|
Name |
Accession |
Description |
Interval |
E-value |
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-229 |
7.13e-113 |
|
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: 323.29 E-value: 7.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAK----TAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfRFQGDLRR 79
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR--RRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 80 NVQMVFQDPYASLHPNHTLWRTLAEPLQIHGIRDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQI 159
Cdd:COG1124 80 RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 160 LLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALVNG 229
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-217 |
8.95e-84 |
|
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: 258.29 E-value: 8.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTF-----GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQ-GD 76
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 LRRNVQMVFQDPYASLHPNHTLWRTLAEPLQIHGI---RDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARAL 153
Cdd:COG1123 340 LRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLlsrAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 154 LLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-217 |
1.71e-82 |
|
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: 245.49 E-value: 1.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTF----GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP-GFRFQGDL 77
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQDPYASLHPNHTLWRTLAEPLQIHGIRDVAP----RVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARAL 153
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEarkeAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 154 LLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-212 |
1.89e-80 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 243.87 E-value: 1.89e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKT-----------AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT-PG 70
Cdd:COG4608 7 LLEVRDLKKHFPVRGglfgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITgLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 71 FRFQGDLRRNVQMVFQDPYASLHPNHTLWRTLAEPLQIHGIRDVAP---RVTTALEQVGLAADAVRRYPHQLSGGQRQRV 147
Cdd:COG4608 87 GRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAErreRVAELLELVGLRPEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 148 AIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFM 212
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVM 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-212 |
3.70e-75 |
|
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: 229.94 E-value: 3.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTF----GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWR---GSVDLLGQAIT--PGFRF 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLklSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 74 QgDLR-RNVQMVFQDPYASLHPNHTLWRTLAEPLQIHGI---RDVAPRVTTALEQVGL--AADAVRRYPHQLSGGQRQRV 147
Cdd:COG0444 81 R-KIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGlskAEARERAIELLERVGLpdPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 148 AIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFM 212
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-217 |
6.48e-72 |
|
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: 228.03 E-value: 6.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTF-----------GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREwRGSVDLLGQAITpGF 71
Cdd:COG4172 275 LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLD-GL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 72 RFQGD--LRRNVQMVFQDPYASLHPNHTLWRTLAEPLQIHGI----RDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQ 145
Cdd:COG4172 353 SRRALrpLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPglsaAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523681378 146 RVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-212 |
5.41e-60 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 191.72 E-value: 5.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 18 AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT-PGFRFQGDLRRNVQMVFQDPYASLHPNH 96
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkADPEAQKLLRQKIQIVFQNPYGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 97 TLWRTLAEPLQIHGIRDVAPRVTTALE---QVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSV 173
Cdd:PRK11308 110 KVGQILEEPLLINTSLSAAERREKALAmmaKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 523681378 174 QAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFM 212
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-217 |
8.03e-58 |
|
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: 191.44 E-value: 8.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGA----KTAVSAASFRVDAGETFSLIGASGCGKS----TILRVLAGLQREWRGSVDLLGQAIT--PG 70
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLglSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 71 FRFQGdLR-RNVQMVFQDPYASLHPNHTLWRTLAEPLQIH-GIRDVA--PRVTTALEQVGLAADAVR--RYPHQLSGGQR 144
Cdd:COG4172 84 RELRR-IRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHrGLSGAAarARALELLERVGIPDPERRldAYPHQLSGGQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 145 QRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-212 |
1.67e-56 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 182.60 E-value: 1.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKT-------------AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP 69
Cdd:PRK15079 8 LLEVADLKVHFDIKDgkqwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 70 GFRFQ-GDLRRNVQMVFQDPYASLHPNHTLWRTLAEPLQIH----GIRDVAPRVTTALEQVGLAADAVRRYPHQLSGGQR 144
Cdd:PRK15079 88 MKDDEwRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYhpklSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 145 QRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFM 212
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-226 |
1.99e-55 |
|
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: 184.72 E-value: 1.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTF--GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQR---EWRGSVDLLGQAITPgfRFQGD 76
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLE--LSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 LRRNVQMVFQDPYASLHPnHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALL 154
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGLsrAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523681378 155 LRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREAL 226
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
4.17e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 177.21 E-value: 4.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT---PGfrfqgdl 77
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPE------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQDpYAsLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARAlll 155
Cdd:COG3842 76 KRNVGMVFQD-YA-LFPHLTVAENVAFGLRMRGVpkAEIRARVAELLELVGLEGLA-DRYPHQLSGGQQQRVALARAlap 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 156 rpqilllDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHD-ADVIAhMSDRAAFMAEGVIQ 218
Cdd:COG3842 153 eprvlllDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqEEALA-LADRIAVMNDGRIE 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-220 |
2.14e-53 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 171.16 E-value: 2.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfqgDL---RRNVQ 82
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-------GVppeRRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPyaSLHPNHTLWRTLAEPLQIHGIR--DVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQIL 160
Cdd:cd03259 76 MVFQDY--ALFPHLTVAENIAFGLKLRGVPkaEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 161 LLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRF 220
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-215 |
9.99e-52 |
|
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: 165.44 E-value: 9.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDLRRNVQM 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDPyaslhpnhTLWRTLaeplqihgirdvaprvtTALEQVGLAadavrryphqLSGGQRQRVAIARALLLRPQILLLD 163
Cdd:cd03229 81 VFQDF--------ALFPHL-----------------TVLENIALG----------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 523681378 164 EPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-208 |
1.44e-51 |
|
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: 166.49 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFG----AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfqgDLRRNV 81
Cdd:cd03293 3 VRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-------GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDPyaSLHPnhtlWRTLAE----PLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLL 155
Cdd:cd03293 76 GYVFQQD--ALLP----WLTVLDnvalGLELQGVpkAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 156 RPQILLLDEPTSALD----MSVQAEILNLLnrlkQEHGMTYLLVSHDADVIAHMSDR 208
Cdd:cd03293 149 DPDVLLLDEPFSALDaltrEQLQEELLDIW----RETGKTVLLVTHDIDEAVFLADR 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-220 |
7.01e-51 |
|
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: 165.10 E-value: 7.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfrfQGDLRRNVQM 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN----LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDpYAsLHPNHTLWRTLAEPLQIHGIR--DVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQILL 161
Cdd:cd03300 77 VFQN-YA-LFPHLTVFENIAFGLRLKKLPkaEIKERVAEALDLVQLEGYA-NRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 162 LDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRF 220
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQI 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-217 |
9.03e-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: 165.06 E-value: 9.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAK----TAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQG--- 75
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT---LLSGkel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 -DLRRNVQMVFQdpyaslHPNhTLW-RTLAE----PLQIHGIR--DVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRV 147
Cdd:cd03258 78 rKARRRIGMIFQ------HFN-LLSsRTVFEnvalPLEIAGVPkaEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 148 AIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-219 |
4.46e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 162.91 E-value: 4.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTFG----AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT-------PG 70
Cdd:COG1136 3 PLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslserelAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 71 FRfqgdlRRNVQMVFQDPYasLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVA 148
Cdd:COG1136 83 LR-----RRHIGFVFQFFN--LLPELTALENVALPLLLAGVsrKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 149 IARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADvIAHMSDRAAFMAEGVIQR 219
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVS 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
1.04e-49 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 162.95 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTF----GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfrfqgd 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 LRRNVQMVFQDPyaSLHPnhtlWRTLAE----PLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIA 150
Cdd:COG1116 78 PGPDRGVVFQEP--ALLP----WLTVLDnvalGLELRGVpkAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 151 RALLLRPQILLLDEPTSALD----MSVQAEILNLLnrlkQEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDaltrERLQDELLRLW----QETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-217 |
2.28e-49 |
|
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: 160.73 E-value: 2.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGA----KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT-PGFRFQGDLR 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISkLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 79 R-NVQMVFQDPYasLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLL 155
Cdd:cd03255 81 RrHIGFVFQSFN--LLPDLTALENVELPLLLAGVpkKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523681378 156 RPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADvIAHMSDRAAFMAEGVI 217
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-231 |
4.91e-49 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 169.65 E-value: 4.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 18 AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFRFQGdLRRNVQMVFQDPYASLHPN 95
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlSPGKLQA-LRRDIQFIFQDPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 96 HTLWRTLAEPLQIHGIRD---VAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMS 172
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPgkaAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 173 VQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALV-NGEH 231
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFeNPQH 557
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-231 |
9.67e-49 |
|
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: 160.14 E-value: 9.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP-GFRFQGDLRRN 80
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQMVFQDP--YASLhpnhTLWRTLAEPLQIHG------IRDvapRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARA 152
Cdd:COG1127 84 IGMLFQGGalFDSL----TVFENVAFPLREHTdlseaeIRE---LVLEKLELVGLP-GAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 153 lllrpqilllDEPTSALD--MSvqAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALVNGE 230
Cdd:COG1127 156 laldpeillyDEPTAGLDpiTS--AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
.
gi 523681378 231 H 231
Cdd:COG1127 234 D 234
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-219 |
2.00e-48 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 160.00 E-value: 2.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTF---------GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPG- 70
Cdd:COG4167 2 SALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 71 --FRFQgdlrrNVQMVFQDPYASLHPNHTLWRTLAEPLQIHGIRDVAPR---VTTALEQVGLAADAVRRYPHQLSGGQRQ 145
Cdd:COG4167 82 ykYRCK-----HIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEReerIFATLRLVGLLPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 146 RVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEG-VIQR 219
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGeVVEY 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-223 |
3.73e-48 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 158.23 E-value: 3.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDLRRNVQ 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDpyASLHPNHTLWR--TLAePLQIHGI-RDVA-PRVTTALEQVGLA--ADAvrrYPHQLSGGQRQRVAIARALLLR 156
Cdd:COG1126 81 MVFQQ--FNLFPHLTVLEnvTLA-PIKVKKMsKAEAeERAMELLERVGLAdkADA---YPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 157 PQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI------QRFFDR 223
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIveegppEEFFEN 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-217 |
7.87e-47 |
|
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: 154.22 E-value: 7.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDLRRNVQM 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDpyASLHPNHTLWRTLAE-PLQIHGI--RDVAPRVTTALEQVGLA--ADAvrrYPHQLSGGQRQRVAIARALLLRPQ 158
Cdd:cd03262 81 VFQQ--FNLFPHLTVLENITLaPIKVKGMskAEAEERALELLEKVGLAdkADA---YPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 159 ILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-217 |
9.79e-47 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 157.55 E-value: 9.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAK----TAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFRFQgD 76
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalSERELR-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 LRRNVQMVFQdpyaslHPNhTLW-RTLAE----PLQIHGI--RDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAI 149
Cdd:COG1135 80 ARRKIGMIFQ------HFN-LLSsRTVAEnvalPLEIAGVpkAEIRKRVAELLELVGLSDKA-DAYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 150 ARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-217 |
2.85e-46 |
|
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: 153.43 E-value: 2.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP-GFRFQGDLRRNVQ 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDP--YASLhpnhTLWRTLAEPLQIHG------IRDvapRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALL 154
Cdd:cd03261 81 MLFQSGalFDSL----TVFENVAFPLREHTrlseeeIRE---IVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 155 LRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-217 |
6.66e-46 |
|
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: 153.28 E-value: 6.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpGFRFQgDLRRNVQ 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSRR-ELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPYASL------------HPNHTLWRTLAEplqihgiRDVApRVTTALEQVGLAADAVRRYpHQLSGGQRQRVAIA 150
Cdd:COG1120 79 YVPQEPPAPFgltvrelvalgrYPHLGLFGRPSA-------EDRE-AVEEALERTGLEHLADRPV-DELSGGERQRVLIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 151 RALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-217 |
6.89e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.51 E-value: 6.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfrFQG-DLRRNVQMV 84
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA---MPPpEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 85 FQDPYaslhpnhtLWRT-----LAEPLQIHGIRDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQI 159
Cdd:COG4619 80 PQEPA--------LWGGtvrdnLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 160 LLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-217 |
6.91e-46 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 153.69 E-value: 6.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 14 GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQ-GDLRRNVQMVFQDPYASL 92
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrKAFRRDIQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 93 HPNHTLWRTLAEPLQiHGI----RDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSA 168
Cdd:PRK10419 103 NPRKTVREIIREPLR-HLLsldkAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523681378 169 LDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-217 |
6.91e-45 |
|
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: 151.11 E-value: 6.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 14 GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGD-LRRNVQMVFQDPYASL 92
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRaFRRDVQLVFQDSPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 93 HPNHTLWRTLAEPLQIHGIRDVA---PRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSAL 169
Cdd:TIGR02769 102 NPRMTVRQIIGEPLRHLTSLDESeqkARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 170 DMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-219 |
7.25e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 149.43 E-value: 7.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 14 GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP-GFRFQGDLRRNVQMVFQDpyASL 92
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRRIGVVFQD--FRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 93 HPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALD 170
Cdd:COG2884 91 LPDRTVYENVALPLRVTGKsrKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523681378 171 MSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQR 219
Cdd:COG2884 170 PETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-202 |
7.52e-45 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 156.79 E-value: 7.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTF-----------GAKTAVSAASFRVDAGETFSLIGASGCGKST----ILRVLAGlqrewRGSVDLLGQAI 67
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 68 TPGFRFQG-DLRRNVQMVFQDPYASLHPNHTLWRTLAEPLQIH----GIRDVAPRVTTALEQVGLAADAVRRYPHQLSGG 142
Cdd:PRK15134 350 HNLNRRQLlPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqptlSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGG 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 143 QRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVI 202
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVV 489
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-218 |
1.97e-44 |
|
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: 148.17 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfqgDLR---RN 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-------DLPpkdRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQMVFQDpYAsLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAAdAVRRYPHQLSGGQRQRVAIARALLLRPQ 158
Cdd:cd03301 74 IAMVFQN-YA-LYPHMTVYDNIAFGLKLRKVpkDEIDERVREVAELLQIEH-LLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 159 ILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQ 218
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-234 |
5.88e-44 |
|
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: 147.48 E-value: 5.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTF-GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdLRRNVQ 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE--LRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPYASL-HPnhTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLA--ADavrRYPHQLSGGQRQRVAIARALLLRP 157
Cdd:COG1122 79 LVFQNPDDQLfAP--TVEEDVAFGPENLGLprEEIRERVEEALELVGLEhlAD---RPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 158 QILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFD-REALVNGEHRMR 234
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTpREVFSDYELLEE 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-226 |
1.66e-43 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 146.17 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGL-----QREWRGSVDLLGQAITPGFRFQGDLR 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 79 RNVQMVFQDPY---ASLHPNhtlwrtLAEPLQIHGIRD---VAPRVTTALEQVGLAADAVRR-YPHQLSGGQRQRVAIAR 151
Cdd:cd03260 81 RRVGMVFQKPNpfpGSIYDN------VAYGLRLHGIKLkeeLDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 152 ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhgMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREAL 226
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-217 |
7.56e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.82 E-value: 7.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRfqgDLRRNVQM 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA---EVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDPyaSLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILL 161
Cdd:COG1131 78 VPQEP--ALYPDLTVRENLRFFARLYGLprKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 162 LDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-215 |
8.91e-43 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 151.40 E-value: 8.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTF----GAKTAVSAASFRVDAGETFSLIGASGCGKS----TILRVLAGLQREW-RGSVDLLGQAI--TP 69
Cdd:PRK15134 3 QPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYpSGDIRFHGESLlhAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 70 GFRFQGDLRRNVQMVFQDPYASLHPNHTLWRTLAEPLQIH-GIRDVAPR--VTTALEQVGL--AADAVRRYPHQLSGGQR 144
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHrGMRREAARgeILNCLDRVGIrqAAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 145 QRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-215 |
1.09e-42 |
|
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: 143.38 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdLRRNVQMVFQDPYASLHpNHTLWRTL 102
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE--LRRKVGLVFQNPDDQFF-GPTVEEEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 103 AEPLQIHGI--RDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNL 180
Cdd:cd03225 98 AFGLENLGLpeEEIEERVEEALELVGLEGLR-DRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 523681378 181 LNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:cd03225 177 LKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-217 |
2.40e-42 |
|
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: 143.34 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTF----GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP-------G 70
Cdd:COG4181 7 PIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedaraR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 71 FRfqgdlRRNVQMVFQdpyaSLH--PNHTLWRTLAEPLQIHGIRDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVA 148
Cdd:COG4181 87 LR-----ARHVGFVFQ----SFQllPTLTALENVMLPLELAGRRDARARARALLERVGLGHRL-DHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 149 IARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADvIAHMSDRAAFMAEGVI 217
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGRL 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-218 |
5.50e-42 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 146.25 E-value: 5.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfqgDL--- 77
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-------HVpae 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQDpYAsLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAVRRyPHQLSGGQRQRVAIARALLL 155
Cdd:PRK09452 85 NRHVNTVFQS-YA-LFPHMTVFENVAFGLRMQKTpaAEITPRVMEALRMVQLEEFAQRK-PHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 156 RPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQ 218
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-217 |
7.98e-42 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 140.26 E-value: 7.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAItpgfrfqgdlrrnvqmvf 85
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 qdpyASLHPnhtlwRTLAeplqihgiRDVApRVTTALEQVGLAADAVRRYpHQLSGGQRQRVAIARALLLRPQILLLDEP 165
Cdd:cd03214 64 ----ASLSP-----KELA--------RKIA-YVPQALELLGLAHLADRPF-NELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 523681378 166 TSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-218 |
1.17e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.83 E-value: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfqgDL--- 77
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-------DLppk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQDpYAsLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLL 155
Cdd:COG3839 74 DRNIAMVFQS-YA-LYPHMTVYENIAFPLKLRKVpkAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 156 RPQILLLDEPTSALD----MSVQAEILnllnRLKQEHGMTYLLVSHD-ADVIAhMSDRAAFMAEGVIQ 218
Cdd:COG3839 151 EPKVFLLDEPLSNLDaklrVEMRAEIK----RLHRRLGTTTIYVTHDqVEAMT-LADRIAVMNDGRIQ 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-225 |
4.81e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 139.89 E-value: 4.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 5 NLQDLQVTFGAKTAvsAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT---PGfrfqgdlRRNV 81
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTalpPA-------ERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDpyASLHPNHTLWRTLAepLQIH-GIRDVAP---RVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRP 157
Cdd:COG3840 74 SMLFQE--NNLFPHLTVAQNIG--LGLRpGLKLTAEqraQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 158 QILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI------QRFFDREA 225
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIaadgptAALLDGEP 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-215 |
3.78e-40 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 140.24 E-value: 3.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTF----GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLqrewrgsvdLLGQAITPG-FRFQG 75
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL---------LAANGRIGGsATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 D------------LR-RNVQMVFQDPYASLHPNHTLWRTLAEPLQIHGIRDVAprvtTALEQVGLAADAV---------R 133
Cdd:PRK09473 81 ReilnlpekelnkLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKA----EAFEESVRMLDAVkmpearkrmK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 134 RYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMA 213
Cdd:PRK09473 157 MYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMY 236
|
..
gi 523681378 214 EG 215
Cdd:PRK09473 237 AG 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-217 |
1.53e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 139.17 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAK----TAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT----PGFRfqgDL 77
Cdd:PRK11153 4 LKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalseKELR---KA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQdpyaslHPNHTLWRTLAE----PLQIHGI--RDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIAR 151
Cdd:PRK11153 81 RRQIGMIFQ------HFNLLSSRTVFDnvalPLELAGTpkAEIKARVTELLELVGLSDKA-DRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 152 ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-222 |
8.45e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.80 E-value: 8.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTF-GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQG----D 76
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVT---ALRGralrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 LRRNVQMVFQDPY---------ASLH---PNHTLWRTLaepLQIHGIRDVApRVTTALEQVGLAADAVRRyPHQLSGGQR 144
Cdd:COG3638 78 LRRRIGMIFQQFNlvprlsvltNVLAgrlGRTSTWRSL---LGLFPPEDRE-RALEALERVGLADKAYQR-ADQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 145 QRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIqrFFD 222
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--VFD 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
1.36e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.06 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRF------Q 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyvpqR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 75 GDLRRN--------VQMvfqdpyaSLHPNHTLWRTLaeplqihGIRDVApRVTTALEQVGLAADAVRRYpHQLSGGQRQR 146
Cdd:COG1121 84 AEVDWDfpitvrdvVLM-------GRYGRRGLFRRP-------SRADRE-AVDEALERVGLEDLADRPI-GELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 147 VAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI-----QRFF 221
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVahgppEEVL 226
|
....*
gi 523681378 222 DREAL 226
Cdd:COG1121 227 TPENL 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-220 |
2.56e-38 |
|
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: 133.23 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVnLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfQGDLR-R 79
Cdd:cd03296 1 MSIE-VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-----DVPVQeR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 80 NVQMVFQDpYAsLHPNHTLWRTLAEPLQIHGIRDVAP------RVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARAL 153
Cdd:cd03296 75 NVGFVFQH-YA-LFRHMTVFDNVAFGLRVKPRSERPPeaeiraKVHELLKLVQLDWLA-DRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 154 LLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRF 220
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQV 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-217 |
3.11e-38 |
|
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: 133.92 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 13 FGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQ-GDLRRN-VQMVFQDpyA 90
Cdd:cd03294 34 TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElRELRRKkISMVFQS--F 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 91 SLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSA 168
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGVprAEREERAAEALELVGLEGWE-HKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523681378 169 LDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03294 191 LDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-217 |
3.69e-38 |
|
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: 134.93 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 34 LIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFRfqgdlrRNVQMVFQDpYAsLHPNHTLWRTLAEPLQIHGI 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTnvPPHL------RHINMVFQS-YA-LFPHMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 112 --RDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHG 189
Cdd:TIGR01187 73 prAEIKPRVLEALRLVQLEEFA-DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180
....*....|....*....|....*...
gi 523681378 190 MTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKI 179
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-212 |
1.83e-37 |
|
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: 130.04 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQ-AITPGFRFQGDLRRN-VQM 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQeTPPLNSKKASKFRREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDpYAsLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADaVRRYPHQLSGGQRQRVAIARALLLRPQILL 161
Cdd:TIGR03608 81 LFQN-FA-LIENETVEENLDLGLKYKKLskKEKREKKKEALEKVGLNLK-LKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 523681378 162 LDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDAdVIAHMSDRAAFM 212
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-217 |
5.91e-37 |
|
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: 127.51 E-value: 5.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAItpgFRFQGDLRRNVQM 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI---KKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDPyaSLHPNHTLWRTLaeplqihgirdvaprvttaleqvglaadavrryphQLSGGQRQRVAIARALLLRPQILLLD 163
Cdd:cd03230 78 LPEEP--SLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523681378 164 EPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-217 |
6.99e-37 |
|
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: 130.26 E-value: 6.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKT-----AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQG-DL 77
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQdpyaslHPNHTLW-RTLAEplqihgirDVA--P------------RVTTALEQVGLAADAVRRYPHQLSGG 142
Cdd:TIGR04521 81 RKKVGLVFQ------FPEHQLFeETVYK--------DIAfgPknlglseeeaeeRVKEALELVGLDEEYLERSPFELSGG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 143 QRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:TIGR04521 147 QMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-215 |
8.01e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 126.59 E-value: 8.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdLRRNVQMVF 85
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE--LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QdpyaslhpnhtlwrtlaeplqihgirdvaprvttaleqvglaadavrryphqLSGGQRQRVAIARALLLRPQILLLDEP 165
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 523681378 166 TSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-217 |
1.22e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.42 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVnLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQ----AITPGfrfqgd 76
Cdd:COG1118 1 MSIE-VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftNLPPR------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 lRRNVQMVFQDpYAsLHPNHTLWRTLAEPLQI--HGIRDVAPRVTTALEQVGLA--ADavrRYPHQLSGGQRQRVAIARA 152
Cdd:COG1118 74 -ERRVGFVFQH-YA-LFPHMTVAENIAFGLRVrpPSKAEIRARVEELLELVQLEglAD---RYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 153 LLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-208 |
1.65e-36 |
|
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: 127.91 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 17 TAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGD----LRRNVQMVFQDpyASL 92
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS---DLRGRaipyLRRKIGVVFQD--FRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 93 HPNHTLWRTLAEPLQI--HGIRDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALD 170
Cdd:cd03292 90 LPDRNVYENVAFALEVtgVPPREIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 523681378 171 MSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDR 208
Cdd:cd03292 169 PDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHR 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-218 |
3.94e-36 |
|
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: 126.64 E-value: 3.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 29 GETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGfRFQGDL---RRNVQMVFQDpyASLHPNHTLWRTLAEP 105
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDS-RKKINLppqQRKIGLVFQQ--YALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 106 LQIHGIRDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLK 185
Cdd:cd03297 100 LKRKRNREDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIK 178
|
170 180 190
....*....|....*....|....*....|...
gi 523681378 186 QEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQ 218
Cdd:cd03297 179 KNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-222 |
7.80e-36 |
|
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: 126.91 E-value: 7.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGA-KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFRFQgDLRRNVQ 82
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALR-QLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDP------------YASLHPNHTLWRTLAEPLQIHGIRdvapRVTTALEQVGLAADAVRRyPHQLSGGQRQRVAIA 150
Cdd:cd03256 82 MIFQQFnlierlsvlenvLSGRLGRRSTWRSLFGLFPKEEKQ----RALAALERVGLLDKAYQR-ADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523681378 151 RALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIqrFFD 222
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI--VFD 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-233 |
2.75e-35 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 126.06 E-value: 2.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 18 AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPG---FRFQgdlrrNVQMVFQDPYASLHP 94
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdysYRSQ-----RIRMIFQDPSTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 95 NHTLWRTLAEPLQIHGIRDVAPR---VTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDM 171
Cdd:PRK15112 103 RQRISQILDFPLRLNTDLEPEQRekqIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 172 SVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEG-VIQRFFDREALVNGEHRM 233
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGeVVERGSTADVLASPLHEL 245
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-217 |
3.79e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 127.17 E-value: 3.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKT----AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLqrewrgsVDLLGQAITPGFRFQG- 75
Cdd:PRK11022 1 MALLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-------IDYPGRVMAEKLEFNGq 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 DLRR------------NVQMVFQDPYASLHPNHTLWRTLAEPLQIHGIRDVAPRVTTALE---QVGLAADAVRR--YPHQ 138
Cdd:PRK11022 74 DLQRisekerrnlvgaEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDllnQVGIPDPASRLdvYPHQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 139 LSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-167 |
7.43e-35 |
|
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: 121.60 E-value: 7.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRfqGDLRRNVQMVFQDPyaSLHPNHTLWRTL 102
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER--KSLRKEIGYVFQDP--QLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 103 AEPLQIHGIRDVAP--RVTTALEQVGL---AADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTS 167
Cdd:pfam00005 81 RLGLLLKGLSKREKdaRAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-220 |
1.84e-34 |
|
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: 123.18 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 10 QVTF---GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfQGD---LRRNVQM 83
Cdd:cd03295 5 NVTKrygGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-----EQDpveLRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDpyASLHPNHTLWRTLAEPLQIHG-----IRDvapRVTTALEQVGL-AADAVRRYPHQLSGGQRQRVAIARALLLRP 157
Cdd:cd03295 80 VIQQ--IGLFPHMTVEENIALVPKLLKwpkekIRE---RADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 158 QILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRF 220
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
10-208 |
2.66e-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: 121.97 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 10 QVTF---GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGD----LRRNVQ 82
Cdd:TIGR02673 6 NVSKaypGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVN---RLRGRqlplLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDpyASLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQIL 160
Cdd:TIGR02673 83 VVFQD--FRLLPDRTVYENVALPLEVRGKkeREIQRRVGAALRQVGLE-HKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 161 LLDEPTSALDMSVQAEILNLLNRLKQeHGMTYLLVSHDADVIAHMSDR 208
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHR 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-217 |
3.60e-34 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.49 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQaitpgfrFQGDLRRNVQMVF 85
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-------PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QDPYASLHPNHTLWRTLAEPLQIHGI------RDVAPRVTTALEQVGLAADAVRRYpHQLSGGQRQRVAIARALLLRPQI 159
Cdd:cd03235 75 QRRSIDRDFPISVRDVVLMGLYGHKGlfrrlsKADKAKVDEALERVGLSELADRQI-GELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 160 LLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
13-219 |
8.36e-34 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 121.45 E-value: 8.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 13 FGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfQGDLR-RNVQMVFQDpYAs 91
Cdd:TIGR00968 10 FGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDAT-----RVHARdRKIGFVFQH-YA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 92 LHPNHTLWRTLAEPLQI--HGIRDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSAL 169
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIrkHPKAKIKARVEELLELVQLEGLG-DRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 523681378 170 DMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQR 219
Cdd:TIGR00968 162 DAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQ 211
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
4-215 |
8.42e-34 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 124.34 E-value: 8.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQRE--WRGSVDLLGQAIT--PGFRfqgdlrR 79
Cdd:TIGR03258 6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLThaPPHK------R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 80 NVQMVFQDpYAsLHPNHTLWRTLAEPL--QIHGIRDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRP 157
Cdd:TIGR03258 80 GLALLFQN-YA-LFPHLKVEDNVAFGLraQKMPKADIAERVADALKLVGLG-DAAAHLPAQLSGGMQQRIAIARAIAIEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 158 QILLLDEPTSALDMSVQAEILNLLNRLKQE-HGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:TIGR03258 157 DVLLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDG 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-217 |
1.40e-33 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 121.32 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVdLLGQAITpgfrfqGDLRRNVQMVF 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPL------AEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QDpyASLHPnhtlWRTLAEPLQIhGIR-DVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:PRK11247 88 QD--ARLLP----WKKVIDNVGL-GLKgQWRDAALQALAAVGLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 523681378 165 PTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-217 |
1.75e-33 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 120.96 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 19 VSAASFRVDAGETFSLIGASGCGKS----TILRVLAGLQREWRGSVDLLGQAITPGfrfqgDLR-RNVQMVFQDPYASLH 93
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPC-----ALRgRKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 94 PNHTLWRTLAEPLQIHGIRDVAPRVTTALEQVGLAADA--VRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDM 171
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 523681378 172 SVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-217 |
3.67e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.81 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDLRRNVQ 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPYasLHPNHTLWRTLA-EPLQIHGI-RDVAPRVTTAL-EQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQI 159
Cdd:PRK09493 81 MVFQQFY--LFPHLTALENVMfGPLRVRGAsKEEAEKQARELlAKVGLAERA-HHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 160 LLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-215 |
3.82e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 123.02 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQ--AITPGFRfqgdlrRN 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlSHVPPYQ------RP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQMVFQDpYAsLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAVRRyPHQLSGGQRQRVAIARALLLRPQ 158
Cdd:PRK11607 93 INMMFQS-YA-LFPHMTVEQNIAFGLKQDKLpkAEIASRVNEMLGLVHMQEFAKRK-PHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 159 ILLLDEPTSALDMSV----QAEILNLLNRLkqehGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK11607 170 LLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-217 |
3.97e-33 |
|
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: 119.96 E-value: 3.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 5 NLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRfqgDLRRNVQMV 84
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR---EARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 85 FQDPYasLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAVRRYpHQLSGGQRQRVAIARALLLRPQILLL 162
Cdd:COG4555 80 PDERG--LYDRLTVRENIRYFAELYGLfdEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 163 DEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-217 |
4.10e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 120.23 E-value: 4.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 11 VTF----GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLG-QAITPGFRFqgDLRRNVQMVF 85
Cdd:TIGR04520 6 VSFsypeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLW--EIRKKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QDPyaslhpNHTLWRTLAEplqihgiRDVA--------------PRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIAR 151
Cdd:TIGR04520 84 QNP------DNQFVGATVE-------DDVAfglenlgvpreemrKRVDEALKLVGME-DFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 152 ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADViAHMSDRAAFMAEGVI 217
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEE-AVLADRVIVMNKGKI 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-222 |
5.08e-33 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 119.71 E-value: 5.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFG-AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQG----DL 77
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDIT---KLRGkklrKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQDpYA----------SLHPN---HTLWRTLAEPLQIHGIRdvapRVTTALEQVGLAADAVRRyPHQLSGGQR 144
Cdd:TIGR02315 78 RRRIGMIFQH-YNlierltvlenVLHGRlgyKPTWRSLLGRFSEEDKE----RALSALERVGLADKAYQR-ADQLSGGQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 145 QRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIqrFFD 222
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI--VFD 227
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
23-215 |
5.16e-33 |
|
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: 118.99 E-value: 5.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAI-TPGFRFQGDLR-RNVQMVFQdpYASLHPNHTLWR 100
Cdd:TIGR02211 25 SLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsKLSSNERAKLRnKKLGFIYQ--FHHLLPDFTALE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 101 TLAEPLQIHG--IRDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEIL 178
Cdd:TIGR02211 103 NVAMPLLIGKksVKEAKERAYEMLEKVGLE-HRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIF 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 523681378 179 NLLNRLKQEHGMTYLLVSHDADVIAHMsDRAAFMAEG 215
Cdd:TIGR02211 182 DLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-220 |
6.97e-33 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 121.75 E-value: 6.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 22 ASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAItpgfrFQGDL-------RRNVQMVFQDpyASLHP 94
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-----QDSARgiflpphRRRIGYVFQE--ARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 95 NHT--------LWRTLAeplqihgiRDVAPRVTTALEQVGLAAdAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPT 166
Cdd:COG4148 91 HLSvrgnllygRKRAPR--------AERRISFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523681378 167 SALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRF 220
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-217 |
7.64e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.96 E-value: 7.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIvNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAI----TPGFRFQGD 76
Cdd:PRK11124 1 MSI-QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfskTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 LRRNVQMVFQDpYaSLHPNHTLWRTLAE-PLQIHGI-RDVA-PRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARAL 153
Cdd:PRK11124 80 LRRNVGMVFQQ-Y-NLWPHLTVQQNLIEaPCRVLGLsKDQAlARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 154 LLRPQILLLDEPTSALDMSVQAEILNLLNRLkQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-227 |
1.21e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.35 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTF--GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFqgDLRRN 80
Cdd:PRK13635 5 IIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW--DVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQMVFQDPyaslhPNHTLWRTLAEP----LQIHGI-RD-VAPRVTTALEQVGLAADAVRRyPHQLSGGQRQRVAIARALL 154
Cdd:PRK13635 83 VGMVFQNP-----DNQFVGATVQDDvafgLENIGVpREeMVERVDQALRQVGMEDFLNRE-PHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 155 LRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHmSDRAAFM------AEGVIQRFFDR-EALV 227
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMnkgeilEEGTPEEIFKSgHMLQ 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-228 |
5.64e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 117.38 E-value: 5.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDL------ 77
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 -----RRNVQMVFQdpYASLHPNHTLWRTLAE-PLQIHGI--RDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAI 149
Cdd:PRK10619 86 qlrllRTRLTMVFQ--HFNLWSHMTVLENVMEaPIQVLGLskQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 150 ARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALVN 228
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-230 |
1.10e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 115.83 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQ---AITPGfrfqgdlRRNVQMVFQDpyASLHPNHTLW 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtTTPPS-------RRPVSMLFQE--NNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 100 RTLAepLQIH-GIR-DVAPR--VTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQA 175
Cdd:PRK10771 90 QNIG--LGLNpGLKlNAAQRekLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 176 EILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALVNGE 230
Cdd:PRK10771 167 EMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-215 |
1.35e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 116.29 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLqrewrgsVDLlgqaiTPGFRFQGD----- 76
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRM-------NDL-----IPGARVEGEilldg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 ------------LRRNVQMVFQdpyaslHPN---HTLWRTLAEPLQIHGIRD---VAPRVTTALEQVGL---AADAVRRY 135
Cdd:COG1117 78 ediydpdvdvveLRRRVGMVFQ------KPNpfpKSIYDNVAYGLRLHGIKSkseLDEIVEESLRKAALwdeVKDRLKKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 136 PHQLSGGQRQRVAIARALLLRPQILLLDEPTSALD-MSVQAeILNLLNRLKQEHgmTYLLVSHDADVIAHMSDRAAFMAE 214
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYL 228
|
.
gi 523681378 215 G 215
Cdd:COG1117 229 G 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-215 |
1.47e-31 |
|
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: 118.29 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 22 ASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGfRFQGDL---RRNVQMVFQDpyASLHPNHTL 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDS-RKGIFLppeKRRIGYVFQE--ARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 99 WRTLaeplqIHGIRDVAPRVTTA-----LEQVGLAAdAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSV 173
Cdd:TIGR02142 93 RGNL-----RYGMKRARPSERRIsfervIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 523681378 174 QAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-217 |
1.70e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 114.66 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRfqgdlRRNVQMVFQDPYASLHPNhTLWRTL 102
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER-----RKSIGYVMQDVDYQLFTD-SVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 103 AepLQIHGIRDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLN 182
Cdd:cd03226 94 L--LGLKELDAGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIR 170
|
170 180 190
....*....|....*....|....*....|....*
gi 523681378 183 RLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03226 171 ELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-233 |
2.20e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 115.40 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGL-----QREWRGSVDLLGQAItpgfrFQG 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDI-----FKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 D---LRRNVQMVFQDPYASlhPNHTLWRTLAEPLQIHGI----RDVAPRVTTALEQVGLAADAVRRY---PHQLSGGQRQ 145
Cdd:PRK14247 76 DvieLRRRVQMVFQIPNPI--PNLSIFENVALGLKLNRLvkskKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 146 RVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhgMTYLLVSHDADVIAHMSDRAAFMAEG-VIQRFFDRE 224
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGqIVEWGPTRE 231
|
....*....
gi 523681378 225 ALVNGEHRM 233
Cdd:PRK14247 232 VFTNPRHEL 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-215 |
2.84e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 120.73 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 18 AVSAASFRVDAGETFSLIGASGCGKS----TILRVL--AG---------LQREWRGSVDLLGQAITPGFRFQGdlrRNVQ 82
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmlLRRRSRQVIELSEQSAAQMRHVRG---ADMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPYASLHPNHTLWRTLAEPLQIH---GIRDVAPRVTTALEQVGL--AADAVRRYPHQLSGGQRQRVAIARALLLRP 157
Cdd:PRK10261 108 MIFQEPMTSLNPVFTVGEQIAESIRLHqgaSREEAMVEAKRMLDQVRIpeAQTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 158 QILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-204 |
3.54e-31 |
|
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: 113.73 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGDLRRnv 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR---DAREDYRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDPYASLHPNHTLWRTLAEPLQIHGIRDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILL 161
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLA-GLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 523681378 162 LDEPTSALDMSVQAEILNLLNRLKQEHGMTyLLVSHDADVIAH 204
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQPLELAA 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-218 |
3.65e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.60 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFqgDLRRNVQMVFQDPyaslhPNH----TL 98
Cdd:PRK13650 27 SFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVW--DIRHKIGMVFQNP-----DNQfvgaTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 99 WRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAE 176
Cdd:PRK13650 100 EDDVAFGLENKGIphEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 523681378 177 ILNLLNRLKQEHGMTYLLVSHDADVIAhMSDRAAFMAEGVIQ 218
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVE 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-228 |
3.75e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 114.72 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIvNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAitpgFRFQGD---- 76
Cdd:COG4161 1 MSI-QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ----FDFSQKpsek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 ----LRRNVQMVFQDpYaSLHPNHTLWRTLAE-PLQIHGI-RDVA-PRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAI 149
Cdd:COG4161 76 airlLRQKVGMVFQQ-Y-NLWPHLTVMENLIEaPCKVLGLsKEQArEKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 150 ARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALVN 228
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-208 |
5.03e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 116.54 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTF----GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQRE-WRGSVDLlgqaitpgFRFQG 75
Cdd:COG4170 1 MPLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnWHVTADR--------FRWNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 -DL------------RRNVQMVFQDPYASLHPNHTLWRTLAEPL----------QIHGIRdvAPRVTTALEQVGLA--AD 130
Cdd:COG4170 73 iDLlklsprerrkiiGREIAMIFQEPSSCLDPSAKIGDQLIEAIpswtfkgkwwQRFKWR--KKRAIELLHRVGIKdhKD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 131 AVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDR 208
Cdd:COG4170 151 IMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADT 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-228 |
8.65e-31 |
|
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: 113.33 E-value: 8.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT-PGfrfqgdlrRNVQMVFQDpyASLHPnhtlWRT 101
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITePG--------PDRMVVFQN--YSLLP----WLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 102 LAE--PLQIHGIRDVAPR------VTTALEQVGLAAdAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSV 173
Cdd:TIGR01184 71 VREniALAVDRVLPDLSKserraiVEEHIALVGLTE-AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 174 QAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGV-----------IQRFFDREALVN 228
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPaanigqilevpFPRPRDRLEVVE 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-200 |
4.24e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.03 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGlqrewrgsvdllgqAITPGFRFQGDL-------- 77
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG--------------TLSPAFSASGEVllngrrlt 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 -----RRNVQMVFQDPYasLHPNHTLWRTL--AEPLQIHGiRDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIA 150
Cdd:COG4136 70 alpaeQRRIGILFQDDL--LFPHLSVGENLafALPPTIGR-AQRRARVEQALEEAGLAGFA-DRDPATLSGGQRARVALL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 523681378 151 RALLLRPQILLLDEPTSALDMSVQAEILNL-LNRLKQEHGMTyLLVSHDAD 200
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPA-LLVTHDEE 195
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-215 |
4.32e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 111.51 E-value: 4.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 13 FGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGD----LRRNVQMVFQDP 88
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIT---RLKNRevpfLRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 89 YasLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPT 166
Cdd:PRK10908 89 H--LLMDRTVYDNVAIPLIIAGAsgDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523681378 167 SALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-217 |
4.98e-30 |
|
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: 111.31 E-value: 4.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 7 QDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGDLRRNVQMVFQ 86
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV---REPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 87 DPyaSLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:cd03265 81 DL--SVDDELTGWENLYIHARLYGVpgAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 523681378 165 PTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-224 |
5.36e-30 |
|
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: 111.27 E-value: 5.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfrFQGDlRRNVQMVFQDpYAsLHPNHTLWRTL 102
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN---LPPE-KRDISYVPQN-YA-LFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 103 AEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNL 180
Cdd:cd03299 93 AYGLKKRKVdkKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 523681378 181 LNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDRE 224
Cdd:cd03299 172 LKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-217 |
8.76e-30 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 111.43 E-value: 8.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDL-------- 77
Cdd:COG4598 11 VRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELvpadrrql 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 ---RRNVQMVFQdpyaslhpNHTLW--RTLAE-----PLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQ 145
Cdd:COG4598 91 qriRTRLGMVFQ--------SFNLWshMTVLEnvieaPVHVLGRpkAEAIERAEALLAKVGLA-DKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523681378 146 RVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-217 |
8.88e-30 |
|
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: 116.01 E-value: 8.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTF-GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpGFRfQGDLRRNVQMV 84
Cdd:COG4988 339 LEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLD-PASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 85 FQDPY---ASLHPNHTLWRTLAEPLQIHgirdvaprvtTALEQVGLAaDAVRRYPH-----------QLSGGQRQRVAIA 150
Cdd:COG4988 417 PQNPYlfaGTIRENLRLGRPDASDEELE----------AALEAAGLD-EFVAALPDgldtplgeggrGLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 151 RALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHgmTYLLVSHDADVIAHMsDRAAFMAEGVI 217
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQA-DRILVLDDGRI 549
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-217 |
1.25e-29 |
|
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: 110.90 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFR------ 72
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglPPHRiarlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 73 ---FQ-----GDL--RRNVQMVFQdpyasLHPNHTLWRTLAE-PLQIHGIRDVAPRVTTALEQVGLAADAvRRYPHQLSG 141
Cdd:COG0411 82 artFQnprlfPELtvLENVLVAAH-----ARLGRGLLAALLRlPRARREEREARERAEELLERVGLADRA-DEPAGNLSY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 142 GQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-217 |
1.73e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.29 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 15 AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDLRRNVQMVFQDPYASLHp 94
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYPEYQLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 95 NHTLWRTLAEPLQIHGIRD--VAPRVTTALEQVGLAADAVR-RYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDM 171
Cdd:PRK13637 98 EETIEKDIAFGPINLGLSEeeIENRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 523681378 172 SVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-220 |
1.78e-29 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 111.72 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 14 GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfQGD---LRRNVQMVFQDpyA 90
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIR-----DLDpveLRRRIGYVIQQ--I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 91 SLHPNHTLWRTLAEPLQIHG-----IRDvapRVTTALEQVGLAADAVR-RYPHQLSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:COG1125 86 GLFPHMTVAENIATVPRLLGwdkerIRA---RVDELLELVGLDPEEYRdRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 165 PTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRF 220
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQY 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-217 |
5.58e-29 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 108.35 E-value: 5.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 26 VDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrFQGDLRRNVQMVFQD----PYASLHPNHTLWRT 101
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT----AAPPADRPVSMLFQEnnlfAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 102 laePlQIHGIRDVAPRVTTALEQVGLAADAVRRyPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLL 181
Cdd:cd03298 97 ---P-GLKLTAEDRQAIEVALARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 523681378 182 NRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-217 |
9.04e-29 |
|
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: 113.39 E-value: 9.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 10 QVTFG----AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSV-----DLlgQAITPGfrfqgDLRRN 80
Cdd:COG2274 478 NVSFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgiDL--RQIDPA-----SLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQMVFQDPY---ASLHPNHTLWRTLAEPLQIHgirdvaprvtTALEQVGLAADaVRRYPH-----------QLSGGQRQR 146
Cdd:COG2274 551 IGVVLQDVFlfsGTIRENITLGDPDATDEEII----------EAARLAGLHDF-IEALPMgydtvvgeggsNLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 147 VAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQehGMTYLLVSHDADVIAHmSDRAAFMAEGVI 217
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRI 687
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
9.73e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.80 E-value: 9.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFG----AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT-PGfrfqg 75
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgPG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 dLRRNVqmVFQDpyaslhpnHTL--WRTLAE----PLQIHGI-----RDVAPRVttaLEQVGLAaDAVRRYPHQLSGGQR 144
Cdd:COG4525 76 -ADRGV--VFQK--------DALlpWLNVLDnvafGLRLRGVpkaerRARAEEL---LALVGLA-DFARRRIWQLSGGMR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523681378 145 QRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHD 198
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-231 |
1.18e-28 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 110.28 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTF----GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQRE-WR--------GSVDLLgqAI 67
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnWRvtadrmrfDDIDLL--RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 68 TPGFRfQGDLRRNVQMVFQDPYASLHPNHTLWRTLAEPL----------QIHGIRdvAPRVTTALEQVGLAA--DAVRRY 135
Cdd:PRK15093 79 SPRER-RKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgrwwQRFGWR--KRRAIELLHRVGIKDhkDAMRSF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 136 PHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
250
....*....|....*.
gi 523681378 216 VIQRFFDREALVNGEH 231
Cdd:PRK15093 236 QTVETAPSKELVTTPH 251
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.19e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVnLQDLQVTFGAKT-----AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQG 75
Cdd:PRK13634 1 MDIT-FQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 --DLRRNVQMVFQDPYASLHpNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIAR 151
Cdd:PRK13634 80 lkPLRKKVGIVFQFPEHQLF-EETVEKDICFGPMNFGVseEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 152 ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQR 219
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-233 |
1.66e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.01 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 8 DLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRV---LAGLQREWR--GSVDLLGQAITPGFRFQGDLRRNVQ 82
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARveGEVRLFGRNIYSPDVDPIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQdpYASLHPNHTLWRTLAEPLQIHGI----RDVAPRVTTALEQVGL---AADAVRRYPHQLSGGQRQRVAIARALLL 155
Cdd:PRK14267 89 MVFQ--YPNPFPHLTIYDNVAIGVKLNGLvkskKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 156 RPQILLLDEPTSALDMSVQAEILNLLNRLKQEHgmTYLLVSHDADVIAHMSDRAAFMAEG-VIQRFFDREALVNGEHRM 233
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGkLIEVGPTRKVFENPEHEL 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-215 |
1.76e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.21 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPG---FRFQG-DLR 78
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGkdiFQIDAiKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 79 RNVQMVFQDPyaSLHPNHTLWRTLAEPLQIHGI---RDVAPRVTTALEQVGL---AADAVRRYPHQLSGGQRQRVAIARA 152
Cdd:PRK14246 90 KEVGMVFQQP--NPFPHLSIYDNIAYPLKSHGIkekREIKKIVEECLRKVGLwkeVYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 153 LLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhgMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-217 |
2.21e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.53 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSV---DLLGQAITPGFRFQG-- 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgDITIDTARSLSQQKGli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 -DLRRNVQMVFQDpyASLHPNHTLWRTLAE-PLQIHGI--RDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIAR 151
Cdd:PRK11264 81 rQLRQHVGFVFQN--FNLFPHRTVLENIIEgPVIVKGEpkEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 152 ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHgMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-215 |
3.25e-28 |
|
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: 104.77 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 11 VTF----GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRF-QGDLRRNVQMVF 85
Cdd:cd03228 6 VSFsypgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR---DLdLESLRKNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QDPYaslhpnhtLW-RTLAEPLqihgirdvaprvttaleqvglaadavrryphqLSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:cd03228 83 QDPF--------LFsGTIRENI--------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 523681378 165 PTSALDMSVQAEILNLLNRLKQehGMTYLLVSHDADVIAHMsDRAAFMAEG 215
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-215 |
4.68e-28 |
|
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: 106.37 E-value: 4.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpGFRFQGDLRRNVQMVF 85
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT-GLPPHEIARLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QDPyaSLHPNHTLWRTLAEPLQIHG------------IRDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARAL 153
Cdd:cd03219 82 QIP--RLFPELTVLENVMVAAQARTgsglllararreEREARERAEELLERVGLADLA-DRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523681378 154 LLRPQILLLDEPTSALDMSVQAEILNLLNRLKqEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-217 |
4.80e-28 |
|
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: 105.71 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdlrRNVQMVFQDpyASLHPNHTLWRTL 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ----RPVSMLFQE--NNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 103 AepLQIH-GIRDVA---PRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEIL 178
Cdd:TIGR01277 92 G--LGLHpGLKLNAeqqEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 523681378 179 NLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-217 |
5.51e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.65 E-value: 5.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdlrRNVQM 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ----RDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDpYAsLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLA--ADavrRYPHQLSGGQRQRVAIARALLLRPQI 159
Cdd:PRK11432 83 VFQS-YA-LFPHMSLGENVGYGLKMLGVpkEERKQRVKEALELVDLAgfED---RYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 160 LLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-219 |
6.19e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 6.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 13 FGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGDLRRnVQMVFQDpYAsL 92
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS---RLHARDRK-VGFVFQH-YA-L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 93 HPNHTLWRTLAeplqiHGIRdVAPR------------VTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQIL 160
Cdd:PRK10851 86 FRHMTVFDNIA-----FGLT-VLPRrerpnaaaikakVTQLLEMVQLAHLA-DRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 161 LLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQR 219
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-218 |
3.60e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.47 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 7 QDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDLRRNVQmvfq 86
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 87 dpyaslhPNHTlwrTLAEPLQIH------------GIRDVAPRVTTALEQVGLAADAVRRYPhQLSGGQRQRVAIARALL 154
Cdd:PRK13548 82 -------PQHS---SLSFPFTVEevvamgraphglSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 155 LRPQILLL------DEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQ 218
Cdd:PRK13548 151 QLWEPDGPprwlllDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
4.53e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.82 E-value: 4.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKT-AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfRFQGDLRRNV 81
Cdd:PRK13647 4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA--ENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDP----YASlhpnhTLWRTLAEPLQIHGIR--DVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLL 155
Cdd:PRK13647 82 GLVFQDPddqvFSS-----TVWDDVAFGPVNMGLDkdEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 156 RPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALVN 228
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-218 |
5.30e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 103.74 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP-GFRFQGDLRrNVQMVFQDPYASLHPNHTLWRT 101
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAELR-NQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 102 LAEPLQIHGIR--DVAPRVTTALEQVGLAADAVRRyPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILN 179
Cdd:PRK11629 108 VAMPLLIGKKKpaEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 523681378 180 LLNRLKQEHGMTYLLVSHDADVIAHMSdRAAFMAEGVIQ 218
Cdd:PRK11629 187 LLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLT 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-232 |
5.81e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.09 E-value: 5.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVL---AGLQRE--WRGSVDLLGQAITPGFRFQGD 76
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEvtITGSIVYNGHNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 LRRNVQMVFQDPyaslHP-NHTLWRTLAEPLQIHGIRDVApRVTTALEQVGLAA---DAVRRYPHQ----LSGGQRQRVA 148
Cdd:PRK14239 84 LRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQ-VLDEAVEKSLKGAsiwDEVKDRLHDsalgLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 149 IARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHgmTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFD-REALV 227
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDtKQMFM 236
|
....*
gi 523681378 228 NGEHR 232
Cdd:PRK14239 237 NPKHK 241
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-217 |
8.76e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 102.30 E-value: 8.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGDLRRNVQM 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ---KNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VfqdPYASLHPNHTLWRTLAEPLQIHGIRDvaPRVTTALEQVGLAADAVRRYpHQLSGGQRQRVAIARALLLRPQILLLD 163
Cdd:cd03268 78 I---EAPGFYPNLTARENLRLLARLLGIRK--KRIDEVLDVVGLKDSAKKKV-KGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523681378 164 EPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-218 |
9.13e-27 |
|
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: 102.58 E-value: 9.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 13 FGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRfqgDLRRNVQMVFQDpyasl 92
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK---AARQSLGYCPQF----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 93 hpnHTLWRTL--AEPLQIHGI------RDVAPRVTTALEQVGLAADAVRRyPHQLSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:cd03263 84 ---DALFDELtvREHLRFYARlkglpkSEIKEEVELLLRVLGLTDKANKR-ARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523681378 165 PTSALDMSVQAEILNLLNRLKQEHGMtyLLVSHDADVIAHMSDRAAFMAEGVIQ 218
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-217 |
4.46e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.08 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKT-AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDLRRNV 81
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDPYASLHPNHTLWRTLAEPLQIhGI--RDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQI 159
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVAFGPLNL-GLskEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 160 LLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-227 |
5.80e-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: 104.88 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQ-----VTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVD-LLGQ----AITPGFR 72
Cdd:TIGR03269 279 IIKVRNVSkryisVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDewvdMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 73 FQGDLRRNVQMVFQDpYaSLHPNHTLWRTLAEPLQIHGIRDVAPR-VTTALEQVGLAADAVR----RYPHQLSGGQRQRV 147
Cdd:TIGR03269 359 GRGRAKRYIGILHQE-Y-DLYPHRTVLDNLTEAIGLELPDELARMkAVITLKMVGFDEEKAEeildKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 148 AIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALV 227
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-220 |
6.23e-26 |
|
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: 99.96 E-value: 6.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGeTFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGDLRRNVQM 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL---KQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDPyaSLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILL 161
Cdd:cd03264 77 LPQEF--GVYPNFTVREFLDYIAWLKGIpsKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 162 LDEPTSALDMSVQAEILNLLNRLKQEHgmTYLLVSHDADVIAHMSDRAAFMAEGVIQRF 220
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-217 |
8.22e-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: 100.20 E-value: 8.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFRFqgdLRRNVQM 83
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglPPHER---ARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDP--YASLhpnhtlwrTLAEPLQIHGIRDVAPRVTTALEQVgLA-----ADAVRRYPHQLSGGQRQRVAIARALLLR 156
Cdd:cd03224 80 VPEGRriFPEL--------TVEENLLLGAYARRRAKRKARLERV-YElfprlKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 157 PQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
1.04e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.03 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTF-GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfRFQGDLRR 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK--ENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 80 NVQMVFQDPYASLHpNHTLWRTLA-EPLQIhGIRD--VAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLR 156
Cdd:PRK13652 79 FVGLVFQNPDDQIF-SPTVEQDIAfGPINL-GLDEetVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 157 PQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSD------RAAFMAEGVIQRFFDREALVNGE 230
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADyiyvmdKGRIVAYGTVEEIFLQPDLLARV 235
|
.
gi 523681378 231 H 231
Cdd:PRK13652 236 H 236
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-217 |
1.42e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 102.23 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKT-AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfqgDLR- 78
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-------ELEp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 79 --RNVQMVFQDpYAsLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAVRRyPHQLSGGQRQRVAIARALL 154
Cdd:PRK11650 74 adRDIAMVFQN-YA-LYPHMSVRENMAYGLKIRGMpkAEIEERVAEAARILELEPLLDRK-PRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 155 LRPQILLLDEPTSALD--MSVQ--AEILNLLNRLKQehgmTYLLVSHDaDVIAH-MSDRAAFMAEGVI 217
Cdd:PRK11650 151 REPAVFLFDEPLSNLDakLRVQmrLEIQRLHRRLKT----TSLYVTHD-QVEAMtLADRVVVMNGGVA 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-208 |
2.12e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 99.08 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 26 VDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQ-GDLR-RNVQMVFQDpyASLHPNHTLWRTLA 103
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArAKLRaKHVGFVFQS--FMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 104 EPLQIHGIRDVAPRVTTA--LEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLL 181
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKalLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170 180
....*....|....*....|....*..
gi 523681378 182 NRLKQEHGMTYLLVSHDADVIAHMSDR 208
Cdd:PRK10584 190 FSLNREHGTTLILVTHDLQLAARCDRR 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-217 |
8.00e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.01 E-value: 8.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 19 VSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFqgDLRRNVQMVFQDPYASLhPNHTL 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVW--NLRRKIGMVFQNPDNQF-VGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 99 WRTLAEPLQIHGI--RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAE 176
Cdd:PRK13642 100 EDDVAFGMENQGIprEEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 523681378 177 ILNLLNRLKQEHGMTYLLVSHDADVIAHmSDRAAFMAEGVI 217
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-215 |
9.75e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.16 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdLRRNVQ 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPYA----SLH--------PNHTLWRTLAEplqihgiRDVApRVTTALEQVGLAADAVRRYPhQLSGGQRQRVAIA 150
Cdd:PRK11231 80 LLPQHHLTpegiTVRelvaygrsPWLSLWGRLSA-------EDNA-RVNQAMEQTRINHLADRRLT-DLSGGQRQRAFLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 151 RALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANG 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-213 |
9.78e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.23 E-value: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT-PGfrfqgdLRRNV 81
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgPG------AERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 qmVFQDpyASLHPNHTLWRTLAEPLQIHGIrDVAPRVTTALE---QVGLAAdAVRRYPHQLSGGQRQRVAIARALLLRPQ 158
Cdd:PRK11248 75 --VFQN--EGLLPWRNVQDNVAFGLQLAGV-EKMQRLEIAHQmlkKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 159 ILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDAdviahmsDRAAFMA 213
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI-------EEAVFMA 196
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-217 |
1.11e-24 |
|
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: 101.38 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTF--GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfRFQGDLRRNV 81
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD--LDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDPY--ASlhpnhtlwrTLAEPLQIhgirdVAPRVT-----TALEQVGLAaDAVRRYPH-----------QLSGGQ 143
Cdd:COG4987 412 AVVPQRPHlfDT---------TLRENLRL-----ARPDATdeelwAALERVGLG-DWLAALPDgldtwlgeggrRLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 144 RQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLnrLKQEHGMTYLLVSHDADVIAHMsDRAAFMAEGVI 217
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLERM-DRILVLEDGRI 547
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-207 |
1.50e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.09 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTFGAKTAVSAASFRVDAGEtFSLI-GASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFRFqgdlR 78
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIY----R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 79 RNVQMVFQDPyaSLHpNHTLWRTLAEPLQIHGIRDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQ 158
Cdd:PRK10247 81 QQVSYCAQTP--TLF-GDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523681378 159 ILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSD 207
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADK 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-197 |
1.53e-24 |
|
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: 96.89 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 18 AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLG---QAITPGfrfqgDLRRNVQMVFQDP---YAS 91
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPA-----DLRRNIGYVPQDVtlfYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 92 LHPNHTLWRTLAEplqihgirDVapRVTTALEQVGLAaDAVRRYPH-----------QLSGGQRQRVAIARALLLRPQIL 160
Cdd:cd03245 94 LRDNITLGAPLAD--------DE--RILRAAELAGVT-DFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 523681378 161 LLDEPTSALDMSVQAEILNLLNRLKQehGMTYLLVSH 197
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITH 197
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
10-217 |
1.94e-24 |
|
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: 101.10 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 10 QVTF---GAKT-AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfQ---GDLRRNVQ 82
Cdd:TIGR03375 468 NVSFaypGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR-----QidpADLRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDP---YASLHPNHTLWRTLAEplqihgirDVapRVTTALEQVGLAaDAVRRYPH-----------QLSGGQRQRVA 148
Cdd:TIGR03375 543 YVPQDPrlfYGTLRDNIALGAPYAD--------DE--EILRAAELAGVT-EFVRRHPDgldmqigergrSLSGGQRQAVA 611
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 149 IARALLLRPQILLLDEPTSALDMSVQAEilnLLNRLKQE-HGMTYLLVSHDADVIAhMSDRAAFMAEGVI 217
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEER---FKDRLKRWlAGKTLVLVTHRTSLLD-LVDRIIVMDNGRI 677
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-215 |
1.99e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.98 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP--GFRFQGDLRRNVQMVFQDPYASLHPNHTLWR 100
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetGNKNLKKLRKKVSLVFQFPEAQLFENTVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 101 TLAEPLQIHGIRDVAP-RVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILN 179
Cdd:PRK13641 107 VEFGPKNFGFSEDEAKeKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 523681378 180 LLNRLkQEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK13641 187 LFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-217 |
2.79e-24 |
|
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: 94.42 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfqgdlrrnvqmvF 85
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----------------F 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QDPYASLHpnhtlwrtlaeplqiHGIRDVaprvttaleqvglaadavrrypHQLSGGQRQRVAIARALLLRPQILLLDEP 165
Cdd:cd03216 67 ASPRDARR---------------AGIAMV----------------------YQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 523681378 166 TSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-211 |
3.15e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.16 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 7 QDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQrewrgsvDLLgqaitPGFRFQGDL--------- 77
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLN-------DLI-----PGFRVEGKVtfhgknlya 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 --------RRNVQMVFQDPY---ASLHPNhtlwrtLAEPLQIHGIR-DVAPRVTTALEQVGL---AADAVRRYPHQLSGG 142
Cdd:PRK14243 82 pdvdpvevRRRIGMVFQKPNpfpKSIYDN------IAYGARINGYKgDMDELVERSLRQAALwdeVKDKLKQSGLSLSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 143 QRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHgmTYLLVSHDADVIAHMSDRAAF 211
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAF 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-198 |
4.19e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.56 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQRewrgsvdllgqaITPGFRFQGDLR-- 78
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED------------ITSGDLFIGEKRmn 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 79 ------RNVQMVFQDpYAsLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAVRRyPHQLSGGQRQRVAIA 150
Cdd:PRK11000 69 dvppaeRGVGMVFQS-YA-LYPHLSVAENMSFGLKLAGAkkEEINQRVNQVAEVLQLAHLLDRK-PKALSGGQRQRVAIG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 151 RALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHD 198
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-226 |
4.29e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.23 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKT-AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDLRRNV 81
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDPYASLHPNHTLWRTLAEPLQIHGIRD-VAPRVTTALEQVGLAAdaVRRYP-HQLSGGQRQRVAIARALLLRPQI 159
Cdd:PRK13636 85 GMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDeVRKRVDNALKRTGIEH--LKDKPtHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 160 LLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI-------QRFFDREAL 226
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVilqgnpkEVFAEKEML 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-231 |
5.67e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 95.92 E-value: 5.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRG-SVDLLGQaitpgfRFQG---- 75
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE------RRGGedvw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 DLRRNVQMVFQDPYASLHPNHT--------------LWRTLaEPLQIHgirdvapRVTTALEQVGLAADAVRRYpHQLSG 141
Cdd:COG1119 75 ELRKRIGLVSPALQLRFPRDETvldvvlsgffdsigLYREP-TDEQRE-------RARELLELLGLAHLADRPF-GTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 142 GQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFF 221
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
250
....*....|
gi 523681378 222 DREALVNGEH 231
Cdd:COG1119 226 PKEEVLTSEN 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-217 |
5.98e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.62 E-value: 5.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKT-----AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRF---QGDL 77
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikeVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQDPYASLHpNHTLWRTLA-EPLQI-HGIRDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLL 155
Cdd:PRK13645 89 RKEIGLVFQFPEYQLF-QETIEKDIAfGPVNLgENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523681378 156 RPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-217 |
6.81e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.36 E-value: 6.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP-GFRfqgDLRRNVQMVFQDPYASLhPNHTLWRT 101
Cdd:PRK13648 29 SFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFE---KLRKHIGIVFQNPDNQF-VGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 102 LAEPLQIHGI--RDVAPRVTTALEQVGLAADAVRRyPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILN 179
Cdd:PRK13648 105 VAFGLENHAVpyDEMHRRVSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 523681378 180 LLNRLKQEHGMTYLLVSHDADVIAHmSDRAAFMAEGVI 217
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-218 |
1.13e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 7 QDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGD--------LR 78
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA---AWSPWelarrravLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 79 RNVQMVFqdPYaslhpnhtlwrTLAE-------PLQIHGIRDVApRVTTALEQVGLAADAVRRYPhQLSGGQRQRVAIAR 151
Cdd:COG4559 82 QHSSLAF--PF-----------TVEEvvalgraPHGSSAAQDRQ-IVREALALVGLAHLAGRSYQ-TLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 152 ALLLRPQILLL-------DEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQ 218
Cdd:COG4559 147 VLAQLWEPVDGgprwlflDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-217 |
3.24e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 14 GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFRFQGDLRRNVQMVFQDpyAS 91
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkiSDAELREVRRKKIAMVFQS--FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 92 LHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSAL 169
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGInaEERREKALDALRQVGLENYA-HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 170 DMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-217 |
5.97e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.10 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTF--GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGL---QREWRGSVDLLGqaITPGFRFQGDL 77
Cdd:PRK13640 5 IVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDG--ITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQDPyaslhPNHTLWRTLAEplqihgirDVA--------PR------VTTALEQVGLAaDAVRRYPHQLSGGQ 143
Cdd:PRK13640 83 REKVGIVFQNP-----DNQFVGATVGD--------DVAfglenravPRpemikiVRDVLADVGML-DYIDSEPANLSGGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 144 RQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADViAHMSDRAAFMAEGVI 217
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKL 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
10-205 |
6.19e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 96.59 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 10 QVTF---GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFrfQGDLRRNVQMVFQ 86
Cdd:TIGR02857 326 GVSVaypGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD--ADSWRDQIAWVPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 87 DPYaslhpnhTLWRTLAEPLQiHGIRDVAP-RVTTALEQVGLAaDAVRRYP-----------HQLSGGQRQRVAIARALL 154
Cdd:TIGR02857 404 HPF-------LFAGTIAENIR-LARPDASDaEIREALERAGLD-EFVAALPqgldtpigeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 155 LRPQILLLDEPTSALDMSVQAEILNLLNRLKQehGMTYLLVSHD------ADVIAHM 205
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRlalaalADRIVVL 529
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-217 |
6.32e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.66 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIvNLQDLQVTFGAKT-----AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQG 75
Cdd:PRK13649 1 MGI-NLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 --DLRRNVQMVFQDPYASLHpNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIAR 151
Cdd:PRK13649 80 ikQIRKKVGLVFQFPESQLF-EETVLKDVAFGPQNFGVsqEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 152 ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-215 |
1.55e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.30 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 7 QDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQ-GDLRRNVQM-- 83
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAlSEAERRRLLrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 ----VFQDPYASLHPNHTLWRTLAEPLQIHG------IRDVAprvTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARAL 153
Cdd:PRK11701 90 ewgfVHQHPRDGLRMQVSAGGNIGERLMAVGarhygdIRATA---GDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523681378 154 LLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-221 |
1.83e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.46 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 16 KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAiTPGFRFQGDLRRNVQMVFQDPyaslhpN 95
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWDIRNKAGMVFQNP------D 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 96 HTLWRTLAEplqihgiRDVA--------------PRVTTALEQVGLAAdaVRRY-PHQLSGGQRQRVAIARALLLRPQIL 160
Cdd:PRK13633 96 NQIVATIVE-------EDVAfgpenlgippeeirERVDESLKKVGMYE--YRRHaPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 161 LLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSH------DADVIAHMsDRAAFMAEGVIQRFF 221
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHymeeavEADRIIVM-DSGKVVMEGTPKEIF 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-217 |
2.02e-22 |
|
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: 89.97 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRfqGDLRRNVQMVFQDpyASLHPNhtlwrTL 102
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP--NELGDHVGYLPQD--DELFSG-----SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 103 AEPLqihgirdvaprvttaleqvglaadavrryphqLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLN 182
Cdd:cd03246 93 AENI--------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*
gi 523681378 183 RLKqEHGMTYLLVSHDADVIAhMSDRAAFMAEGVI 217
Cdd:cd03246 141 ALK-AAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-207 |
3.38e-22 |
|
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: 90.75 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 11 VTFG---AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfRFQGDLRRNVQMVFQD 87
Cdd:cd03253 6 VTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE--VTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 88 pyaSLHPNHTLWrtlaeplqiHGIRDVAPRVTTalEQVGLAA------DAVRRYPHQ-----------LSGGQRQRVAIA 150
Cdd:cd03253 84 ---TVLFNDTIG---------YNIRYGRPDATD--EEVIEAAkaaqihDKIMRFPDGydtivgerglkLSGGEKQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 151 RALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQehGMTYLLVSH------DADVIAHMSD 207
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHrlstivNADKIIVLKD 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-215 |
3.47e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 34 LIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDLRRNVQMVFQDP-----YASLHPNhtlwrtLAEPLQI 108
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPeqqifYTDIDSD------IAFSLRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 109 HGI--RDVAPRVTTALEQVGlaADAVRRYPHQ-LSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLK 185
Cdd:PRK13638 106 LGVpeAEITRRVDEALTLVD--AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
170 180 190
....*....|....*....|....*....|
gi 523681378 186 QEhGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK13638 184 AQ-GNHVIISSHDIDLIYEISDAVYVLRQG 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-204 |
7.91e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 7.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTA-VSAASFRVDAGETFSLIGASGCGKSTILRVLAGLqreW---RGSVDLlgqaitPgfrfqgdlrRNV 81
Cdd:COG4178 365 LEDLTLRTPDGRPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL---WpygSGRIAR------P---------AGA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVF--QDPYAslhPNHTLWRTLAEPLQIHGIRDvaPRVTTALEQVGLAA-----DAVRRYPHQLSGGQRQRVAIARALL 154
Cdd:COG4178 427 RVLFlpQRPYL---PLGTLREALLYPATAEAFSD--AELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 523681378 155 LRPQILLLDEPTSALDMSVQAEILNLLNRlkQEHGMTYLLVSHDADVIAH 204
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAF 549
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-211 |
1.38e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.10 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVL---AGLQREWR--GSVDLLGQAITPGFRFQGDLR 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmNELESEVRveGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 79 RNVQMVFQDPyaSLHPnHTLWRTLAEPLQIHGIR---DVAPRVTTALEQVGLAaDAVRRYPHQ----LSGGQRQRVAIAR 151
Cdd:PRK14258 88 RQVSMVHPKP--NLFP-MSVYDNVAYGVKIVGWRpklEIDDIVESALKDADLW-DEIKHKIHKsaldLSGGQQQRLCIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 152 ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAF 211
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAF 223
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-217 |
1.86e-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: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 24 FRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGDLRRNVQMVFQDPYASLHPNHTLWRTLA 103
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 104 EPLQIHGIRDVAPrVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNR 183
Cdd:TIGR03771 81 GWLRRPCVADFAA-VRDALRRVGLTELA-DRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIE 158
|
170 180 190
....*....|....*....|....*....|....
gi 523681378 184 LKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:TIGR03771 159 LAGA-GTAILMTTHDLAQAMATCDRVVLLNGRVI 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-207 |
2.21e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 92.15 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 11 VTF---GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRF-QGDLRRNVQMVFQ 86
Cdd:COG1132 345 VSFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR---DLtLESLRRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 87 DPY---ASLHPNHTLWR---TLAEplqihgirdvaprVTTALEQVGlAADAVRRYPH-----------QLSGGQRQRVAI 149
Cdd:COG1132 422 DTFlfsGTIRENIRYGRpdaTDEE-------------VEEAAKAAQ-AHEFIEALPDgydtvvgergvNLSGGQRQRIAI 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 150 ARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQehGMTYLLVSH------DADVIAHMSD 207
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHrlstirNADRILVLDD 549
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-217 |
2.57e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 15 AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLlGQAITPGFRFQGDL---RRNVQMVFQDPYAS 91
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIkpvRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 92 LHpNHTLWRTLAEPLQIHGI-RDVAPRVTT-ALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSAL 169
Cdd:PRK13643 97 LF-EETVLKDVAFGPQNFGIpKEKAEKIAAeKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 170 DMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK13643 176 DPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-234 |
3.44e-21 |
|
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: 88.12 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFRF----- 73
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITglPPHRIarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 74 ----QGdlRRnvqmVFqdpyASLhpnhtlwrTLAEPLQIHG-IRDVAPRVTTALEQVglaadaVRRYP------HQ---- 138
Cdd:COG0410 81 gyvpEG--RR----IF----PSL--------TVEENLLLGAyARRDRAEVRADLERV------YELFPrlkerrRQragt 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 139 LSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQ 218
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIV 215
|
250
....*....|....*.
gi 523681378 219 RFFDREALVNGEHRMR 234
Cdd:COG0410 216 LEGTAAELLADPEVRE 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-217 |
3.72e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.07 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 16 KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFR--FQGDLRRNVQMVFQDPYASLH 93
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkYIRPVRKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 94 PNHTLWRTLAEP----LQIHGIRDVAPRVttaLEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSAL 169
Cdd:PRK13646 100 EDTVEREIIFGPknfkMNLDEVKNYAHRL---LMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 170 DMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-222 |
5.62e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.15 E-value: 5.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGL---QREWRGSVDLLGQAITPGFRFQGDLRR 79
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 80 ---------------NVQMVFQDPYASLHPNHTLWRTLAEPLQihgiRDVAPRVTTALEQVGLAADAVRRYPhQLSGGQR 144
Cdd:PRK09984 84 srantgyifqqfnlvNRLSVLENVLIGALGSTPFWRTCFSWFT----REQKQRALQALTRVGMVHFAHQRVS-TLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 145 QRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIqrFFD 222
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV--FYD 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-208 |
8.71e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.08 E-value: 8.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAItpgfRFQGD---L 77
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV----RFRSPrdaQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQDPyaSLHPNhtlwRTLAE------PLQIHGIRD---VAPRVTTALEQVGLAADA---VRRyphqLSGGQRQ 145
Cdd:COG1129 78 AAGIAIIHQEL--NLVPN----LSVAEniflgrEPRRGGLIDwraMRRRARELLARLGLDIDPdtpVGD----LSVAQQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 146 RVAIARALLLRPQILLLDEPTSALDmSVQAEIL-NLLNRLKqEHGMTYLLVSHDADVIAHMSDR 208
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLT-EREVERLfRIIRRLK-AQGVAIIYISHRLDEVFEIADR 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-217 |
1.26e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfRFQGDLRRN 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA--LSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQMVFQDpyASLHPNHTLwRTLAE--------PLQIHGIRDVAPrVTTALEQVGLAADAVRRYPhQLSGGQRQRVAIARA 152
Cdd:PRK09536 79 VASVPQD--TSLSFEFDV-RQVVEmgrtphrsRFDTWTETDRAA-VERAMERTGVAQFADRPVT-SLSGGERQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 153 LLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-203 |
1.79e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.36 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 13 FGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVD--------LLGQAITPGFRFQGDLRRNVQMv 84
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRraggarvaYVPQRSEVPDSLPLTVRDLVAM- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 85 fqdpyaSLHPNHTLWRTLAeplqihgiRDVAPRVTTALEQVGLAADAVRRYpHQLSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:NF040873 81 ------GRWARRGLWRRLT--------RDDRAAVDDALERVGLADLAGRQL-GELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 523681378 165 PTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIA 203
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-226 |
1.31e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.67 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKT-----AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGD- 76
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 -------------LRRNVQMVFQdpyaslHPNHTLWRTLAEP--------LQIHGIrDVAPRVTTALEQVGLAADAVRRY 135
Cdd:PRK13631 101 tnpyskkiknfkeLRRRVSMVFQ------FPEYQLFKDTIEKdimfgpvaLGVKKS-EAKKLAKFYLNKMGLDDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 136 PHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250
....*....|....*...
gi 523681378 216 VI-------QRFFDREAL 226
Cdd:PRK13631 253 KIlktgtpyEIFTDQHII 270
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-218 |
2.06e-19 |
|
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: 83.54 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 16 KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGqaITPGFRfQGDLRRNVQMVFQDpyaslhpN 95
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKR-RKKFLRRIGVVFGQ-------K 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 96 HTLWRTL--AEPLQ-IHGIRDVAP--------RVTTALEQVGLAADAVRryphQLSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:cd03267 104 TQLWWDLpvIDSFYlLAAIYDLPParfkkrldELSELLDLEELLDTPVR----QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523681378 165 PTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQ 218
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-217 |
3.00e-19 |
|
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: 81.59 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFG--AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGqaiTPGFRFQGDLRRNV 81
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG---VPVSDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDPYaslhpnhtLWRTlaeplqihgirdvaprvtTALEQVGLaadavrryphQLSGGQRQRVAIARALLLRPQILL 161
Cdd:cd03247 78 SVLNQRPY--------LFDT------------------TLRNNLGR----------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 162 LDEPTSALDMSVQAEILNLLnrLKQEHGMTYLLVSHDADVIAHMsDRAAFMAEGVI 217
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-224 |
3.26e-19 |
|
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: 85.86 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 14 GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAI------TPGfRFQGDLRRNVQmvfqd 87
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLkqwdreTFG-KHIGYLPQDVE----- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 88 pyasLHPNhtlwrTLAEPLQIHGiRDVAPRVTTALEQVGLAADAVRRYPH-----------QLSGGQRQRVAIARALLLR 156
Cdd:TIGR01842 403 ----LFPG-----TVAENIARFG-ENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 157 PQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAhMSDRAAFMAEGVIQRFFDRE 224
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLG-CVDKILVLQDGRIARFGERD 538
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-198 |
3.46e-19 |
|
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: 85.49 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTF-GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfRFQGDLRRNVQMV 84
Cdd:TIGR02868 337 LRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS--LDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 85 FQDPyaslhpnHTLWRTLAEPLQIhGIRDVAPR-VTTALEQVGLAaDAVRRYPH-----------QLSGGQRQRVAIARA 152
Cdd:TIGR02868 415 AQDA-------HLFDTTVRENLRL-ARPDATDEeLWAALERVGLA-DWLRALPDgldtvlgeggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 523681378 153 LLLRPQILLLDEPTSALDMSVQAEILNLLnrLKQEHGMTYLLVSHD 198
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-217 |
4.88e-19 |
|
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: 81.94 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP--GFRF------QG 75
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIaaRNRIgylpeeRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 dLRRNVQMVFQDPYaslhpnhtlwrtLAeplQIHG--IRDVAPRVTTALEQVGLAADAVRRYpHQLSGGQRQRVAIARAL 153
Cdd:cd03269 81 -LYPKMKVIDQLVY------------LA---QLKGlkKEEARRRIDEWLERLELSEYANKRV-EELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 154 LLRPQILLLDEPTSALDmSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03269 144 IHDPELLILDEPFSGLD-PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-217 |
7.16e-19 |
|
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: 81.80 E-value: 7.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 5 NLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP-----------GFRF 73
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlppheraragiAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 74 QGdlrrnvQMVFqdPYASLHPNhtlWRTLAEPL--QIHGIRDVAPRVTTALEQVglaadaVRRYPHQLSGGQRQRVAIAR 151
Cdd:TIGR03410 82 QG------REIF--PRLTVEEN---LLTGLAALprRSRKIPDEIYELFPVLKEM------LGRRGGDLSGGQQQQLAIAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 152 ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-207 |
7.29e-19 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 82.20 E-value: 7.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLaglQREW---RGSVDLLGQAItpgfRFQG--DLRRNVQMVFQDPyaslhpnHT 97
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLL---ERFYdptSGEILLDGVDI----RDLNlrWLRSQIGLVSQEP-------VL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 98 LWRTLAEplqihGIRDVAPRVTTA-LEQVGLAADA---VRRYPH-----------QLSGGQRQRVAIARALLLRPQILLL 162
Cdd:cd03249 89 FDGTIAE-----NIRYGKPDATDEeVEEAAKKANIhdfIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 523681378 163 DEPTSALDMSVQAEILNLLNRLKQehGMTYLLVSH------DADVIAHMSD 207
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMK--GRTTIVIAHrlstirNADLIAVLQN 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-215 |
8.58e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFRF--QGDLR 78
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIarMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 79 --RNVQMvFQDPYA--------SLHPNHTLWRTL-AEPLQIHGIRDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRV 147
Cdd:PRK11300 85 tfQHVRL-FREMTVienllvaqHQQLKTGLFSGLlKTPAFRRAESEALDRAATWLERVGLLEHA-NRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 148 AIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-203 |
1.01e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.39 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGD----LRR-NVQMVFQDPYasLHPNHT 97
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVA---TLDADalaqLRReHFGFIFQRYH--LLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 98 LWRTLAEPLQIHGIRDVA--PRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQA 175
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQrlLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180
....*....|....*....|....*...
gi 523681378 176 EILNLLNRLkQEHGMTYLLVSHDADVIA 203
Cdd:PRK10535 182 EVMAILHQL-RDRGHTVIIVTHDPQVAA 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-217 |
1.01e-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: 81.26 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKT----AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRfqgDLR 78
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA---EAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 79 RNVQMVFQDpyASLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAVRRYpHQLSGGQRQRVAIARALLLR 156
Cdd:cd03266 78 RRLGFVSDS--TGLYDRLTARENLEYFAGLYGLkgDELTARLEELADRLGMEELLDRRV-GGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 157 PQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-215 |
1.05e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQdlqVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQRE-----WRGSVDLLGQAITpGFRFQG 75
Cdd:PRK14271 22 MAAVNLT---LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIF-NYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 DLRRNVQMVFQDPyaSLHPNHTLWRTLAeplqihGIR--DVAPR------VTTALEQVGL---AADAVRRYPHQLSGGQR 144
Cdd:PRK14271 98 EFRRRVGMLFQRP--NPFPMSIMDNVLA------GVRahKLVPRkefrgvAQARLTEVGLwdaVKDRLSDSPFRLSGGQQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 145 QRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhgMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDG 238
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-217 |
1.90e-18 |
|
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: 80.74 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 11 VTFG----AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpGFRFQgDLRRNVQMVFQ 86
Cdd:cd03251 6 VTFRypgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR-DYTLA-SLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 87 DPYASlhpNHTLWRTLAeplqiHGIRDVAP-RVTTALEQVGlAADAVRRYPH-----------QLSGGQRQRVAIARALL 154
Cdd:cd03251 84 DVFLF---NDTVAENIA-----YGRPGATReEVEEAARAAN-AHEFIMELPEgydtvigergvKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 155 LRPQILLLDEPTSALDMSVQAEILNLLNRLKQehGMTYLLVSHDADVIAHmSDRAAFMAEGVI 217
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
23-217 |
1.97e-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: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpGFRFQGdLRRNVQMVFQDpyASLHPNhTLWRTL 102
Cdd:TIGR03797 473 SLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLA-GLDVQA-VRRQLGVVLQN--GRLMSG-SIFENI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 103 A--EPLQIHgirdvapRVTTALEQVGLAADaVRRYPHQ-----------LSGGQRQRVAIARALLLRPQILLLDEPTSAL 169
Cdd:TIGR03797 548 AggAPLTLD-------EAWEAARMAGLAED-IRAMPMGmhtvisegggtLSGGQRQRLLIARALVRKPRILLFDEATSAL 619
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 170 DMSVQAEILNLLNRLKqehgMTYLLVSHDADVIAHmSDRAAFMAEGVI 217
Cdd:TIGR03797 620 DNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRV 662
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-198 |
2.31e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 7 QDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQG-DLRRNVQMVF 85
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ---HYASkEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QDpyASLHPNHTLWRTLA------EPLQIHGIRDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQI 159
Cdd:PRK10253 88 QN--ATTPGDITVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 523681378 160 LLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHD 198
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHD 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-198 |
6.26e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.77 E-value: 6.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLqrewrgsvdllgqaITPGfrfQGDLRRNVQ 82
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL--------------VAPD---EGVIKRNGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPYASLHPNHTLWRTLAEPLQIH-GIR--DVAPrvttALEQVglAADAVRRYPHQ-LSGGQRQRVAIARALLLRPQ 158
Cdd:PRK09544 67 LRIGYVPQKLYLDTTLPLTVNRFLRLRpGTKkeDILP----ALKRV--QAGHLIDAPMQkLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 523681378 159 ILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHD 198
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
7.66e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 7.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVnLQDLQVTFGAKT-----AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGL----------------------Q 53
Cdd:PRK13651 1 MQIK-VKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdeknkkktkE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 54 REWRGSVDLLGQAITPGFRFQGDLRRNVQMVFQdpYASlhpnHTLWRTLAEPLQIHGIR-------DVAPRVTTALEQVG 126
Cdd:PRK13651 80 KEKVLEKLVIQKTRFKKIKKIKEIRRRVGVVFQ--FAE----YQLFEQTIEKDIIFGPVsmgvskeEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 127 LAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMS 206
Cdd:PRK13651 154 LDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWT 232
|
250
....*....|.
gi 523681378 207 DRAAFMAEGVI 217
Cdd:PRK13651 233 KRTIFFKDGKI 243
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
10-202 |
1.23e-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: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 10 QVTFG----AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQ---AITPGFrfqgdLRRNVQ 82
Cdd:TIGR03796 482 NITFGysplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIpreEIPREV-----LANSVA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPY---ASLHPNHTLW-RTLAEPLQIHGIRDVAprvttaleqvglAADAVRRYPHQ-----------LSGGQRQRV 147
Cdd:TIGR03796 557 MVDQDIFlfeGTVRDNLTLWdPTIPDADLVRACKDAA------------IHDVITSRPGGydaelaegganLSGGQRQRL 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 148 AIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRlkqeHGMTYLLVSH------DADVI 202
Cdd:TIGR03796 625 EIARALVRNPSILILDEATSALDPETEKIIDDNLRR----RGCTCIIVAHrlstirDCDEI 681
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-215 |
1.59e-17 |
|
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: 78.24 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTF-----GAKT--AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDllgqaitpgFRFQ 74
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL---------VRHD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 75 GDLrrnVQMVfqdpyaslhpnhtlwrtLAEPLQIHGIR-----------DVAPRVTT------ALEQVGLAADAVRR--- 134
Cdd:COG4778 74 GGW---VDLA-----------------QASPREILALRrrtigyvsqflRVIPRVSAldvvaePLLERGVDREEARArar 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 135 ---------------YPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDA 199
Cdd:COG4778 134 ellarlnlperlwdlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDE 212
|
250
....*....|....*.
gi 523681378 200 DVIAHMSDRAAFMAEG 215
Cdd:COG4778 213 EVREAVADRVVDVTPF 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-215 |
1.67e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.46 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdlRRNV 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA---RQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQdpYASLHPNHtlwrTLAEPLQIHG------IRDVAPRVTTALEQVGL--AADAVRRyphQLSGGQRQRVAIARAL 153
Cdd:PRK13537 83 GVVPQ--FDNLDPDF----TVRENLLVFGryfglsAAAARALVPPLLEFAKLenKADAKVG---ELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 154 LLRPQILLLDEPTSALDmsVQAEILnLLNRLKQ--EHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLD--PQARHL-MWERLRSllARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-197 |
1.70e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.81 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLqreW---RGSVDLLGqaitpgfrfqgdlRRNVQMVFQDPYAslhPNHTLw 99
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGL---WpwgSGRIGMPE-------------GEDLLFLPQRPYL---PLGTL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 100 rtlaeplqihgirdvaprvttaLEQVglaadavrRYP--HQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEI 177
Cdd:cd03223 81 ----------------------REQL--------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
170 180
....*....|....*....|
gi 523681378 178 LNLLnrlkQEHGMTYLLVSH 197
Cdd:cd03223 131 YQLL----KELGITVISVGH 146
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
1.80e-17 |
|
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: 77.09 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVtfgaKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGfRFQGDLRRNV 81
Cdd:cd03215 3 PVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR-SPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDPYAS-LHPNHTLWRTLAeplqihgirdvaprvttaleqvglaadavrrYPHQLSGGQRQRVAIARALLLRPQIL 160
Cdd:cd03215 78 AYVPEDRKREgLVLDLSVAENIA-------------------------------LSSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 161 LLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-217 |
1.80e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.59 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAI--TPGfrfqGDLRRNVQM 83
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVatTPS----RELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDPYASL------------HPnHTLWRTLAEPLQIhgirdvaprVTTALEQVGLA--ADavrRYPHQLSGGQRQRVAI 149
Cdd:COG4604 80 LRQENHINSrltvrelvafgrFP-YSKGRLTAEDREI---------IDEAIAYLDLEdlAD---RYLDELSGGQRQRAFI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 150 ARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-219 |
2.21e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.49 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 16 KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdLRRNVQMVFQDPyaslhPN 95
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE--IRKKIGIIFQNP-----DN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 96 htlwrtlaeplQIHGIR---DVA--------PR------VTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQ 158
Cdd:PRK13632 95 -----------QFIGATvedDIAfglenkkvPPkkmkdiIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 159 ILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADViAHMSDRAAFMAEGVIQR 219
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDE-AILADKVIVFSEGKLIA 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-181 |
2.62e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 8 DLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfqgDLRRNVQMVF-- 85
Cdd:PRK13539 7 DLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID-------DPDVAEACHYlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 -QD---PYASLHPNHTLWRtlaeplQIHGIRDvaPRVTTALEQVGLAADAVRRYPHqLSGGQRQRVAIARALLLRPQILL 161
Cdd:PRK13539 80 hRNamkPALTVAENLEFWA------AFLGGEE--LDIAAALEAVGLAPLAHLPFGY-LSAGQKRRVALARLLVSNRPIWI 150
|
170 180
....*....|....*....|
gi 523681378 162 LDEPTSALDMSVQAEILNLL 181
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELI 170
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-208 |
2.82e-17 |
|
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: 75.56 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGlqrewrgsvdllgqAITPgfrfqgdlrrnvqm 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG--------------ELEP-------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 vfqdpyaslhpnhtlwrtlaeplqIHGIRDVAPRVTTAleqvglaadavrrYPHQLSGGQRQRVAIARALLLRPQILLLD 163
Cdd:cd03221 53 ------------------------DEGIVTWGSTVKIG-------------YFEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 523681378 164 EPTSALDM-SVQAeilnLLNRLKQEHGmTYLLVSHD-------ADVIAHMSDR 208
Cdd:cd03221 96 EPTNHLDLeSIEA----LEEALKEYPG-TVILVSHDryfldqvATKIIELEDG 143
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-208 |
3.11e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVdllgqAITPGFRF-----------Q 74
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-----SIPKGLRIgylpqepplddD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 75 GDLRRNVQMVFQDPYASLHPNHTLWRTLAEP-------------LQIHGIRDVAPRVTTALEQVGLAADAVRRYPHQLSG 141
Cdd:COG0488 76 LTVLDTVLDGDAELRALEAELEELEAKLAEPdedlerlaelqeeFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 142 GQRQRVAIARALLLRPQILLLDEPTSALDmsvqAE-ILNLLNRLKQEHGmTYLLVSHD-------ADVIAHMSDR 208
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLD----LEsIEWLEEFLKNYPG-TVLVVSHDryfldrvATRILELDRG 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
10-224 |
3.12e-17 |
|
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: 79.79 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 10 QVTFGA----KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAItpgfrFQ---GDLRRNVQ 82
Cdd:COG4618 335 NLTVVPpgskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL-----SQwdrEELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPyaSLHPNhtlwrTLAEplQIHGIRDVAP-RVTTALEQVGlAADAVRRYP-----------HQLSGGQRQRVAIA 150
Cdd:COG4618 410 YLPQDV--ELFDG-----TIAE--NIARFGDADPeKVVAAAKLAG-VHEMILRLPdgydtrigeggARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 151 RALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKqEHGMTYLLVSHDADVIAHMsDRAAFMAEGVIQRFFDRE 224
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGPRD 551
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-197 |
4.41e-17 |
|
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: 76.24 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGDLRRNVQMVF 85
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---EQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QDPyaSLHPNHTLWRTLAEPLQIHGIRDVAprVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEP 165
Cdd:TIGR01189 80 HLP--GLKPELSALENLHFWAAIHGGAQRT--IEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 523681378 166 TSALDMSVQAEILNLLNRLKQEHGMTyLLVSH 197
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIV-LLTTH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-198 |
7.81e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLlGQAITPGFrfqgdlrrnvq 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIGY----------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 mvF-QDpYASLHPNHTLWRTlaeplqihgIRDVAPRVTTA-----LEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLR 156
Cdd:COG0488 383 --FdQH-QEELDPDKTVLDE---------LRDGAPGGTEQevrgyLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 523681378 157 PQILLLDEPTSALDMsvqaEILNLLNRLKQEHGMTYLLVSHD 198
Cdd:COG0488 451 PNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHD 488
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-216 |
8.01e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdlRRNVQM 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA---RARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQdpYASLHPNHtlwrTLAEPLQIHG------IRDVAPRVTTALEQVGLAADAVRRYPhQLSGGQRQRVAIARALLLRP 157
Cdd:PRK13536 119 VPQ--FDNLDLEF----TVRENLLVFGryfgmsTREIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 158 QILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGV 216
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-217 |
8.39e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 78.71 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFG----AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAglqREW---RGSVDLLGQAITpGFRfQGD 76
Cdd:PRK11160 337 VSLTLNNVSFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT---RAWdpqQGEILLNGQPIA-DYS-EAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 LRRNVQMVFQDPyaslhpnHTLWRTLAEPLQI--HGIRDvaPRVTTALEQVGLAA-------------DAVRryphQLSG 141
Cdd:PRK11160 412 LRQAISVVSQRV-------HLFSATLRDNLLLaaPNASD--EALIEVLQQVGLEKlleddkglnawlgEGGR----QLSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 142 GQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQehGMTYLLVSHDADVIAHMsDRAAFMAEGVI 217
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-215 |
8.82e-17 |
|
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: 78.71 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 12 TFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGL--QREWRGSVDLLGQAITPGfRFQGDLRRNVQMVFQD-- 87
Cdd:TIGR02633 10 TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKAS-NIRDTERAGIVIIHQElt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 88 --PYASLHPNHTLWRTLAEPLQIHGIRDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEP 165
Cdd:TIGR02633 89 lvPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 523681378 166 TSALDMSVQAEILNLLNRLKQeHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-234 |
1.07e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.61 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 36 GASGCGKSTILRVLAGLQREWRGSVDLLGQAItpgFRFQGDL-----RRNVQMVFQDpyASLHPNHTLWRTLAeplqiHG 110
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVL---FDAEKGIclppeKRRIGYVFQD--ARLFPHYKVRGNLR-----YG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 111 IRDVAP----RVTTALeqvGLAAdAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQ 186
Cdd:PRK11144 101 MAKSMVaqfdKIVALL---GIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 187 EHGMTYLLVSHDADVIAHMSDRAAFMAEGVIqRFFDREALVNGEHRMR 234
Cdd:PRK11144 177 EINIPILYVSHSLDEILRLADRVVVLEQGKV-KAFGPLEEVWASSAMR 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-228 |
1.78e-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: 77.92 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQR------------------EWRGSVDLLGQ 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvalcekcGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 66 A---------------ITPGFRFQGDLRRNVQMVFQDPYAsLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLA 128
Cdd:TIGR03269 81 PcpvcggtlepeevdfWNLSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGYegKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 129 adavRRYPH---QLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHM 205
Cdd:TIGR03269 160 ----HRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|...
gi 523681378 206 SDRAAFMAEGVIQRFFDREALVN 228
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-217 |
1.95e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 77.69 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 11 VTF---GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpGFRFQGdLRRNVQMVFQD 87
Cdd:PRK13657 340 VSFsydNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR-TVTRAS-LRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 88 PYaslhpnhTLWRTLAEPLQIhGIRDVAP-RVTTALEQVGlAADAVRRYPH-----------QLSGGQRQRVAIARALLL 155
Cdd:PRK13657 418 AG-------LFNRSIEDNIRV-GRPDATDeEMRAAAERAQ-AHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523681378 156 RPQILLLDEPTSALDMSVQAEILNLLNRLKqeHGMTYLLVSHDADVIAHmSDRAAFMAEGVI 217
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-217 |
2.26e-16 |
|
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: 74.49 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQ--REWRGSVDLLGQAIT---PGFRFqgdlRRN 80
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITdlpPEERA----RLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQMVFQdpyaslhpnhtlwrtlaEPLQIHGIRdvaprvttaleqvglAADAVRRYPHQLSGGQRQRVAIARALLLRPQIL 160
Cdd:cd03217 79 IFLAFQ-----------------YPPEIPGVK---------------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 161 LLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHM-SDRAAFMAEGVI 217
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-208 |
2.51e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRV-------------DAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpGFR 72
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVpgrtllhplsltfPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE-SWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 73 FQGDLRRNVQMVFQDPYAS-----------LHPNH-TLWRTLAEPLQihgirdvapRVTTALEQVGLAADAvRRYPHQLS 140
Cdd:PRK10575 80 SKAFARKVAYLPQQLPAAEgmtvrelvaigRYPWHgALGRFGAADRE---------KVEEAISLVGLKPLA-HRLVDSLS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 141 GGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDR 208
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDY 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-197 |
4.92e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.68 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfQGD---LRRNVQMVFQDPyaslhpnhTLW 99
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-----QYDhhyLHRQVALVGQEP--------VLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 100 RTLAEPLQIHGIRDVAPRVTTALEQVGLAADAVRRYPH-----------QLSGGQRQRVAIARALLLRPQILLLDEPTSA 168
Cdd:TIGR00958 568 SGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180
....*....|....*....|....*....
gi 523681378 169 LDmsvqAEILNLLNRLKQEHGMTYLLVSH 197
Cdd:TIGR00958 648 LD----AECEQLLQESRSRASRTVLLIAH 672
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-226 |
8.52e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 9 LQVT-FGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP---------GF------- 71
Cdd:COG1129 257 LEVEgLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairaGIayvpedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 72 RFQG-----DLRRNVQMVFQDPYASLHP-NHTLWRTLAEPLqihgIRDVAPRVTTALEQVGlaadavrryphQLSGGQRQ 145
Cdd:COG1129 337 KGEGlvldlSIRENITLASLDRLSRGGLlDRRRERALAEEY----IKRLRIKTPSPEQPVG-----------NLSGGNQQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 146 RVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREA 225
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDREE 480
|
.
gi 523681378 226 L 226
Cdd:COG1129 481 A 481
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-208 |
1.01e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 16 KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGqaITPgFRFQGDLRRNVQMVF----Qdpyas 91
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVP-FKRRKEFARRIGVVFgqrsQ----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 92 lhpnhtLW---------RTLAEplqIHGIRDVAPR-----VTTALEQVGLAADAVRryphQLSGGQRQRVAIARALLLRP 157
Cdd:COG4586 107 ------LWwdlpaidsfRLLKA---IYRIPDAEYKkrldeLVELLDLGELLDTPVR----QLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 523681378 158 QILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDR 208
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDR 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-217 |
1.22e-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: 73.07 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 22 ASFRVDAGETFSLIGASGCGKSTILRVLAGLQREW---RGSVDLLGQAITPGfrfqgDLRRNVQMVFQDPYasLHPNHTL 98
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPD-----QFQKCVAYVRQDDI--LLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 99 WRTLAEPLQIHGIRDVAPRVTTAL-EQVGLAADAVRRYPH----QLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSV 173
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRvEDVLLRDLALTRIGGnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 523681378 174 QAEILNLLNRLKQEhGMTYLLVSHD--ADvIAHMSDRAAFMAEGVI 217
Cdd:cd03234 179 ALNLVSTLSQLARR-NRIVILTIHQprSD-LFRLFDRILLLSSGEI 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-230 |
1.47e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 73.21 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 19 VSAASFRvdAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLG-------QAITPgfRFQGDLRRNVQMVFQDPYas 91
Cdd:cd03237 17 VEGGSIS--ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsykpQYIKA--DYEGTVRDLLSSITKDFY-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 92 lhpNHTLWRT-LAEPLQIHGIRDvaprvttaleqvglaadavRRYPhQLSGGQRQRVAIARALLLRPQILLLDEPTSALD 170
Cdd:cd03237 91 ---THPYFKTeIAKPLQIEQILD-------------------REVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 171 MSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRaafmaegVIqrFFDREALVNGE 230
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADR-------LI--VFEGEPSVNGV 198
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-198 |
1.48e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.58 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGA-----KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT--PGFRFQG 75
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 76 DLRRnvqmVFQDPYASLHPNhtlwRTLAEPLQI----HGIRDVAPRVTTA---------------LE-----QVGLaada 131
Cdd:COG1101 81 YIGR----VFQDPMMGTAPS----MTIEENLALayrrGKRRGLRRGLTKKrrelfrellatlglgLEnrldtKVGL---- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 132 vrryphqLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHD 198
Cdd:COG1101 149 -------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-202 |
1.85e-15 |
|
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: 72.64 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 16 KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdLRRNVQMVFQDPYaslhpn 95
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS--LRSMIGVVLQDTF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 96 hTLWRTLAEPLQIHGIRDVAPRVTTALEQVGlAADAVRRYP-----------HQLSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:cd03254 88 -LFSGTIMENIRLGRPNATDEEVIEAAKEAG-AHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 523681378 165 PTSALDMSVQAEILNLLNRLKqeHGMTYLLVSH------DADVI 202
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLM--KGRTSIIIAHrlstikNADKI 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-217 |
1.86e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQrEWRGSVDLLGQAITpgfrfQGDL---RRNVQMVFQDP---YASLHPNH 96
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELR-----ELDPeswRKHLSWVGQNPqlpHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 97 TLWRTLAEPLQIHgirdvaprvtTALEQVGlAADAVRRYPH-----------QLSGGQRQRVAIARALLLRPQILLLDEP 165
Cdd:PRK11174 444 LLGNPDASDEQLQ----------QALENAW-VSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 523681378 166 TSALDMSVQAEILNLLNRLKQEHgmTYLLVSHDADVIAHMsDRAAFMAEGVI 217
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-217 |
1.92e-15 |
|
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: 74.75 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 18 AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgFRFQgDLRRNVQMVFQDPyaslhpnHT 97
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD-YTLA-SLRRQVALVSQDV-------VL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 98 LWRTLAEPLQiHGIRDVAPR--VTTALeQVGLAADAVRRYP---HQ--------LSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:TIGR02203 418 FNDTIANNIA-YGRTEQADRaeIERAL-AAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 523681378 165 PTSALDMSVQAEILNLLNRLKQehGMTYLLVSHDADVIAHmSDRAAFMAEGVI 217
Cdd:TIGR02203 496 ATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-207 |
2.29e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 12 TFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGL--QREWRGSVDLLGQAItpgfRFQG--DLRRN-VQMVFQ 86
Cdd:PRK13549 14 TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEEL----QASNirDTERAgIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 87 D----PYASLHPNHTLWRtlaEPLQiHGIRD---VAPRVTTALEQVGLAADAVRRYPHqLSGGQRQRVAIARALLLRPQI 159
Cdd:PRK13549 90 ElalvKELSVLENIFLGN---EITP-GGIMDydaMYLRAQKLLAQLKLDINPATPVGN-LGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 160 LLLDEPTSALDMSVQAEILNLLNRLKQeHGMTYLLVSHDADVIAHMSD 207
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISD 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-215 |
2.56e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.43 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 14 GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGlQREW---RGSVDLLGQAITPGfrfqgDLRRNVQMVFQDPYa 90
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG-RRTGlgvSGEVLINGRPLDKR-----SFRKIIGYVPQDDI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 91 sLHPNHTLWRTLAEPLQIHGIrdvaprvttaleqvglaadavrryphqlSGGQRQRVAIARALLLRPQILLLDEPTSALD 170
Cdd:cd03213 93 -LHPTLTVRETLMFAAKLRGL----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 523681378 171 MSVQAEILNLLNRLKQEhGMTYLLVSHDA-DVIAHMSDRAAFMAEG 215
Cdd:cd03213 144 SSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQG 188
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
9-198 |
2.93e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 71.76 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 9 LQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGDLRRNVQMVFQDP 88
Cdd:cd03231 6 LTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD---FQRDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 89 ----YASLHPNHTLWRTLAEPLQIHgirdvaprvtTALEQVGLAAdaVRRYP-HQLSGGQRQRVAIARALLLRPQILLLD 163
Cdd:cd03231 83 giktTLSVLENLRFWHADHSDEQVE----------EALARVGLNG--FEDRPvAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|....*
gi 523681378 164 EPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHD 198
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-234 |
3.26e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQ-GDLRRNV 81
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDpyASLHPNHTLWRTLAEPLQIHG------IRDVaprVTTALEQVGLAAdAVRRYPHQLSGGQRQRVAIARALLL 155
Cdd:PRK11831 87 SMLFQS--GALFTDMNVFDNVAYPLREHTqlpaplLHST---VMMKLEAVGLRG-AAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 156 RPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREAL-VNGEHRMR 234
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALqANPDPRVR 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-217 |
7.04e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.94 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 18 AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQGdLRRNVQMVFQDPYASLhpnht 97
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQG-IRKLVGIVFQNPETQF----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 98 LWRTLAEPLQIHGIRDVAP------RVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDM 171
Cdd:PRK13644 91 VGRTVEEDLAFGPENLCLPpieirkRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 523681378 172 SVQAEILNLLNRLkQEHGMTYLLVSHDADVIaHMSDRAAFMAEGVI 217
Cdd:PRK13644 170 DSGIAVLERIKKL-HEKGKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-207 |
8.69e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 8.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTF-GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAItpgfrfQGDLRRNV- 81
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT------RQALQKNLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 -------------QMVFQDPYASLHPNHTLWRTLAEPlqihgiRDVApRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVA 148
Cdd:PRK15056 81 ayvpqseevdwsfPVLVEDVVMMGRYGHMGWLRRAKK------RDRQ-IVTAALARVDMV-EFRHRQIGELSGGQKKRVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 149 IARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSD 207
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
139-224 |
1.49e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 139 LSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQ 218
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
....*.
gi 523681378 219 RFFDRE 224
Cdd:PRK10762 475 GEFTRE 480
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-217 |
1.86e-14 |
|
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: 69.81 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDlqVTFGAKT-----AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfQGD- 76
Cdd:cd03248 11 IVKFQN--VTFAYPTrpdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-----QYEh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 77 --LRRNVQMVFQDPYASLhpnhtlwRTLAEPLQiHGIRDVAPRVTTALEQVGLAADAVRRYPH-----------QLSGGQ 143
Cdd:cd03248 84 kyLHSKVSLVGQEPVLFA-------RSLQDNIA-YGLQSCSFECVKEAAQKAHAHSFISELASgydtevgekgsQLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 144 RQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHgmTYLLVSHDADVIAHmSDRAAFMAEGVI 217
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-217 |
2.31e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.87 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTfgakTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREwRGSVDLLGQAIT--PGF---RFQGDLRRN 80
Cdd:COG4138 3 LNDVAVA----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSdwSAAelaRHRAYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQMVFQDP---YASLHpnhtLWRTLAEPLQIHGIRDVAprvttalEQVGLAaDAVRRYPHQLSGGQRQRVAIARA----- 152
Cdd:COG4138 78 QSPPFAMPvfqYLALH----QPAGASSEAVEQLLAQLA-------EALGLE-DKLSRPLTQLSGGEWQRVRLAAVllqvw 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 153 --LLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:COG4138 146 ptINPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-204 |
2.74e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQGDLRRNvqMVFQDPYASLHPNHTLWRTL 102
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR---RQRDEYHQD--LLYLGHQPGIKTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 103 AEPLQIHGIRDvAPRVTTALEQVGLA--ADAvrryP-HQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILN 179
Cdd:PRK13538 96 RFYQRLHGPGD-DEALWEALAQVGLAgfEDV----PvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170 180
....*....|....*....|....*
gi 523681378 180 LLNRLKQEHGMTYLLVSHDADVIAH 204
Cdd:PRK13538 171 LLAQHAEQGGMVILTTHQDLPVASD 195
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-217 |
3.16e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 71.31 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFG-AKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRfqGDLRRNVQ 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDR--HTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPY---ASLHPNHTL-------WRTLAEPLQIHGIRDVAPRVTTALeQVGLAADAVrryphQLSGGQRQRVAIARA 152
Cdd:TIGR01193 552 YLPQEPYifsGSILENLLLgakenvsQDEIWAACEIAEIKDDIENMPLGY-QTELSEEGS-----SISGGQKQRIALARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 153 LLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhgmTYLLVSHDADViAHMSDRAAFMAEGVI 217
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSV-AKQSDKIIVLDHGKI 686
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-227 |
3.65e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.10 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 11 VTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgFRFQGD-LRRNVQMVFQDpy 89
Cdd:PRK11288 12 KTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--FASTTAaLAAGVAIIYQE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 90 asLH--PNhtlwRTLAEPL------QIHGI---RDVAPRVTTALEQVGLAADAVRRYPHqLSGGQRQRVAIARALLLRPQ 158
Cdd:PRK11288 88 --LHlvPE----MTVAENLylgqlpHKGGIvnrRLLNYEAREQLEHLGVDIDPDTPLKY-LSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 159 ILLLDEPTSALDmSVQAEIL-NLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFF------DREALV 227
Cdd:PRK11288 161 VIAFDEPTSSLS-AREIEQLfRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVATFddmaqvDRDQLV 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-212 |
5.54e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 12 TFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgFRFQGD-LRRNVQMVFQDPya 90
Cdd:COG3845 14 RFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR--IRSPRDaIALGIGMVHQHF-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 91 SLHPNHTLWRTLA---EPLQIHGI--RDVAPRVTTALEQVGLAADaVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEP 165
Cdd:COG3845 90 MLVPNLTVAENIVlglEPTKGGRLdrKAARARIRELSERYGLDVD-PDAKVEDLSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523681378 166 TSALdmSVQ--AEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFM 212
Cdd:COG3845 169 TAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVL 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-199 |
6.01e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.34 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 24 FRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGfrfqgdlRRNVQMVFQDPYASLHPNHTLWRTLA 103
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-------DRSRFMAYLGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 104 EPLQIHGIRdvaPRVT--TALEQVGLA--ADAVRRyphQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMsvqaEILN 179
Cdd:PRK13543 105 FLCGLHGRR---AKQMpgSALAIVGLAgyEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGIT 174
|
170 180
....*....|....*....|...
gi 523681378 180 LLNRLKQEH---GMTYLLVSHDA 199
Cdd:PRK13543 175 LVNRMISAHlrgGGAALVTTHGA 197
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-217 |
6.51e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.09 E-value: 6.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGlqrewrgsvDLLGQAITPGFRFQGDLRRNVQ 82
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---------DLTGGGAPRGARVTGDVTLNGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPYASLHPNHTLWRTLAEP----------------------LQIHGIRDVAPRvttALEQVGlAADAVRRYPHQLS 140
Cdd:PRK13547 72 PLAAIDAPRLARLRAVLPQAAQPafafsareivllgrypharragALTHRDGEIAWQ---ALALAG-ATALVGRDVTTLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 141 GGQRQRVAIARA---------LLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRAAF 211
Cdd:PRK13547 148 GGELARVQFARVlaqlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAM 227
|
....*.
gi 523681378 212 MAEGVI 217
Cdd:PRK13547 228 LADGAI 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-215 |
8.08e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.98 E-value: 8.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfrfqgDLRRNV---- 81
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP------EDRRRIgylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 -------------QMVFqdpyaslhpnhtlwrtLAeplQIHGI--RDVAPRVTTALEQVGL---AADAVRryphQLSGGQ 143
Cdd:COG4152 78 eerglypkmkvgeQLVY----------------LA---RLKGLskAEAKRRADEWLERLGLgdrANKKVE----ELSKGN 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 144 RQRVAIARALLLRPQILLLDEPTSALDmSVQAEIL-NLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLD-PVNVELLkDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKG 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-170 |
1.96e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.00 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 7 QDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfrfqGDL--RRNVQMV 84
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA-----GDIatRRRVGYM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 85 FQ--DPYASLhpnhtlwrTLAEPLQIH------GIRDVAPRVTTALEQVGLaADAVRRYPHQLSGGQRQRVAIARALLLR 156
Cdd:NF033858 345 SQafSLYGEL--------TVRQNLELHarlfhlPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHK 415
|
170
....*....|....
gi 523681378 157 PQILLLDEPTSALD 170
Cdd:NF033858 416 PELLILDEPTSGVD 429
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-202 |
2.20e-13 |
|
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: 68.69 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQ---AITpgfrfQGDLRRNVQMVFQDPyaSLHpNHTLW 99
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirDVT-----QASLRAAIGIVPQDT--VLF-NDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 100 RTLAeplqiHGiRDVAPRvttalEQVGLAADA------VRRYPHQ-----------LSGGQRQRVAIARALLLRPQILLL 162
Cdd:COG5265 450 YNIA-----YG-RPDASE-----EEVEAAARAaqihdfIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 523681378 163 DEPTSALDMSVQAEILNLLNRLKQEHgmTYLLVSH------DADVI 202
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVARGR--TTLVIAHrlstivDADEI 562
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-222 |
3.71e-13 |
|
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: 66.40 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 14 GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQaITPGFR----FQGDL--RRNVQMvfqd 87
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLGlgggFNPELtgRENIYL---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 88 pyaslhpNHTLW-RTLAEPLQIhgIRDVAprvttALEQVGLAADA-VRRYphqlSGGQRQRVAIARALLLRPQILLLDEP 165
Cdd:cd03220 108 -------NGRLLgLSRKEIDEK--IDEII-----EFSELGDFIDLpVKTY----SSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 166 TSALDMSVQAEILNLLNRLKqEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIqRFFD 222
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKI-RFDG 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-217 |
4.48e-13 |
|
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: 66.36 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAItpGFRFQGDLRRNVQMVFQDpyaslhpNHTLWRTL 102
Cdd:cd03252 22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL--ALADPAWLRRQVGVVLQE-------NVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 103 AEPLqihGIRDVAPRVTTALEQVGLAA--DAVRRYPH-----------QLSGGQRQRVAIARALLLRPQILLLDEPTSAL 169
Cdd:cd03252 93 RDNI---ALADPGMSMERVIEAAKLAGahDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 170 DMSVQAEILNLLNRLKQehGMTYLLVSHDADVIAHmSDRAAFMAEGVI 217
Cdd:cd03252 170 DYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-216 |
5.38e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQrEWRGSVDLLGQAIT--PGF---RFQGDLRRNVQMVFQDP---YASLHp 94
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEawSAAelaRHRAYLSQQQTPPFAMPvfqYLTLH- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 95 nhtlwrtLAEPLQIHGIRDVAPRVTtalEQVGLaADAVRRYPHQLSGGQRQRVAIA-------RALLLRPQILLLDEPTS 167
Cdd:PRK03695 94 -------QPDKTRTEAVASALNEVA---EALGL-DDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523681378 168 ALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGV 216
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-217 |
7.44e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpGFRFQGDLRRN 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT-DWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQMVFQD----PYASLHPNHTLWRTLAEPLQ----IHGIRDVAPRvttaleqvgLAADAVRRyPHQLSGGQRQRVAIARA 152
Cdd:PRK11614 82 VAIVPEGrrvfSRMTVEENLAMGGFFAERDQfqerIKWVYELFPR---------LHERRIQR-AGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 153 LLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
23-217 |
7.48e-13 |
|
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: 67.07 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfQGD---LRRNVQMVFQDpyaslhpNHTLW 99
Cdd:TIGR01846 477 NLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA-----IADpawLRRQMGVVLQE-------NVLFS 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 100 RTLAEPLQIHGIRDVAPRVTTALEQVGlAADAVRRYPH-----------QLSGGQRQRVAIARALLLRPQILLLDEPTSA 168
Cdd:TIGR01846 545 RSIRDNIALCNPGAPFEHVIHAAKLAG-AHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523681378 169 LDMSVQAEILNLLNRLKQehGMTYLLVSHDADVIAHmSDRAAFMAEGVI 217
Cdd:TIGR01846 624 LDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQI 669
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-220 |
9.96e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.49 E-value: 9.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 16 KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQaITP----GFRFQGDL--RRNVQMVFQdpy 89
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAllelGAGFHPELtgRENIYLNGR--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 90 aslhpnhtlwrtlaeplqIHGI--RDVAPRVTTALE--QVGLAADA-VRRYphqlSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:COG1134 115 ------------------LLGLsrKEIDEKFDEIVEfaELGDFIDQpVKTY----SSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 165 PTSALDMSVQAEILNLLNRLKqEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRF 220
Cdd:COG1134 173 VLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-217 |
3.98e-12 |
|
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: 63.33 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP---------G------ 70
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmhkrarlGigylpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 71 ----FRfqgDL--RRNVQMVFQDPYASLHPNHTLWRTLAEPLQIHGIRDvaprvttaleQVGLAadavrryphqLSGGQR 144
Cdd:cd03218 83 easiFR---KLtvEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRK----------SKASS----------LSGGER 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 145 QRVAIARALLLRPQILLLDEPTSALD-MSVQaEILNLLNRLKqEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:cd03218 140 RRVEIARALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-203 |
4.47e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGA------KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQRewrgsvdllgqaitpgfrfqgdlRR 79
Cdd:COG2401 27 VAIVLEAFGVelrvveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-----------------------GT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 80 NVQMVFQDPYASLHPNHTLwrtlaepLQIHGIRDVAPRVTTALEQVGLAaDAV--RRYPHQLSGGQRQRVAIARALLLRP 157
Cdd:COG2401 84 PVAGCVDVPDNQFGREASL-------IDAIGRKGDFKDAVELLNAVGLS-DAVlwLRRFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 523681378 158 QILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIA 203
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
10-197 |
6.67e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.27 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 10 QVTF---GAKT-AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgFRFQgDLRRNVQMVF 85
Cdd:PRK11176 346 NVTFtypGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD-YTLA-SLRNQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QdpyaslhpnhtlwrtlaeplQIHGIRD-VAPRVTTAL------EQVGLAA------DAVRRYPH-----------QLSG 141
Cdd:PRK11176 424 Q--------------------NVHLFNDtIANNIAYARteqysrEQIEEAArmayamDFINKMDNgldtvigengvLLSG 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 142 GQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHgmTYLLVSH 197
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH 537
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-215 |
1.78e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQA---ITP--------GFR 72
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHklaaqlgiGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 73 FQGDLRRNVQMVFQDPYASLHPNHTLWrtlaePLQIHGIRDVAPRVTTALEQVGLAADaVRRYPHQLSGGQRQRVAIARA 152
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKVC-----GVNIIDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 153 LLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-197 |
2.92e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.46 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLqreWRgsvdllgqaiTPGFRFQGDLRRNVQMVFQDPYASLhpnhtlwRTL 102
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGEL---WP----------VYGGRLTKPAKGKLFYVPQRPYMTL-------GTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 103 ---------AEPLQIHGIRD-------VAPRVTTALEQVGlAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPT 166
Cdd:TIGR00954 532 rdqiiypdsSEDMKRRGLSDkdleqilDNVQLTHILEREG-GWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 523681378 167 SALDMSVQAEILNLLnrlkQEHGMTYLLVSH 197
Cdd:TIGR00954 611 SAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-220 |
3.26e-11 |
|
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: 60.50 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAI-TPGFRfqgDLRRNVQMVFQDPyaslhpnhTLWR- 100
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIsTIPLE---DLRSSLTIIPQDP--------TLFSg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 101 TLAEPLQIHGIRDVApRVTTALEqvglaadaVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNL 180
Cdd:cd03369 97 TIRSNLDPFDEYSDE-EIYGALR--------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 523681378 181 LNRLKQehGMTYLLVSHDADVIAHMsDRAAFMAEGVIQRF 220
Cdd:cd03369 168 IREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEY 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-215 |
3.84e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.99 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 29 GETFSLIGASGCGKSTILRVLAGLQR---EWRGSVDLLGQAITPGFrfqgdLRRNVQMVFQDP--YASLhpnhtlwrTLA 103
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKE-----MRAISAYVQQDDlfIPTL--------TVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 104 EPLQIHGI----RDVAP-----RVTTALEQVGL--AADAVRRYPHQ---LSGGQRQRVAIARALLLRPQILLLDEPTSAL 169
Cdd:TIGR00955 118 EHLMFQAHlrmpRRVTKkekreRVDEVLQALGLrkCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 523681378 170 DMSVQAEILNLLNRLKQEhGMTYLLVSHD-ADVIAHMSDRAAFMAEG 215
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEG 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-217 |
4.52e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT---PGFRFQGDL-----RRNVQMVFQDP------ 88
Cdd:PRK15439 283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINalsTAQRLARGLvylpeDRQSSGLYLDAplawnv 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 89 YASLHPNHTLW-RTLAEPLQIHGIRDVAPRVTTALEQvglaadAVRRyphqLSGGQRQRVAIARALLLRPQILLLDEPTS 167
Cdd:PRK15439 363 CALTHNRRGFWiKPARENAVLERYRRALNIKFNHAEQ------AART----LSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 523681378 168 ALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-234 |
1.76e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 19 VSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP---------GFRFQGDLRRNvqmvfqdpy 89
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspldavkkGMAYITESRRD--------- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 90 ASLHPNHTLWRTLAEPLQIH--------GIRDVAPRVTTALEQ---VGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQ 158
Cdd:PRK09700 350 NGFFPNFSIAQNMAISRSLKdggykgamGLFHEVDEQRTAENQrelLALKCHSVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 159 ILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALVNGEHRMR 234
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMA 504
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-197 |
2.98e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 2 AIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfrfqgdlrrnv 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 qmvFQDPYASLHPNHTLwrtlaeplqIHGIRDVAPRVTTAlEQVGL------------------AADA------VRRYPH 137
Cdd:PRK10762 70 ---FNGPKSSQEAGIGI---------IHQELNLIPQLTIA-ENIFLgrefvnrfgridwkkmyaEADKllarlnLRFSSD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 138 QLSG----GQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLK-QEHGMTYllVSH 197
Cdd:PRK10762 137 KLVGelsiGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKsQGRGIVY--ISH 199
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-217 |
3.03e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.12 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP---------G- 70
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhkrarlGi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 71 ---------FRfqgDL--RRNVQMVfqdpyaslhpnhtlwrtlaepLQIHGI--RDVAPRVTTALEQVGLAAdaVRRYP- 136
Cdd:COG1137 81 gylpqeasiFR---KLtvEDNILAV---------------------LELRKLskKEREERLEELLEEFGITH--LRKSKa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 137 HQLSGGQRQRVAIARALLLRPQILLLDEPTSALD-MSVqAEILNLLNRLKqEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVLITDHNVRETLGICDRAYIISEG 212
|
..
gi 523681378 216 VI 217
Cdd:COG1137 213 KV 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-208 |
3.55e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfRFQGDLRRN 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVA--RLQQDPPRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQ-MVF--------------QDPYASLH-----PNHTLWRTLA---EPLQIHGIRDVAPRVTTALEQVGLAADAVRRyph 137
Cdd:PRK11147 79 VEgTVYdfvaegieeqaeylKRYHDISHlvetdPSEKNLNELAklqEQLDHHNLWQLENRINEVLAQLGLDPDAALS--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 138 QLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVqaeILNLLNRLKQEHGmTYLLVSHDADVIAHMSDR 208
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQG-SIIFISHDRSFIRNMATR 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-220 |
5.22e-10 |
|
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: 57.50 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAIT-----------------PgFRFQGDLRRNVqmvf 85
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiglhdlrsrisiipqdP-VLFSGTIRSNL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 qDPYaSLHPNHTLWRtlaeplqihgirdvaprvttALEQVGLAaDAVRRYPHQL-----------SGGQRQRVAIARALL 154
Cdd:cd03244 99 -DPF-GEYSDEELWQ--------------------ALERVGLK-EFVESLPGGLdtvveeggenlSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 155 LRPQILLLDEPTSALDMSVQAEILNLLNRlkQEHGMTYLLVSHDADVIAHmSDRAAFMAEGVIQRF 220
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEF 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-208 |
5.30e-10 |
|
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: 58.64 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 29 GETFSLIGASGCGKSTILRVLAGLQREWRGSVDLL------GQAITPGFrfQGDLRRNVQMVFQDPYASlhpnhTLWRT- 101
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQYISPDY--DGTVEEFLRSANTDDFGS-----SYYKTe 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 102 LAEPLQIHGIRDvaprvttaleqvglaadavrRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLL 181
Cdd:COG1245 439 IIKPLGLEKLLD--------------------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170 180
....*....|....*....|....*..
gi 523681378 182 NRLKQEHGMTYLLVSHDADVIAHMSDR 208
Cdd:COG1245 499 RRFAENRGKTAMVVDHDIYLIDYISDR 525
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-209 |
8.78e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 8.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 29 GETFSLIGASGCGKSTILRVLAGLQREWRGSVDLL------GQAITPGFRFQ-GDLRRNVQMVFQDPYaslhpnhtLWRT 101
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPDYDGTvEDLLRSITDDLGSSY--------YKSE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 102 LAEPLQIHGIRDvaprvttaleqvglaadavrRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLL 181
Cdd:PRK13409 437 IIKPLQLERLLD--------------------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170 180
....*....|....*....|....*...
gi 523681378 182 NRLKQEHGMTYLLVSHDADVIAHMSDRA 209
Cdd:PRK13409 497 RRIAEEREATALVVDHDIYMIDYISDRL 524
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-220 |
1.28e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGlqrewrgsvDLLGQAitpgfrfqGDLRR--NVQM 83
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG---------QLQADS--------GRIHCgtKLEV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDPY-ASLHPNHTLWRTLAEPLQ---IHGIrdvaPRVTTALEQVGLAADAVRRYP-HQLSGGQRQRVAIARALLLRPQ 158
Cdd:PRK11147 385 AYFDQHrAELDPEKTVMDNLAEGKQevmVNGR----PRHVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSN 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 159 ILLLDEPTSALDMsvqaEILNLLNRLKQEHGMTYLLVSHDADVIahmsDRAA-----FMAEGVIQRF 220
Cdd:PRK11147 461 LLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQFV----DNTVtecwiFEGNGKIGRY 519
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-198 |
1.30e-09 |
|
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: 57.64 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 34 LIGASGCGKSTILRVLAGLQREWRGSVdllgqAITPGFRfqgdlrrnVQMVFQDPYasLHPNHTLWRTLAEPLQihGIRD 113
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEA-----RPQPGIK--------VGYLPQEPQ--LDPTKTVRENVEEGVA--EIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 114 VAPR---VTTAL------------------------------EQVGLAADAVRRYP-----HQLSGGQRQRVAIARALLL 155
Cdd:TIGR03719 99 ALDRfneISAKYaepdadfdklaaeqaelqeiidaadawdldSQLEIAMDALRCPPwdadvTKLSGGERRRVALCRLLLS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 523681378 156 RPQILLLDEPTSALDmsvqAEILNLLNRLKQEHGMTYLLVSHD 198
Cdd:TIGR03719 179 KPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-207 |
1.40e-09 |
|
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: 56.19 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 19 VSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVdLLGQAITPGFRFQGDLRRNVQMVfqdPYASLHP---N 95
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-HWSNKNESEPSFEATRSRNRYSV---AYAAQKPwllN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 96 HTLWR--TLAEPLQihgirdvAPRVTTALEQVGLAADaVRRYPH-----------QLSGGQRQRVAIARALLLRPQILLL 162
Cdd:cd03290 93 ATVEEniTFGSPFN-------KQRYKAVTDACSLQPD-IDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 163 DEPTSALDMSV-----QAEILNLLnrlkQEHGMTYLLVSHD------ADVIAHMSD 207
Cdd:cd03290 165 DDPFSALDIHLsdhlmQEGILKFL----QDDKRTLVLVTHKlqylphADWIIAMKD 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-226 |
3.56e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVT-FGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRFQgdlRRNVQMV 84
Cdd:COG3845 260 VENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE---RRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 85 F--QDPYAS-LHPNHTLWRTLA------EPLQIHGIRDVAprvttALEQvgLAADAVRRY------PHQ----LSGGQRQ 145
Cdd:COG3845 337 YipEDRLGRgLVPDMSVAENLIlgryrrPPFSRGGFLDRK-----AIRA--FAEELIEEFdvrtpgPDTparsLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 146 RVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREA 225
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
.
gi 523681378 226 L 226
Cdd:COG3845 489 A 489
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-217 |
4.49e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQA---ITPGFRFQgdlrRNVQ 82
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcarLTPAKAHQ----LGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPYasLHPNHTLWRTLAEPLQIHgiRDVAPRVTTALEQVGLAADavrryPHQLSG----GQRQRVAIARALLLRPQ 158
Cdd:PRK15439 90 LVPQEPL--LFPNLSVKENILFGLPKR--QASMQKMKQLLAALGCQLD-----LDSSAGslevADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 159 ILLLDEPTSALdmsVQAEILNLLNRLK--QEHGMTYLLVSHDADVIAHMSDRAAFMAEGVI 217
Cdd:PRK15439 161 ILILDEPTASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-217 |
4.56e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 22 ASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgFRFQGD-LRRNVQMVFQD-------PYASLH 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID--IRSPRDaIRAGIMLCPEDrkaegiiPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 94 PN--------HTLWRTLaeplqIHGIRDVAprvtTALEQVglAADAVR-RYPHQ----LSGGQRQRVAIARALLLRPQIL 160
Cdd:PRK11288 350 DNinisarrhHLRAGCL-----INNRWEAE----NADRFI--RSLNIKtPSREQlimnLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 523681378 161 LLDEPTSALDMSVQAEILNLLNRLKqEHGMTYLLVSHD-ADVIAhMSDRAAFMAEGVI 217
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDlPEVLG-VADRIVVMREGRI 474
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-207 |
4.57e-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: 56.11 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQ-AITPGFRF-QGD-LRRNVqmVFQDPyasLHPNHtlW 99
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvAYVPQQAWiQNDsLRENI--LFGKA---LNEKY--Y 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 100 RTLAEPLQIHGIRDVAPrvttALEQVGLAADAVrryphQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILN 179
Cdd:TIGR00957 731 QQVLEACALLPDLEILP----SGDRTEIGEKGV-----NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180 190
....*....|....*....|....*....|....*...
gi 523681378 180 --------LLN--RLKQEHGMTYLlvsHDADVIAHMSD 207
Cdd:TIGR00957 802 hvigpegvLKNktRILVTHGISYL---PQVDVIIVMSG 836
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-215 |
4.72e-09 |
|
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: 54.40 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAG-LQREwRGSVDLLGQ-AITP--GFRFQGDLRRNVqmVFQDPYaslhpNHtl 98
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKL-SGSVSVPGSiAYVSqePWIQNGTIRENI--LFGKPF-----DE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 99 wrtlaeplqihgirdvaPRVTTALEQVGLAADaVRRYPHQ-----------LSGGQRQRVAIARALLLRPQILLLDEPTS 167
Cdd:cd03250 95 -----------------ERYEKVIKACALEPD-LEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 523681378 168 ALDMSVQAEILN--LLNRLKqeHGMTYLLVSHDADVIAHmSDRAAFMAEG 215
Cdd:cd03250 157 AVDAHVGRHIFEncILGLLL--NNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-218 |
5.22e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 16 KTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAG-LQREWRGSVDLLGQ-AITP--GFRFQGDLRRNVqmVFQDPYAS 91
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSvAYVPqvSWIFNATVRENI--LFGSDFES 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 92 lhpnHTLWRTL-AEPLQiHGIRDVAPRVTTALEQVGLaadavrryphQLSGGQRQRVAIARALLLRPQILLLDEPTSALD 170
Cdd:PLN03232 708 ----ERYWRAIdVTALQ-HDLDLLPGRDLTEIGERGV----------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523681378 171 MSVQAEILNllNRLKQE-HGMTYLLVSHDADVIAHMsDRAAFMAEGVIQ 218
Cdd:PLN03232 773 AHVAHQVFD--SCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK 818
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-208 |
6.61e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.18 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 12 TFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREwrGSVDllGQAItpgfrFQGDLRRnvqmvFQD---- 87
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH--GSYE--GEIL-----FDGEVCR-----FKDirds 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 88 ---------------PYASLHPNHTLWRTLAEplqiHGIRD---VAPRVTTALEQVGLAADAVRRYPHqLSGGQRQRVAI 149
Cdd:NF040905 76 ealgiviihqelaliPYLSIAENIFLGNERAK----RGVIDwneTNRRARELLAKVGLDESPDTLVTD-IGVGKQQLVEI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 150 ARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKqEHGMTYLLVSHDADVIAHMSDR 208
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELK-AQGITSIIISHKLNEIRRVADS 208
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-197 |
7.66e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAItpgfrfQGDL-RRNV 81
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI------KKDLcTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 82 QMVFQDPYASLHPNHTLWRTLAEPLQIHgirdvaprvTTALEQVGLAA----DAVRRYP-HQLSGGQRQRVAIARALLLR 156
Cdd:PRK13540 75 QLCFVGHRSGINPYLTLRENCLYDIHFS---------PGAVGITELCRlfslEHLIDYPcGLLSSGQKRQVALLRLWMSK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 523681378 157 PQILLLDEPTSALDmsvQAEILNLLNRLkQEH---GMTYLLVSH 197
Cdd:PRK13540 146 AKLWLLDEPLVALD---ELSLLTIITKI-QEHrakGGAVLLTSH 185
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-234 |
9.19e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.13 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 1 MAIVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgFRFQGDLRRN 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-LPLHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 VQMVFQDpyASLHPNHTLWRTLAEPLQIhgirdvapRVTTALEQVGLAADAVRRYPH----------QLSGGQRQRVAIA 150
Cdd:PRK10895 80 IGYLPQE--ASIFRRLSVYDNLMAVLQI--------RDDLSAEQREDRANELMEEFHiehlrdsmgqSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 151 RALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKqEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALVNGE 230
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
....
gi 523681378 231 HRMR 234
Cdd:PRK10895 229 HVKR 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-215 |
1.40e-08 |
|
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: 53.02 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 33 SLIGASGCGKSTILRVLAglQREWRGSV--DLL--GQAITPGF-RFQGdlrrnvqmvfqdpYASLHPNHTLWRTLAEPLQ 107
Cdd:cd03232 37 ALMGESGAGKTTLLDVLA--GRKTAGVItgEILinGRPLDKNFqRSTG-------------YVEQQDVHSPNLTVREALR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 108 IHgirdvaprvttaleqvglaadAVRRyphQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKqE 187
Cdd:cd03232 102 FS---------------------ALLR---GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA-D 156
|
170 180
....*....|....*....|....*....
gi 523681378 188 HGMTYLLVSHD-ADVIAHMSDRAAFMAEG 215
Cdd:cd03232 157 SGQAILCTIHQpSASIFEKFDRLLLLKRG 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-207 |
2.16e-08 |
|
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: 53.14 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 29 GETFSLIGASGCGKSTILRVLAGLQR----------EWRGSVDLL-GQAITPGFR--FQGDLR--RNVQMVFQDPYA--- 90
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKpnlgkfddppDWDEILDEFrGSELQNYFTklLEGDVKviVKPQYVDLIPKAvkg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 91 -------SLHPNHTLwRTLAEPLQIHGIRDvaprvttaleqvglaadavrRYPHQLSGGQRQRVAIARALLLRPQILLLD 163
Cdd:cd03236 106 kvgellkKKDERGKL-DELVDQLELRHVLD--------------------RNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 523681378 164 EPTSALDMSVQAEILNLLNRLkQEHGMTYLLVSHDADVIAHMSD 207
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSD 207
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
33-202 |
2.17e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.95 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 33 SLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPgfRFQGDLRRNVQMVFQDPY---ASLHPNHTLWRTLAEPlqih 109
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS--LSHSVLRQGVAMVQQDPVvlaDTFLANVTLGRDISEE---- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 110 girdvapRVTTALEQVGLAaDAVRRYP-----------HQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEIL 178
Cdd:PRK10790 445 -------QVWQALETVQLA-ELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQ 516
|
170 180 190
....*....|....*....|....*....|
gi 523681378 179 NLLnRLKQEHgMTYLLVSH------DADVI 202
Cdd:PRK10790 517 QAL-AAVREH-TTLVVIAHrlstivEADTI 544
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-226 |
3.20e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 19 VSAASFRVDAGETFSLIGASGCGKSTILRVLAGL-QREWRGSVDLLGQAI---TPgfrfQGDLRRNVQMVFQD------- 87
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVkirNP----QQAIAQGIAMVPEDrkrdgiv 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 88 PYASLHPNHTL--------WRTLAEPLQIHGIRDVAPR--VTTALEQVGLAadavrryphQLSGGQRQRVAIARALLLRP 157
Cdd:PRK13549 354 PVMGVGKNITLaaldrftgGSRIDDAAELKTILESIQRlkVKTASPELAIA---------RLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 158 QILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREAL 226
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNL 492
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-215 |
3.51e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.48 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 33 SLIGASGCGKSTILRVLAGLQREWRGSVDLLGQaitpgfrfqgDLRRNVQMVFQDpyASLHPNHTLW---RTLAEPL--- 106
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK----------DIETNLDAVRQS--LGMCPQHNILfhhLTVAEHIlfy 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 107 -QIHG--IRDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLnr 183
Cdd:TIGR01257 1028 aQLKGrsWEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL-- 1104
|
170 180 190
....*....|....*....|....*....|..
gi 523681378 184 LKQEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-198 |
5.03e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLlgqaitpgfrfqGDlrrNVQ 82
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------------GE---TVK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVFQDPY-ASLHPNHTLWRTLAEPLQIH--GIRDVAPRVTTAL---------EQVGlaadavrryphQLSGGQRQRVAIA 150
Cdd:TIGR03719 387 LAYVDQSrDALDPNKTVWEEISGGLDIIklGKREIPSRAYVGRfnfkgsdqqKKVG-----------QLSGGERNRVHLA 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 151 RALLLRPQILLLDEPTSALDMsvqaEILNLLNRLKQEHGMTYLLVSHD 198
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD 499
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
139-232 |
5.22e-08 |
|
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: 51.03 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 139 LSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSDRA-AFMAE-GV 216
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIhVFEGEpGV 151
|
90
....*....|....*.
gi 523681378 217 IQRFFDREALVNGEHR 232
Cdd:cd03222 152 YGIASQPKGTREGINR 167
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-215 |
5.79e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.57 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 8 DLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAG-LQrewrgSVDLLGQAITPGFRFQGDLRRNVQMVFQ 86
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQ-----GNNFTGTILANNRKPTKQILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 87 DPYasLHPNHTLWRTL--AEPLQIhgirdvaPRVTTALEQVgLAADAV---------------RRYPHQLSGGQRQRVAI 149
Cdd:PLN03211 148 DDI--LYPHLTVRETLvfCSLLRL-------PKSLTKQEKI-LVAESViselgltkcentiigNSFIRGISGGERKRVSI 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 150 ARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHD-ADVIAHMSDRAAFMAEG 215
Cdd:PLN03211 218 AHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-170 |
6.16e-08 |
|
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: 52.99 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQV--TFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQ------------------REWRGSVDLL 63
Cdd:TIGR01271 1218 MDVQGLTAkyTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLstegeiqidgvswnsvtlQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 64 GQAItpgFRFQGDLRRNVqmvfqDPYASlHPNHTLWRTLAEPlqihGIRDVAPRVTTALEQVGLAADAVrryphqLSGGQ 143
Cdd:TIGR01271 1298 PQKV---FIFSGTFRKNL-----DPYEQ-WSDEEIWKVAEEV----GLKSVIEQFPDKLDFVLVDGGYV------LSNGH 1358
|
170 180
....*....|....*....|....*..
gi 523681378 144 RQRVAIARALLLRPQILLLDEPTSALD 170
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-215 |
1.26e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 50.34 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGlQREWRGSV--DLLGQAITP---GFRFQGDLRRNVQmvfQDpyasLH-PNH 96
Cdd:cd03233 27 SGVVKPGEMVLVLGRPGSGCSTLLKALAN-RTEGNVSVegDIHYNGIPYkefAEKYPGEIIYVSE---ED----VHfPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 97 TLWRTLaeplqihgirDVAPRvttaleqvgLAADAVRRyphQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAE 176
Cdd:cd03233 99 TVRETL----------DFALR---------CKGNEFVR---GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 523681378 177 ILNLLNRLKQEHGMTYLL-VSHDADVIAHMSDRAAFMAEG 215
Cdd:cd03233 157 ILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEG 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-226 |
1.89e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAG------------LQREWRGSVDLLGQAITPGFRfqgdlRRNVQMVfqdpya 90
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGelpllsgerqsqFSHITRLSFEQLQKLVSDEWQ-----RNNTDML------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 91 SLHPNHTlWRTLAEPLQiHGIRDVApRVTTALEQVGLAADAVRRYPHqLSGGQRQRVAIARALLLRPQILLLDEPTSALD 170
Cdd:PRK10938 92 SPGEDDT-GRTTAEIIQ-DEVKDPA-RCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 171 MSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREAL 226
Cdd:PRK10938 168 VASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-230 |
3.09e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgfRFQ-GDLRRNVQMVFQ-------------DP 88
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA---KFGlTDLRRVLSIIPQspvlfsgtvrfniDP 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 89 YaSLHPNHTLWrtlaEPLQIHGIRDVAPRvttalEQVGLAADaVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSA 168
Cdd:PLN03232 1333 F-SEHNDADLW----EALERAHIKDVIDR-----NPFGLDAE-VSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523681378 169 LDMSVQAeilnLLNRLKQEH--GMTYLLVSHDADVIAHmSDRAAFMAEGVIQRFFDREALVNGE 230
Cdd:PLN03232 1402 VDVRTDS----LIQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-226 |
3.62e-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: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 19 VSAASFRVDAGETFSLIGASGCGKSTILRVLAGL-QREWRGSVDLLGQAI---TPgfrfQGDLRRNVQMVFQD------- 87
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirNP----AQAIRAGIAMVPEDrkrhgiv 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 88 PYASLHPNHTLwRTLAEPLQIHGIRDVAPR--VTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEP 165
Cdd:TIGR02633 352 PILGVGKNITL-SVLKSFCFKMRIDAAAELqiIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 166 TSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREAL 226
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL 490
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-222 |
6.44e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 18 AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQ----AITPGFRFQGDLRRNVQMvfqdpyaslh 93
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaaliAISSGLNGQLTGIENIEL---------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 94 pnhtlwRTLAEPLQIHGIRDVAPRVTTALEQVGLAADAVRRYphqlSGGQRQRVAIARALLLRPQILLLDEPTSALDMSV 173
Cdd:PRK13545 109 ------KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTY----SSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523681378 174 QAEILNLLNRLKqEHGMTYLLVSHDADVIAHMSDRAAFMAEGVIQRFFD 222
Cdd:PRK13545 179 TKKCLDKMNEFK-EQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGD 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-198 |
1.05e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 34 LIGASGCGKSTILRVLAGLQREWRGSVdLLGQAITPGFRFQ-------GDLRRNVQMVFQDPYASLHPNHTLWRTLAEP- 105
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEA-RPAPGIKVGYLPQepqldpeKTVRENVEEGVAEVKAALDRFNEIYAAYAEPd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 106 ----------------LQIHGIRDVAPRvttaLEQvglAADAVRRYP-----HQLSGGQRQRVAIARALLLRPQILLLDE 164
Cdd:PRK11819 117 adfdalaaeqgelqeiIDAADAWDLDSQ----LEI---AMDALRCPPwdakvTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
170 180 190
....*....|....*....|....*....|....*
gi 523681378 165 PTSALDmsvqAEILNLLNR-LKQEHGmTYLLVSHD 198
Cdd:PRK11819 190 PTNHLD----AESVAWLEQfLHDYPG-TVVAVTHD 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-198 |
1.24e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 4 VNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAitpgfrfqgdlrrNVQM 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA-------------NIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 84 VFQDPYASLHPNHTL------WRTLAEPLQIhgIRDVAPRVTtaleqvgLAADAVRRYPHQLSGGQRQRVAIARALLLRP 157
Cdd:PRK15064 387 YAQDHAYDFENDLTLfdwmsqWRQEGDDEQA--VRGTLGRLL-------FSQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 523681378 158 QILLLDEPTSALDM-SVQAeiLNllNRLKQEHGmTYLLVSHD 198
Cdd:PRK15064 458 NVLVMDEPTNHMDMeSIES--LN--MALEKYEG-TLIFVSHD 494
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-202 |
1.25e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQ--------------------REWRGSVDLLGQaiTPgFRFQGDLRRNVQ 82
Cdd:PTZ00265 405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYdptegdiiindshnlkdinlKWWRSKIGVVSQ--DP-LLFSNSIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 83 MVF-----------------QDPYASLHPNHTLWRTLAEPLQ-----------IHG------IRDvaPRVTTALEQVgLA 128
Cdd:PTZ00265 482 YSLyslkdlealsnyynedgNDSQENKNKRNSCRAKCAGDLNdmsnttdsnelIEMrknyqtIKD--SEVVDVSKKV-LI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 129 ADAVRRYP-----------HQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSH 197
Cdd:PTZ00265 559 HDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
....*
gi 523681378 198 DADVI 202
Cdd:PTZ00265 639 RLSTI 643
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-215 |
1.31e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 18 AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITpgFRFQGD-LRRNVQMVFQDPYASLHPN- 95
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID--FKSSKEaLENGISMVHQELNLVLQRSv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 96 -HTLW--------------------RTLAEPLQIhgirDVAPRVTTAleqvglaadavrryphQLSGGQRQRVAIARALL 154
Cdd:PRK10982 91 mDNMWlgryptkgmfvdqdkmyrdtKAIFDELDI----DIDPRAKVA----------------TLSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 155 LRPQILLLDEPTSALDMSVQAEILNLLNRLKqEHGMTYLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-170 |
1.47e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.93 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTF--GAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQ------------------REWRGSVDLLGQ 65
Cdd:cd03289 5 VKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLntegdiqidgvswnsvplQKWRKAFGVIPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 66 AItpgFRFQGDLRRNVqmvfqDPYASlHPNHTLWRTLAEPlqihGIRDVAPRVTTALEQVGLAADAVrryphqLSGGQRQ 145
Cdd:cd03289 85 KV---FIFSGTFRKNL-----DPYGK-WSDEEIWKVAEEV----GLKSVIEQFPGQLDFVLVDGGCV------LSHGHKQ 145
|
170 180
....*....|....*....|....*
gi 523681378 146 RVAIARALLLRPQILLLDEPTSALD 170
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-218 |
2.35e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKT-AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRfqGDLRRNVQMV 84
Cdd:PRK10522 325 LRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP--EDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 85 FQDPYaslhpnhtLWRTLAEPlqiHGIRDVAPRVTTALEQVGLAaDAVRRYPH-----QLSGGQRQRVAIARALLLRPQI 159
Cdd:PRK10522 403 FTDFH--------LFDQLLGP---EGKPANPALVEKWLERLKMA-HKLELEDGrisnlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 160 LLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSHDaDVIAHMSDRAAFMAEGVIQ 218
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-197 |
2.97e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 46.60 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQRE--WRGSVDLLGQAITpgfrfqgDL------ 77
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILLDGEDIL-------ELspdera 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 78 RRNVQMVFQDPYA----SlhpNHTLWRTL--AEPLQIHGIRDVAPRVTTALEQVGLAADAVRRYPHQ-LSGGQRQRVAIA 150
Cdd:COG0396 76 RAGIFLAFQYPVEipgvS---VSNFLRTAlnARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523681378 151 RALLLRPQILLLDEPTSALDM-SVQAeILNLLNRLKQEHgMTYLLVSH 197
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKLRSPD-RGILIITH 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-218 |
3.04e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.70 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKT--AVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFrfqGDLRRN 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNI---SDVHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 81 vqMVFQDPYASLHPNHTLWRTLAEPLQIHGI--RDVAPRVTTALEQVGLAADAvRRYPHQLSGGQRQRVAIARALLLRPQ 158
Cdd:TIGR01257 2014 --MGYCPQFDAIDDLLTGREHLYLYARLRGVpaEEIEKVANWSIQSLGLSLYA-DRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 159 ILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSDRAAFMAEGVIQ 218
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-219 |
3.06e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.40 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 16 KTAVSAASFRVDAGETFSLIGASGCGKSTILrvlAGLQREWRgsvdllgqaITPG-FRFQG---------DLRRNVQMVF 85
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLL---SLIQRHFD---------VSEGdIRFHDipltklqldSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 86 QDPYA---SLHPNHTLWRTLAEPLQIhgirdvaprvttalEQVGLAA---DAVRRYPH-----------QLSGGQRQRVA 148
Cdd:PRK10789 396 QTPFLfsdTVANNIALGRPDATQQEI--------------EHVARLAsvhDDILRLPQgydtevgergvMLSGGQKQRIS 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523681378 149 IARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQehGMTYLLVSHDADVIAHMSDRAAFMAEGVIQR 219
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHIAQR 530
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-208 |
4.66e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 9 LQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLG-------QAITPG-------FRFQ 74
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvNQETPAlpqpaleYVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 75 GDlRRNVQMVFQDPYASLHPNHTLWRTLAEPLQIHGIRDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALL 154
Cdd:PRK10636 87 GD-REYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523681378 155 LRPQILLLDEPTSALDMSVqaeILNLLNRLKQEHGmTYLLVSHDADVIAHMSDR 208
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHDRDFLDPIVDK 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
139-218 |
8.95e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 139 LSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNllNRLKQE-HGMTYLLVSHDADVIAHMsDRAAFMAEGVI 217
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
.
gi 523681378 218 Q 218
Cdd:PLN03130 818 K 818
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-197 |
2.03e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 2.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681378 135 YPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMTYLLVSH 197
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-220 |
2.51e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVdllgqaitpgFRfqgdlRRNVQM-VFQDPYAS---LHPNHTL 98
Cdd:PLN03073 529 NFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV----------FR-----SAKVRMaVFSQHHVDgldLSSNPLL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 99 WRTLAEPlqihGIRDvaPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDM-SVQAEI 177
Cdd:PLN03073 594 YMMRCFP----GVPE--QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALI 667
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 523681378 178 LNLLnrLKQEhgmTYLLVSHDADVIAHMSDRAAFMAEGVIQRF 220
Cdd:PLN03073 668 QGLV--LFQG---GVLMVSHDEHLISGSVDELWVVSEGKVTPF 705
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-148 |
3.00e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 44.40 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITPGFRfqGDLRRNVQMVFQDPYaslhpnhtLWRTL 102
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR--EAYRQLFSAVFSDFH--------LFDRL 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 523681378 103 aepLQIHGIRDVApRVTTALEQVGLaADAVRRYPH-----QLSGGQRQRVA 148
Cdd:COG4615 422 ---LGLDGEADPA-RARELLERLEL-DHKVSVEDGrfsttDLSQGQRKRLA 467
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-220 |
4.34e-05 |
|
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: 44.17 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP-GFRfqgDLRRNVQMVFQDPY---ASLHPNhtl 98
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiGLH---DLRFKITIIPQDPVlfsGSLRMN--- 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 99 wrtlAEPLQIHGIRDVaprvTTALEQVGLAaDAVRRYP----HQ-------LSGGQRQRVAIARALLLRPQILLLDEPTS 167
Cdd:TIGR00957 1380 ----LDPFSQYSDEEV----WWALELAHLK-TFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 168 ALDMS----VQAEILNllnrlkQEHGMTYLLVSHDADVIAHMSdRAAFMAEGVIQRF 220
Cdd:TIGR00957 1451 AVDLEtdnlIQSTIRT------QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEF 1500
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
139-215 |
4.90e-05 |
|
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: 42.70 E-value: 4.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 139 LSGGQRQRVAIAR--ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHmSDRAAFMAEG 215
Cdd:cd03238 88 LSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
137-211 |
5.50e-05 |
|
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: 42.35 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 137 HQLSGGQRQRVAIA----RALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQeHGMTYLLVSHD------ADVIAHMS 206
Cdd:cd03227 76 LQLSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLpelaelADKLIHIK 154
|
....*
gi 523681378 207 DRAAF 211
Cdd:cd03227 155 KVITG 159
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
122-204 |
5.82e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 122 LEQVGLAADAVRRYPHQLSGGQRQRVAIAR--ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQeHGMTYLLVSHDA 199
Cdd:cd03270 121 LVDVGLGYLTLSRSAPTLSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDE 199
|
....*
gi 523681378 200 DVIAH 204
Cdd:cd03270 200 DTIRA 204
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-87 |
6.86e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 6.86e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523681378 13 FGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVdllgqAITPGFRFqGDLRRNvQMVFQD 87
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----SLDPNERL-GKLRQD-QFAFEE 78
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-64 |
7.23e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 7.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLG 64
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG 62
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-178 |
9.25e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 43.36 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQ-AITPGFRF--QGDLRRNVqmVFQDPYASLHpnhtlW 99
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSPQTSWimPGTIKDNI--IFGLSYDEYR-----Y 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 100 RTLAEPLQIH-GIRDVAPRVTTALEQVGLAadavrryphqLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEIL 178
Cdd:TIGR01271 519 TSVIKACQLEeDIALFPEKDKTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-233 |
1.25e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQAITP-GFRfqgDLRRNVQMVFQ-------------DP 88
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLM---DLRKVLGIIPQapvlfsgtvrfnlDP 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 89 YaSLHPNHTLWrtlaEPLQIHGIRDVAPRvttalEQVGLAADaVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSA 168
Cdd:PLN03130 1336 F-NEHNDADLW----ESLERAHLKDVIRR-----NSLGLDAE-VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523681378 169 LDMSVQAEIlnlLNRLKQE-HGMTYLLVSHDADVIAHmSDRAAFMAEGVIQRFFDREALVNGEHRM 233
Cdd:PLN03130 1405 VDVRTDALI---QKTIREEfKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSA 1466
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-197 |
1.47e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.94 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 3 IVNLQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAG------LQrewrGSVDLLGQAI---TPGFRF 73
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykiLE----GDILFKGESIldlEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 74 QgdlrRNVQMVFQDP---------------YASLHPNHTLwrTLAEPLQIHGIrdvaprVTTALEQVGLAADAVRRYPHQ 138
Cdd:CHL00131 83 H----LGIFLAFQYPieipgvsnadflrlaYNSKRKFQGL--PELDPLEFLEI------INEKLKLVGMDPSFLSRNVNE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 139 -LSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMTYLLVSH 197
Cdd:CHL00131 151 gFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
139-218 |
1.72e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 139 LSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILN--LLNRLkqeHGMTYLLVSHDADVIAHmSDRAAFMAEGV 216
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGAL---AGKTRVLATHQVHVVPR-ADYVVALGDGR 858
|
..
gi 523681378 217 IQ 218
Cdd:PTZ00243 859 VE 860
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-177 |
2.36e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 41.38 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLGQ-AITPGFRF--QGDLRRNVqmVFQDPYaslhpNHTLW 99
Cdd:cd03291 57 NLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRiSFSSQFSWimPGTIKENI--IFGVSY-----DEYRY 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523681378 100 RTLAEPLQIH-GIRDVAPRVTTALEQVGLAadavrryphqLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEI 177
Cdd:cd03291 130 KSVVKACQLEeDITKFPEKDNTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
112-217 |
2.88e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 112 RDVAPRVTTALEQVGLAaDAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEhGMT 191
Cdd:NF000106 119 KDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196
|
90 100 110
....*....|....*....|....*....|..
gi 523681378 192 YLLVSH---DADVIAH---MSDRAAFMAEGVI 217
Cdd:NF000106 197 VLLTTQymeEAEQLAHeltVIDRGRVIADGKV 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-207 |
3.38e-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: 41.31 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 34 LIGASGCGKSTILRVLAGLQR----------EWRGSVDllgqaitpgfRFQGDLrrnVQMVFQDPYaslhpNHTLwRTLA 103
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKpnlgdydeepSWDEVLK----------RFRGTE---LQDYFKKLA-----NGEI-KVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 104 EPLQIhgirDVAPRVTT-----ALEQV---GLAADAVR---------RYPHQLSGGQRQRVAIARALLLRPQILLLDEPT 166
Cdd:COG1245 165 KPQYV----DLIPKVFKgtvreLLEKVderGKLDELAEklglenildRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 523681378 167 SALDMSVQAEILNLLNRLKQEhGMTYLLVSHDADVIAHMSD 207
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLAD 280
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
138-207 |
3.51e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 3.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 138 QLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEHGMtyLLVSHDADVIAHMSD 207
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYV--LVVEHDLAVLDYLAD 279
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-215 |
4.52e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 23 SFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLLG---------QAITPGFRFQGDLRR------NVQMVFQD 87
Cdd:PRK10982 268 SFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnhnanEAINHGFALVTEERRstgiyaYLDIGFNS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 88 PYASLHPNHTLWRTLAEPLQIHGIRDV--APRVTTALEQVGLAAdavrryphqLSGGQRQRVAIARALLLRPQILLLDEP 165
Cdd:PRK10982 348 LISNIRNYKNKVGLLDNSRMKSDTQWVidSMRVKTPGHRTQIGS---------LSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 523681378 166 TSALDMSVQAEILNLLNRL-KQEHGMtyLLVSHDADVIAHMSDRAAFMAEG 215
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNG 467
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-230 |
5.38e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.28 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 29 GETFSLIGASGCGKSTILRVLAGLqrewrgsvdllgqaitpgfrfqgdlrrnvqmvfqdpyasLHPNHtlwrtlaeplqi 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARE---------------------------------------LGPPG------------ 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 109 HGIRDVAPRVTTALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKQEH 188
Cdd:smart00382 31 GGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 523681378 189 gmtyLLVSHDADVIAHMSDRAAFMAEGVIQRFFDREALVNGE 230
Cdd:smart00382 111 ----LKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-170 |
1.40e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 7 QDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLlgqaitpgfrfqGDlrrNVQMVFQ 86
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------------GE---TVKLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 87 DPY-ASLHPNHTLWRTLAEPLQI--HGIRDVAPRVTTAL------EQ---VGlaadavrryphQLSGGQRQRVAIARALL 154
Cdd:PRK11819 393 DQSrDALDPNKTVWEEISGGLDIikVGNREIPSRAYVGRfnfkggDQqkkVG-----------VLSGGERNRLHLAKTLK 461
|
170
....*....|....*.
gi 523681378 155 LRPQILLLDEPTSALD 170
Cdd:PRK11819 462 QGGNVLLLDEPTNDLD 477
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-220 |
1.73e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 13 FGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAGLQREWRGSVDLlGQAITPGFRFQGDLRrnvqmvfqdpyasl 92
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLGYFAQHQLE-------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 93 hpnhtLWRTLAEPLQiHGIRdVAPRVTTA-----LEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLLDEPTS 167
Cdd:PRK10636 387 -----FLRADESPLQ-HLAR-LAPQELEQklrdyLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523681378 168 ALDMSV-QAeilnLLNRLKQEHGmTYLLVSHDADVIAHMSDRAAFMAEGVIQRF 220
Cdd:PRK10636 460 HLDLDMrQA----LTEALIDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKVEPF 508
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
121-203 |
1.96e-03 |
|
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: 38.36 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 121 ALEQVGLAADAVRRYPHQLSGGQRQRVAIARALLLRPQILLL---DEPTSALDMSVQAEILNLLNRLKqEHGMTYLLVSH 197
Cdd:cd03271 152 TLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTLyilDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVVVIEH 230
|
....*.
gi 523681378 198 DADVIA 203
Cdd:cd03271 231 NLDVIK 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-202 |
2.14e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 139 LSGGQRQRVAIAR---ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKqEHGMTYLLVSHDADVI 202
Cdd:TIGR00630 830 LSGGEAQRIKLAKelsKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLV-DKGNTVVVIEHNLDVI 895
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
138-207 |
2.57e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.59 E-value: 2.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681378 138 QLSGGQRQ------RVAIARALLLRPQILLLDEPTSALDM-SVQAEILNLLNRLKQEHGMTYLLVSHDADVIAHMSD 207
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADH 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-220 |
2.99e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.46 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 6 LQDLQVTFGAKTAVSAASFRVDAGETFSLIGASGCGKSTILRVLAG-----------LQREWRGSvdllGQAITpgfrfq 74
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS----GETIW------ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 75 gDLRRNVQMVfqdpYASLHPNHTLwRTLAEPLQIHGIRD---VAPRVTTALEQ--------VGLAADAVRRYPHQLSGGQ 143
Cdd:PRK10938 333 -DIKKHIGYV----SSSLHLDYRV-STSVRNVILSGFFDsigIYQAVSDRQQKlaqqwldiLGIDKRTADAPFHSLSWGQ 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 144 RQRVAIARALLLRPQILLLDEPTSALDMsvqaeilnlLNRL--KQ------EHGMTYLL-VSH-DADVIAHMSDRAAFMA 213
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDP---------LNRQlvRRfvdvliSEGETQLLfVSHhAEDAPACITHRLEFVP 477
|
....*..
gi 523681378 214 EGVIQRF 220
Cdd:PRK10938 478 DGDIYRY 484
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-229 |
3.79e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681378 120 TALEQVGLAADAVRRYPHQLSGGQRQRVAIAR--ALLLRPQILLLDEPTSALDMSVQAEILNLLNRLKqEHGMTYLLVSH 197
Cdd:PRK00635 458 SILIDLGLPYLTPERALATLSGGEQERTALAKhlGAELIGITYILDEPSIGLHPQDTHKLINVIKKLR-DQGNTVLLVEH 536
|
90 100 110
....*....|....*....|....*....|..
gi 523681378 198 DADVIAhMSDRAAFMAEGViqRFFDREALVNG 229
Cdd:PRK00635 537 DEQMIS-LADRIIDIGPGA--GIFGGEVLFNG 565
|
|
| |
