|
Name |
Accession |
Description |
Interval |
E-value |
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-360 |
3.00e-132 |
|
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: 381.76 E-value: 3.00e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 1 MSIKVDISLQRADFALQIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIA 79
Cdd:COG4148 1 MMLEVDFRLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPdSGRIRLGGEVLQDSARGIFLPPHRRRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 80 YLFQEARLLPHLSIEDNIRLNLKLRKVHKSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEP 159
Cdd:COG4148 81 YVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 160 LSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFA--EHSALFDQEQLASVF 237
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSrpDLLPLAGGEEAGSVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 238 EATITELDQENSLSKAEIKGSQtgapiaVWIGEQALSEGQKIRLRVTARDVSISRFPNTEQSILNVLPARIKNIkHTSES 317
Cdd:COG4148 241 EATVAAHDPDYGLTRLALGGGR------LWVPRLDLPPGTRVRVRIRARDVSLALEPPEGSSILNILPGRVVEI-EPADG 313
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1024600867 318 HSVRIKLAIGDNTLHALITKRSLKKLNLKIDQEVWAQVKALSI 360
Cdd:COG4148 314 GQVLVRLDLGGQTLLARITRRSADELGLAPGQTVYAQIKSVAL 356
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
3-360 |
6.64e-94 |
|
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: 284.31 E-value: 6.64e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 3 IKVDISLQRADFALQIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNTWLAPAKRNIAYL 81
Cdd:TIGR02142 1 LSARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDeGEIVLNGRTLFDSRKGIFLPPEKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 82 FQEARLLPHLSIEDNIRLNLKLRKVHKSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLS 161
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 162 ALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHS-ALFDQEQLASVFEAT 240
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDlPWLAREDQGSLIEGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 241 ITELDQENSLSKAEIKGSqtgapiAVWIGEQALSEGQKIRLRVTARDVSISRFPNTEQSILNVLPARIKNIKHtSESHSV 320
Cdd:TIGR02142 241 VAEHDQHYGLTALRLGGG------HLWVPENLGPTGARLRLRVPARDVSLALQKPEATSIRNILPARVVEIED-SDIGRV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1024600867 321 RIKLAIGDNTLHALITKRSLKKLNLKIDQEVWAQVKALSI 360
Cdd:TIGR02142 314 GVVLESGGKTLWARITRWARDELGIAPGTPVFAQIKAVAL 353
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
3-360 |
5.69e-84 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 258.65 E-value: 5.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 3 IKVDISLQRADFALQIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNTWLAPAKRNIAYL 81
Cdd:PRK11144 2 LELNFKQQLGDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQkGRIVLNGRVLFDAEKGICLPPEKRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 82 FQEARLLPHLSIEDNIRLNLKlrKVHKSDLD-ITRVLddcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPL 160
Cdd:PRK11144 82 FQDARLFPHYKVRGNLRYGMA--KSMVAQFDkIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 161 SALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAeHSALFD---QEQLASVF 237
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWA-SSAMRPwlpKEEQSSIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 238 EATITELDQENSLSKAEIkGSQtgapiAVWIGEQALSEGQKIRLRVTARDVSISRFPNTEQSILNVLPARIKNIkhTSES 317
Cdd:PRK11144 236 KVTVLEHHPHYAMTALAL-GDQ-----HLWVNKLDAPLGTALRIRIQASDVSLVLQPPQQSSIRNILRAKVVEI--YDDN 307
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1024600867 318 HSVRIKLAIGDNTLHALITKRSLKKLNLKIDQEVWAQVKALSI 360
Cdd:PRK11144 308 GQVEVKLEVGGKTLWARITPWARDELALKPGQWLYAQIKSVSI 350
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-361 |
7.63e-71 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 224.64 E-value: 7.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 1 MSIKV-DISLQRADFAL--QIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWqrsscNTWLAPAKR 76
Cdd:COG1118 1 MSIEVrNISKRFGSFTLldDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPdSGRIVLNGRDL-----FTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 77 NIAYLFQEARLLPHLSIEDNIRLNLKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLI 154
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRarVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 155 LMDEPLSALDATSK----RQMLRLIQRFKSSSstpIFyVSHSIDEIAQLADDILLMQQGEAAYLGPAlqtfaehSALFDQ 230
Cdd:COG1118 156 LLDEPFGALDAKVRkelrRWLRRLHDELGGTT---VF-VTHDQEEALELADRVVVMNQGRIEQVGTP-------DEVYDR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 231 EqlASVFEATITEldqENSLSKAEIKGSQtgapiaVWIGEQALSEGQKI-----RLRVTARDVSISRFPNTEqsilNVLP 305
Cdd:COG1118 225 P--ATPFVARFLG---CVNVLRGRVIGGQ------LEADGLTLPVAEPLpdgpaVAGVRPHDIEVSREPEGE----NTFP 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1024600867 306 ARIKNIKHTseSHSVRIKLAIGDNT---LHALITKRSLKKLNLKIDQEVWAQVKALSIF 361
Cdd:COG1118 290 ATVARVSEL--GPEVRVELKLEDGEgqpLEAEVTKEAWAELGLAPGDPVYLRPRPARVF 346
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-209 |
1.95e-65 |
|
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: 206.22 E-value: 1.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQRefknTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWqrsscnTWLAPAKRNIAYLFQEARLLPHL 91
Cdd:cd03259 18 DLSLTVEP----GEFLALLGPSGCGKTTLLRLIAGLERPdSGEILIDGRDV------TGVPPERRNIGMVFQDYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 92 SIEDNIRLNLKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKR 169
Cdd:cd03259 88 TVAENIAFGLKLRGVPKAEIRarVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLRE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1024600867 170 QMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:cd03259 168 ELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-357 |
5.73e-65 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 209.95 E-value: 5.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQR-EFkntgLTgVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWqrsscnTWLAPAKRNIAYLFQEARLLPH 90
Cdd:COG3842 23 DVSLSIEPgEF----VA-LLGPSGCGKTTLLRMIAGFETPdSGRILLDGRDV------TGLPPEKRNVGMVFQDYALFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 91 LSIEDNIRLNLKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:COG3842 92 LTVAENVAFGLRMRGVPKAEIRarVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 169 RQM---LRLIQRfksSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPAlqtfaehSALFDQEQ---------LASV 236
Cdd:COG3842 172 EEMreeLRRLQR---ELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP-------EEIYERPAtrfvadfigEANL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 237 FEATITELDQEnslsKAEIKGSQTGAPiavwiGEQALSEGQKIRLRVTARDVSISRfpnteQSILNVLPARIKNIKHTSE 316
Cdd:COG3842 242 LPGTVLGDEGG----GVRTGGRTLEVP-----ADAGLAAGGPVTVAIRPEDIRLSP-----EGPENGLPGTVEDVVFLGS 307
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1024600867 317 SHSVRIKLAIGDnTLHALITKRSLkkLNLKIDQEVWAQVKA 357
Cdd:COG3842 308 HVRYRVRLGDGQ-ELVVRVPNRAA--LPLEPGDRVGLSWDP 345
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
3-215 |
2.46e-63 |
|
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: 200.98 E-value: 2.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 3 IKVDISLQRADFALQIQREFkNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYL 81
Cdd:cd03297 2 LCVDIEKRLPDFTLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPdGGTIVLNGTVLFDSRKKINLPPQQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 82 FQEARLLPHLSIEDNIRLNLKlRKVHKSDLD-ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPL 160
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLK-RKRNREDRIsVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 161 SALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
13-362 |
6.74e-61 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 199.14 E-value: 6.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQR-EFkntglTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWqrsscnTWLAPAKRNIAYLFQEARLLPH 90
Cdd:COG3839 21 DIDLDIEDgEF-----LVLLGPSGCGKSTLLRMIAGLEDPtSGEILIGGRDV------TDLPPKDRNIAMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 91 LSIEDNIRLNLKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:COG3839 90 MTVYENIAFPLKLRKVPKAEIDrrVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 169 RQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFdqeqLAS--------VFEAT 240
Cdd:COG3839 170 VEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLF----VAGfigsppmnLLPGT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 241 ITEldqenslSKAEIKGSQTGAPIAVwigeqALSEGQKIRLRVTARDVSISRFPNteqsilNVLPARIKNIKHT-SESHs 319
Cdd:COG3839 246 VEG-------GGVRLGGVRLPLPAAL-----AAAAGGEVTLGIRPEHLRLADEGD------GGLEATVEVVEPLgSETL- 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1024600867 320 vrIKLAIGDNTLHALITKRSlkklNLKIDQEVWAQVKA--LSIFD 362
Cdd:COG3839 307 --VHVRLGGQELVARVPGDT----RLRPGDTVRLAFDPerLHLFD 345
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
13-206 |
3.81e-59 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 191.84 E-value: 3.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQR-EFkntglTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVwqrsscntwLAPAKRNIAYLFQEARLLPH 90
Cdd:COG1116 29 DVSLTVAAgEF-----VALVGPSGCGKSTLLRLIAGLEKPtSGEVLVDGKP---------VTGPGPDRGVVFQEPALLPW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 91 LSIEDNIRLNLKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:COG1116 95 LTVLDNVALGLELRGVPKAERRerARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTR 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1024600867 169 RQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLM 206
Cdd:COG1116 175 ERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-206 |
7.76e-57 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 184.60 E-value: 7.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQR-EFkntglTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVwqrsscntwLAPAKRNIAYLFQEARLLPH 90
Cdd:cd03293 22 DISLSVEEgEF-----VALVGPSGCGKSTLLRIIAGLERPtSGEVLVDGEP---------VTGPGPDRGYVFQQDALLPW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 91 LSIEDNIRLNLKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:cd03293 88 LTVLDNVALGLELQGVPKAEARerAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTR 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1024600867 169 RQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLM 206
Cdd:cd03293 168 EQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
31-215 |
2.37e-51 |
|
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: 170.13 E-value: 2.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 31 FGPSGCGKTSLLRCIAGLEQP-HGEISVN-KQVwqrsscnTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHK 108
Cdd:cd03301 32 LGPSGCGKTTTLRMIAGLEEPtSGRIYIGgRDV-------TDLPPKDRDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPI 186
Cdd:cd03301 105 DEIDerVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTT 184
|
170 180
....*....|....*....|....*....
gi 1024600867 187 FYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03301 185 IYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
16-210 |
2.41e-50 |
|
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: 167.67 E-value: 2.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 16 LQIQR-EFkntglTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQEARLLPHLSI 93
Cdd:cd03255 25 LSIEKgEF-----VAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPDLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 94 EDNIRLNLKLRKVHKSD--LDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:cd03255 100 LENVELPLLLAGVPKKErrERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEV 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1024600867 172 LRLIQRFKSSSSTPIFYVSHSiDEIAQLADDILLMQQGE 210
Cdd:cd03255 180 MELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
28-216 |
3.14e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.93 E-value: 3.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVN-KQVWQRSscntwlAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRK 105
Cdd:COG1131 29 FGLLGPNGAGKTTTIRMLLGLLRPtSGEVRVLgEDVARDP------AEVRRRIGYVPQEPALYPDLTVRENLRFFARLYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:COG1131 103 LPRKEARerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGK 182
|
170 180 190
....*....|....*....|....*....|...
gi 1024600867 184 TpIFYVSHSIDEIAQLADDILLMQQGEAAYLGP 216
Cdd:COG1131 183 T-VLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-210 |
3.33e-50 |
|
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: 165.82 E-value: 3.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQR-EFkntglTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTwlAPAKRNIAYLFQEARLLPH 90
Cdd:cd03229 18 DVSLNIEAgEI-----VALLGPSGSGKSTLLRCIAGLEEPdSGSILIDGEDLTDLEDEL--PPLRRRIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 91 LSIEDNIRLnlklrkvhksdlditrvlddcglsrlrsqrpdTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ 170
Cdd:cd03229 91 LTVLENIAL--------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1024600867 171 MLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03229 139 VRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
29-237 |
8.16e-50 |
|
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: 167.29 E-value: 8.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVN-KQVWQRsscntWLAPAKRNIAYLFQEAR--LLPHLSIEDNIRLNLKLR 104
Cdd:COG1124 35 GLVGESGSGKSTLLRALAGLERPwSGEVTFDgRPVTRR-----RRKAFRRRVQMVFQDPYasLHPRHTVDRILAEPLRIH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHKSDLDITRVLDDCGL-SRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:COG1124 110 GLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERG 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1024600867 184 TPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLASVF 237
Cdd:COG1124 190 LTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELLAASL 243
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
21-241 |
8.64e-49 |
|
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: 164.26 E-value: 8.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScntwlAPAKRNIAYLFQEARLLPHLSIEDNIRL 99
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLRMLAGLLKPdSGSILIDGEDVRKEP-----REARRQIGVLPDERGLYDRLTVRENIRY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 NLKLRKVHKSDL--DITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQR 177
Cdd:COG4555 98 FAELYGLFDEELkkRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024600867 178 FKSSSSTPIFyVSHSIDEIAQLADDILLMQQGEAAYLGPAlqtfAEHSALFDQEQLASVFEATI 241
Cdd:COG4555 178 LKKEGKTVLF-SSHIMQEVEALCDRVVILHKGKVVAQGSL----DELREEIGEENLEDAFVALI 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-210 |
9.77e-48 |
|
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: 161.35 E-value: 9.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVN-KQVwqrsscnTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVH 107
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPdSGKILLNgKDI-------TNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRKVD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSD-----LDITRVLddcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSS 182
Cdd:cd03299 103 KKEierkvLEIAEML---GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEF 179
|
170 180
....*....|....*....|....*...
gi 1024600867 183 STPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03299 180 GVTVLHVTHDFEEAWALADKVAIMLNGK 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-231 |
8.95e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 158.76 E-value: 8.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 6 DISLQRADFALQIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVwqrsscNTWLAPAKRNIAYLFQE 84
Cdd:COG3840 6 DLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDsGRILWNGQD------LTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 85 ARLLPHLSIEDNIRL----NLKLRKVHKSDLDitRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPL 160
Cdd:COG3840 80 NNLFPHLTVAQNIGLglrpGLKLTAEQRAQVE--QALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 161 SALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPAlqtfaehSALFDQE 231
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT-------AALLDGE 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
32-210 |
1.04e-46 |
|
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: 158.55 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRsscntwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHKSD 110
Cdd:cd03300 33 GPSGCGKTTLLRLIAGFETPtSGEILLDGKDITN------LPPHKRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 111 LD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFY 188
Cdd:cd03300 107 IKerVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVF 186
|
170 180
....*....|....*....|..
gi 1024600867 189 VSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03300 187 VTHDQEEALTMSDRIAVMNKGK 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
29-236 |
1.17e-45 |
|
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: 163.15 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNTwLAPAKRNIAYLFQ--EARLLPHLSIEDNIRLNLKLRK 105
Cdd:COG1123 295 GLVGESGSGKSTLARLLLGLLRPTsGSILFDGKDLTKLSRRS-LRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VH-KSDLD--ITRVLDDCGLSR-LRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSS 181
Cdd:COG1123 374 LLsRAERRerVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRE 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 182 SSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLASV 236
Cdd:COG1123 454 LGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAV 508
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
28-210 |
2.47e-45 |
|
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: 154.97 E-value: 2.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScNTWLAPAKRNIAYLFQEAR--LLPHLSIEDNIR--LNLK 102
Cdd:cd03257 34 LGLVGESGSGKSTLARAILGLLKPtSGSIIFDGKDLLKLS-RRLRKIRRKEIQMVFQDPMssLNPRMTIGEQIAepLRIH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKVHKSDLDITRVLDDCGL---SRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:cd03257 113 GKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQ 192
|
170 180 190
....*....|....*....|....*....|.
gi 1024600867 180 SSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03257 193 EELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
30-351 |
6.05e-45 |
|
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: 156.88 E-value: 6.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISV-NKQVWQRsscntwlAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVH 107
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPdSGSIMLdGEDVTNV-------PPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLDiTRVLDDCGLSRLR---SQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSST 184
Cdd:TIGR01187 74 RAEIK-PRVLEALRLVQLEefaDRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 185 PIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLA--SVFEATITELDQEnslskAEIKGSQTGA 262
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGeiNVFEATVIERKSE-----QVVLAGVEGR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 263 PIAVWigeQALSEGQKIRLRVTARDVSISRFPNTEQSILNVLPARIKNIKHTSESHSVRIKLAIGDNTLHALITKRSLKK 342
Cdd:TIGR01187 228 RCDIY---TDVPVEKDQPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSEFFNEDDPH 304
|
....*....
gi 1024600867 343 LNLKIDQEV 351
Cdd:TIGR01187 305 MSPSIGDRV 313
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-210 |
2.72e-44 |
|
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: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQR-EFKntgltGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQvwqrsSCNTWLAPA-KRNIAYLFQEARLLP 89
Cdd:COG4619 18 PVSLTLEAgECV-----AITGPSGSGKSTLLRALADLDPPTsGEIYLDGK-----PLSAMPPPEwRRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 90 HlSIEDNIRLNLKLRKVHKSDLDITRVLDDCGLS-RLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:COG4619 88 G-TVRDNLPFPFQLRERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1024600867 169 RQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:COG4619 167 RRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-209 |
1.45e-43 |
|
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: 150.57 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 1 MSIKV-DISLQRADF-AL-QIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPHgeisvNKQVWQRSSCNTWLAPAKRN 77
Cdd:cd03296 1 MSIEVrNVSKRFGDFvALdDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD-----SGTILFGGEDATDVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 78 IAYLFQEARLLPHLSIEDNIRLNLKLRKVHK--SDLDITR----VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEP 151
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRVKPRSErpPEAEIRAkvheLLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1024600867 152 DLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-299 |
1.71e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 154.33 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQR-EFkntgLTgVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrssCNTWLAPAKRNIAYLFQEARLLPH 90
Cdd:PRK09452 32 NLDLTINNgEF----LT-LLGPSGCGKTTVLRLIAGFETPdSGRIMLDGQ------DITHVPAENRHVNTVFQSYALFPH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 91 LSIEDNIRLNLKLRKVHKSDLDiTRVLDDCGLSRLRS---QRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATS 167
Cdd:PRK09452 101 MTVFENVAFGLRMQKTPAAEIT-PRVMEALRMVQLEEfaqRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 168 KRQM---LRLIQRfkSSSSTPIFyVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAE----HSALFDQEqlASVFEAT 240
Cdd:PRK09452 180 RKQMqneLKALQR--KLGITFVF-VTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEpknlFVARFIGE--INIFDAT 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1024600867 241 ITELDQENSLsKAEIKGsqTGAPIAVwigEQALSEGQKIRLRVTARDVSISRFPNTEQS 299
Cdd:PRK09452 255 VIERLDEQRV-RANVEG--RECNIYV---NFAVEPGQKLHVLLRPEDLRVEEINDDEHA 307
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
16-210 |
2.31e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.81 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 16 LQIQR-EFkntglTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQEARLLPHLSI 93
Cdd:COG1136 29 LSIEAgEF-----VAIVGPSGSGKSTLLNILGGLDRPtSGEVLIDGQDISSLSERELARLRRRHIGFVFQFFNLLPELTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 94 EDNIRLNLKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:COG1136 104 LENVALPLLLAGVSRKERRerARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEV 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1024600867 172 LRLIQRFKSSSSTPIFYVSHSiDEIAQLADDILLMQQGE 210
Cdd:COG1136 184 LELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
28-227 |
7.67e-43 |
|
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: 148.63 E-value: 7.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSScntwLAPAKRNIAYLFQ--EARLLpHLSIEDNIRLNLKLR 104
Cdd:COG1122 30 VAIIGPNGSGKSTLLRLLNGLLKPTsGEVLVDGKDITKKN----LRELRRKVGLVFQnpDDQLF-APTVEEDVAFGPENL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSS 182
Cdd:COG1122 105 GLPREEIRerVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 183 STpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSAL 227
Cdd:COG1122 185 KT-VIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
28-210 |
1.44e-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: 147.23 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSScntwLAPAKRNIAYLFQEARL-LPHLSIEDNIRLNLKLRK 105
Cdd:cd03225 30 VLIVGPNGSGKSTLLRLLNGLLGPTsGEVLVDGKDLTKLS----LKELRRKVGLVFQNPDDqFFGPTVEEEVAFGLENLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:cd03225 106 LPEEEIEerVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGK 185
|
170 180
....*....|....*....|....*..
gi 1024600867 184 TpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03225 186 T-IIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-206 |
4.04e-42 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 147.70 E-value: 4.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 12 ADFALQIQREfkntGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScntwlapAKRniAYLFQEARLLPH 90
Cdd:COG4525 24 QDVSLTIESG----EFVVALGASGCGKTTLLNLIAGFLAPsSGEITLDGVPVTGPG-------ADR--GVVFQKDALLPW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 91 LSIEDNIRLNLKLRKVHKSD-LDI-TRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:COG4525 91 LNVLDNVAFGLRLRGVPKAErRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTR 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1024600867 169 RQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLM 206
Cdd:COG4525 171 EQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
30-219 |
4.92e-42 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 150.57 E-value: 4.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VF-GPSGCGKTSLLRCIAGLEQ-PHGEISVNKQVWQRsscntwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVH 107
Cdd:PRK11000 33 VFvGPSGCGKSTLLRMIAGLEDiTSGDLFIGEKRMND------VPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRF-KSSSST 184
Cdd:PRK11000 107 KEEINqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRT 186
|
170 180 190
....*....|....*....|....*....|....*
gi 1024600867 185 PIfYVSHSIDEIAQLADDILLMQQGEAAYLGPALQ 219
Cdd:PRK11000 187 MI-YVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
28-227 |
1.21e-41 |
|
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: 152.36 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQE--ARLLPhLSIEDNIRLNLKLRK 105
Cdd:COG1123 35 VALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:COG1123 114 LSRAEARarVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERG 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1024600867 184 TPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSAL 227
Cdd:COG1123 194 TTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
27-243 |
1.67e-41 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.57 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVN-KQVWQRSScnTWLApakRNIAYLFQEARLLPHLSIEDNIRLNLK-- 102
Cdd:COG1120 29 VTALLGPNGSGKSTLLRALAGLLKPSsGEVLLDgRDLASLSR--RELA---RRIAYVPQEPPAPFGLTVRELVALGRYph 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 ---LRKVHKSDLDI-TRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRF 178
Cdd:COG1120 104 lglFGRPSAEDREAvEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 179 KSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPAlqtfaehSALFDQEQLASVF--EATITE 243
Cdd:COG1120 184 ARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP-------EEVLTPELLEEVYgvEARVIE 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-216 |
1.72e-40 |
|
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: 142.32 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 6 DISLQRADFAL--QIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH------GEISVN-KQVWQRSSCNTWLapaKR 76
Cdd:cd03260 5 DLNVYYGDKHAlkDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdeGEVLLDgKDIYDLDVDVLEL---RR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 77 NIAYLFQEARLLPhLSIEDNIRLNLKLRKVHKSDLDITRV---LDDCGLSR--LRSQRPDTLSGGQRQRACLARAIVCEP 151
Cdd:cd03260 82 RVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVeeaLRKAALWDevKDRLHALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 152 DLILMDEPLSALDATSKRQMLRLIQRFKssSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGP 216
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
32-211 |
4.49e-40 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 144.99 E-value: 4.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQ-PHGEISVNKQVwqrssCNTwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHKSD 110
Cdd:PRK11650 37 GPSGCGKSTLLRMVAGLERiTSGEIWIGGRV-----VNE-LEPADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 111 LD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMlRL-IQRFKSSSSTPIF 187
Cdd:PRK11650 111 IEerVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM-RLeIQRLHRRLKTTSL 189
|
170 180
....*....|....*....|....
gi 1024600867 188 YVSHSIDEIAQLADDILLMQQGEA 211
Cdd:PRK11650 190 YVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
29-222 |
6.17e-40 |
|
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: 141.18 E-value: 6.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVH 107
Cdd:cd03258 35 GIIGRSGAGKSTLIRCINGLERPtSGSVLVDGTDLTLLS-GKELRKARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTP 185
Cdd:cd03258 114 KAEIEerVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLT 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 186 IFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFA 222
Cdd:cd03258 194 IVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
28-210 |
1.15e-39 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 138.30 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScntwlAPAKRNIAYLFQEARLLPHLSIEDNIRLnlklrkv 106
Cdd:cd03230 29 YGLLGPNGAGKTTLIKIILGLLKPdSGEIKVLGKDIKKEP-----EEVKRRIGYLPEEPSLYENLTVRENLKL------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 hksdlditrvlddcglsrlrsqrpdtlSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTpI 186
Cdd:cd03230 97 ---------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKT-I 148
|
170 180
....*....|....*....|....
gi 1024600867 187 FYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03230 149 LLSSHILEEAERLCDRVAILNNGR 172
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
27-224 |
2.81e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 2.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVwqrsscntwLAPAKRNIAYLFQEA---RLLPhLSIEDNIRLNLK 102
Cdd:COG1121 34 FVAIVGPNGAGKSTLLKAILGLLPPTsGTVRLFGKP---------PRRARRRIGYVPQRAevdWDFP-ITVRDVVLMGRY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 -----LRKVHKSDLD-ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:COG1121 104 grrglFRRPSRADREaVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1024600867 177 RFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGEAAYlGPALQTFAEH 224
Cdd:COG1121 184 ELRREGKT-ILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPE 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
32-215 |
3.80e-39 |
|
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: 139.36 E-value: 3.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVNKQVwqrsscNTWLAPAK--RNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHK 108
Cdd:cd03295 34 GPSGSGKTTTMKMINRLIEPtSGEIFIDGED------IREQDPVElrRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLDiTRV---LDDCGL--SRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:cd03295 108 EKIR-ERAdelLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELG 186
|
170 180 190
....*....|....*....|....*....|..
gi 1024600867 184 TPIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03295 187 KTIVFVTHDIDEAFRLADRIAIMKNGEIVQVG 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
28-219 |
1.30e-38 |
|
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: 137.25 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrsSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKV 106
Cdd:cd03263 31 FGLLGHNGAGKTTTLKMLTGELRPtSGTAYINGY-----SIRTDRKAARQSLGYCPQFDALFDELTVREHLRFYARLKGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSt 184
Cdd:cd03263 106 PKSEIKeeVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRS- 184
|
170 180 190
....*....|....*....|....*....|....*
gi 1024600867 185 pIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQ 219
Cdd:cd03263 185 -IILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
28-222 |
1.34e-38 |
|
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: 137.63 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSScNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKlRKV 106
Cdd:cd03261 29 LAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDISGLS-EAELYRLRRRMGMLFQSGALFDSLTVFENVAFPLR-EHT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDLDITRV----LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSS 182
Cdd:cd03261 107 RLSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKEL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1024600867 183 STPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFA 222
Cdd:cd03261 187 GLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-215 |
2.02e-38 |
|
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: 136.47 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 4 KVDISLQRADFALQIQreFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWqrsscnTWLAPAKRNIAYLF 82
Cdd:cd03298 5 KIRFSYGEQPMHFDLT--FAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLINGVDV------TAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 83 QEARLLPHLSIEDNIRL----NLKLRKVHKSDLDitRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDE 158
Cdd:cd03298 77 QENNLFAHLTVEQNVGLglspGLKLTAEDRQAIE--VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 159 PLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
32-208 |
6.27e-38 |
|
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: 134.91 E-value: 6.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISvnkqvWQRSSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHKSD 110
Cdd:COG4133 35 GPNGSGKTTLLRILAGLLPPsAGEVL-----WNGEPIRDAREDYRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 111 LDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTpIFYVS 190
Cdd:COG4133 110 EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTT 188
|
170
....*....|....*...
gi 1024600867 191 HsiDEIAQLADDILLMQQ 208
Cdd:COG4133 189 H--QPLELAAARVLDLGD 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
32-243 |
1.51e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 137.93 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVN-KQVWQRSSCNtwlapakRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHKS 109
Cdd:PRK11432 39 GPSGCGKTTVLRLVAGLEKPtEGQIFIDgEDVTHRSIQQ-------RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 110 DLDiTRV---LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM---LR-LIQRFKSSS 182
Cdd:PRK11432 112 ERK-QRVkeaLELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMrekIReLQQQFNITS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024600867 183 stpiFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQL--ASVFEATITE 243
Cdd:PRK11432 191 ----LYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMgdANIFPATLSG 249
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
14-216 |
1.93e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 134.32 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 14 FALQIQREFKntglTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSScntwlaPAKRNIAYLFQEARLLPHLS 92
Cdd:PRK10771 18 FDLTVERGER----VAILGPSGAGKSTLLNLIAGFLTPAsGSLTLNGQDHTTTP------PSRRPVSMLFQENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 93 IEDNIRL----NLKLRKVHKSDL-DITRV--LDDCgLSRLRSQrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDA 165
Cdd:PRK10771 88 VAQNIGLglnpGLKLNAAQREKLhAIARQmgIEDL-LARLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 166 TSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGP 216
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
30-210 |
2.48e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 132.49 E-value: 2.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISvnkqvwqrsSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLK--LRKv 106
Cdd:PRK11247 43 VVGRSGCGKSTLLRLLAGLETPsAGELL---------AGTAPLAEAREDTRLMFQDARLLPWKKVIDNVGLGLKgqWRD- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 hksdlDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPI 186
Cdd:PRK11247 113 -----AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTV 187
|
170 180
....*....|....*....|....
gi 1024600867 187 FYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK11247 188 LLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-161 |
4.91e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 128.15 E-value: 4.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRsscnTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRK 105
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPtEGTILLDGQDLTD----DERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLLLKG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 106 VHKSDLD--ITRVLDDCGLSRLRSQRPD----TLSGGQRQRACLARAIVCEPDLILMDEPLS 161
Cdd:pfam00005 89 LSKREKDarAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
16-210 |
6.33e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.17 E-value: 6.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 16 LQIQR-EFkntgltgVF--GPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrsscNtwLAPAKRN-IAYL-------FQ 83
Cdd:COG2884 23 LEIEKgEF-------VFltGPSGAGKSTLLKLLYGEERPtSGQVLVNGQ-------D--LSRLKRReIPYLrrrigvvFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 84 EARLLPHLSIEDNIRLNLKLRKVHKSDL--DITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLS 161
Cdd:COG2884 87 DFRLLPDRTVYENVALPLRVTGKSRKEIrrRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1024600867 162 ALDATSKRQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:COG2884 167 NLDPETSWEIMELLEEINRRGTT-VLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-206 |
7.11e-36 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 129.58 E-value: 7.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScntwlapakRNIAYLFQEA---RLLPhLSIEDN 96
Cdd:cd03235 21 EVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtSGSIRVFGKPLEKER---------KRIGYVPQRRsidRDFP-ISVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 97 IRLNL--------KLRKVHKSDldITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:cd03235 91 VLMGLyghkglfrRLSKADKAK--VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1024600867 169 RQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLM 206
Cdd:cd03235 169 EDIYELLRELRREGMT-ILVVTHDLGLVLEYFDRVLLL 205
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
16-217 |
7.50e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.56 E-value: 7.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 16 LQIQR-EFkntglTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVN-KQVWQRSScnTWLAPAKRNIAYLFQEARLLPHLS 92
Cdd:COG3638 24 LEIERgEF-----VALIGPSGAGKSTLLRCLNGLVEPtSGEILVDgQDVTALRG--RALRRLRRRIGMIFQQFNLVPRLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 93 IEDNI---RLN----LK--LRKVHKSDLDIT-RVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSA 162
Cdd:COG3638 97 VLTNVlagRLGrtstWRslLGLFPPEDRERAlEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVAS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 163 LDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPA 217
Cdd:COG3638 177 LDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
28-216 |
1.49e-35 |
|
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: 129.71 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKv 106
Cdd:COG1127 34 LAIIGGSGSGKSVLLKLIIGLLRPdSGEILVDGQDITGLSEKE-LYELRRRIGMLFQGGALFDSLTVFENVAFPLREHT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDLDITR----VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSS 182
Cdd:COG1127 112 DLSEAEIRElvleKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDEL 191
|
170 180 190
....*....|....*....|....*....|....
gi 1024600867 183 STPIFYVSHSIDEIAQLADDILLMQQGEAAYLGP 216
Cdd:COG1127 192 GLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
30-210 |
1.86e-35 |
|
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: 130.46 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHK 108
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPtSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPI 186
Cdd:cd03294 135 AEREerAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTI 214
|
170 180
....*....|....*....|....
gi 1024600867 187 FYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03294 215 VFITHDLDEALRLGDRIAIMKDGR 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
32-311 |
2.86e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 129.43 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLE-QPHGEISVNKQVWQRsscntwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHKS- 109
Cdd:PRK10851 35 GPSGSGKTTLLRIIAGLEhQTSGHIRFHGTDVSR------LHARDRKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERp 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 110 -----DLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR----LIQRFKS 180
Cdd:PRK10851 109 naaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRwlrqLHEELKF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 181 SSstpiFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLASVfeatiteldqeNSLsKAEIKGSQt 260
Cdd:PRK10851 189 TS----VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV-----------NRL-QGTIRGGQ- 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 261 gapiaVWIGEQALSEGQ------KIRLRVTARDVSISRfpntEQSILNVLPARIKNI 311
Cdd:PRK10851 252 -----FHVGAHRWPLGYtpayqgPVDLFLRPWEVDISR----RTSLDSPLPVQVLEV 299
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-215 |
7.01e-34 |
|
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: 124.59 E-value: 7.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrssCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRL----NLKLR 104
Cdd:TIGR01277 29 IMGPSGAGKSTLLNLIAGFIEPaSGSIKVNDQ------SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLglhpGLKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHKSDldITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSST 184
Cdd:TIGR01277 103 AEQQEK--VVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQR 180
|
170 180 190
....*....|....*....|....*....|.
gi 1024600867 185 PIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:TIGR01277 181 TLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
30-210 |
1.45e-33 |
|
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: 123.79 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNtwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNL-KLRKVH 107
Cdd:cd03262 31 IIGPSGSGKSTLLRCINLLEEPDsGTIIIDGLKLTDDKKN--INELRQKVGMVFQQFNLFPHLTVLENITLAPiKVKGMS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLDIT--RVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTP 185
Cdd:cd03262 109 KAEAEERalELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTM 188
|
170 180
....*....|....*....|....*
gi 1024600867 186 IFyVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03262 189 VV-VTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-210 |
5.59e-33 |
|
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: 120.43 E-value: 5.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSScntwLAPAKRNIAYLFQearllphlsiednirl 99
Cdd:cd00267 21 TLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTsGEILIDGKDIAKLP----LEELRRRIGYVPQ---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 nlklrkvhksdlditrvlddcglsrlrsqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:cd00267 81 ---------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA 127
|
170 180 190
....*....|....*....|....*....|.
gi 1024600867 180 SSSSTpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd00267 128 EEGRT-VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
27-237 |
6.94e-33 |
|
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: 122.68 E-value: 6.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQ---VWQRSSCNTWlapaKRNIAYLFQEARLLPHLSIEDNI---RL 99
Cdd:cd03256 29 FVALIGPSGAGKSTLLRCLNGLVEPtSGSVLIDGTdinKLKGKALRQL----RRQIGMIFQQFNLIERLSVLENVlsgRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 NLK------LRKVHKSDLDITR-VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQML 172
Cdd:cd03256 105 GRRstwrslFGLFPKEEKQRALaALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 173 RLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPalqtfaehSALFDQEQLASVF 237
Cdd:cd03256 185 DLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP--------PAELTDEVLDEIY 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
27-215 |
1.05e-32 |
|
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: 120.23 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQ-VWQRSScnTWLApakRNIAYLFQearllphlsiednirlnlklr 104
Cdd:cd03214 27 IVGILGPNGAGKSTLLKTLAGLLKPSsGEILLDGKdLASLSP--KELA---RKIAYVPQ--------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 kvhksdlditrVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSST 184
Cdd:cd03214 81 -----------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGK 149
|
170 180 190
....*....|....*....|....*....|.
gi 1024600867 185 PIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03214 150 TVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
30-250 |
2.97e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.18 E-value: 2.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRsscntwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHK 108
Cdd:PRK11607 50 LLGASGCGKSTLLRMLAGFEQPtAGQIMLDGVDLSH------VPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLDiTRVLDDCGLSRLR---SQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM-LRLIQRFKSSSST 184
Cdd:PRK11607 124 AEIA-SRVNEMLGLVHMQefaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVT 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024600867 185 PIFyVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLASV--FEATITElDQENSL 250
Cdd:PRK11607 203 CVM-VTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVnvFEGVLKE-RQEDGL 268
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
29-215 |
4.34e-32 |
|
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: 122.47 E-value: 4.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH----GEISVNKQvwqrsscNTWLAPAK-------RNIAYLFQE--ARLLPHLSIED 95
Cdd:COG0444 35 GLVGESGSGKSTLARAILGLLPPPgitsGEILFDGE-------DLLKLSEKelrkirgREIQMIFQDpmTSLNPVMTVGD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 96 NIRLNLKL-RKVHKSDLD--ITRVLDDCGL----SRLRsQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:COG0444 108 QIAEPLRIhGGLSKAEARerAIELLERVGLpdpeRRLD-RYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1024600867 169 RQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMqqgeaaYLG 215
Cdd:COG0444 187 AQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM------YAG 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
27-210 |
4.86e-32 |
|
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: 120.23 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQ-VWQrsscntwLAPAKRN---IAYLFQEARLLPHLSIEDNIRLNL 101
Cdd:cd03219 28 IHGLIGPNGAGKTTLFNLISGFLRPtSGSVLFDGEdITG-------LPPHEIArlgIGRTFQIPRLFPELTVLENVMVAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVHKSDLDITR------------VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKR 169
Cdd:cd03219 101 QARTGSGLLLARARreereareraeeLLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1024600867 170 QMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03219 181 ELAELIRELRERGIT-VLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
27-215 |
8.96e-32 |
|
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: 120.14 E-value: 8.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRsscntwLAPAKRN---IAYLFQEARLLPHLSIEDNIRL--- 99
Cdd:COG0411 32 IVGLIGPNGAGKTTLFNLITGFYRPtSGRILFDGRDITG------LPPHRIArlgIARTFQNPRLFPELTVLENVLVaah 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 ----------NLKLRKVHKSDLDIT----RVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDA 165
Cdd:COG0411 106 arlgrgllaaLLRLPRARREEREAReraeELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 166 TSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGE-----------------AAYLG 215
Cdd:COG0411 186 EETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRviaegtpaevradprviEAYLG 252
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
32-210 |
1.26e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.33 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVN-KQVWQRSSCntwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNL-KLRKVHK 108
Cdd:COG1126 34 GPSGSGKSTLLRCINLLEEPdSGTITVDgEDLTDSKKD---INKLRRKVGMVFQQFNLFPHLTVLENVTLAPiKVKKMSK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLDIT--RVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPI 186
Cdd:COG1126 111 AEAEERamELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMV 190
|
170 180
....*....|....*....|....
gi 1024600867 187 FyVSHSIDEIAQLADDILLMQQGE 210
Cdd:COG1126 191 V-VTHEMGFAREVADRVVFMDGGR 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
27-209 |
1.29e-31 |
|
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: 118.47 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRsscntwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRK 105
Cdd:cd03268 28 IYGFLGPNGAGKTTTMKIILGLIKPdSGEITFDGKSYQK------NIEALRRIGALIEAPGFYPNLTARENLRLLARLLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLDitRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTp 185
Cdd:cd03268 102 IRKKRID--EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGIT- 178
|
170 180
....*....|....*....|....
gi 1024600867 186 IFYVSHSIDEIAQLADDILLMQQG 209
Cdd:cd03268 179 VLISSHLLSEIQKVADRIGIINKG 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
30-174 |
2.28e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.58 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQPH----GEISVNKQvwqrsSCNTwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNL--KL 103
Cdd:COG4136 32 LMGPSGSGKSTLLAAIAGTLSPAfsasGEVLLNGR-----RLTA-LPAEQRRIGILFQDDLLFPHLSVGENLAFALppTI 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 104 RKVHKSDLdITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:COG4136 106 GRAQRRAR-VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
30-209 |
3.01e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 118.65 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScntwlapAKRNIayLFQEARLLPHLSIEDNIRLNLKLRKVHK 108
Cdd:PRK11248 32 VLGPSGCGKTTLLNLIAGFVPYqHGSITLDGKPVEGPG-------AERGV--VFQNEGLLPWRNVQDNVAFGLQLAGVEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLDIT--RVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPI 186
Cdd:PRK11248 103 MQRLEIahQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQV 182
|
170 180
....*....|....*....|...
gi 1024600867 187 FYVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK11248 183 LLITHDIEEAVFMATELVLLSPG 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
29-222 |
4.63e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 120.18 E-value: 4.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQ-VWQRSScnTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKV 106
Cdd:COG1135 35 GIIGYSGAGKSTLIRCINLLERPtSGSVLVDGVdLTALSE--RELRAARRKIGMIFQHFNLLSSRTVAENVALPLEIAGV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDLDiTRV---LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:COG1135 113 PKAEIR-KRVaelLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELG 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 1024600867 184 TPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFA 222
Cdd:COG1135 192 LTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
21-217 |
6.34e-31 |
|
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: 117.40 E-value: 6.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTwLAPAKRNIAYLFQEARLLPHLSIEDNI-- 97
Cdd:TIGR02315 24 NINPGEFVAIIGPSGAGKSTLLRCINRLVEPsSGSILLEGTDITKLRGKK-LRKLRRRIGMIFQHYNLIERLTVLENVlh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 -RLNLK------LRKVHKSDLDIT-RVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKR 169
Cdd:TIGR02315 103 gRLGYKptwrslLGRFSEEDKERAlSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1024600867 170 QMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPA 217
Cdd:TIGR02315 183 QVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAP 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
28-216 |
1.39e-30 |
|
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: 122.64 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVN----KQVWQRSscntwLApakRNIAYLFQEARLLpHLSIEDNIRLNlk 102
Cdd:COG2274 504 VAIVGRSGSGKSTLLKLLLGLYEPtSGRILIDgidlRQIDPAS-----LR---RQIGVVLQDVFLF-SGTIRENITLG-- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 lrKVHKSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:COG2274 573 --DPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 172 LRLIQRFKSSSSTpIFyVSHSiDEIAQLADDILLMQQGEAAYLGP 216
Cdd:COG2274 651 LENLRRLLKGRTV-II-IAHR-LSTIRLADRIIVLDKGRIVEDGT 692
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
27-210 |
2.01e-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: 121.79 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLapakRNIAYLFQEARLlPHLSIEDNIRLNlklrK 105
Cdd:COG4988 365 RVALVGPSGAGKSTLLNLLLGFLPPySGSILINGVDLSDLDPASWR----RQIAWVPQNPYL-FAGTIRENLRLG----R 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:COG4988 436 PDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA 515
|
170 180 190
....*....|....*....|....*....|....*.
gi 1024600867 175 IQRFkSSSSTPIFyVSHSIDEIAQlADDILLMQQGE 210
Cdd:COG4988 516 LRRL-AKGRTVIL-ITHRLALLAQ-ADRILVLDDGR 548
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
28-210 |
7.37e-30 |
|
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: 112.48 E-value: 7.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNTWlapaKRNIAYLFQEARLLpHLSIEDNIrlnlklrkv 106
Cdd:cd03228 31 VAIVGPSGSGKSTLLKLLLRLYDPTsGEILIDGVDLRDLDLESL----RKNIAYVPQDPFLF-SGTIRENI--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 hksdlditrvlddcglsrlrsqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSStpI 186
Cdd:cd03228 97 --------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKT--V 148
|
170 180
....*....|....*....|....
gi 1024600867 187 FYVSHSIDEIaQLADDILLMQQGE 210
Cdd:cd03228 149 IVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-215 |
5.97e-29 |
|
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: 110.72 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAG-LEQPH--GEISVNKQvwqRSSCNTWlapaKRNIAYLFQEARLLPHLSIEDNIRLNLKL 103
Cdd:cd03213 37 LTAIMGPSGAGKSTLLNALAGrRTGLGvsGEVLINGR---PLDKRSF----RKIIGYVPQDDILHPTLTVRETLMFAAKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 RKvhksdlditrvlddcglsrlrsqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:cd03213 110 RG---------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR 162
|
170 180 190
....*....|....*....|....*....|..
gi 1024600867 184 TPIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03213 163 TIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-219 |
7.63e-29 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 111.79 E-value: 7.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRsscntwlaPAKRNIAyLFQEARLLPHLSIEDNIRLNLK--LRKV 106
Cdd:TIGR01184 16 LIGHSGCGKSTLLNLISGLAQPtSGGVILEGKQITE--------PGPDRMV-VFQNYSLLPWLTVRENIALAVDrvLPDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQML-RLIQRFKSSSS 183
Cdd:TIGR01184 87 SKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQeELMQIWEEHRV 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1024600867 184 TPIFyVSHSIDEIAQLADDILLMQQGEAAYLGPALQ 219
Cdd:TIGR01184 167 TVLM-VTHDVDEALLLSDRVVMLTNGPAANIGQILE 201
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
29-211 |
9.01e-29 |
|
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: 110.83 E-value: 9.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISVNkqvwqrsscNTWLAPAKRN-IAYLFQEARLLPHLSIEDNIRLNLKLRKV 106
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPDsGEVLFD---------GKPLDIAARNrIGYLPEERGLYPKMKVIDQLVYLAQLKGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDL--DITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSST 184
Cdd:cd03269 101 KKEEArrRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKT 180
|
170 180
....*....|....*....|....*..
gi 1024600867 185 PIFyVSHSIDEIAQLADDILLMQQGEA 211
Cdd:cd03269 181 VIL-STHQMELVEELCDRVLLLNKGRA 206
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-215 |
1.52e-28 |
|
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: 110.82 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH----GEISVNKQvwqRSSCNTWlapaKRNIAYLFQEARLLPHLSIED- 95
Cdd:cd03234 29 HVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttsGQILFNGQ---PRKPDQF----QKCVAYVRQDDILLPGLTVREt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 96 -----NIRLNLKLRKVHKSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ 170
Cdd:cd03234 102 ltytaILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 171 MLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03234 182 LVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
28-210 |
7.22e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 109.74 E-value: 7.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGL--EQPH----GEISVNKQvwqrsscNTwLAPA------KRNIAYLFQEARLLPHlSIED 95
Cdd:COG1117 40 TALIGPSGCGKSTLLRCLNRMndLIPGarveGEILLDGE-------DI-YDPDvdvvelRRRVGMVFQKPNPFPK-SIYD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 96 NIRLNLKLRKVH-KSDLD--ITRVLDDCGL-----SRLRsQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATS 167
Cdd:COG1117 111 NVAYGLRLHGIKsKSELDeiVEESLRKAALwdevkDRLK-KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1024600867 168 KRQMLRLIQRFKSSSStpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:COG1117 190 TAKIEELILELKKDYT--IVIVTHNMQQAARVSDYTAFFYLGE 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
28-217 |
1.73e-27 |
|
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: 107.52 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPH-GEISVN-KQVwqrsscnTWLAP---AKRNIAYLFQEARLLPHLSIEDNIRLNLK 102
Cdd:cd03224 29 VALLGRNGAGKTTLLKTIMGLLPPRsGSIRFDgRDI-------TGLPPherARAGIGYVPEGRRIFPELTVEENLLLGAY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKVHKSDLDITRVLD---DcgLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:cd03224 102 ARRRAKRKARLERVYElfpR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1024600867 180 SSSSTpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPA 217
Cdd:cd03224 180 DEGVT-ILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
27-209 |
3.22e-27 |
|
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: 107.05 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRK 105
Cdd:TIGR02211 33 IVAIVGSSGSGKSTLLHLLGGLDNPtSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQFHHLLPDFTALENVAMPLLIGK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:TIGR02211 113 KSVKEAKerAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELN 192
|
170 180
....*....|....*....|....*.
gi 1024600867 184 TPIFYVSHSIdEIAQLADDILLMQQG 209
Cdd:TIGR02211 193 TSFLVVTHDL-ELAKKLDRVLEMKDG 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-222 |
3.75e-27 |
|
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: 112.09 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRSSCNTWLaPAKRNIAYLFQE--ARLLPHLSIEDNIRLNLKlrkV 106
Cdd:COG4172 316 GLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALR-PLRRRMQVVFQDpfGSLSPRMTVGQIIAEGLR---V 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDLD-------ITRVLDDCGLSRLRSQR-PDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLI--- 175
Cdd:COG4172 392 HGPGLSaaerrarVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLrdl 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1024600867 176 -QRFKSSsstpifYV--SHSIDEIAQLADDILLMQQGEAAYLGPALQTFA 222
Cdd:COG4172 472 qREHGLA------YLfiSHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-210 |
3.91e-27 |
|
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: 106.40 E-value: 3.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 10 QRADFALQ-IQREFKNTGLTGVFGPSGCGKTSLLRCIAG-LEQPHGEISVNKqvwqrsscntwlapakrNIAYLFQEARL 87
Cdd:cd03250 15 QETSFTLKdINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSVSVPG-----------------SIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 88 LPhLSIEDNIRLNlklrkvhkSDLDITR---VLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDL 153
Cdd:cd03250 78 QN-GTIRENILFG--------KPFDEERyekVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1024600867 154 ILMDEPLSALDA-TSKRQMLRLIQRFKSSSSTPIFyVSHSIdEIAQLADDILLMQQGE 210
Cdd:cd03250 149 YLLDDPLSAVDAhVGRHIFENCILGLLLNNKTRIL-VTHQL-QLLPHADQIVVLDNGR 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
29-164 |
4.42e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.04 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQ------VWQRsscntwlapAKRNIAYLFQEARLLPHLSIEDNIRLNL 101
Cdd:COG1137 33 GLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDGEdithlpMHKR---------ARLGIGYLPQEASIFRKLTVEDNILAVL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 102 KLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALD 164
Cdd:COG1137 104 ELRKLSKKEREerLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
29-210 |
4.62e-27 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 106.86 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQ------VWQRsscntwlapAKRNIAYLFQEARLLPHLSIEDNIRLNL 101
Cdd:cd03218 30 GLLGPNGAGKTTTFYMIVGLVKPdSGKILLDGQditklpMHKR---------ARLGIGYLPQEASIFRKLTVEENILAVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:cd03218 101 EIRGLSKKEREekLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK 180
|
170 180 190
....*....|....*....|....*....|.
gi 1024600867 180 sSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03218 181 -DRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-221 |
5.09e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 107.24 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 18 IQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQV--WQRSSCNTWLAP--AKRNIAYLFQEARLLPHLSI 93
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVrlFGRNIYSPDVDPieVRREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 94 EDNIRLNLKLRKVHKSDLDITRVLD---------DCGLSRLRSqRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALD 164
Cdd:PRK14267 103 YDNVAIGVKLNGLVKSKKELDERVEwalkkaalwDEVKDRLND-YPSNLSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 165 ATSKRQMLRLIQRFKSSSStpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTF 221
Cdd:PRK14267 182 PVGTAKIEELLFELKKEYT--IVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
25-215 |
6.99e-27 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 105.74 E-value: 6.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 25 TGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrsSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKL 103
Cdd:cd03264 25 PGMYGLLGPNGAGKTTLMRILATLTPPsSGTIRIDGQ-----DVLKQPQKLRRRIGYLPQEFGVYPNFTVREFLDYIAWL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 RKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFkss 181
Cdd:cd03264 100 KGIPSKEVKarVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--- 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1024600867 182 SSTPIFYVS-HSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03264 177 GEDRIVILStHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-206 |
6.99e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.01 E-value: 6.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVnkqvwqrsscntwlAPAKRnIAYLFQEARL---LPhLSIEDNIRLNL- 101
Cdd:NF040873 20 LTAVVGPNGSGKSTLLKVLAGVLRPtSGTVRR--------------AGGAR-VAYVPQRSEVpdsLP-LTVRDLVAMGRw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 ----KLRKVHKSD-LDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:NF040873 84 arrgLWRRLTRDDrAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLA 163
|
170 180 190
....*....|....*....|....*....|
gi 1024600867 177 RFKSSSSTpIFYVSHSIDEIAqLADDILLM 206
Cdd:NF040873 164 EEHARGAT-VVVVTHDLELVR-RADPCVLL 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-210 |
9.09e-27 |
|
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: 105.42 E-value: 9.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQV---WQRSscntwlapakRNIAYLFQEA-RLLPHLSIEDNIRLNLK 102
Cdd:cd03226 29 IALTGKNGAGKTTLAKILAGLIKEsSGSILLNGKPikaKERR----------KSIGYVMQDVdYQLFTDSVREELLLGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LrkVHKSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSS 182
Cdd:cd03226 99 E--LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQG 176
|
170 180
....*....|....*....|....*...
gi 1024600867 183 STpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03226 177 KA-VIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-211 |
1.13e-26 |
|
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: 104.22 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrsSCNTWLAPAKR-NIAYLFQEARLLPHlSIEDNIrlnlklrkv 106
Cdd:cd03246 32 AIIGPSGSGKSTLARLILGLLRPtSGRVRLDGA-----DISQWDPNELGdHVGYLPQDDELFSG-SIAENI--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 hksdlditrvlddcglsrlrsqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPI 186
Cdd:cd03246 97 --------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRI 150
|
170 180
....*....|....*....|....*
gi 1024600867 187 FyVSHSIDEIAQlADDILLMQQGEA 211
Cdd:cd03246 151 V-IAHRPETLAS-ADRILVLEDGRV 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
29-264 |
6.65e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 106.04 E-value: 6.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQ-VWQRSscNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKV 106
Cdd:PRK11153 35 GVIGASGAGKSTLIRCINLLERPtSGRVLVDGQdLTALS--EKELRKARRQIGMIFQHFNLLSSRTVFDNVALPLELAGT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDLDiTRV---LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:PRK11153 113 PKAEIK-ARVtelLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 184 TPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLASVFEATITELDQENSLS----------KA 253
Cdd:PRK11153 192 LTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQSTLHLDLPEDYLARLQAepttgsgpllRL 271
|
250
....*....|.
gi 1024600867 254 EIKGSQTGAPI 264
Cdd:PRK11153 272 EFTGESVDAPL 282
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
28-227 |
7.10e-26 |
|
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: 104.84 E-value: 7.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVwQRSSCNTWLAPAKRNIAYLFQ--EARLLphlsiEDNIR------ 98
Cdd:TIGR04521 34 VAIIGHTGSGKSTLIQHLNGLLKPtSGTVTIDGRD-ITAKKKKKLKDLRKKVGLVFQfpEHQLF-----EETVYkdiafg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 99 -LNLKLRK--VHKsdlditRV---LDDCGLSR-LRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:TIGR04521 108 pKNLGLSEeeAEE------RVkeaLELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024600867 172 LRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSAL 227
Cdd:TIGR04521 182 LDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDEL 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
27-215 |
1.25e-25 |
|
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: 102.45 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQPHGE------ISVNKQVwqrsscntwlAPAKRNIAYLFQEARLLPHLSIEDNIRLN 100
Cdd:cd03266 33 VTGLLGPNGAGKTTTLRMLAGLLEPDAGfatvdgFDVVKEP----------AEARRRLGFVSDSTGLYDRLTARENLEYF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 LKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRF 178
Cdd:cd03266 103 AGLYGLKGDELTarLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 179 KSSSSTpIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03266 183 RALGKC-ILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-206 |
3.80e-25 |
|
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: 106.22 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 26 GLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNTWLapakRNIAYLFQEARLLPHlSIEDNIRLnlklR 104
Cdd:TIGR02857 349 ERVALVGPSGAGKSTLLNLLLGFVDPTeGSIAVNGVPLADADADSWR----DQIAWVPQHPFLFAG-TIAENIRL----A 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHKSDLDITRVLDDCGLSRLRSQRPDT-----------LSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR 173
Cdd:TIGR02857 420 RPDASDAEIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE 499
|
170 180 190
....*....|....*....|....*....|...
gi 1024600867 174 LIQRFKSSSSTpiFYVSHSiDEIAQLADDILLM 206
Cdd:TIGR02857 500 ALRALAQGRTV--LLVTHR-LALAALADRIVVL 529
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
30-230 |
4.70e-25 |
|
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: 101.70 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQPhgeiSVNKQVW----QRSSCNTWlaPAKRNIAYLFQE--ARLLPHLSIED-------- 95
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLPP----TYGNDVRlfgeRRGGEDVW--ELRKRIGLVSPAlqLRFPRDETVLDvvlsgffd 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 96 NIRLNLKLrkvhkSDLDITR---VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQML 172
Cdd:COG1119 108 SIGLYREP-----TDEQRERareLLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 173 RLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTF-AEH-SALFDQ 230
Cdd:COG1119 183 ALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLtSENlSEAFGL 242
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-201 |
5.31e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.04 E-value: 5.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 18 IQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPHGEISV-------NKQVWQRsscNTWLAPAKRNIAYLFQEARLLPh 90
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVegrveffNQNIYER---RVNLNRLRRQVSMVHPKPNLFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 91 LSIEDNIRLNLKLRKVH-KSDLD--ITRVLDDCGL-----SRLRSQRPDtLSGGQRQRACLARAIVCEPDLILMDEPLSA 162
Cdd:PRK14258 102 MSVYDNVAYGVKIVGWRpKLEIDdiVESALKDADLwdeikHKIHKSALD-LSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1024600867 163 LDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLAD 201
Cdd:PRK14258 181 LDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-184 |
2.19e-24 |
|
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: 99.02 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTwLAPAKRNIAYLFQEARLLPHLSIEDNIRLnlKLRKVHK 108
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPtSGTIRVNGQDVSDLRGRA-IPYLRRKIGVVFQDFRLLPDRNVYENVAF--ALEVTGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLDITR----VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSST 184
Cdd:cd03292 109 PPREIRKrvpaALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTT 188
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-210 |
3.26e-24 |
|
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: 99.05 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 5 VDIsLQRADFALQiQREFkntglTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVwqrsscntwLAP------AK-- 75
Cdd:COG4181 25 LTI-LKGISLEVE-AGES-----VAIVGASGSGKSTLLGLLAGLDRPtSGTVRLAGQD---------LFAldedarARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 76 -RNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHKSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLI 154
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024600867 155 LMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSiDEIAQLADDILLMQQGE 210
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHD-PALAARCDRVLRLRAGR 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-223 |
4.77e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.05 E-value: 4.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 18 IQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPHG--------EISVNKQVWQRSSCNTWLapaKRNIAYLFQEARLLP 89
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvgdiTIDTARSLSQQKGLIRQL---RQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 90 HLSIEDNIRLNLKLRKVHKSDLDITR---VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDAT 166
Cdd:PRK11264 99 HRTVLENIIEGPVIVKGEPKEEATARareLLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 167 SKRQMLRLIQRFKSSSSTPIFyVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAE 223
Cdd:PRK11264 179 LVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
27-217 |
8.08e-24 |
|
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: 98.13 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVN-KQVwqrsscnTWLAP---AKRNIAYLFQEARLLPHLSIEDNIRL-- 99
Cdd:COG0410 31 IVALLGRNGAGKTTLLKAISGLLPPRsGSIRFDgEDI-------TGLPPhriARLGIGYVPEGRRIFPSLTVEENLLLga 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 -NLKLRKVHKSDLDitRVLD---DcgLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEP---LSALDAtskRQML 172
Cdd:COG0410 104 yARRDRAEVRADLE--RVYElfpR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPslgLAPLIV---EEIF 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 173 RLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPA 217
Cdd:COG0410 177 EIIRRLNREGVT-ILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
30-216 |
1.23e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.86 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQ-PHGEISVNKQvwqrsscnTWLAPA--KRNI----AYLFQEARLLPHLSIEDNIRLN-L 101
Cdd:PRK09493 32 IIGPSGSGKSTLLRCINKLEEiTSGDLIVDGL--------KVNDPKvdERLIrqeaGMVFQQFYLFPHLTALENVMFGpL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVHKSDL-DITR-VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:PRK09493 104 RVRGASKEEAeKQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLA 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 180 SSSSTPIFyVSHSIDEIAQLADDILLMQQGEAAYLGP 216
Cdd:PRK09493 184 EEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
29-215 |
1.84e-23 |
|
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: 96.67 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTwlapaKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVH 107
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPtSGRATVAGHDVVREPREV-----RRRIGIVFQDLSVDDELTGWENLYIHARLYGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTP 185
Cdd:cd03265 105 GAERRerIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMT 184
|
170 180 190
....*....|....*....|....*....|
gi 1024600867 186 IFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03265 185 ILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
30-215 |
2.22e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.11 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHK 108
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPtRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SD-----LDITRvldDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:PRK10070 139 EErrekaLDALR---QVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQ 215
|
170 180 190
....*....|....*....|....*....|..
gi 1024600867 184 TPIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:PRK10070 216 RTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
29-218 |
3.06e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.45 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLApAKRNIAYLFQEA--RLLPHLSIEDNIRLNLKlrk 105
Cdd:PRK10419 42 ALLGRSGCGKSTLARLLVGLESPsQGNVSWRGEPLAKLNRAQRKA-FRRDIQMVFQDSisAVNPRKTVREIIREPLR--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 vHKSDLD-------ITRVLDDCGLS-RLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQR 177
Cdd:PRK10419 118 -HLLSLDkaerlarASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1024600867 178 FKSSSSTPIFYVSHSIDEIAQLADDILLMQQG---EAAYLGPAL 218
Cdd:PRK10419 197 LQQQFGTACLFITHDLRLVERFCQRVMVMDNGqivETQPVGDKL 240
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
28-210 |
3.30e-23 |
|
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: 100.61 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrsSCNTWLAPAKRN-IAYLFQEarllPHLsIEDNIRLNLKLRK 105
Cdd:COG4987 364 VAIVGPSGSGKSTLLALLLRFLDPqSGSITLGGV-----DLRDLDEDDLRRrIAVVPQR----PHL-FDTTLRENLRLAR 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:COG4987 434 PDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD 513
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 175 I-QRFKSSSstpIFYVSHSIDEIAQlADDILLMQQGE 210
Cdd:COG4987 514 LlEALAGRT---VLLITHRLAGLER-MDRILVLEDGR 546
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-210 |
1.57e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.76 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRSSCNTWlapaKRNIAYLFQEArLLPHLSIEDNIRLNlklrKVHKSDL 111
Cdd:PRK11174 383 GPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESW----RKHLSWVGQNP-QLPHGTLRDNVLLG----NPDASDE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 112 DITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKS 180
Cdd:PRK11174 454 QLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR 533
|
170 180 190
....*....|....*....|....*....|
gi 1024600867 181 SSSTpiFYVSHSIDEIAQLaDDILLMQQGE 210
Cdd:PRK11174 534 RQTT--LMVTHQLEDLAQW-DQIWVMQDGQ 560
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-215 |
1.89e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 96.31 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGL-EQPHGEISVNKQVWQRSSCNTWLApAKRNIAYLFQE--ARLLPHLSIEDNIRLNLKLRK 105
Cdd:PRK15079 51 GVVGESGCGKSTFARAIIGLvKATDGEVAWLGKDLLGMKDDEWRA-VRSDIQMIFQDplASLNPRMTIGEIIAEPLRTYH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLDI-TRV---LDDCGL-SRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKS 180
Cdd:PRK15079 130 PKLSRQEVkDRVkamMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQR 209
|
170 180 190
....*....|....*....|....*....|....*
gi 1024600867 181 SSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:PRK15079 210 EMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
27-201 |
2.13e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.85 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLE------QPHGEISVNKQVWQRSSCNTwlAPAKRNIAYLFQEARLLPHlSIEDNIRLN 100
Cdd:PRK14243 38 ITAFIGPSGCGKSTILRCFNRLNdlipgfRVEGKVTFHGKNLYAPDVDP--VEVRRRIGMVFQKPNPFPK-SIYDNIAYG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 LKLRKvHKSDLD--ITRVLDDCGL-----SRLRsQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR 173
Cdd:PRK14243 115 ARING-YKGDMDelVERSLRQAALwdevkDKLK-QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEE 192
|
170 180
....*....|....*....|....*...
gi 1024600867 174 LIQRFKSSSStpIFYVSHSIDEIAQLAD 201
Cdd:PRK14243 193 LMHELKEQYT--IIIVTHNMQQAARVSD 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-221 |
2.62e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.73 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 18 IQREFKNTGLTGVFGPSGCGKTSLLRCIAGL-EQPHGEISVNKQV--WQRSSCNTWLAPAKRNIAYLFQEARLLPHLSIE 94
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSKIKVDGKVlyFGKDIFQIDAIKLRKEVGMVFQQPNPFPHLSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 95 DNIRLNLKLRKVhKSDLDITRVLDDC----GLSRLRSQRPDT----LSGGQRQRACLARAIVCEPDLILMDEPLSALDAT 166
Cdd:PRK14246 109 DNIAYPLKSHGI-KEKREIKKIVEEClrkvGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 167 SKRQMLRLIQRFKSSSStpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTF 221
Cdd:PRK14246 188 NSQAIEKLITELKNEIA--IVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
28-210 |
2.83e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.93 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVN----KQVwqrsSCNTWLapakRNIAYLFQEARLLpHLSIEDNIRLNlk 102
Cdd:COG1132 369 VALVGPSGSGKSTLVNLLLRFYDPtSGRILIDgvdiRDL----TLESLR----RQIGVVPQDTFLF-SGTIRENIRYG-- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 lrKVHKSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:COG1132 438 --RPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALI 515
|
170 180 190
....*....|....*....|....*....|....*....
gi 1024600867 172 LRLIQRFKSSSSTpiFYVSHSIDEIAQlADDILLMQQGE 210
Cdd:COG1132 516 QEALERLMKGRTT--IVIAHRLSTIRN-ADRILVLDDGR 551
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-203 |
2.90e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 35 GCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSScntwlaP--AKRN-IAYLFQEARLLPHLSIEDNIRLNLKLRK---VH 107
Cdd:COG1129 40 GAGKSTLMKILSGVYQPDsGEILLDGEPVRFRS------PrdAQAAgIAIIHQELNLVPNLSVAENIFLGREPRRgglID 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDL--DITRVLDDCGLSRlrsqRPDT----LSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSS 181
Cdd:COG1129 114 WRAMrrRARELLARLGLDI----DPDTpvgdLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ 189
|
170 180
....*....|....*....|..
gi 1024600867 182 SSTpIFYVSHSIDEIAQLADDI 203
Cdd:COG1129 190 GVA-IIYISHRLDEVFEIADRV 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
27-201 |
3.85e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.45 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQ---VWQRSScntwLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLK 102
Cdd:PRK11831 35 ITAIMGPSGIGKTTLLRLIGGQIAPdHGEILFDGEnipAMSRSR----LYTVRKRMSMLFQSGALFTDMNVFDNVAYPLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKVHKSDLDITRV---LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:PRK11831 111 EHTQLPAPLLHSTVmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELN 190
|
170 180
....*....|....*....|..
gi 1024600867 180 SSSSTPIFYVSHSIDEIAQLAD 201
Cdd:PRK11831 191 SALGVTCVVVSHDVPEVLSIAD 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
29-209 |
4.81e-22 |
|
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: 93.04 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISV-NKQVWQrsscntwLAPA--KRNIAYLFQEARLlphlsIEDNIRLNLKLR 104
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLYKPtSGSVLLdGTDIRQ-------LDPAdlRRNIGYVPQDVTL-----FYGTLRDNITLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHKSDLDITRV-----LDDC------GLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRqmlR 173
Cdd:cd03245 102 APLADDERILRAaelagVTDFvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE---R 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 174 LIQRFKSS-SSTPIFYVSHSIdEIAQLADDILLMQQG 209
Cdd:cd03245 179 LKERLRQLlGDKTLIIITHRP-SLLDLVDRIIVMDSG 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-221 |
1.03e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.67 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVW--QRSSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIR 98
Cdd:PRK14247 25 EIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYldGQDIFKMDVIELRRRVQMVFQIPNPIPNLSIFENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 99 LNLKLRKVHKSDLDI-TRV---LDDCGLSRLRSQRPDT----LSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ 170
Cdd:PRK14247 105 LGLKLNRLVKSKKELqERVrwaLEKAQLWDEVKDRLDApagkLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 171 MLRLIQRFKSSSStpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTF 221
Cdd:PRK14247 185 IESLFLELKKDMT--IVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
30-222 |
1.22e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 92.72 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQ---------RSSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRL 99
Cdd:PRK10619 36 IIGSSGSGKSTFLRCINFLEKPsEGSIVVNGQTINlvrdkdgqlKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 N----LKLRKVHKSDLDItRVLDDCGLS-RLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:PRK10619 116 ApiqvLGLSKQEARERAV-KYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRI 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1024600867 175 IQRFKSSSSTPIFyVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFA 222
Cdd:PRK10619 195 MQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
29-215 |
1.39e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 91.83 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVwqrsscnTWLapakrniayLFQEARLLPHLSIEDNIRLNLKLRKVH 107
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLAGIYPPdSGTVTVRGRV-------SSL---------LGLGGGFNPELTGRENIYLNGRLLGLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTp 185
Cdd:cd03220 116 RKEIDekIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKT- 194
|
170 180 190
....*....|....*....|....*....|
gi 1024600867 186 IFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03220 195 VILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
29-217 |
2.05e-21 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 95.20 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVN----KQvWQRSScntwLAPakrNIAYLFQEARLLPHlSIEDNI-RLN-- 100
Cdd:COG4618 362 GVIGPSGSGKSTLARLLVGVWPPtAGSVRLDgadlSQ-WDREE----LGR---HIGYLPQDVELFDG-TIAENIaRFGda 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 --------LKLRKVHksDLdITR-------VLDDCGLsrlrsqrpdTLSGGQRQRACLARAIVCEPDLILMDEPLSALDA 165
Cdd:COG4618 433 dpekvvaaAKLAGVH--EM-ILRlpdgydtRIGEGGA---------RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 166 TSKRQMLRLIQRFKSSSSTpIFYVSHSIdEIAQLADDILLMQQGEAAYLGPA 217
Cdd:COG4618 501 EGEAALAAAIRALKARGAT-VVVITHRP-SLLAAVDKLLVLRDGRVQAFGPR 550
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-222 |
2.51e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.99 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH-GEIsvnkqVWQRSSCN---TWLAPAKRNIAYLFQEA-RLLPHLSIED 95
Cdd:PRK13638 23 DFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkGAV-----LWQGKPLDyskRGLLALRQQVATVFQDPeQQIFYTDIDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 96 NIRLNLklRKVHKSDLDITRVLDDC----GLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:PRK13638 98 DIAFSL--RNLGVPEAEITRRVDEAltlvDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 172 LRLIQRFKSSSSTPIFyVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFA 222
Cdd:PRK13638 176 IAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
30-238 |
3.00e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQ--EARLLphlsiEDNIR-------- 98
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPtTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLF-----EDTVEreiifgpk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 99 -LNLKLRKVHKsdlDITRVLDDCGLSR-LRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:PRK13646 113 nFKMNLDEVKN---YAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLK 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024600867 177 RFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAE-------HSALFDQEQLASVFE 238
Cdd:PRK13646 190 SLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDkkkladwHIGLPEIVQLQYDFE 258
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-227 |
3.06e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.03 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 1 MSIKVD----ISLQRADF---ALQ-IQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNK-QVWQRsscNTW 70
Cdd:PRK13637 1 MSIKIEnlthIYMEGTPFekkALDnVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTsGKIIIDGvDITDK---KVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 71 LAPAKRNIAYLFQ--EARLLPHlSIEDNI-----RLNLKLRKVHKSdldITRVLDDCGLSR--LRSQRPDTLSGGQRQRA 141
Cdd:PRK13637 78 LSDIRKKVGLVFQypEYQLFEE-TIEKDIafgpiNLGLSEEEIENR---VKRAMNIVGLDYedYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 142 CLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTF 221
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
....*.
gi 1024600867 222 AEHSAL 227
Cdd:PRK13637 234 KEVETL 239
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
29-209 |
3.22e-21 |
|
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: 94.93 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVN----KQvwqrsscntwLAPA--KRNIAYLFQEARLLpHLSIEDNIrlnl 101
Cdd:TIGR03375 495 AIIGRIGSGKSTLLKLLLGLYQPtEGSVLLDgvdiRQ----------IDPAdlRRNIGYVPQDPRLF-YGTLRDNI---- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVHKSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ 170
Cdd:TIGR03375 560 ALGAPYADDEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEER 639
|
170 180 190
....*....|....*....|....*....|....*....
gi 1024600867 171 MLRLIQRFksSSSTPIFYVSHSIdEIAQLADDILLMQQG 209
Cdd:TIGR03375 640 FKDRLKRW--LAGKTLVLVTHRT-SLLDLVDRIIVMDNG 675
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-280 |
6.82e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.32 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSscntwlapAKRNIAYLFQEARLLPHLSIEDNI----RLN- 100
Cdd:COG4152 29 IFGLLGPNGAGKTTTIRIILGILAPdSGEVLWDGEPLDPE--------DRRRIGYLPEERGLYPKMKVGEQLvylaRLKg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 LKLRKVHKSdldITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKS 180
Cdd:COG4152 101 LSKAEAKRR---ADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 181 SSSTPIFyVSHSIDEIAQLADDILLMQQGEAAYLGP---ALQTFAEH----SALFDQEQLASVFEatITELDQENSLSKA 253
Cdd:COG4152 178 KGTTVIF-SSHQMELVEELCDRIVIINKGRKVLSGSvdeIRRQFGRNtlrlEADGDAGWLRALPG--VTVVEEDGDGAEL 254
|
250 260
....*....|....*....|....*..
gi 1024600867 254 EIKGSQTGAPIAvwigeQALSEGQKIR 280
Cdd:COG4152 255 KLEDGADAQELL-----RALLARGPVR 276
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
32-220 |
7.14e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.72 E-value: 7.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLeQPHGEisvnkqvwqrsscNTWLAPAKRNIAYLFQ----------EARLLPHLsiEDNIrlnl 101
Cdd:COG4178 396 GPSGSGKSTLLRAIAGL-WPYGS-------------GRIARPAGARVLFLPQrpylplgtlrEALLYPAT--AEAF---- 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 klrkvhkSDLDITRVLDDCGLSRLRSQ------RPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLI 175
Cdd:COG4178 456 -------SDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL 528
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 176 QRfkSSSSTPIFYVSHSiDEIAQLADDILLMQQGEAAYLGPALQT 220
Cdd:COG4178 529 RE--ELPGTTVISVGHR-STLAAFHDRVLELTGDGSWQLLPAEAP 570
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
32-209 |
9.20e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.07 E-value: 9.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPH-GEISVNKQVW---QRSSCNTWLApAKRNIAYLFQEARLLPHLSIEDN-IRLNLKLRKV 106
Cdd:COG4161 35 GPSGAGKSSLLRVLNLLETPDsGQLNIAGHQFdfsQKPSEKAIRL-LRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDldiTRVLDDCGLSRLR----SQR-PDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSS 181
Cdd:COG4161 114 SKEQ---AREKAMKLLARLRltdkADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT 190
|
170 180
....*....|....*....|....*...
gi 1024600867 182 SSTPIFyVSHSIDEIAQLADDILLMQQG 209
Cdd:COG4161 191 GITQVI-VTHEVEFARKVASQVVYMEKG 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-223 |
1.11e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.56 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 16 LQIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQ--EARLLPHLS 92
Cdd:PRK13643 23 FDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPtEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 93 IEDNI--RLNLKLRKVHKSDLDITRvLDDCGLSR-LRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKR 169
Cdd:PRK13643 103 LKDVAfgPQNFGIPKEKAEKIAAEK-LEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1024600867 170 QMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAE 223
Cdd:PRK13643 182 EMMQLFESIHQSGQT-VVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-242 |
2.20e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.99 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQvwqrsSCNTW----LApakRNIAYLFQEARLLPHLSIED 95
Cdd:COG4604 23 TIPKGGITALIGPNGAGKSTLLSMISRLLPPDsGEVLVDGL-----DVATTpsreLA---KRLAILRQENHINSRLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 96 NI----------RLNLKLRKVhksdldITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDA 165
Cdd:COG4604 95 LVafgrfpyskgRLTAEDREI------IDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 166 TSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPAlqtfaehSALFDQEQLASVFEATIT 242
Cdd:COG4604 169 KHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP-------EEIITPEVLSDIYDTDIE 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-234 |
2.87e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTS----LLRCIAGleqpHGEISVNKQVWQRSSCNTWLaPAKRNIAYLFQE--ARLLPHLS----IEDNIR 98
Cdd:PRK15134 316 GLVGESGSGKSTtglaLLRLINS----QGEIWFDGQPLHNLNRRQLL-PVRHRIQVVFQDpnSSLNPRLNvlqiIEEGLR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 99 LNLKLRKVHKSDLDITRVLDDCGLS-RLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQR 177
Cdd:PRK15134 391 VHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 178 FKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLA 234
Cdd:PRK15134 471 LQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
29-215 |
3.69e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.79 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTwLAPAKRNIAYLFQE--ARLLPHLSIEDNIRLNLKLRK 105
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPtSGEILFDGQDITGLSGRE-LRPLRRRMQMVFQDpyASLNPRMTVGDIIAEPLRIHG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLDITRV---LDDCGLSRLRSQR-PDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSS 181
Cdd:COG4608 127 LASKAERRERVaelLELVGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDE 206
|
170 180 190
....*....|....*....|....*....|....
gi 1024600867 182 SSTPIFYVSHSIDEIAQLADDILLMqqgeaaYLG 215
Cdd:COG4608 207 LGLTYLFISHDLSVVRHISDRVAVM------YLG 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-221 |
4.24e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 88.29 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 18 IQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRS----SCNTWLAPAKRNIAYLFQEARLLPhLSI 93
Cdd:PRK14239 24 VSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGhniySPRTDTVDLRKEIGMVFQQPNPFP-MSI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 94 EDNIRLNLKLRKVH-KSDLD---------------ITRVLDDCGLSrlrsqrpdtLSGGQRQRACLARAIVCEPDLILMD 157
Cdd:PRK14239 103 YENVVYGLRLKGIKdKQVLDeavekslkgasiwdeVKDRLHDSALG---------LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024600867 158 EPLSALDATSKRQMLRLIQRFKSSSStpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTF 221
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYT--MLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
32-209 |
5.42e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.76 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNT--WLAPAKRNIAYLFQEARLLPHLSIEDN-IRLNLKLRKVH 107
Cdd:PRK11124 35 GPSGAGKSSLLRVLNLLEMPRsGTLNIAGNHFDFSKTPSdkAIRELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLdITRVLDDcgLSRLR----SQR-PDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSS 182
Cdd:PRK11124 115 KDQA-LARAEKL--LERLRlkpyADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETG 191
|
170 180
....*....|....*....|....*..
gi 1024600867 183 STPIFyVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK11124 192 ITQVI-VTHEVEVARKTASRVVYMENG 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
30-192 |
5.44e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 90.88 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVN-KQVWQRSSCNTwlapaKRNIAYLFQEARLLpHLSIEDNIRLNlklrKVH 107
Cdd:TIGR02868 366 ILGPSGSGKSTLLATLAGLLDPlQGEVTLDgVPVSSLDQDEV-----RRRVSVCAQDAHLF-DTTVRENLRLA----RPD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIq 176
Cdd:TIGR02868 436 ATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL- 514
|
170
....*....|....*.
gi 1024600867 177 rFKSSSSTPIFYVSHS 192
Cdd:TIGR02868 515 -LAALSGRTVVLITHH 529
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
27-239 |
5.53e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 87.86 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQvwQRSSCNTW-LApakRNIAYLFQEARLLPHLSIEDNIRLNL-KL 103
Cdd:COG4559 29 LTAIIGPNGAGKSTLLKLLTGELTPSsGEVRLNGR--PLAAWSPWeLA---RRRAVLPQHSSLAFPFTVEEVVALGRaPH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 RKVHKSDLDITR-VLDDCGLSRLRSQRPDTLSGGQRQRACLARAI--VCEPD-----LILMDEPLSALDATSKRQMLRLI 175
Cdd:COG4559 104 GSSAAQDRQIVReALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdggprWLFLDEPTSALDLAHQHAVLRLA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024600867 176 QRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTfaehsalFDQEQLASVFEA 239
Cdd:COG4559 184 RQLARRGGG-VVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV-------LTDELLERVYGA 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-159 |
6.68e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 6 DISLQRADFALqiqreFKNTGLT-------GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVwqrsscntwlapakrN 77
Cdd:COG0488 3 NLSKSFGGRPL-----LDDVSLSinpgdriGLVGRNGAGKSTLLKILAGELEPdSGEVSIPKGL---------------R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 78 IAYLFQEARLLPHLSIEDNI------------RLNLKLRKVHKSDLDITRV------LDDCG-----------LSRLR-- 126
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVldgdaelraleaELEELEAKLAEPDEDLERLaelqeeFEALGgweaearaeeiLSGLGfp 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 127 ----SQRPDTLSGGQRQRACLARAIVCEPDLILMDEP 159
Cdd:COG0488 143 eedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
29-215 |
6.88e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 87.39 E-value: 6.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQV-WQRSScntwlaPAKRNIAYLF-QEARLLPHLSIEDNIRLN----- 100
Cdd:cd03267 51 GFIGPNGAGKTTTLKILSGLLQPtSGEVRVAGLVpWKRRK------KFLRRIGVVFgQKTQLWWDLPVIDSFYLLaaiyd 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 -----LKLRKVHKSD-LDITRVLDdcglSRLRSqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:cd03267 125 lpparFKKRLDELSElLDLEELLD----TPVRQ-----LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1024600867 175 IQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03267 196 LKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
32-164 |
7.74e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 87.55 E-value: 7.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPH-GEISVN-KQVWQRSSCNTWLAPAKR--------NIAYLFQEARLLPHLSIEDN-IRLN 100
Cdd:COG4598 41 GSSGSGKSTFLRCINLLETPDsGEIRVGgEEIRLKPDRDGELVPADRrqlqrirtRLGMVFQSFNLWSHMTVLENvIEAP 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 101 LKLRKVHKSDLdITR---VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALD 164
Cdd:COG4598 121 VHVLGRPKAEA-IERaeaLLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-222 |
1.22e-19 |
|
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: 90.13 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKT----SLLRCIA-GLEQPHGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQE--ARLLPHLSIEDNIRLNLKL- 103
Cdd:COG4172 43 GESGSGKSvtalSILRLLPdPAAHPSGSILFDGQDLLGLSERELRRIRGNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLh 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 RKVHKSDLD--ITRVLDDCGL----SRLRSqRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQR 177
Cdd:COG4172 123 RGLSGAAARarALELLERVGIpdpeRRLDA-YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 178 FKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFA 222
Cdd:COG4172 202 LQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
29-227 |
1.71e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.29 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVwqrsscnTWLapakrniayL-----FQearllPHLSIEDNIRLNLK 102
Cdd:COG1134 56 GIIGRNGAGKSTLLKLIAGILEPtSGRVEVNGRV-------SAL---------LelgagFH-----PELTGRENIYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKVHKSDldITRVLDDC----GLSR-----LRsqrpdTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR 173
Cdd:COG1134 115 LLGLSRKE--IDEKFDEIvefaELGDfidqpVK-----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1024600867 174 LIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSAL 227
Cdd:COG1134 188 RIRELRESGRT-VIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEAL 240
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
27-206 |
1.72e-19 |
|
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: 86.06 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQEArlLPHLSIEDNIRLNLKLRK 105
Cdd:TIGR03771 8 LLGLLGPNGAGKTTLLRAILGLIPPaKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPIS--VAHTVMSGRTGHIGWLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLDITR-VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFkSSSST 184
Cdd:TIGR03771 86 PCVADFAAVRdALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL-AGAGT 164
|
170 180
....*....|....*....|..
gi 1024600867 185 PIFYVSHSIDEIAQLADDILLM 206
Cdd:TIGR03771 165 AILMTTHDLAQAMATCDRVVLL 186
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-210 |
2.01e-19 |
|
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: 84.79 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNTWLapaKRNIAYLfQEAR----LLPHLSIEDNIRLnlkl 103
Cdd:cd03215 30 GIAGLVGNGQTELAEALFGLRPPAsGEITLDGKPVTRRSPRDAI---RAGIAYV-PEDRkregLVLDLSVAENIAL---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 rkvhksdlditrvlddcglsrlrsqrPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:cd03215 102 --------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGK 155
|
170 180
....*....|....*....|....*..
gi 1024600867 184 TpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03215 156 A-VLLISSELDELLGLCDRILVMYEGR 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
30-222 |
2.71e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 87.33 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWlAPAKRNIAYLFQE--ARLLPHLSIED--------NIR 98
Cdd:PRK11308 46 VVGESGCGKSTLARLLTMIETPtGGELYYQGQDLLKADPEAQ-KLLRQKIQIVFQNpyGSLNPRKKVGQileeplliNTS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 99 LNLKLRKvhksdldiTRVLD---DCGLSRLRSQR-PDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:PRK11308 125 LSAAERR--------EKALAmmaKVGLRPEHYDRyPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1024600867 175 IQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFA 222
Cdd:PRK11308 197 MMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
28-210 |
2.95e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPH----GEISVN------KQVWQrsscntwlapAKRNIAYLFQEA-RLLPHLSIEDN 96
Cdd:PRK13640 36 TALIGHNGSGKSTISKLINGLLLPDdnpnSKITVDgitltaKTVWD----------IREKVGIVFQNPdNQFVGATVGDD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 97 IRLNLKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:PRK13640 106 VAFGLENRAVPRPEMIkiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 1024600867 175 IQRFKSSSSTPIFYVSHSIDEiAQLADDILLMQQGE 210
Cdd:PRK13640 186 IRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGK 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
27-210 |
3.28e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVN-KQVWQRSScnTWLApakRNIAYLFQEarllpHLSIED-NIR----- 98
Cdd:PRK11231 30 ITALIGPNGCGKSTLLKCFARLLTPqSGTVFLGdKPISMLSS--RQLA---RRLALLPQH-----HLTPEGiTVRelvay 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 99 -----LNLKLRKVHKSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR 173
Cdd:PRK11231 100 grspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMR 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 174 LIQRFKSSSSTPIfYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK11231 180 LMRELNTQGKTVV-TVLHDLNQASRYCDHLVVLANGH 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-210 |
4.28e-19 |
|
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: 83.25 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScntwLAPAKRN-IAYLFQearllphlsiednirlnlklrk 105
Cdd:cd03216 29 HALLGENGAGKSTLMKILSGLYKPdSGEILVDGKEVSFAS----PRDARRAgIAMVYQ---------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 vhksdlditrvlddcglsrlrsqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTp 185
Cdd:cd03216 83 ---------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVA- 134
|
170 180
....*....|....*....|....*
gi 1024600867 186 IFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03216 135 VIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
27-254 |
6.64e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQPH-GEISV-NKQVWQRSScntwlAPAKRNIAYLFQEARLLPHLSIEDNIRLNlklR 104
Cdd:PRK09536 31 LVGLVGPNGAGKTTLLRAINGTLTPTaGTVLVaGDDVEALSA-----RAASRRVASVPQDTSLSFEFDVRQVVEMG---R 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHKSDLD---------ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLI 175
Cdd:PRK09536 103 TPHRSRFDtwtetdraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 176 QRFKSSSSTPIFYVsHSIDEIAQLADDILLMQQGEAAYLGP--ALQTFAEHSALFDQEQLASVFEAT----ITELDQENS 249
Cdd:PRK09536 183 RRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPpaDVLTADTLRAAFDARTAVGTDPATgaptVTPLPDPDR 261
|
....*
gi 1024600867 250 LSKAE 254
Cdd:PRK09536 262 TEAAA 266
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-216 |
8.01e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.55 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 18 IQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVnkQVWQRSSCNTWLAP-----AKRNIAYLFQEARLLPHL 91
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPtSGEVNV--RVGDEWVDMTKPGPdgrgrAKRYIGILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 92 SIEDN----IRLNL-----KLRKVHksdlditrVLDDCGLSRLRSQR-----PDTLSGGQRQRACLARAIVCEPDLILMD 157
Cdd:TIGR03269 381 TVLDNlteaIGLELpdelaRMKAVI--------TLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1024600867 158 EPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGP 216
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
27-210 |
1.26e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTwlapAKRNIAYLFQEARLLPHLSIEDnirLNLKLRK 105
Cdd:PRK10253 35 FTAIIGPNGCGKSTLLRTLSRLMTPaHGHVWLDGEHIQHYASKE----VARRIGLLAQNATTPGDITVQE---LVARGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VH--------KSDLD-ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:PRK10253 108 PHqplftrwrKEDEEaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLS 187
|
170 180 190
....*....|....*....|....*....|....
gi 1024600867 177 RFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK10253 188 ELNREKGYTLAAVLHDLNQACRYASHLIALREGK 221
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
26-210 |
1.28e-18 |
|
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: 83.73 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 26 GLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNtwlAPAKRNIAYLFQEARLLPHLSIEDNIRLNL--- 101
Cdd:TIGR03410 27 EVTCVLGRNGVGKTTLLKTLMGLLPVKsGSIRLDGEDITKLPPH---ERARAGIAYVPQGREIFPRLTVEENLLTGLaal 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 --KLRKVHKSDLDITRVLDDcglsrLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:TIGR03410 104 prRSRKIPDEIYELFPVLKE-----MLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLR 178
|
170 180 190
....*....|....*....|....*....|.
gi 1024600867 180 SSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:TIGR03410 179 AEGGMAILLVEQYLDFARELADRYYVMERGR 209
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-207 |
1.44e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 9 LQRADFALQiQREFKNtgltgVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWlapaKRNIAYLFQEARL 87
Cdd:PRK10247 23 LNNISFSLR-AGEFKL-----ITGPSGCGKSTLLKIVASLISPtSGTLLFEGEDISTLKPEIY----RQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 88 LPHlSIEDNIRLNLKLRKVHKSDLDITRVLDDCGL-SRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDAT 166
Cdd:PRK10247 93 FGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1024600867 167 SKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQlADDILLMQ 207
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-236 |
1.76e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKT----SLLRCIaglEQPHGEISVNKQVWQRSS-----CNTWLAPAKR-----NIAYLFQE--ARLLPHLS- 92
Cdd:PRK10261 47 IVGESGSGKSvtalALMRLL---EQAGGLVQCDKMLLRRRSrqvieLSEQSAAQMRhvrgaDMAMIFQEpmTSLNPVFTv 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 93 ---IEDNIRLNLKLRKVH-----KSDLDITRVLDDcglSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALD 164
Cdd:PRK10261 124 geqIAESIRLHQGASREEamveaKRMLDQVRIPEA---QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 165 ATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLASV 236
Cdd:PRK10261 201 VTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAV 272
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-209 |
2.95e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.73 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 17 QIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQ--EARLLPHLSI 93
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPsSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfpEAQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 94 EDNI--RLNLKLRKvHKSDLDITRVLDDCGLSR-LRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ 170
Cdd:PRK13641 105 KDVEfgPKNFGFSE-DEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1024600867 171 MLRLIQRFKSSSSTPIFyVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK13641 184 MMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHG 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
32-204 |
5.28e-18 |
|
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: 80.28 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLeQPHGEISVNKqvwqrsscntwlaPAKRNIAYLFQEarllPHLSiednirlnlklrkvhksdl 111
Cdd:cd03223 34 GPSGTGKSSLFRALAGL-WPWGSGRIGM-------------PEGEDLLFLPQR----PYLP------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 112 ditrvlddcgLSRLRSQ--RP--DTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSsstpIF 187
Cdd:cd03223 77 ----------LGTLREQliYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGIT----VI 142
|
170
....*....|....*..
gi 1024600867 188 YVSHSIdEIAQLADDIL 204
Cdd:cd03223 143 SVGHRP-SLWKFHDRVL 158
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
6-223 |
5.29e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 6 DISLQRADFALQIQREFKNTGL------------TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLA 72
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFERRALydvnvsipsgsyVAIIGHTGSGKSTLLQHLNGLLQPtSGTVTIGERVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 73 PAKRNIAYLFQ--EARLLPHlSIEDNIR---LNLKLrKVHKSDLDITRVLDDCGLSR-LRSQRPDTLSGGQRQRACLARA 146
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEE-TVEKDICfgpMNFGV-SEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 147 IVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAE 223
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-209 |
5.41e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.84 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 8 SLQRADFALqiqREFKNTGLTGvfgPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSScNTWLAPAKRNIAYLFQEAR 86
Cdd:PRK10908 17 ALQGVTFHM---RPGEMAFLTG---HSGAGKSTLLKLICGIERPSaGKIWFSGHDITRLK-NREVPFLRRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 87 LLPHLSIEDNIRLNLKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALD 164
Cdd:PRK10908 90 LLMDRTVYDNVAIPLIIAGASGDDIRrrVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 165 ATSKRQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK10908 170 DALSEGILRLFEEFNRVGVT-VLMATHDIGLISRRSYRMLTLSDG 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
27-201 |
7.85e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.40 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEIsvnkqVWQRSSCNTWLAPAK-----RNIAYLFQEARLLPHLSIEDNIRLN 100
Cdd:PRK11629 37 MMAIVGSSGSGKSTLLHLLGGLDTPtSGDV-----IFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALENVAMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 LKLRKVHKSDLDIT--RVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRF 178
Cdd:PRK11629 112 LLIGKKKPAEINSRalEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL 191
|
170 180
....*....|....*....|...
gi 1024600867 179 KSSSSTPIFYVSHSIdeiaQLAD 201
Cdd:PRK11629 192 NRLQGTAFLVVTHDL----QLAK 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
32-236 |
2.67e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGL-EQPHGEISVNKQVWQRSSCNTwLAPAKRNIAYLFQE--ARLLPHLSIEDNIRLNLKLRKVHK 108
Cdd:PRK10261 357 GESGSGKSTTGRALLRLvESQGGEIIFNGQRIDTLSPGK-LQALRRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLDITRV---LDDCGLSRLRSQR-PDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSST 184
Cdd:PRK10261 436 GKAAAARVawlLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGI 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 185 PIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLASV 236
Cdd:PRK10261 516 AYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
30-227 |
2.80e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.83 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQPH-GEISVN------KQVWQrsscntwlapAKRNIAYLFQEarllPH-----LSIEDNI 97
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLLLPEaGTITVGgmvlseETVWD----------VRRQVGMVFQN----PDnqfvgATVQDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 RLNLKLRKVHKSDLdITRV---LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:PRK13635 104 AFGLENIGVPREEM-VERVdqaLRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLET 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1024600867 175 IQRFKSSSSTPIFYVSHSIDEIAQlADDILLMQQGEAAYLGPALQTFAEHSAL 227
Cdd:PRK13635 183 VRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHML 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
30-210 |
3.03e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.91 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGL-EQPHGEISVNKQvwQRSSCNTWlaPAKRNIAYLFQEA-RLLPHLSIEDNIRLNLKLRKVH 107
Cdd:PRK13642 38 IIGQNGSGKSTTARLIDGLfEEFEGKVKIDGE--LLTAENVW--NLRRKIGMVFQNPdNQFVGATVEDDVAFGMENQGIP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLdITRV---LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSST 184
Cdd:PRK13642 114 REEM-IKRVdeaLLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQL 192
|
170 180
....*....|....*....|....*.
gi 1024600867 185 PIFYVSHSIDEIAQlADDILLMQQGE 210
Cdd:PRK13642 193 TVLSITHDLDEAAS-SDRILVMKAGE 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
30-229 |
3.24e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.55 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGL-EQPHGEISVNKQvwQRSSCNTWlaPAKRNIAYLFQEA-RLLPHLSIEDNIRLNLKLRKVH 107
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLlEAESGQIIIDGD--LLTEENVW--DIRHKIGMVFQNPdNQFVGATVEDDVAFGLENKGIP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLdITRV---LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSST 184
Cdd:PRK13650 114 HEEM-KERVneaLELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQM 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 185 PIFYVSHSIDEIAqLADDILLMQQGEAAYLGPALQTFAEHSALFD 229
Cdd:PRK13650 193 TVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDLLQ 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
27-209 |
3.35e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.94 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGL-EQPHGEISVNKQvwqrsscNTWLAP----AKRNIAYLFQEARLLPHLSIEDNIRLNL 101
Cdd:PRK10895 31 IVGLLGPNGAGKTTTFYMVVGIvPRDAGNIIIDDE-------DISLLPlharARRGIGYLPQEASIFRRLSVYDNLMAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVHKSDLDITR---VLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRF 178
Cdd:PRK10895 104 QIRDDLSAEQREDRaneLMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL 183
|
170 180 190
....*....|....*....|....*....|.
gi 1024600867 179 KsSSSTPIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK10895 184 R-DSGLGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-177 |
3.46e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 26 GLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTwlapakrNIAYLFQEARLLPHLSIEDNIRLNLKLR 104
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLRLIAGLLPPaAGTIKLDGGDIDDPDVAE-------ACHYLGHRNAMKPALTVAENLEFWAAFL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024600867 105 KVHksDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQR 177
Cdd:PRK13539 102 GGE--ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
27-239 |
3.69e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.44 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGL----EQPHGEISVNKQVWQRSS-CNTWLAPAKRNIAYLFQEARLLPHLSIEDNI---- 97
Cdd:PRK09984 32 MVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQREGrLARDIRKSRANTGYIFQQFNLVNRLSVLENVliga 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 -----------RLNLKLRKVHKSDLdITRVlddcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDAT 166
Cdd:PRK09984 112 lgstpfwrtcfSWFTREQKQRALQA-LTRV----GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024600867 167 SKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQtfaehsalFDQEQLASVFEA 239
Cdd:PRK09984 187 SARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ--------FDNERFDHLYRS 251
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-167 |
4.02e-17 |
|
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: 78.69 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISvnkqvWQRSSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLnlkLRKVHk 108
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPlAGRVL-----LNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF---WHADH- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1024600867 109 SDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATS 167
Cdd:cd03231 102 SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-222 |
4.53e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.14 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 17 QIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVW--QRSSCNTW-LAPAKRNIAYLFQEARLLPhLSI 93
Cdd:PRK14271 39 QVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlgGRSIFNYRdVLEFRRRVGMLFQRPNPFP-MSI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 94 EDNIRLNLKLRKV--HKSDLDITRV-LDDCGL-----SRLrSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDA 165
Cdd:PRK14271 118 MDNVLAGVRAHKLvpRKEFRGVAQArLTEVGLwdavkDRL-SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 166 TSKRQMLRLIQRFksSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFA 222
Cdd:PRK14271 197 TTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-209 |
4.57e-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: 79.40 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPH-GEISVNKQvwqrsscNTW--LAPA---------KRNIAYLFQEARLLPHLSIEDNIRL 99
Cdd:COG4778 44 GPSGAGKSTLLKCIYGNYLPDsGSILVRHD-------GGWvdLAQAspreilalrRRTIGYVSQFLRVIPRVSALDVVAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 NLKLRKVHKSD-LDITRVLddcgLSRLR-SQR-----PDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQML 172
Cdd:COG4778 117 PLLERGVDREEaRARAREL----LARLNlPERlwdlpPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVV 192
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 173 RLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:COG4778 193 ELIEEAKARGTA-IIGIFHDEEVREAVADRVVDVTPF 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
29-223 |
6.64e-17 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 82.01 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVN----KQvWQRSSCNtwlapakRNIAYLFQEARLLPHlSIEDNI---RLN 100
Cdd:TIGR01842 348 AIIGPSGSGKSTLARLIVGIWPPtSGSVRLDgadlKQ-WDRETFG-------KHIGYLPQDVELFPG-TVAENIarfGEN 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 L---------KLRKVHksDLdITRVLDdcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:TIGR01842 419 AdpekiieaaKLAGVH--EL-ILRLPD--GYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQAL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 172 LRLIQRFKSSSSTPIFyVSHSIDEIaQLADDILLMQQGEAAYLGPALQTFAE 223
Cdd:TIGR01842 494 ANAIKALKARGITVVV-ITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
30-175 |
7.82e-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: 77.78 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISvnkqvWQRSSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLnlkLRKVHK 108
Cdd:TIGR01189 31 VTGPNGIGKTTLLRILAGLLRPdSGEVR-----WNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHF---WAAIHG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024600867 109 S-DLDITRVLDDCGLSRLrSQRP-DTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLI 175
Cdd:TIGR01189 103 GaQRTIEDALAAVGLTGF-EDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
27-217 |
1.19e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.66 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAG-LEQPHGEISVNKQvwQRSSCNTW-LApakRNIAYLFQEARLLPHLSIEDNIRLNL--- 101
Cdd:PRK13548 30 VVAILGPNGAGKSTLLRALSGeLSPDSGEVRLNGR--PLADWSPAeLA---RRRAVLPQHSSLSFPFTVEEVVAMGRaph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVHKSDLdITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIV------CEPDLILMDEPLSALDATSKRQMLRLI 175
Cdd:PRK13548 105 GLSRAEDDAL-VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1024600867 176 QRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPA 217
Cdd:PRK13548 184 RQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
32-222 |
1.28e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.59 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTslLRCIA-------GLEQPHGEISVNKQVwqrsscntwLAPAK---RNIAYLFQEAR--LLPHLSIEDNIRL 99
Cdd:PRK10418 36 GGSGSGKS--LTCAAalgilpaGVRQTAGRVLLDGKP---------VAPCAlrgRKIATIMQNPRsaFNPLHTMHTHARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 NLKLRKVHKSDLDITRVLDDCGLS---RLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:PRK10418 105 TCLALGKPADDATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1024600867 177 RFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFA 222
Cdd:PRK10418 185 SIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-224 |
1.40e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.86 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQPHGEIS---------VNKQVWQRSScntwlapakrniAYLFQEARLLPHLSIEDNI 97
Cdd:TIGR00955 53 LLAVMGSSGAGKTTLMNALAFRSPKGVKGSgsvllngmpIDAKEMRAIS------------AYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 ----RLNLKlRKVHKSD--LDITRVLDDCGLSR---LRSQRPDT---LSGGQRQRACLARAIVCEPDLILMDEPLSALDA 165
Cdd:TIGR00955 121 mfqaHLRMP-RRVTKKEkrERVDEVLQALGLRKcanTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 166 TSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGP---ALQTFAEH 224
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSpdqAVPFFSDL 261
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
29-221 |
2.21e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.00 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRSSCNtwLAPAKRN------IAYLFQE--ARLLPHLSIEDNIRLN 100
Cdd:PRK09473 46 GIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILN--LPEKELNklraeqISMIFQDpmTSLNPYMRVGEQLMEV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 LKLRK-VHKSD--LDITRVLDDCGLSRLRSQR---PDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:PRK09473 124 LMLHKgMSKAEafEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTL 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1024600867 175 IQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTF 221
Cdd:PRK09473 204 LNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVF 250
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-209 |
2.29e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 80.83 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 22 FKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrsSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRL- 99
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPPtSGTVLVGGK-----DIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFy 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 -NLKLRKVHKSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRF 178
Cdd:TIGR01257 1028 aQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170 180 190
....*....|....*....|....*....|.
gi 1024600867 179 KSSSStpIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:TIGR01257 1108 RSGRT--IIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-235 |
2.74e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.74 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 22 FKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISV----NKQVWQRSSCNTWLAPAK--------RNIAYLFQ--EAR 86
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSkYGTIQVgdiyIGDKKNNHELITNPYSKKiknfkelrRRVSMVFQfpEYQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 87 LLPHlSIEDNIRLNLKLRKVHKSDLD--ITRVLDDCGLSRLRSQR-PDTLSGGQRQRACLARAIVCEPDLILMDEPLSAL 163
Cdd:PRK13631 129 LFKD-TIEKDIMFGPVALGVKKSEAKklAKFYLNKMGLDDSYLERsPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGL 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 164 DATSKRQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFaehsalFDQEQLAS 235
Cdd:PRK13631 208 DPKGEHEMMQLILDAKANNKT-VFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF------TDQHIINS 272
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
28-229 |
2.81e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.87 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScntwLAPAKRNIAYLFQ-------------------EARL 87
Cdd:PRK13648 38 TSIVGHNGSGKSTIAKLMIGIEKVkSGEIFYNNQAITDDN----FEKLRKHIGIVFQnpdnqfvgsivkydvafglENHA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 88 LPHlsieDNIRlnlklRKVHKsdlditrVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATS 167
Cdd:PRK13648 114 VPY----DEMH-----RRVSE-------ALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 168 KRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQlADDILLMQQGEAAYLGPALQTFAEHSALFD 229
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTR 238
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
28-227 |
3.32e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.97 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScnTWLAPAKRNIAYLFQEA-RLLPHLSIEDNIR---LNLK 102
Cdd:PRK13636 35 TAILGGNGAGKSTLFQNLNGILKPsSGRILFDGKPIDYSR--KGLMKLRESVGMVFQDPdNQLFSASVYQDVSfgaVNLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRK--VHKSdldITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKS 180
Cdd:PRK13636 113 LPEdeVRKR---VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQK 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1024600867 181 SSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSAL 227
Cdd:PRK13636 190 ELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
29-225 |
8.43e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.56 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQvwqrSSCN-TWLAPAKRNIAYLFQ--EARLLPHlSIEDNIRL---NL 101
Cdd:PRK13644 32 GIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGI----DTGDfSKLQGIRKLVGIVFQnpETQFVGR-TVEEDLAFgpeNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVHKSDLdITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSS 181
Cdd:PRK13644 107 CLPPIEIRKR-VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1024600867 182 SSTpIFYVSHSIDEIaQLADDILLMQQGEAAYLGPALQTFAEHS 225
Cdd:PRK13644 186 GKT-IVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-216 |
1.74e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.28 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVNKQV-WQRSSCNtwlapaKRNIAYLF-QEARLLPHLSIEDNIRLnlkLRKVHK 108
Cdd:COG4586 55 GPNGAGKSTTIKMLTGILVPtSGEVRVLGYVpFKRRKEF------ARRIGVVFgQRSQLWWDLPAIDSFRL---LKAIYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 -SDLDITRVLDDC----GLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:COG4586 126 iPDAEYKKRLDELvellDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERG 205
|
170 180 190
....*....|....*....|....*....|...
gi 1024600867 184 TPIFYVSHSIDEIAQLADDILLMQQGEAAYLGP 216
Cdd:COG4586 206 TTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-209 |
1.94e-15 |
|
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: 74.29 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAG-LEQPHGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQEARLLpHLSIEDNIRLNLKLRK 105
Cdd:cd03290 29 LTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATVEENITFGSPFNK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 V-HKSDLDITRVLDDCGLSRLRSQ-----RPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDA-TSKRQMLRLIQRF 178
Cdd:cd03290 108 QrYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEGILKF 187
|
170 180 190
....*....|....*....|....*....|.
gi 1024600867 179 KSSSSTPIFYVSHSIDEIAQlADDILLMQQG 209
Cdd:cd03290 188 LQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
29-210 |
2.63e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.98 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSScntwlaPA---KRNIAYLfQEAR----LLPHLSIEDNIRLN 100
Cdd:COG1129 282 GIAGLVGAGRTELARALFGADPADsGEIRLDGKPVRIRS------PRdaiRAGIAYV-PEDRkgegLVLDLSIRENITLA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 LkLRKVHKSDL--------DITRVLDDcgLsRLRSQRPD----TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:COG1129 355 S-LDRLSRGGLldrrreraLAEEYIKR--L-RIKTPSPEqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAK 430
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1024600867 169 RQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:COG1129 431 AEIYRLIRELAAEGKA-VIVISSELPELLGLSDRILVMREGR 471
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
29-212 |
3.30e-15 |
|
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: 73.68 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGL-EQPHGEISVNKQVWQRSSCNTWlapaKRNIAYLFQEARLLphlsiEDNIRLNLKLRKVH 107
Cdd:cd03244 34 GIVGRTGSGKSSLLLALFRLvELSSGSILIDGVDISKIGLHDL----RSRISIIPQDPVLF-----SGTIRSNLDPFGEY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 kSDLDITRVLDDCGLSRLRSQRPDTL-----------SGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:cd03244 105 -SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 177 -RFKSSSstpIFYVSHSIDEIAQlADDILLMQQGEAA 212
Cdd:cd03244 184 eAFKDCT---VLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-235 |
3.57e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.67 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIqrefkNTGLT-GVFGPSGCGKT----SLLRCIAG--LEQPHGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQE- 84
Cdd:PRK15134 27 DVSLQI-----EAGETlALVGESGSGKSvtalSILRLLPSppVVYPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 85 -ARLLPHLSIEDNIRLNLKLRKVHKSDL---DITRVLDDCGLsRLRSQR----PDTLSGGQRQRACLARAIVCEPDLILM 156
Cdd:PRK15134 102 mVSLNPLHTLEKQLYEVLSLHRGMRREAargEILNCLDRVGI-RQAAKRltdyPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024600867 157 DEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLAS 235
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNS 259
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
32-177 |
3.92e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.30 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPH-GEISvnkqvWQRSSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHKSD 110
Cdd:PRK13538 34 GPNGAGKTSLLRILAGLARPDaGEVL-----WQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFYQRLHGPGDDE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 111 lDITRVLDDCGLSRlrsqRPD----TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQR 177
Cdd:PRK13538 109 -ALWEALAQVGLAG----FEDvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-233 |
5.59e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.40 E-value: 5.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQ--EARLLPH------- 90
Cdd:PRK13649 29 TIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPtQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEEtvlkdva 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 91 -------LSIEDNIRLNL-KLRKVHKSDlditrvlddcglsRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSA 162
Cdd:PRK13649 109 fgpqnfgVSQEEAEALAReKLALVGISE-------------SLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 163 LDATSKRQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFaEHSALFDQEQL 233
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMT-IVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF-QDVDFLEEKQL 244
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-210 |
5.75e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.02 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 4 KVDISLQRADFAL--QIQREFKNTGLT-------GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrsSCNTWLAP 73
Cdd:PRK11160 336 QVSLTLNNVSFTYpdQPQPVLKGLSLQikagekvALLGRTGCGKSTLLQLLTRAWDPqQGEILLNGQ-----PIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 74 AKRN-IAYLFQEarllPHLsIEDNIRLNLKLRKVHKSDLDITRVLDDCGLSRLRSQ------------RPdtLSGGQRQR 140
Cdd:PRK11160 411 ALRQaISVVSQR----VHL-FSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDdkglnawlgeggRQ--LSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 141 ACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFkSSSSTPIFyVSHSIDEIAQLaDDILLMQQGE 210
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLM-ITHRLTGLEQF-DRICVMDNGQ 550
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-209 |
6.32e-15 |
|
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: 71.96 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQREFKntglTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTwlapaKRNIAYLFQEarllPHL 91
Cdd:cd03247 20 NLSLELKQGEK----IALLGRSGSGKSTLLQLLTGDLKPqQGEITLDGVPVSDLEKAL-----SSLISVLNQR----PYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 92 sIEDNIRLNLKLRkvhksdlditrvlddcglsrlrsqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:cd03247 87 -FDTTLRNNLGRR----------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 1024600867 172 LRLIqrFKSSSSTPIFYVSHSIDEIAQlADDILLMQQG 209
Cdd:cd03247 138 LSLI--FEVLKDKTLIWITHHLTGIEH-MDKILFLENG 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-235 |
6.35e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNTWLAPAkrnIAYLFQEARLLPHLSIEDNI---RLNLKLR 104
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDaGSILIDGQEMRFASTTAALAAG---VAIIYQELHLVPEMTVAENLylgQLPHKGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHKSDLdITRVLDDcgLSRLRSQ-RPDT----LSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:PRK11288 111 IVNRRLL-NYEAREQ--LEHLGVDiDPDTplkyLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELR 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024600867 180 sSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAylgpalQTFAEHSALfDQEQLAS 235
Cdd:PRK11288 188 -AEGRVILYVSHRMEEIFALCDAITVFKDGRYV------ATFDDMAQV-DRDQLVQ 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
32-226 |
9.21e-15 |
|
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: 73.03 E-value: 9.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPH-GEISVN----KQVWQRSscntwlapAKRNIAYLFQEARLLphlsiEDNIRLNLKLRKV 106
Cdd:cd03253 34 GPSGSGKSTILRLLFRFYDVSsGSILIDgqdiREVTLDS--------LRRAIGVVPQDTVLF-----NDTIGYNIRYGRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLI 175
Cdd:cd03253 101 DATDEEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 176 QRFkSSSSTPIFyVSHSIDEIAQlADDILLMQQGEAAYLGPALQTFAEHSA 226
Cdd:cd03253 181 RDV-SKGRTTIV-IAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-227 |
1.01e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.50 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 22 FKNTGLTGVFGPSGCGKTSLLRCIAGLEqphgeISVNKQvwqrSSCNTWLAPA-----------KRNIAYLFQ--EARLL 88
Cdd:PRK13645 34 FKKNKVTCVIGTTGSGKSTMIQLTNGLI-----ISETGQ----TIVGDYAIPAnlkkikevkrlRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 89 PHlSIEDNI-----RLNLKLRKVHKSdldITRVLDDCGLSRLRSQR-PDTLSGGQRQRACLARAIVCEPDLILMDEPLSA 162
Cdd:PRK13645 105 QE-TIEKDIafgpvNLGENKQEAYKK---VPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 163 LDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSAL 227
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELL 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-204 |
1.11e-14 |
|
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: 75.21 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPHGEiSVNKQVwqrsscntwlapakrNIAYLFQEarllphLSIEDNIRLNLKLRKVHK 108
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPDEG-EVDEDL---------------KISYKPQY------ISPDYDGTVEEFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLD----ITRVLDDCGLSRLRSQRPDTLSGGQRQR----ACLARaivcEPDLILMDEPLSALDATSKRQMLRLIQRFKS 180
Cdd:COG1245 428 DDFGssyyKTEIIKPLGLEKLLDKNVKDLSGGELQRvaiaACLSR----DADLYLLDEPSAHLDVEQRLAVAKAIRRFAE 503
|
170 180
....*....|....*....|....
gi 1024600867 181 SSSTPIFYVSHSIDEIAQLADDIL 204
Cdd:COG1245 504 NRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
30-227 |
1.11e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.30 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScntwLAPAKRNIAYLFQEAR-LLPHLSIEDNIR---LNLKLR 104
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPtSGSVLIRGEPITKEN----IREVRKFVGLVFQNPDdQIFSPTVEQDIAfgpINLGLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 K---VHKsdldITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSS 181
Cdd:PRK13652 111 EetvAHR----VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPET 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1024600867 182 SSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSAL 227
Cdd:PRK13652 187 YGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
30-223 |
1.13e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.10 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSScntwLAPAKRNIAYLFQEarllPH-----LSIEDNIRLNLKL 103
Cdd:PRK13632 40 ILGHNGSGKSTISKILTGLLKPQsGEIKIDGITISKEN----LKEIRKKIGIIFQN----PDnqfigATVEDDIAFGLEN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 RKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSS 181
Cdd:PRK13632 112 KKVPPKKMKdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1024600867 182 SSTPIFYVSHSIDEiAQLADDILLMQQGEAAYLGPALQTFAE 223
Cdd:PRK13632 192 RKKTLISITHDMDE-AILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
32-209 |
1.24e-14 |
|
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: 72.57 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVNKQVwQRSSCNTWLapaKRNIAYLFQEarllPHL---SIEDNIRLNLKLRkvh 107
Cdd:cd03249 36 GSSGCGKSTVVSLLERFYDPtSGEILLDGVD-IRDLNLRWL---RSQIGLVSQE----PVLfdgTIAENIRYGKPDA--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 kSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:cd03249 105 -TDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALD 183
|
170 180 190
....*....|....*....|....*....|...
gi 1024600867 177 RFKSSSSTPIfyVSHSIDEIaQLADDILLMQQG 209
Cdd:cd03249 184 RAMKGRTTIV--IAHRLSTI-RNADLIAVLQNG 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-222 |
1.98e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 12 ADFALQIQREFKNTGLTG---------VFGPSGCGKTSLLRCIAGLEQPH---GEISVN-----KQVWQRsscntwlapa 74
Cdd:PLN03211 72 SDETRQIQERTILNGVTGmaspgeilaVLGPSGSGKSTLLNALAGRIQGNnftGTILANnrkptKQILKR---------- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 75 krnIAYLFQEARLLPHLSIEDNI------RLNLKLRKVHK--------SDLDITRvlddCGLSRLRSQRPDTLSGGQRQR 140
Cdd:PLN03211 142 ---TGFVTQDDILYPHLTVRETLvfcsllRLPKSLTKQEKilvaesviSELGLTK----CENTIIGNSFIRGISGGERKR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 141 ACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQT 220
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDA 294
|
..
gi 1024600867 221 FA 222
Cdd:PLN03211 295 MA 296
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
27-210 |
2.68e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.99 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQ-VWQRSscNTWLAPAKR-NIAYLFQEARLLPHLSIEDNIR----- 98
Cdd:PRK10535 36 MVAIVGASGSGKSTLMNILGCLDKPtSGTYRVAGQdVATLD--ADALAQLRReHFGFIFQRYHLLSHLTAAQNVEvpavy 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 99 --LNLKLRKVHKSDLdITRVlddcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:PRK10535 114 agLERKQRLLRAQEL-LQRL----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILH 188
|
170 180 190
....*....|....*....|....*....|....
gi 1024600867 177 RFKSSSSTPIFyVSHSiDEIAQLADDILLMQQGE 210
Cdd:PRK10535 189 QLRDRGHTVII-VTHD-PQVAAQAERVIEIRDGE 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
29-210 |
3.39e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVwqrsscntwlapakrNIAYLFQEARLL-PHLSIEDNIR-LNLKLRK 105
Cdd:COG0488 345 GLIGPNGAGKSTLLKLLAGELEPdSGTVKLGETV---------------KIGYFDQHQEELdPDKTVLDELRdGAPGGTE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHksdldITRVLDDCGLSRLRSQRP-DTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSsst 184
Cdd:COG0488 410 QE-----VRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGT--- 481
|
170 180
....*....|....*....|....*...
gi 1024600867 185 pIFYVSHsiDE--IAQLADDILLMQQGE 210
Cdd:COG0488 482 -VLLVSH--DRyfLDRVATRILEFEDGG 506
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
27-215 |
3.56e-14 |
|
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: 71.36 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScNTWLapaKRNIAYLFQEARLLpHLSIEDNIRLN---LK 102
Cdd:cd03252 30 VVGIVGRSGSGKSTLTKLIQRFYVPeNGRVLVDGHDLALAD-PAWL---RRQVGVVLQENVLF-NRSIRDNIALAdpgMS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKVHKSDL-----DITRVLDDcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQR 177
Cdd:cd03252 105 MERVIEAAKlagahDFISELPE-GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHD 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1024600867 178 FKSSSSTPIfyVSHSIDEIAQlADDILLMQQGEAAYLG 215
Cdd:cd03252 184 ICAGRTVII--IAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
29-210 |
6.51e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 68.24 E-value: 6.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVwqrsscntwlapakrNIAYLFQearllphlsiednirlnlklrkvh 107
Cdd:cd03221 30 GLVGRNGAGKSTLLKLIAGELEPDeGIVTWGSTV---------------KIGYFEQ------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 ksdlditrvlddcglsrlrsqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKsssSTPIF 187
Cdd:cd03221 71 -------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP---GTVIL 122
|
170 180
....*....|....*....|...
gi 1024600867 188 yVSHSIDEIAQLADDILLMQQGE 210
Cdd:cd03221 123 -VSHDRYFLDQVATKIIELEDGK 144
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
29-215 |
6.85e-14 |
|
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: 72.85 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScNTWLapaKRNIAYLFQEARLLPHlSIEDNIRLNlklrkvh 107
Cdd:TIGR01846 487 GIVGPSGSGKSTLTKLLQRLYTPqHGQVLVDGVDLAIAD-PAWL---RRQMGVVLQENVLFSR-SIRDNIALC------- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLDITRVLDDCGL-------SRLRS-------QRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR 173
Cdd:TIGR01846 555 NPGAPFEHVIHAAKLagahdfiSELPQgyntevgEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMR 634
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1024600867 174 liQRFKSSSSTPIFYVSHSIDEIAQlADDILLMQQGEAAYLG 215
Cdd:TIGR01846 635 --NMREICRGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-219 |
7.82e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRcIAGLEQP--HGEISVNKQVwqrssCNTWLAPA-KRNIAYLFQEARLLPHLSIEDNI------ 97
Cdd:PRK10575 39 VTGLIGHNGSGKSTLLK-MLGRHQPpsEGEILLDAQP-----LESWSSKAfARKVAYLPQQLPAAEGMTVRELVaigryp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 ------RLNLKLRKvhKSDLDITRVlddcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:PRK10575 113 whgalgRFGAADRE--KVEEAISLV----GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1024600867 172 LRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQ 219
Cdd:PRK10575 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
35-210 |
8.03e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 35 GCGKTSLLRCIAGLEQP-HGEISVN-KQVWQRSscntwlaPA---KRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHKS 109
Cdd:COG3845 41 GAGKSTLMKILYGLYQPdSGEILIDgKPVRIRS-------PRdaiALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 110 DLD-----ITRVLDDCGLsRLRSQRP-DTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:COG3845 114 DRKaararIRELSERYGL-DVDPDAKvEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGK 192
|
170 180
....*....|....*....|....*..
gi 1024600867 184 TpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:COG3845 193 S-IIFITHKLREVMAIADRVTVLRRGK 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-216 |
1.08e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 72.67 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAG-LEQPHGEISVnkqvwqrsscntwlapaKRNIAYLFQEArLLPHLSIEDNIRLNLKLR- 104
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAeMDKVEGHVHM-----------------KGSVAYVPQQA-WIQNDSLRENILFGKALNe 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHKSDLDITRVLDDcgLSRLRS-------QRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQR 177
Cdd:TIGR00957 728 KYYQQVLEACALLPD--LEILPSgdrteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG 805
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1024600867 178 FKS--SSSTPIFyVSHSIDEIAQLaDDILLMQQGEAAYLGP 216
Cdd:TIGR00957 806 PEGvlKNKTRIL-VTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
29-210 |
1.48e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWLAPAKRNIA-----YLFQEAR--LLPHLSIEDNI--R 98
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPdAGEVHYRMRDGQLRDLYALSEAERRRLLrtewgFVHQHPRdgLRMQVSAGGNIgeR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 99 L---------NLK------LRKVhksDLDITRvLDDcglsrlrsqRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSAL 163
Cdd:PRK11701 116 LmavgarhygDIRatagdwLERV---EIDAAR-IDD---------LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1024600867 164 DATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK11701 183 DVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
32-210 |
1.58e-13 |
|
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: 71.90 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEI---SVNKQVWQRSSCNTWLAPAKRNIaYLFqearllphlsiEDNIRLNLKLRKVH 107
Cdd:TIGR03796 512 GGSGSGKSTIAKLVAGLYQPwSGEIlfdGIPREEIPREVLANSVAMVDQDI-FLF-----------EGTVRDNLTLWDPT 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:TIGR03796 580 IPDADLVRACKDAAIHDVITSRPGgydaelaeggaNLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR 659
|
170 180 190
....*....|....*....|....*....|....
gi 1024600867 177 RfksSSSTPIFyVSHSIDEIAQlADDILLMQQGE 210
Cdd:TIGR03796 660 R---RGCTCII-VAHRLSTIRD-CDEIIVLERGK 688
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-206 |
1.58e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLE---QPHGEISVNKQVWQRsscntwlapakrniaylfqEARLLPHLSIEDNI 97
Cdd:COG2401 52 EIEPGEIVLIVGASGSGKSTLLRLLAGALkgtPVAGCVDVPDNQFGR-------------------EASLIDAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 rlnlklrkvhksdLDITRVLDDCGLSR----LRsqRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR 173
Cdd:COG2401 113 -------------KDAVELLNAVGLSDavlwLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180 190
....*....|....*....|....*....|...
gi 1024600867 174 LIQRFKSSSSTPIFYVSHSIDEIAQLADDILLM 206
Cdd:COG2401 178 NLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
32-210 |
2.01e-13 |
|
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: 68.79 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNTWlapaKRNIAYLFQEARLLPHlSIEDNIRLN---------L 101
Cdd:cd03254 36 GPTGAGKTTLINLLMRFYDPQkGQILIDGIDIRDISRKSL----RSMIGVVLQDTFLFSG-TIMENIRLGrpnatdeevI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVHKSDLDITRVLDdcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDA-TSKR--QMLRLIQRF 178
Cdd:cd03254 111 EAAKEAGAHDFIMKLPN--GYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTeTEKLiqEALEKLMKG 188
|
170 180 190
....*....|....*....|....*....|..
gi 1024600867 179 KSSsstpiFYVSHSIDEIaQLADDILLMQQGE 210
Cdd:cd03254 189 RTS-----IIIAHRLSTI-KNADKILVLDDGK 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-191 |
2.15e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.65 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQ-PHGEISVNKQVWQRSSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLR--KVHK 108
Cdd:PRK10584 43 GESGSGKSTLLAILAGLDDgSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRgeSSRQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFY 188
Cdd:PRK10584 123 SRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLIL 202
|
...
gi 1024600867 189 VSH 191
Cdd:PRK10584 203 VTH 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-217 |
2.22e-13 |
|
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: 68.97 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQR-EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPHG---EISVNKqvwqrsscntwlapakrnIAYLFQEARLL 88
Cdd:cd03237 12 EFTLEVEGgSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEgdiEIELDT------------------VSYKPQYIKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 89 PHLSIEDniRLNLKLRKVHKSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQR----ACLARaivcEPDLILMDEPLSALD 164
Cdd:cd03237 74 YEGTVRD--LLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRvaiaACLSK----DADIYLLDEPSAYLD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1024600867 165 ATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMqQGEAAYLGPA 217
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVA 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
30-215 |
3.05e-13 |
|
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: 67.67 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGL----EQPHGEISVN----KQVWQRsscntwlapAKRNIAYLFQEARLLPHLSIEDNIRLNL 101
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRtegnVSVEGDIHYNgipyKEFAEK---------YPGEIIYVSEEDVHFPTLTVRETLDFAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRkvhksdlditrvlddcGLSRLRSqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRF-KS 180
Cdd:cd03233 109 RCK----------------GNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMaDV 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1024600867 181 SSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03233 168 LKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
32-227 |
5.38e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.99 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrSSCNTWLAPAKRNIAYLFQEARLLPHlSIEDNIRL------NLKLR 104
Cdd:PRK13657 368 GPTGAGKSTLINLLQRVFDPqSGRILIDGT----DIRTVTRASLRRNIAVVFQDAGLFNR-SIEDNIRVgrpdatDEEMR 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHK----SDLdITRVLDdcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKS 180
Cdd:PRK13657 443 AAAEraqaHDF-IERKPD--GYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1024600867 181 SSSTpiFYVSHSIDEIAQlADDILLMQQGEAAYLGpalqTFAEHSAL 227
Cdd:PRK13657 520 GRTT--FIIAHRLSTVRN-ADRILVFDNGRVVESG----SFDELVAR 559
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
32-215 |
8.89e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRsscntwLAP---AKRNIAYLFQEARLLPHLSIEDNIRL-NLKLRKV 106
Cdd:PRK09700 38 GENGAGKSTLMKVLSGIHEPtKGTITINNINYNK------LDHklaAQLGIGIIYQELSVIDELTVLENLYIgRHLTKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 --------HKSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRF 178
Cdd:PRK09700 112 cgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL 191
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 179 KsSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:PRK09700 192 R-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
29-209 |
9.07e-13 |
|
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: 69.21 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQvwQRSSCNtwLAPAKRNIAYLFQEARLLPHlSIEDNI----RLNLK- 102
Cdd:TIGR03797 483 AIVGPSGSGKSTLLRLLLGFETPEsGSVFYDGQ--DLAGLD--VQAVRRQLGVVLQNGRLMSG-SIFENIaggaPLTLDe 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 ----LRKVHKSDlDITRVldDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQmlrLIQRF 178
Cdd:TIGR03797 558 aweaARMAGLAE-DIRAM--PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAI---VSESL 631
|
170 180 190
....*....|....*....|....*....|.
gi 1024600867 179 KSSSSTPIFyVSHSIDEIAQlADDILLMQQG 209
Cdd:TIGR03797 632 ERLKVTRIV-IAHRLSTIRN-ADRIYVLDAG 660
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-221 |
1.76e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.46 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRSSCNTWLAPAKRNI-----AYLFQEA--RLLPHLSIEDNIRLNL 101
Cdd:PRK11022 37 GIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLvgaevAMIFQDPmtSLNPCYTVGFQIMEAI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KlrkVHKSDLDITR------VLDDCGL----SRLrSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:PRK11022 117 K---VHQGGNKKTRrqraidLLNQVGIpdpaSRL-DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQI 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1024600867 172 LRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTF 221
Cdd:PRK11022 193 IELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
32-231 |
2.27e-12 |
|
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: 65.71 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVNKQvwqrSSCNTWLAPAKRNIAYLFQEARLLpHLSIEDNIRLNLK-------- 102
Cdd:cd03251 35 GPSGSGKSTLVNLIPRFYDVdSGRILIDGH----DVRDYTLASLRRQIGLVSQDVFLF-NDTVAENIAYGRPgatreeve 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 --LRKVHKSDLdITRvLDDcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKS 180
Cdd:cd03251 110 eaARAANAHEF-IME-LPE-GYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 181 SSSTpiFYVSHSIDEIAQlADDILLMQQGEAAYLGpalqtfaEHSALFDQE 231
Cdd:cd03251 187 NRTT--FVIAHRLSTIEN-ADRIVVLEDGKIVERG-------THEELLAQG 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
32-233 |
2.63e-12 |
|
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: 67.82 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSScntwLAPAKRNIAYLFQEARLLPHlSIEDNIRLNlklRKVHKSD 110
Cdd:TIGR02203 365 GRSGSGKSTLVNLIPRFYEPDsGQILLDGHDLADYT----LASLRRQVALVSQDVVLFND-TIANNIAYG---RTEQADR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 111 LDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:TIGR02203 437 AEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1024600867 180 SSSSTPIfyVSHSIDEIaQLADDILLMQQGEAAYLGPalqtfaeHSALFDQEQL 233
Cdd:TIGR02203 517 QGRTTLV--IAHRLSTI-EKADRIVVMDDGRIVERGT-------HNELLARNGL 560
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-223 |
2.90e-12 |
|
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: 66.42 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAG-LEQPHGEISVNKQVwQRSSCNTWLAPA--KRNIAY--LFQEARllpHLSIEDNIRLNL 101
Cdd:cd03291 65 MLAITGSTGSGKTSLLMLILGeLEPSEGKIKHSGRI-SFSSQFSWIMPGtiKENIIFgvSYDEYR---YKSVVKACQLEE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVHKSDldiTRVLDDCGLsrlrsqrpdTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSS 181
Cdd:cd03291 141 DITKFPEKD---NTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMA 208
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1024600867 182 SSTPIFyVSHSIDEIaQLADDILLMQQGEAAYLGpalqTFAE 223
Cdd:cd03291 209 NKTRIL-VTSKMEHL-KKADKILILHEGSSYFYG----TFSE 244
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-218 |
3.05e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.30 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNtWLapaKRNIAYLFQEAR-LLPHLSIEDNIR---LNLK 102
Cdd:PRK13647 34 TALLGPNGAGKSTLLLHLNGIYLPQrGRVKVMGREVNAENEK-WV---RSKVGLVFQDPDdQVFSSTVWDDVAfgpVNMG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKvhkSDLDiTRV---LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:PRK13647 110 LDK---DEVE-RRVeeaLKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLH 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1024600867 180 SSSSTpIFYVSHSIDEIAQLADDILLMQQGEA-AYLGPAL 218
Cdd:PRK13647 186 NQGKT-VIVATHDVDLAAEWADQVIVLKEGRVlAEGDKSL 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-209 |
3.14e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.78 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISV-NKQVWQRSSCntwlapAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKV 106
Cdd:PRK13536 71 GLLGPNGAGKSTIARMILGMTSPDaGKITVlGVPVPARARL------ARARIGVVPQFDNLDLEFTVRENLLVFGRYFGM 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKR---QMLR-LIQRFKS 180
Cdd:PRK13536 145 STREIEavIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHliwERLRsLLARGKT 224
|
170 180
....*....|....*....|....*....
gi 1024600867 181 ssstpIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK13536 225 -----ILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-210 |
3.34e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQ------VWQRSscntwlapakRNIAYLFQEARL--LPHLSIEDNI--- 97
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAGSLPPdSGSILIDGKdvtklpEYKRA----------KYIGRVFQDPMMgtAPSMTIEENLala 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 -----RLNLKLRkVHKSDLDITRVLddcgLSRLR---SQRPDT----LSGGQRQRACLARAIVCEPDLILMDEPLSALDA 165
Cdd:COG1101 107 yrrgkRRGLRRG-LTKKRRELFREL----LATLGlglENRLDTkvglLSGGQRQALSLLMATLTKPKLLLLDEHTAALDP 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 166 TSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:COG1101 182 KTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
30-210 |
3.62e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVN----------------KQVWQRSScnTWLAPAKRNIAYLFQEARLLPHLS 92
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPtSGELLIDdhplhfgdysyrsqriRMIFQDPS--TSLNPRQRISQILDFPLRLNTDLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 93 IED-NIRLNLKLRKVhksdlditrvlddcGLSRLR-SQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ 170
Cdd:PRK15112 122 PEQrEKQIIETLRQV--------------GLLPDHaSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1024600867 171 MLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK15112 188 LINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-227 |
3.69e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.44 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSllrCIAGLE---QPH-GEISVNKQVWQRSSCNTWlapaKRNIAYLFQEARLLPHlSIEDNIRLNLKl 103
Cdd:TIGR00958 510 VALVGPSGSGKST---VAALLQnlyQPTgGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLFSG-SVRENIAYGLT- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 rkvHKSDLDITRVLDDCGLSRLRSQRPDT-----------LSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKrqml 172
Cdd:TIGR00958 581 ---DTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE---- 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 173 RLIQRFKSSSSTPIFYVSHSIdEIAQLADDILLMQQGEAAYLGPALQTFAEHSAL 227
Cdd:TIGR00958 654 QLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLMEDQGCY 707
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-179 |
4.06e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.27 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 8 SLQRADFALQIQRE-FKNTGLT-------GVFGPSGCGKTSLLRCIAGLEQPH-GEisvnkqvwqrsscnTWLAPAkRNI 78
Cdd:TIGR03719 6 TMNRVSKVVPPKKEiLKDISLSffpgakiGVLGLNGAGKSTLLRIMAGVDKDFnGE--------------ARPQPG-IKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 79 AYLFQEARLLPHLSIEDNI------------RLNLKLRKVHKSDLDITR----------VLDDCGLSRLRSQ-------- 128
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVeegvaeikdaldRFNEISAKYAEPDADFDKlaaeqaelqeIIDAADAWDLDSQleiamdal 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1024600867 129 R-PD------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:TIGR03719 151 RcPPwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-209 |
5.57e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.60 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISV-NKQVWQRSScntwlaPAKRNIAYLFQEARLLPHLSIEDNIRL------- 99
Cdd:PRK13537 37 GLLGPNGAGKTTTLRMLLGLTHPDaGSISLcGEPVPSRAR------HARQRVGVVPQFDNLDPDFTVRENLLVfgryfgl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 -NLKLRKVHKSDLDITRvLDDCGLSRLRSqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLrliQRF 178
Cdd:PRK13537 111 sAAAARALVPPLLEFAK-LENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW---ERL 181
|
170 180 190
....*....|....*....|....*....|...
gi 1024600867 179 KS--SSSTPIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK13537 182 RSllARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-204 |
5.64e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQP-HGEISvnkqvwqrsscntwlapAKRNIAYLFQEARLLPHLSIEDNirlnlkLRKVh 107
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPdEGEVD-----------------PELKISYKPQYIKPDYDGTVEDL------LRSI- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLD----ITRVLDDCGLSRLRSQRPDTLSGGQRQR----ACLARaivcEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:PRK13409 425 TDDLGssyyKSEIIKPLQLERLLDKNVKDLSGGELQRvaiaACLSR----DADLYLLDEPSAHLDVEQRLAVAKAIRRIA 500
|
170 180
....*....|....*....|....*
gi 1024600867 180 SSSSTPIFYVSHSIDEIAQLADDIL 204
Cdd:PRK13409 501 EEREATALVVDHDIYMIDYISDRLM 525
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
32-209 |
6.10e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.01 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRSSCNtwlAPAKRNIAYLFQEARLLPHLSIEDNI------RLNLKL- 103
Cdd:PRK11300 38 GPNGAGKTTVFNCLTGFYKPTgGTILLRGQHIEGLPGH---QIARMGVVRTFQHVRLFREMTVIENLlvaqhqQLKTGLf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 ---------RKVHKSDLDITRV-LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR 173
Cdd:PRK11300 115 sgllktpafRRAESEALDRAATwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDE 194
|
170 180 190
....*....|....*....|....*....|....*.
gi 1024600867 174 LIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK11300 195 LIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-223 |
6.17e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.70 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRSSCnTWLAPAKR------NIAYLFQEAR--LLPHLSIEDNIRLN 100
Cdd:COG4170 37 GLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDL-LKLSPRERrkiigrEIAMIFQEPSscLDPSAKIGDQLIEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 L-------------KLRKVHKSDLdITRVlddcGL---SRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALD 164
Cdd:COG4170 116 IpswtfkgkwwqrfKWRKKRAIEL-LHRV----GIkdhKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAME 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1024600867 165 ATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAE 223
Cdd:COG4170 191 STTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
27-210 |
1.08e-11 |
|
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: 63.64 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVN-KQVWQRSSCntWLapaKRNIAYLFQEARLLPHlSIEDNIRLNLKlr 104
Cdd:cd03248 42 VTALVGPSGSGKSTVVALLENFYQPQgGQVLLDgKPISQYEHK--YL---HSKVSLVGQEPVLFAR-SLQDNIAYGLQ-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 kvHKSDLDITRVLDDCG----LSRLRS-------QRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR 173
Cdd:cd03248 114 --SCSFECVKEAAQKAHahsfISELASgydtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQ 191
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 174 LIQrfKSSSSTPIFYVSHSIDEIaQLADDILLMQQGE 210
Cdd:cd03248 192 ALY--DWPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-210 |
1.14e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGL--EQPHGEISVN-KQVWQRSScntwlAPAKRNIAYLFQEAR----LLPHLSIEDNIRLNL 101
Cdd:TIGR02633 290 GVAGLVGAGRTELVQALFGAypGKFEGNVFINgKPVDIRNP-----AQAIRAGIAMVPEDRkrhgIVPILGVGKNITLSV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVHKSDLDITRVLD--DCGLSRL--RSQRPD----TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR 173
Cdd:TIGR02633 365 LKSFCFKMRIDAAAELQiiGSAIQRLkvKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYK 444
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 174 LIQRFkSSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:TIGR02633 445 LINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
114-223 |
1.32e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 64.34 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 114 TRVlDDC----GLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYV 189
Cdd:PRK13633 123 ERV-DESlkkvGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILI 201
|
90 100 110
....*....|....*....|....*....|....
gi 1024600867 190 SHSIDEIAQlADDILLMQQGEAAYLGPALQTFAE 223
Cdd:PRK13633 202 THYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-227 |
1.58e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 65.70 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 6 DISLQRADFALQIQREFKNTG-------LTGVFGPSGCGKTSLLRCIAG-LEQPHGEISVNKQVwQRSSCNTWLAPA--K 75
Cdd:TIGR01271 426 DDGLFFSNFSLYVTPVLKNISfklekgqLLAVAGSTGSGKSSLLMMIMGeLEPSEGKIKHSGRI-SFSPQTSWIMPGtiK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 76 RNIAY--LFQEARllpHLSIEDNIRLNLKLRKVHKSDldiTRVLDDCGLsrlrsqrpdTLSGGQRQRACLARAIVCEPDL 153
Cdd:TIGR01271 505 DNIIFglSYDEYR---YTSVIKACQLEEDIALFPEKD---KTVLGEGGI---------TLSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024600867 154 ILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSidEIAQLADDILLMQQGEAAYLGpalqTFAEHSAL 227
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKL--EHLKKADKILLLHEGVCYFYG----TFSELQAK 637
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-216 |
1.83e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRsscntwLAPAKRN---IAYLFQEARLLPHLSIEDNIRLNLKLRKVH 107
Cdd:PRK15439 44 GGNGAGKSTLMKIIAGIVPPDsGTLEIGGNPCAR------LTPAKAHqlgIYLVPQEPLLFPNLSVKENILFGLPKRQAS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLdiTRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSsTPIF 187
Cdd:PRK15439 118 MQKM--KQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQG-VGIV 194
|
170 180
....*....|....*....|....*....
gi 1024600867 188 YVSHSIDEIAQLADDILLMQQGEAAYLGP 216
Cdd:PRK15439 195 FISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
78-210 |
2.28e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 78 IAYLFQEARLLPHLSIEDNIRLN---------LKLRKVHKsdlDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIV 148
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGrefvnrfgrIDWKKMYA---EADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 149 CEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRG-IVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-215 |
2.98e-11 |
|
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: 61.88 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQP---HGEISVNKQvwQRSSCNTwlapakRNIAYLFQEARLLPHLSIEDNIRLNLKL 103
Cdd:cd03232 35 LTALMGESGAGKTTLLDVLAGRKTAgviTGEILINGR--PLDKNFQ------RSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 RKvhksdlditrvlddcglsrlrsqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:cd03232 107 RG---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ 159
|
170 180 190
....*....|....*....|....*....|...
gi 1024600867 184 TPIFYVSHSIDEIAQLADDILLMQQ-GEAAYLG 215
Cdd:cd03232 160 AILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-230 |
4.80e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.55 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRSSCNTWlapaKRNIAYLFQEARLLphlsiEDNIRLNLKLRKvHK 108
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTW----RKAFGVIPQKVFIF-----SGTFRKNLDPYE-QW 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 109 SDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSkRQMLRLIQR 177
Cdd:TIGR01271 1319 SDEEIWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT-LQIIRKTLK 1397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1024600867 178 FKSSSSTPIFyVSHSIDeiAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQ 230
Cdd:TIGR01271 1398 QSFSNCTVIL-SEHRVE--ALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-210 |
5.23e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLeQPHG----EISVNKQVWQ-RSSCNTwlapAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKV 106
Cdd:PRK13549 38 GENGAGKSTLMKVLSGV-YPHGtyegEIIFEGEELQaSNIRDT----ERAGIAIIHQELALVKELSVLENIFLGNEITPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 HKSD-----LDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSS 181
Cdd:PRK13549 113 GIMDydamyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH 192
|
170 180
....*....|....*....|....*....
gi 1024600867 182 SSTPIfYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK13549 193 GIACI-YISHKLNEVKAISDTICVIRDGR 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
32-208 |
6.41e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQPhgeisvnkqvwqrsSCNTWLAPAKRNIAYLFQEARLLPHLSIedNIRLNLKLRKVHKSDl 111
Cdd:PRK09544 37 GPNGAGKSTLVRVVLGLVAP--------------DEGVIKRNGKLRIGYVPQKLYLDTTLPL--TVNRFLRLRPGTKKE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 112 DITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSH 191
Cdd:PRK09544 100 DILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
|
170
....*....|....*..
gi 1024600867 192 SIDEIAQLADDILLMQQ 208
Cdd:PRK09544 180 DLHLVMAKTDEVLCLNH 196
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-191 |
8.91e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 3 IKVDISLQRADFALQIQREFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISvnkqvWQRSSCNTWLAPAKRNIAYL 81
Cdd:PRK13540 5 IELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEIL-----FERQSIKKDLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 82 FQEARLLPHLSIEDNIRLNLKLRKvhkSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLS 161
Cdd:PRK13540 80 GHRSGINPYLTLRENCLYDIHFSP---GAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|
gi 1024600867 162 ALDATSKRQMLRLIQRFKSSSSTpIFYVSH 191
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGA-VLLTSH 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
32-221 |
1.01e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQ-PHGEISVNKQVWQRsscntwlAPAKRNIAYLFQEARL---LPHLsIEDNIRLNLK----- 102
Cdd:PRK15056 40 GVNGSGKSTLFKALMGFVRlASGKISILGQPTRQ-------ALQKNLVAYVPQSEEVdwsFPVL-VEDVVMMGRYghmgw 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKVHKSDLDI-TRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSS 181
Cdd:PRK15056 112 LRRAKKRDRQIvTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1024600867 182 SSTpIFYVSHSIDEIAQLAdDILLMQQGEAAYLGPALQTF 221
Cdd:PRK15056 192 GKT-MLVSTHNLGSVTEFC-DYTVMVKGTVLASGPTETTF 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-212 |
1.73e-10 |
|
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: 60.12 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCI-AGLEQPHGEISVNKQvwqrSSCNTWLAPAKRNIAYLFQEARLLphlsiEDNIRLNLKlRKVH 107
Cdd:cd03369 38 GIVGRTGAGKSTLILALfRFLEAEEGKIEIDGI----DISTIPLEDLRSSLTIIPQDPTLF-----SGTIRSNLD-PFDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLDITRVLDdcglsrlRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQrfKSSSSTPIF 187
Cdd:cd03369 108 YSDEEIYGALR-------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR--EEFTNSTIL 178
|
170 180
....*....|....*....|....*
gi 1024600867 188 YVSHSIDEIAQLaDDILLMQQGEAA 212
Cdd:cd03369 179 TIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-210 |
1.99e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.76 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLeQPHG----EISVNKQVWQRSSCNTwlaPAKRNIAYLFQEARLLPHLSIEDNI------- 97
Cdd:TIGR02633 31 GLCGENGAGKSTLMKILSGV-YPHGtwdgEIYWSGSPLKASNIRD---TERAGIVIIHQELTLVPELSVAENIflgneit 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 -------------RLNLKLRKVHKSDLDITRVLDDCGlsrlrsqrpdtlsGGQRQRACLARAIVCEPDLILMDEPLSALD 164
Cdd:TIGR02633 107 lpggrmaynamylRAKNLLRELQLDADNVTRPVGDYG-------------GGQQQLVEIAKALNKQARLLILDEPSSSLT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1024600867 165 ATSKRQMLRLIQRFKSSSSTPIfYVSHSIDEIAQLADDILLMQQGE 210
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHGVACV-YISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-247 |
2.31e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQPHGEISVNKQvwqrsSCNTWLAP--AKRNiAYLFQEARLLPHLSIEDNIRLNLKlRKVH 107
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLPGSGSIQFAGQ-----PLEAWSAAelARHR-AYLSQQQTPPFAMPVFQYLTLHQP-DKTR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSdlDITRVLDD-CGLSRLRSQ--RP-DTLSGGQRQRACLA-------RAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:PRK03695 100 TE--AVASALNEvAEALGLDDKlgRSvNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 177 RFkSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEhsalfdqEQLASVFEATITELDQE 247
Cdd:PRK03695 178 EL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTP-------ENLAQVFGVNFRRLDVE 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-248 |
2.51e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.10 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAG-LEQPHGEisvnkqVWqrsscntwlapAKRNIAYLFQEARLLpHLSIEDNI-------- 97
Cdd:PTZ00243 688 LTVVLGATGSGKSTLLQSLLSqFEISEGR------VW-----------AERSIAYVPQQAWIM-NATVRGNIlffdeeda 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 -RLNLKLRkVHKSDLDITRVldDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQ 176
Cdd:PTZ00243 750 aRLADAVR-VSQLEADLAQL--GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF 826
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 177 RFKSSSSTPIFyVSHSIdEIAQLADDILLMQQGEAAylgpalqtFAEHSALFdqeqLASVFEATITELDQEN 248
Cdd:PTZ00243 827 LGALAGKTRVL-ATHQV-HVVPRADYVVALGDGRVE--------FSGSSADF----MRTSLYATLAAELKEN 884
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
32-210 |
2.88e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGL-EQPHGEISVNKQVWQRSSCNTWLapaKRNIAYLFQEARLLPHLSIEDNI---RLNLKLRKVH 107
Cdd:PRK10982 31 GENGAGKSTLLKCLFGIyQKDSGSILFQGKEIDFKSSKEAL---ENGISMVHQELNLVLQRSVMDNMwlgRYPTKGMFVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDL--DITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTp 185
Cdd:PRK10982 108 QDKMyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCG- 186
|
170 180
....*....|....*....|....*
gi 1024600867 186 IFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK10982 187 IVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-210 |
3.59e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.09 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSscNTWLAPAKRNIAYLFQ---EARLLPhlSIEDNIR---LNLK 102
Cdd:PRK13639 33 LLGPNGAGKSTLFLHFNGILKPtSGEVLIKGEPIKYD--KKSLLEVRKTVGIVFQnpdDQLFAP--TVEEDVAfgpLNLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRK--VHKSdldITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKS 180
Cdd:PRK13639 109 LSKeeVEKR---VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK 185
|
170 180 190
....*....|....*....|....*....|
gi 1024600867 181 SSSTpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK13639 186 EGIT-IIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
76-228 |
3.71e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 76 RNIAYLFQEARLLPHLSIEDNIrlnlKLRKVHKSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLA 144
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFNMSIYENI----KFGKEDATREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIA 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 145 RAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQlADDILLMQQGEAAylGPALQTFAEH 224
Cdd:PTZ00265 1371 RALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNPDRT--GSFVQAHGTH 1447
|
....
gi 1024600867 225 SALF 228
Cdd:PTZ00265 1448 EELL 1451
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
32-209 |
4.44e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.12 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVNKQV---WQRSSCntwlapAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVH 107
Cdd:PRK11614 38 GANGAGKTTLLGTLCGDPRAtSGRIVFDGKDitdWQTAKI------MREAVAIVPEGRRVFSRMTVEENLAMGGFFAERD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDLDITRVLDDcgLSRL---RSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSST 184
Cdd:PRK11614 112 QFQERIKWVYEL--FPRLherRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMT 189
|
170 180
....*....|....*....|....*
gi 1024600867 185 pIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK11614 190 -IFLVEQNANQALKLADRGYVLENG 213
|
|
| MopI |
COG3585 |
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism]; |
273-360 |
8.46e-10 |
|
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism];
Pssm-ID: 442804 [Multi-domain] Cd Length: 141 Bit Score: 56.62 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 273 LSEGQKIRLRVTARDVSISRFPNTEQSILNVLPARIKNIKHTSESHSVRIKLAiGDNTLHALITKRSLKKLNLKIDQEVW 352
Cdd:COG3585 49 LVGGKEVAALKKASVVILATDDAMKLSARNQLKGTVTRIERGAVNSEVVLDLG-GGTTLTAVITNESVEELGLKEGDEVT 127
|
....*...
gi 1024600867 353 AQVKALSI 360
Cdd:COG3585 128 ALFKASSV 135
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-210 |
9.18e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQ-PHGEISVN-KQVWQRSScntwLAPAKRNIAYLFQEAR---LLPHLSIEDNIRLNLKL 103
Cdd:PRK09700 293 GFAGLVGSGRTELMNCLFGVDKrAGGEIRLNgKDISPRSP----LDAVKKGMAYITESRRdngFFPNFSIAQNMAISRSL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 RK---------VHKSD----LDITRVLDDCGLSRLrSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ 170
Cdd:PRK09700 369 KDggykgamglFHEVDeqrtAENQRELLALKCHSV-NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAE 447
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1024600867 171 MLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK09700 448 IYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-209 |
1.15e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAG-LEQPHGEISVNKQVWQRSSCNTWLApakRNIAYLfQEAR----LLPHLSIEDNIRLNlKL 103
Cdd:PRK10762 282 GVSGLMGAGRTELMKVLYGaLPRTSGYVTLDGHEVVTRSPQDGLA---NGIVYI-SEDRkrdgLVLGMSVKENMSLT-AL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 104 RKVHKSDLDITR------VLDDCGLSRL----RSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR 173
Cdd:PRK10762 357 RYFSRAGGSLKHadeqqaVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ 436
|
170 180 190
....*....|....*....|....*....|....*.
gi 1024600867 174 LIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK10762 437 LINQFKAEGLS-IILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-210 |
1.32e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQ--PHGEISVNKQVWQRSSCNTWLApakRNIAYLfQEAR----LLPHLSIEDNIRLNLK 102
Cdd:PRK13549 292 GIAGLVGAGRTELVQCLFGAYPgrWEGEIFIDGKPVKIRNPQQAIA---QGIAMV-PEDRkrdgIVPVMGVGKNITLAAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKVHKSDLDITRVLDDCG--LSRLRSQRPD------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:PRK13549 368 DRFTGGSRIDDAAELKTILesIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKL 447
|
170 180 190
....*....|....*....|....*....|....*.
gi 1024600867 175 IQRFkSSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK13549 448 INQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
29-167 |
1.73e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEisvnkqvwqrsscnTWLAPAKRnIAYLFQEARLLPHLSIEDNI---------- 97
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFeGE--------------ARPAPGIK-VGYLPQEPQLDPEKTVRENVeegvaevkaa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 --RLN---------------L-----KLR-KVHKSDL-DITRVLD---DCglsrLRSQRPDT----LSGGQRQRACLARA 146
Cdd:PRK11819 102 ldRFNeiyaayaepdadfdaLaaeqgELQeIIDAADAwDLDSQLEiamDA----LRCPPWDAkvtkLSGGERRRVALCRL 177
|
170 180
....*....|....*....|.
gi 1024600867 147 IVCEPDLILMDEPLSALDATS 167
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDAES 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-210 |
1.91e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 26 GLTGVF-GPSGCGKTSLLRCIAGLEQP-HGEISVN-----KQV---WQRSSCNT-------WLAPAKRNIAYLFQEARLL 88
Cdd:PTZ00265 411 GKTYAFvGESGCGKSTILKLIERLYDPtEGDIIINdshnlKDInlkWWRSKIGVvsqdpllFSNSIKNNIKYSLYSLKDL 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 89 PHLSIE---------DNIRLNLKLRKVHKSDL-DITRVLDDCGLSRLR------------------------SQRPDT-- 132
Cdd:PTZ00265 491 EALSNYynedgndsqENKNKRNSCRAKCAGDLnDMSNTTDSNELIEMRknyqtikdsevvdvskkvlihdfvSALPDKye 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 133 ---------LSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIaQLADDI 203
Cdd:PTZ00265 571 tlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTI 649
|
....*..
gi 1024600867 204 LLMQQGE 210
Cdd:PTZ00265 650 FVLSNRE 656
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
21-219 |
2.44e-09 |
|
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: 56.04 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFKNTGLTGVFGPSGCGKTSLLRCIAGLEQPHGEisvnKQVWqrsscntwlapakrniaylfqearllphlsieDNIRLN 100
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD----NDEW--------------------------------DGITPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 LKLRKVhksdlditrvlddcglsrlrsqrpdTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKS 180
Cdd:cd03222 65 YKPQYI-------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 1024600867 181 SSSTPIFYVSHSIDEIAQLAdDILLMQQGEAAYLGPALQ 219
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYLS-DRIHVFEGEPGVYGIASQ 157
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-252 |
3.06e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 18 IQREFKNTGLTGVFGPSGCGKTSLLRCIAGlEQPHGEISvnkQVWQRSScntwlapakrnIAYLFQEARLLpHLSIEDNI 97
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELSHAETS---SVVIRGS-----------VAYVPQVSWIF-NATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 RLNLKLR-KVHKSDLDITRVLDDCGLSRLRS-----QRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:PLN03232 700 LFGSDFEsERYWRAIDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 172 LRLIQRFKSSSSTPIFyVSHSIDEIAQLaDDILLMQQGEAAYLGpalqTFAE---HSALFDQ-EQLASVFEATITELDQE 247
Cdd:PLN03232 780 FDSCMKDELKGKTRVL-VTNQLHFLPLM-DRIILVSEGMIKEEG----TFAElskSGSLFKKlMENAGKMDATQEVNTND 853
|
....*
gi 1024600867 248 NSLSK 252
Cdd:PLN03232 854 ENILK 858
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
29-230 |
3.52e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.19 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIagleQPH-----GEISVNKQVWQRSSCNTWlapaKRNIAYLFQEARLLPHlSIEDNIRLN--- 100
Cdd:PRK10789 345 GICGPTGSGKSTLLSLI----QRHfdvseGDIRFHDIPLTKLQLDSW----RSRLAVVSQTPFLFSD-TVANNIALGrpd 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 ---------LKLRKVHKsdlDITRVLDdcGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:PRK10789 416 atqqeiehvARLASVHD---DILRLPQ--GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1024600867 172 LRLIQRFKSSSSTPIfyVSHSIDEIAQlADDILLMQQGEAAYLGPalqtfaeHSALFDQ 230
Cdd:PRK10789 491 LHNLRQWGEGRTVII--SAHRLSALTE-ASEILVMQHGHIAQRGN-------HDQLAQQ 539
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
132-210 |
3.97e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 3.97e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024600867 132 TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFkSSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK15439 403 TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
10-192 |
4.93e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 10 QRADFALQIQreFKNTGLTGVFGPSGCGKTSLLRCIAGLEQP-HGEIsvnkqVWQRSSCNTWlapAKRNIAYLFQEARLL 88
Cdd:PRK13541 13 QKNLFDLSIT--FLPSAITYIKGANGCGKSSLLRMIAGIMQPsSGNI-----YYKNCNINNI---AKPYCTYIGHNLGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 89 PHLSIEDNIRLnlkLRKVHKSDLDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:PRK13541 83 LEMTVFENLKF---WSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
170 180
....*....|....*....|....
gi 1024600867 169 RQMLRLIQrFKSSSSTPIFYVSHS 192
Cdd:PRK13541 160 DLLNNLIV-MKANSGGIVLLSSHL 182
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
29-210 |
5.62e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.73 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRSSCNTWLAPAKR-----NIAYLFQEAR--LLPHLSIEDNI---- 97
Cdd:PRK15093 37 GLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPRERRklvghNVSMIFQEPQscLDPSERVGRQLmqni 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 -----------RLNLKLRK----VH----KSDLDITRVLddcglsrlrsqrPDTLSGGQRQRACLARAIVCEPDLILMDE 158
Cdd:PRK15093 117 pgwtykgrwwqRFGWRKRRaielLHrvgiKDHKDAMRSF------------PYELTEGECQKVMIAIALANQPRLLIADE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 159 PLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:PRK15093 185 PTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-217 |
8.57e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAG-LEQPHgeISVNKQVWQRSSCNTWLAPAKR-NIAYLFQEARLLPHLSIEDNIRLNLKLR 104
Cdd:TIGR00956 89 LTVVLGRPGSGCSTLLKTIASnTDGFH--IGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTVGETLDFAARCK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHKSDLDITR----------VLDDCGLSRLRsqrpDT---------LSGGQRQRACLARAIVCEPDLILMDEPLSALDA 165
Cdd:TIGR00956 167 TPQNRPDGVSReeyakhiadvYMATYGLSHTR----NTkvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1024600867 166 TSKRQMLRLIQRFKS-SSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGPA 217
Cdd:TIGR00956 243 ATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPA 295
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-177 |
1.34e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAG---LEQphGEISV-----NKQVWQRSSCntwlapakRNIAYLFQE--ARLLPHLSIEDNI- 97
Cdd:NF033858 31 GLIGPDGVGKSSLLSLIAGarkIQQ--GRVEVlggdmADARHRRAVC--------PRIAYMPQGlgKNLYPTLSVFENLd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 ---RL---NLKLRKVHksdldITRVLDDCGLSRLRSqRP-DTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ 170
Cdd:NF033858 101 ffgRLfgqDAAERRRR-----IDELLRATGLAPFAD-RPaGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQ 174
|
....*..
gi 1024600867 171 MLRLIQR 177
Cdd:NF033858 175 FWELIDR 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
113-229 |
1.73e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 113 ITRVLDDCGLSrlrsqrPDT----LSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSsstpIFY 188
Cdd:PRK11147 139 INEVLAQLGLD------PDAalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS----IIF 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 189 VSHSIDEIAQLADDILLMQQGE--------AAYL---GPALQTFAEHSALFD 229
Cdd:PRK11147 209 ISHDRSFIRNMATRIVDLDRGKlvsypgnyDQYLlekEEALRVEELQNAEFD 260
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-164 |
2.02e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQPH-GEISVNKQVWQRsscntwlAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVHK 108
Cdd:PRK13543 42 VQGDNGAGKTTLLRVLAGLLHVEsGQIQIDGKTATR-------GDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRA 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024600867 109 SDLDiTRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALD 164
Cdd:PRK13543 115 KQMP-GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-212 |
3.03e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPH-GEISVN-KQVWQRSScntwlAPAKRNIAYLFQEAR----LLPHLSIEDNIrlNLK 102
Cdd:PRK11288 283 GLFGLVGAGRSELMKLLYGATRRTaGQVYLDgKPIDIRSP-----RDAIRAGIMLCPEDRkaegIIPVHSVADNI--NIS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKVHKS-----DLDITRVLDDCGLSRLRSQRPD------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQM 171
Cdd:PRK11288 356 ARRHHLRagcliNNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEI 435
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1024600867 172 LRLIQRFKSSSSTPIFyVSHSIDEIAQLADDILLMQQGEAA 212
Cdd:PRK11288 436 YNVIYELAAQGVAVLF-VSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-213 |
3.66e-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: 53.91 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 26 GLTGVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQ------RSS---------CNTWLAPAKRNiaylfQEARLLPH 90
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDeildefRGSelqnyftklLEGDVKVIVKP-----QYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 91 lSIEDNIRLNLKlRKVHKSDLDItrVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ 170
Cdd:cd03236 102 -AVKGKVGELLK-KKDERGKLDE--LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1024600867 171 MLRLIQRFkSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAY 213
Cdd:cd03236 178 AARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPGAY 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
29-164 |
4.39e-08 |
|
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: 53.70 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRSSCNTWlapaKRNIAYLFQEARLLphlsiEDNIRLNLKLRKVHk 108
Cdd:cd03289 34 GLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKW----RKAFGVIPQKVFIF-----SGTFRKNLDPYGKW- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 109 SDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALD 164
Cdd:cd03289 104 SDEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-216 |
4.83e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 16 LQIQRE----FKNTGLTGVFGPSGCGKTSLLRCIAGLEQP---HGEISV-----NKQVWQRSScntwlapakrniAYLFQ 83
Cdd:PLN03140 893 LQLLREvtgaFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyiEGDIRIsgfpkKQETFARIS------------GYCEQ 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 84 EARLLPHLSIEDNIRLNLKLR---KVHKSD--LDITRVLDDCGLSRLRSQ---RPDT--LSGGQRQRACLARAIVCEPDL 153
Cdd:PLN03140 961 NDIHSPQVTVRESLIYSAFLRlpkEVSKEEkmMFVDEVMELVELDNLKDAivgLPGVtgLSTEQRKRLTIAVELVANPSI 1040
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 154 ILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSH-SIDeIAQLADDILLMQQ-GEAAYLGP 216
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpSID-IFEAFDELLLMKRgGQVIYSGP 1104
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-210 |
7.28e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 26 GLTGVfgpSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSScntwlaPAKR---NIAYLfQEAR----LLPHLSIEDNI 97
Cdd:COG3845 288 GIAGV---AGNGQSELAEALAGLRPPaSGSIRLDGEDITGLS------PRERrrlGVAYI-PEDRlgrgLVPDMSVAENL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 98 RLN------------LKLRKVHK------SDLDItrvlddcglsrlRSQRPDT----LSGGQRQRACLARAIVCEPDLIL 155
Cdd:COG3845 358 ILGryrrppfsrggfLDRKAIRAfaeeliEEFDV------------RTPGPDTparsLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 156 MDEPLSALDATSKRQMLRLI--QRfksSSSTPIFYVSHSIDEIAQLADDILLMQQGE 210
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLleLR---DAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
30-217 |
7.45e-08 |
|
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: 52.14 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQP---HGEISVNKQVWqrsscnTWLAP---AKRNIAYLFQEARLLPHLSIEDNIR-LNlk 102
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMGHPKYevtEGEILFKGEDI------TDLPPeerARLGIFLAFQYPPEIPGVKNADFLRyVN-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 lrkvhksdlditrvlddcglsrlrsqrpDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSS 182
Cdd:cd03217 103 ----------------------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEG 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 183 STPIFyVSHSiDEIAQL--ADDILLMQQGEAAYLGPA 217
Cdd:cd03217 155 KSVLI-ITHY-QRLLDYikPDRVHVLYDGRIVKSGDK 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
130-215 |
7.99e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.17 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 130 PDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDLDNVLEWTKRTIFFKDG 241
|
....*.
gi 1024600867 210 EAAYLG 215
Cdd:PRK13651 242 KIIKDG 247
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-285 |
1.12e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQPH-GEISVnkqvwqrsscntwlapaKRNIAYLFQEARLLPHLSIEDNIRLNLKLRK 105
Cdd:PRK13545 52 IVGIIGLNGSGKSTLSNLIAGVTMPNkGTVDI-----------------KGSAALIAISSGLNGQLTGIENIELKGLMMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:PRK13545 115 LTKEKIKeiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 184 TpIFYVSHSIDEIAQLADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLASVFEATITELDQENSLSKAEIKGSQTGAP 263
Cdd:PRK13545 195 T-IFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQMSVEERKDFREEQISQFQHGLLQEDQTGRE 273
|
250 260
....*....|....*....|..
gi 1024600867 264 IAVWIGEQALSEGQKIRLRVTA 285
Cdd:PRK13545 274 RKRKKGKKTSRKFKKKRVLITG 295
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-216 |
1.21e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAGLEQ----PHGEISVNKQVWQRSscntwlapAKRNIAYLFQEARLLPHLSIEDNIRLNLK 102
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNVLAERVTtgviTGGDRLVNGRPLDSS--------FQRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LR---KVHKSDLD--ITRVLDDCGLSRLRsqrpDTLSG--------GQRQRACLARAIVCEPDLIL-MDEPLSALDATSK 168
Cdd:TIGR00956 863 LRqpkSVSKSEKMeyVEEVIKLLEMESYA----DAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1024600867 169 RQMLRLIQRFKSSSSTpIFYVSH--SIDEIAQLaDDILLMQQG-EAAYLGP 216
Cdd:TIGR00956 939 WSICKLMRKLADHGQA-ILCTIHqpSAILFEEF-DRLLLLQKGgQTVYFGD 987
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
133-259 |
1.46e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 133 LSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFyVSHSIDEIAQLaDDILLMQQGEAA 212
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVL-VTNQLHFLSQV-DRIILVHEGMIK 818
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024600867 213 YLGpalqTFAEHSA---LFDQ--EQLAS----VFEATITELDQENSLSKAEIKGSQ 259
Cdd:PLN03130 819 EEG----TYEELSNngpLFQKlmENAGKmeeyVEENGEEEDDQTSSKPVANGNANN 870
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-164 |
2.01e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 13 DFALQIQREFKntglTGVFGPSGCGKTSLLRCIAGLEQP-HGEISvnkqvwqrssCNTwlapaKRNIAYLFQ-EARLLPH 90
Cdd:PRK11147 337 DFSAQVQRGDK----IALIGPNGCGKTTLLKLMLGQLQAdSGRIH----------CGT-----KLEVAYFDQhRAELDPE 397
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024600867 91 LSIEDNIRLNLKLRKVHKSDLDITRVLDDCGLSRLRSQRP-DTLSGGQRQRACLARAIVCEPDLILMDEPLSALD 164
Cdd:PRK11147 398 KTVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| TOBE |
pfam03459 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
300-357 |
2.67e-07 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulfate. Found in ABC transporters immediately after the ATPase domain.
Pssm-ID: 427310 [Multi-domain] Cd Length: 60 Bit Score: 46.89 E-value: 2.67e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1024600867 300 ILNVLPARIKNIKHTSESHSVRIKLAiGDNTLHALITKRSLKKLNLKIDQEVWAQVKA 357
Cdd:pfam03459 1 ARNQLPGTVTVIEPLGSEVEVRVDLG-GGLTLTARITRDSAEELGLAPGDEVWALIKA 57
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-203 |
3.00e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLeQPH----GEISVNKQVWQRSSCNtwlAPAKRNIAYLFQEARLLPHLSIEDNIRL-NLKLRK- 105
Cdd:NF040905 34 GENGAGKSTLMKVLSGV-YPHgsyeGEILFDGEVCRFKDIR---DSEALGIVIIHQELALIPYLSIAENIFLgNERAKRg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 ---VHKSDLDITRVLDDCGLsrlrSQRPDTLSG----GQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRF 178
Cdd:NF040905 110 vidWNETNRRARELLAKVGL----DESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL 185
|
170 180
....*....|....*....|....*
gi 1024600867 179 KSSSSTPIFyVSHSIDEIAQLADDI 203
Cdd:NF040905 186 KAQGITSII-ISHKLNEIRRVADSI 209
|
|
| Mop |
TIGR00638 |
molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin ... |
299-360 |
3.10e-07 |
|
molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin binding proteins of about 70 amino acids in Clostridium pasteurianum, as a tandemly-repeated domain C-terminal to an unrelated domain in ModE, a molybdate transport gene repressor of E. coli, and in single or tandemly paired domains in several related proteins. [Transport and binding proteins, Anions]
Pssm-ID: 273189 [Multi-domain] Cd Length: 69 Bit Score: 47.35 E-value: 3.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024600867 299 SILNVLPARIKNIKHTSESHSVRIKLAiGDNTLHALITKRSLKKLNLKIDQEVWAQVKALSI 360
Cdd:TIGR00638 4 SARNQLKGKVVAIEDGDVNAEVDLLLG-GGTKLTAVITLESVAELGLKPGKEVYAVIKAPWV 64
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-215 |
3.31e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.32 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAG-LEQPHGEISVNKQvwqrsSCNTWLAPAKRNIAYLFQEARLLPHLSIEDNIRLNLKLRKVH 107
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGdTTVTSGDATVAGK-----SILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDldITRV----LDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:TIGR01257 2044 AEE--IEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR 2121
|
170 180 190
....*....|....*....|....*....|..
gi 1024600867 184 TpIFYVSHSIDEIAQLADDILLMQQGEAAYLG 215
Cdd:TIGR01257 2122 A-VVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
133-247 |
4.18e-07 |
|
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: 51.73 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 133 LSGGQRQRACLARAIVCEPDLILMDEPLSALD-ATSKRQMLRLIQRFKSSSSTPIFyVSHSIDEIAQLADDILLMQQGEA 211
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLVHNALEEAVKASGISMVL-TSHWPEVIEDLSDKAIWLENGEI 247
|
90 100 110
....*....|....*....|....*....|....*.
gi 1024600867 212 AYLGpalqtfaehsalfDQEQLASVFEATITELDQE 247
Cdd:TIGR03269 248 KEEG-------------TPDEVVAVFMEGVSEVEKE 270
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
133-210 |
4.27e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.56 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 133 LSGGQRQRACLARAIVCE-PDLILmDEPLSALDATSKRQM---LRLIQRFKSSsstpiFYVSHSIDEIAQlADDILLMQQ 208
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDsPILIL-DEATSALDTESERAIqaaLDELQKNRTS-----LVIAHRLSTIEK-ADEILVVED 553
|
..
gi 1024600867 209 GE 210
Cdd:PRK11176 554 GE 555
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
30-191 |
1.01e-06 |
|
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: 50.52 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQPHGeisvnkqvwqrsscNTWLAPAKRNIAYLFQEarllPHLS---IEDNI-----RLNL 101
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGELWPVYG--------------GRLTKPAKGKLFYVPQR----PYMTlgtLRDQIiypdsSEDM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 KLRKVhkSDLDITRVLDDCGLSRLRSQR---------PDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQML 172
Cdd:TIGR00954 545 KRRGL--SDKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY 622
|
170
....*....|....*....
gi 1024600867 173 RLIQRFKSSsstpIFYVSH 191
Cdd:TIGR00954 623 RLCREFGIT----LFSVSH 637
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-210 |
1.11e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGLEQPhgeisvnkqvwqrSSCNTWL--AP-------AKRNIAYLFQEARLLPHLSIEDNIRL 99
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPA-------------SEGEAWLfgQPvdagdiaTRRRVGYMSQAFSLYGELTVRQNLEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 100 NLKLRKVHKSDLD--ITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK----RQMLR 173
Cdd:NF033858 363 HARLFHLPAAEIAarVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARdmfwRLLIE 442
|
170 180 190
....*....|....*....|....*....|....*..
gi 1024600867 174 LIQRFKSSsstpIFYVSHSIDEiAQLADDILLMQQGE 210
Cdd:NF033858 443 LSREDGVT----IFISTHFMNE-AERCDRISLMHAGR 474
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-164 |
1.33e-06 |
|
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: 49.93 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 26 GLTGVFGPSGCGKTSLLRCIAGLEQPH-GEISV------------------NKQVWQR-SSCNTWLAPAKRNI---AYLF 82
Cdd:TIGR03719 349 GIVGVIGPNGAGKSTLFRMITGQEQPDsGTIEIgetvklayvdqsrdaldpNKTVWEEiSGGLDIIKLGKREIpsrAYVG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 83 qearllphlsiedniRLNLKlrkvhKSDlditrvlddcglsrlRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSA 162
Cdd:TIGR03719 429 ---------------RFNFK-----GSD---------------QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
|
..
gi 1024600867 163 LD 164
Cdd:TIGR03719 474 LD 475
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
27-216 |
1.66e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLLRCIAG-LEQP--------HGEISVNKQVW-----QRSSCNTWLAP--AKRNIAYLFQEARLL-- 88
Cdd:PRK13547 29 VTALLGRNGAGKSTLLKALAGdLTGGgaprgarvTGDVTLNGEPLaaidaPRLARLRAVLPqaAQPAFAFSAREIVLLgr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 89 -PH------LSIEDnirlnlklRKVhksdldITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAI---------VCEPD 152
Cdd:PRK13547 109 yPHarragaLTHRD--------GEI------AWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024600867 153 LILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAYLGP 216
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
121-236 |
2.28e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 121 GLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLA 200
Cdd:PRK10938 124 GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGIT-LVLVLNRFDEIPDFV 202
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1024600867 201 D------DILLMQQGEAAYLgpalqtfaEHSALFDQ----EQLASV 236
Cdd:PRK10938 203 QfagvlaDCTLAETGEREEI--------LQQALVAQlahsEQLEGV 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-191 |
2.53e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGlEQPHGeiSVNKQVW---QRSSCNT-WlaPAKRNIAYLfqEARLlpHLsiedNIRLNLKLRKVH 107
Cdd:PRK10938 293 GPNGAGKSTLLSLITG-DHPQG--YSNDLTLfgrRRGSGETiW--DIKKHIGYV--SSSL--HL----DYRVSTSVRNVI 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 KSDL-----------DITRVLDDCGLSRL--RSQRPD----TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ 170
Cdd:PRK10938 360 LSGFfdsigiyqavsDRQQKLAQQWLDILgiDKRTADapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQL 439
|
170 180
....*....|....*....|.
gi 1024600867 171 MLRLIQRFKSSSSTPIFYVSH 191
Cdd:PRK10938 440 VRRFVDVLISEGETQLLFVSH 460
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
121-215 |
4.48e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 121 GLS---RLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSkrqMLRLIQRFKSSSSTPIFyVSHSIDEIA 197
Cdd:PLN03073 330 GLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIV-VSHAREFLN 405
|
90
....*....|....*....
gi 1024600867 198 QLADDILLMQ-QGEAAYLG 215
Cdd:PLN03073 406 TVVTDILHLHgQKLVTYKG 424
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
116-208 |
6.33e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 116 VLDDCGLSRLRSQRP-DTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSkrqMLRLIQRFKSSSSTPIFyVSHSID 194
Cdd:PRK10636 132 LLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLIL-ISHDRD 207
|
90
....*....|....
gi 1024600867 195 EIAQLADDILLMQQ 208
Cdd:PRK10636 208 FLDPIVDKIIHIEQ 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
27-215 |
1.09e-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: 45.39 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 27 LTGVFGPSGCGKTSLlrciagleqphgeisvnkqvwqrssCNTWLAPAKRNiaylfQEARLLPHLSIEDNIRLnlklrkv 106
Cdd:cd03238 23 LVVVTGVSGSGKSTL-------------------------VNEGLYASGKA-----RLISFLPKFSRNKLIFI------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 107 hksdlDITRVLDDCGLSRLRSQRP-DTLSGGQRQRACLARAIVCEPD--LILMDEPLSALDATSKRQMLRLIQRFKSSSS 183
Cdd:cd03238 66 -----DQLQFLIDVGLGYLTLGQKlSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN 140
|
170 180 190
....*....|....*....|....*....|..
gi 1024600867 184 TpIFYVSHSiDEIAQLADDILLMQQGEAAYLG 215
Cdd:cd03238 141 T-VILIEHN-LDVLSSADWIIDFGPGSGKSGG 170
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-213 |
1.14e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPH-GEISVnkqvwqrsscntwlAPAKRNIAYLFQEARLLPHLS--IEDNIRLNLK-- 102
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNlGDYDE--------------EPSWDEVLKRFRGTELQDYFKklANGEIKVAHKpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 ----LRKVHK---SDL----DITRVLDDC----GLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATS 167
Cdd:COG1245 168 yvdlIPKVFKgtvRELlekvDERGKLDELaeklGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1024600867 168 KRQMLRLIQRFkSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAAY 213
Cdd:COG1245 248 RLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHILYGEPGVY 292
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-164 |
1.48e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 26 GLTGVFGPSGCGKTSLLRCIAGLEQP-HGEISV------------------NKQVWQR-SSCNTWLAPAKRNI---AYLf 82
Cdd:PRK11819 351 GIVGIIGPNGAGKSTLFKMITGQEQPdSGTIKIgetvklayvdqsrdaldpNKTVWEEiSGGLDIIKVGNREIpsrAYV- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 83 qearllphlsiednIRLNLKlrkvhKSDlditrvlddcglsrlRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSA 162
Cdd:PRK11819 430 --------------GRFNFK-----GGD---------------QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTND 475
|
..
gi 1024600867 163 LD 164
Cdd:PRK11819 476 LD 477
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
134-209 |
1.51e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 1.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024600867 134 SGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQG 209
Cdd:PRK13546 145 SSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKT-IFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
30-217 |
1.81e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.79 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGleQPHGEISVNKQVWQRSSCNTwLAP---AKRNIAYLFQEARLLPHLSIEDNIRL--NLKLR 104
Cdd:CHL00131 38 IMGPNGSGKSTLSKVIAG--HPAYKILEGDILFKGESILD-LEPeerAHLGIFLAFQYPIEIPGVSNADFLRLayNSKRK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 105 KVHKSDLD-------ITRVLDDCGLSR--LRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLI 175
Cdd:CHL00131 115 FQGLPELDplefleiINEKLKLVGMDPsfLSRNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGI 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 176 QRFKSSSSTpIFYVSHS---IDEIaqLADDILLMQQGEAAYLGPA 217
Cdd:CHL00131 195 NKLMTSENS-IILITHYqrlLDYI--KPDYVHVMQNGKIIKTGDA 236
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-224 |
3.21e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 30 VFGPSGCGKTSLLRCIAGLEQPhgeisvnkqvwqrsSCNTWLAPAKRNIAYLFQEArlLPHLSIEDNIRLNL-------- 101
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQP--------------SSGTVFRSAKVRMAVFSQHH--VDGLDLSSNPLLYMmrcfpgvp 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 102 --KLRkVHKSDLDITrvlddcglSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFK 179
Cdd:PLN03073 604 eqKLR-AHLGSFGVT--------GNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ 674
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024600867 180 SSsstpIFYVSHSIDEIAQLADDILLMQQGEAAylgPALQTFAEH 224
Cdd:PLN03073 675 GG----VLMVSHDEHLISGSVDELWVVSEGKVT---PFHGTFHDY 712
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
112-238 |
4.33e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.48 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 112 DITRVLDDCGLSRLRSQrPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKR---QMLRLIQRfksssSTPIFY 188
Cdd:PRK10790 457 ELARSLPDGLYTPLGEQ-GNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQaiqQALAAVRE-----HTTLVV 530
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1024600867 189 VSHSIDEIAQlADDILLMQQGEAAYLGPALQTFAEHSALFDQEQLASVFE 238
Cdd:PRK10790 531 IAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGE 579
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-205 |
6.03e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPHGEISvnkqvwqrsscntwlapakrniaylfqearllphlsiednIRLNLKlrkvh 107
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------------IYIDGE----- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 108 ksdlDITRVLDDCGLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQ-----MLRLIQRFKSSS 182
Cdd:smart00382 40 ----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALlllleELRLLLLLKSEK 115
|
170 180
....*....|....*....|...
gi 1024600867 183 STPIFYVSHSIDEIAQLADDILL 205
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-212 |
7.90e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGL-EQPHGEISVNKQVWQRSSCNTwlapAKRNIAYLFQEAR----LLPHLSIEDN-IRLNLK 102
Cdd:PRK10982 278 GIAGLVGAKRTDIVETLFGIrEKSAGTITLHGKKINNHNANE----AINHGFALVTEERrstgIYAYLDIGFNsLISNIR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKVHKSDLDITRVLDDCG--LSRLRSQRPD------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:PRK10982 354 NYKNKVGLLDNSRMKSDTQwvIDSMRVKTPGhrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQL 433
|
170 180 190
....*....|....*....|....*....|....*...
gi 1024600867 175 IQRFkSSSSTPIFYVSHSIDEIAQLADDILLMQQGEAA 212
Cdd:PRK10982 434 IAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
133-216 |
8.71e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 133 LSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRF-KSSSSTPIFYVSHSIDEIAQLADDILLMQQGEA 211
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIvHLTEATVLMSLLQPAPETFDLFDDIILLSEGQI 416
|
....*
gi 1024600867 212 AYLGP 216
Cdd:PLN03140 417 VYQGP 421
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
133-210 |
9.48e-05 |
|
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: 44.43 E-value: 9.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024600867 133 LSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTPIfyVSHSIDEIAQlADDILLMQQGE 210
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV--IAHRLSTIVD-ADEILVLEAGR 569
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-215 |
9.55e-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: 44.55 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAG-LEQPHGEISVNKqvwqrsscntwLAPAKRNIAYLFQEARLLPHLSI--EDNIRLNLKLRK 105
Cdd:TIGR00957 1316 GIVGRTGAGKSSLTLGLFRiNESAEGEIIIDG-----------LNIAKIGLHDLRFKITIIPQDPVlfSGSLRMNLDPFS 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHkSDLDITRVLDDCGLSRLRSQRPD-----------TLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKrqmlRL 174
Cdd:TIGR00957 1385 QY-SDEEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD----NL 1459
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1024600867 175 IQ---RFKSSSSTpIFYVSHSIDEIAQLAdDILLMQQGEAAYLG 215
Cdd:TIGR00957 1460 IQstiRTQFEDCT-VLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-228 |
9.91e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 29 GVFGPSGCGKTSLLRCIAGL-EQPHGEISVNkqvwqrsSCNTwlapAKRNIAYLFQEARLLPHLSI--EDNIRLNLKLRK 105
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIvELEKGRIMID-------DCDV----AKFGLTDLRRVLSIIPQSPVlfSGTVRFNIDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 106 VHkSDLDITRVLDDCGLSRLRSQRP-----------DTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRL 174
Cdd:PLN03232 1335 EH-NDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024600867 175 I-QRFKSSSstpIFYVSHSIDEIAQlADDILLMQQGEA-AYLGPALQTFAEHSALF 228
Cdd:PLN03232 1414 IrEEFKSCT---MLVIAHRLNTIID-CDKILVLSSGQVlEYDSPQELLSRDTSAFF 1465
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
121-228 |
3.42e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.82 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 121 GLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQR-FKSSSSTPIFYVSHSIDEiaql 199
Cdd:cd03288 145 GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTaFADRTVVTIAHRVSTILD---- 220
|
90 100
....*....|....*....|....*....
gi 1024600867 200 ADDILLMQQGEAAYLGPALQTFAEHSALF 228
Cdd:cd03288 221 ADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-178 |
4.27e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 28 TGVFGPSGCGKTSLLRCIAGLEQPhgeisvnkqvwqrSSCNTWLAPAKRNIAYLFQEARLLPHLS--IEDNIRLNLK--- 102
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIP-------------NLGDYEEEPSWDEVLKRFRGTELQNYFKklYNGEIKVVHKpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 ---LRKVHK---SDL----DITRVLDDC----GLSRLRSQRPDTLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSK 168
Cdd:PRK13409 169 vdlIPKVFKgkvRELlkkvDERGKLDEVverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQR 248
|
170
....*....|
gi 1024600867 169 RQMLRLIQRF 178
Cdd:PRK13409 249 LNVARLIREL 258
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
134-215 |
4.50e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 134 SGGQRQRACLARAIVCE-PDLILMDEPLSALDATSKRQmlrlIQRFKSS--SSTPIFYVSHSIDEIAQLaDDILLMQQGE 210
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQ----IQATVMSafSAYTVITIAHRLHTVAQY-DKIIVMDHGA 1521
|
....*
gi 1024600867 211 AAYLG 215
Cdd:PTZ00243 1522 VAEMG 1526
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
32-210 |
4.62e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.88 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 32 GPSGCGKTSLLRCIAGLEQP-HGEISVNKQVWQRSSCNTWlapaKRNIAYLFQEARLLPHL------SIEDNI------R 98
Cdd:PRK10522 356 GGNGSGKSTLAMLLTGLYQPqSGEILLDGKPVTAEQPEDY----RKLFSAVFTDFHLFDQLlgpegkPANPALvekwleR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 99 LNLKlrkvHKSDLDITRVLDdcglsrLRsqrpdtLSGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLR-LIQR 177
Cdd:PRK10522 432 LKMA----HKLELEDGRISN------LK------LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQvLLPL 495
|
170 180 190
....*....|....*....|....*....|...
gi 1024600867 178 FKSSSSTpIFYVSHSiDEIAQLADDILLMQQGE 210
Cdd:PRK10522 496 LQEMGKT-IFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
134-274 |
4.91e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 134 SGGQRQRACLARAIVCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTpIFYVSHSIDEIAQLADDILLMQQG---- 209
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGrvia 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024600867 210 -------EAAYLGPALQTFAEHSALFDQeQLASVFEATITEL-----DQENSLSKAEIKGSQTGAPIAVWIGEQALS 274
Cdd:NF000106 225 dgkvdelKTKVGGRTLQIRPAHAAELDR-MVGAIAQAGLDGIagataDHEDGVVNVPIVSDEQLSAVVGMLGERGFT 300
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
103-204 |
5.97e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 103 LRKVHKSDLDITRVLD----------DCGLSRLRSQRP-DTLSGGQRQRACLARAIVCEPDLI--LMDEPLSALDATSKR 169
Cdd:PRK00635 436 LSQLPSKSLSIEEVLQglksrlsiliDLGLPYLTPERAlATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTH 515
|
90 100 110
....*....|....*....|....*....|....*
gi 1024600867 170 QMLRLIQRFKSSSSTpIFYVSHSiDEIAQLADDIL 204
Cdd:PRK00635 516 KLINVIKKLRDQGNT-VLLVEHD-EQMISLADRII 548
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
115-203 |
1.40e-03 |
|
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: 39.55 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 115 RVLDDCGLSRLR-SQRPDTLSGGQRQRACLARAIVCEPDLIL--MDEPLSALDATSKRQMLRLIQRFKSSSSTpIFYVSH 191
Cdd:cd03270 119 GFLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNT-VLVVEH 197
|
90
....*....|..
gi 1024600867 192 SIDEIaQLADDI 203
Cdd:cd03270 198 DEDTI-RAADHV 208
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
115-204 |
1.40e-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: 40.77 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 115 RVLDDCGLSRLRSQRP-DTLSGGQRQRACLARAI---VCEPDLILMDEPLSALDATSKRQMLRLIQRFKSSSSTpIFYVS 190
Cdd:TIGR00630 811 QTLCDVGLGYIRLGQPaTTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNT-VVVIE 889
|
90
....*....|....
gi 1024600867 191 HSIDEIAQlADDIL 204
Cdd:TIGR00630 890 HNLDVIKT-ADYII 902
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
21-204 |
2.96e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.36 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 21 EFkNTGLTGVFGPSGCGKTSLLRCIAGLEQPHGEISVNKQVWQRSSCNTwlapaKRNIAYlfqearllphlsiednIRLN 100
Cdd:cd03240 19 EF-FSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIRE-----GEVRAQ----------------VKLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024600867 101 LKLRKVHKsdLDITR---VLDDCGLSR------LRSQRPDTLSGGQRQRAC------LARAIVCEPDLILMDEPLSALDA 165
Cdd:cd03240 77 FENANGKK--YTITRslaILENVIFCHqgesnwPLLDMRGRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1024600867 166 TSKRQMLRLIQRFKSSSSTP-IFYVSHSiDEIAQLADDIL 204
Cdd:cd03240 155 ENIEESLAEIIEERKSQKNFqLIVITHD-EELVDAADHIY 193
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
115-177 |
9.84e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.90 E-value: 9.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024600867 115 RVLDDCGLSRLRSQRPDTLSGGQRQRA---CLARAIV---CE-------PDLILMDEPLSALDATSKRQMLRLIQR 177
Cdd:pfam13558 15 EVRDEDGSEVETYRRSGGLSGGEKQLLaylPLAAALAaqyGSaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| |
