYTAE--ARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1566271202 158 TALITSPRLIVADEPTTALDSITQRQIVDlsvsLVDEAGASMLFITHD 205
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDINTIRWLED----VLNERNSTMIIISHD 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-209 |
9.66e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 9.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 146 LSGGQRQRVGIATALITS---PRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFITHDFSVL 209
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVV 875
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-177 |
1.06e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 20 GVDLSigdgERVGLIGSSGSGKSMIARAMLGLLPPdvtVAGSVMLGGSEVIGAADRTLADlrgrytGMVFqnpgaSLNPV 99
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISGELQP---SSGTVFRSAKVRMAVFSQHHVD------GLDL-----SSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 100 LPVGR----QVELPLRLHydltrservervnamLAKVGLPADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTA 175
Cdd:PLN03073 593 LYMMRcfpgVPEQKLRAH---------------LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
..
gi 1566271202 176 LD 177
Cdd:PLN03073 658 LD 659
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-212 |
1.41e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.16 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 3 VDIRDLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEVigaaDRTLADLRG 82
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE---KGEILFERQSI----KKDLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 83 RytgMVFQNPGASLNPVLPVGRQVELPlrLHYDLTRSERVERVNamLAKVGLPADVAAKFpheLSGGQRQRVGIATALIT 162
Cdd:PRK13540 75 Q---LCFVGHRSGINPYLTLRENCLYD--IHFSPGAVGITELCR--LFSLEHLIDYPCGL---LSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1566271202 163 SPRLIVADEPTTALDSITQRQIVDlSVSLVDEAGASMLFITHDFSVLTRA 212
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIIT-KIQEHRAKGGAVLLTSHQDLPLNKA 193
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
7-54 |
1.62e-03 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 39.58 E-value: 1.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1566271202 7 DLRIAIGGKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPP 54
Cdd:PRK09862 189 DLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPD 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-202 |
3.13e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.76 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 14 GKEIVHGVDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDVTvaGSVMLGGSEV--------IGAADRTLADLRGRYt 85
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWE--GEIFIDGKPVkirnpqqaIAQGIAMVPEDRKRD- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 86 GMVfqnpgaslnPVLPVGRQVELPLrlhydLTRSERVERVNAMLAKVGLPADVAA---KFPH------ELSGGQRQRVGI 156
Cdd:PRK13549 351 GIV---------PVMGVGKNITLAA-----LDRFTGGSRIDDAAELKTILESIQRlkvKTASpelaiaRLSGGNQQKAVL 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1566271202 157 ATALITSPRLIVADEPTTALDSITQRQIVDLSVSLVDEaGASMLFI 202
Cdd:PRK13549 417 AKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI 461
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-177 |
4.76e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 37.52 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566271202 21 VDLSIGDGERVGLIGSSGSGKSMIARAMLGLLPPDvtvAGSVMLGGSEViGAADRTladlrgRYTGMVFQNPGasLNPVL 100
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVE---SGQIQIDGKTA-TRGDRS------RFMAYLGHLPG--LKADL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566271202 101 PVGRQVELPLRLHydlTRSERVERVNAmLAKVGLpADVAAKFPHELSGGQRQRVGIATALITSPRLIVADEPTTALD 177
Cdd:PRK13543 98 STLENLHFLCGLH---GRRAKQMPGSA-LAIVGL-AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| |
